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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
      <dc:identifier>doi:10.1073/iti1526123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;With the death of Charles Weissmann, molecular biology has lost of one of its most productive, outstanding, and critical representatives. A molecular biologist who became famous through his ground-breaking discoveries, as well as his scientific ...</description>
      <dc:title>Charles Weissmann (1931–2025), an outstanding and captivating molecular biologist</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606086123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Piet BorstRichard A. FlavellaDivision of Cell Biology, The Netherlands Cancer Institute, Amsterdam 1066CX, NetherlandsbDepartment of Immunobiology, Yale School of Medicine, New Haven, CT 06519</dc:creator>
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      <title>Demystifying invasivorism as a management strategy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2507779123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Demystifying invasivorism as a management strategy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2507779123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Francisco J. OficialdeguiSergio BedmarAntonín KoubaGiovanni VimercatiIvo RoessinkMiguel ClaveroaFaculty of Fisheries and Protection of Waters, South Bohemian Research Center of Aquaculture and Biodiversity of Hydrocenoses University of South Bohemia in České Budějovice, Vodňany 389 01, Czech RepublicbDepartment of Conservation Biology and Global Change, Doñana Biological Station, Spanish National Research Council, Seville 41092, SpaincDepartment of Biology, University of Fribourg, Fribourg 1700, SwitzerlanddTeam Environmental Risk Assessment, Wageningen Environmental Risk Assessment, Wageningen 6708PB, Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2507779123</prism:doi>
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      <title>Toward the simultaneous detection of multiple diseases with a highly cost-effective cell-free DNA methylome test</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518347123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceCell-free DNA (cfDNA) in blood carries molecular signals from multiple organs, offering a powerful, noninvasive way to detect disease and monitor health. Current cfDNA methylation tests are costly and usually focus on a single condition. We ...</description>
      <dc:title>Toward the simultaneous detection of multiple diseases with a highly cost-effective cell-free DNA methylome test</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518347123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Weihua ZengChun-Chi LiuShuo LiYonggang ZhouMary L. StackpoleYing XiaoRan HuCaitlin TangQiao LiuWanwen ZengAngela YehAndrew MelehyBenjamin TranZorawar NoorMegumi YokomizoDominic AmaraShreya GumatePreeti AhujaDavid Yuanze LiJunting ZhaoInga RoseCattlena WalkerSadaf MalikYazhen ZhuHsian-Rong TsengEdward B. GaronSamuel W. FrenchClara E. MagyarSarah M. DryClara M. LajonchereDaniel GeschwindGina ChoiSammy SaabAkshay ShettyCarrie R. WongKevin G. KingDavid S. LuSteven S. RamanXiyan XiangKirti ShettyLopa MishraSanaz MemarzadehYan LiuFrank AlbeWilliam HsuKostyantyn KrysanSteven M. DubinettDenise R. AberleVatche AgopianSteven-Huy B. HanWing Hung WongXiaohui NiWenyuan LiXianghong Jasmine ZhouaDepartment of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095bEarlyDiagnostics Inc., Agoura Hills, CA 91301cDepartment of Statistics, Stanford University, Stanford, CA 94305dDepartment of Medicine, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095eDepartment of Surgery, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095fDepartment of Radiological Sciences, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095gThousand Oaks High School, Thousand Oaks, CA 91360hSage Hill School, Newport Coast, CA 92657iReference Medicine, Phoenix, AZ 85040jCrown Bioscience, San Diego, CA 92127kJonsson Comprehensive Cancer Center, University of California at Los Angeles, Los Angeles, CA 90095lDepartment of Molecular and Medical Pharmacology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA 90095mInstitute for Precision Health, University of California at Los Angeles, Los Angeles, CA 90095nVatche and Tamar Manoukian Division of Digestive Diseases, Department of Medicine, University of California, Los Angeles, CA 90095oThe Institute for Bioelectronic Medicine, Feinstein Institutes for Medical Research and Cold Spring Harbor Laboratory, Department of Medicine, Division of Gastroenterology and Hepatology, Northwell Health, NY 11030pDivision of Gastroenterology and Hepatology, School of Medicine, University of Maryland, Baltimore, MD 21201qDepartment of Surgery, George Washington University, Washington, DC 20037rDepartment of Obstetrics and Gynecology, David Geffen School, University of California at Los Angeles, Los Angeles, CA 90095sEli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, University of California Los Angeles, Los Angeles, CA 90095tMolecular Biology Institute, University of California Los Angeles, Los Angeles, CA 90095uThe VA Greater Los Angeles Healthcare System, Los Angeles, CA 90073vDepartment of Computer Science, University of Southern California, Los Angeles, CA 90089wDepartment of Microbiology, Immunology and Molecular Genetics, University of California at Los Angeles, Los Angeles, CA 90095xInstitute for Quantitative and Computational Biosciences, University of California at Los Angeles, Los Angeles, CA 90095yDepartment of Bioengineering, Samueli School of Engineering, University of California at Los Angeles, Los Angeles, CA 90095zDepartment of Biomedical Data Science, Stanford University, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518347123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518347123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2513997123?af=R">
      <title>Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2513997123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceRecluse spider venoms carry a unique toxin that is not found in other spider venoms and triggers a medical syndrome called loxoscelism, which can involve severe localized skin and tissue damage as well as systemic effects. The toxin is an ...</description>
      <dc:title>Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference</dc:title>
      <dc:identifier>doi:10.1073/pnas.2513997123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Alexandra K. SundmanGreta J. BinfordWilliam R. MontfortMatthew H. J. CordesaDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85701bDepartment of Biology, Lewis &amp; Clark College, Portland, OR 97219</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2513997123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2513997123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R">
      <title>Hydraulic stress limits thermal acclimation in trees under chronic drought</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFuture forest resilience depends on whether trees can acclimate to rising heat and drought. Using multiyear manipulations of soil moisture and air temperature, we tested how long-term acclimation shapes leaf cooling and damage inFagus ...</description>
      <dc:title>Hydraulic stress limits thermal acclimation in trees under chronic drought</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531865123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Alyssa T. KullbergArianna MilanoAlvaro PorettiYike MaPatrick FavreKate M. JohnsonGiovanni BortolamiMaxwell BergströmThibaut JuillardJin WuZhengfei GuoJonas GislerMarcus SchaubCharlotte GrossiordaPlant Ecology Research Laboratory, School of Architecture, Civil and Environmental Engineering, École polytechnique fédérale de Lausanne, Lausanne CH-1015, SwitzerlandbForest and Soil Ecology Research Unit, Swiss Federal Institute for Forest, Snow, and Landscape Research, Birmensdorf CH-8903, SwitzerlandcCentre for Ecological Research and Forestry Applications, Barcelona 08193, SpaindSchool of Biological Sciences and Institute for Climate and Carbon Neutrality, The University of Hong Kong, ChinaeState Key Laboratory of Agrobiotechnology, Chinese University of Hong Kong, Hong Kong, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531865123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521536123?af=R">
      <title>Performative planning creates a values mismatch between wildfire plans and community needs</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521536123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceAs the size and intensity of wildfire in the United States increases, managing wildfire will require addressing multiple interconnected impacts. Most Community Wildfire Protection Plans (CWPPs) prioritize the built environment and human health,...</description>
      <dc:title>Performative planning creates a values mismatch between wildfire plans and community needs</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521536123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Nicola UlibarriRyan J. McCartyMatthew HamiltonHolly K. NesbittMatthew A. WilliamsonaDepartment of Urban Planning and Public Policy, University of California, Irvine, CA 92697bDry Scientific, Inc., Irvine, CA 92617cHaub School of Environment and Natural Resources, University of Wyoming, Laramie, WY 82072dHuman-Environment Systems, Boise State University, Boise, ID 83706</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521536123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521536123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516197123?af=R">
      <title>Reefense: Living shoreline mosaics can achieve ecological and engineering outcomes with interdisciplinary design</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516197123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;Living shorelines that comprise oyster reefs within a mosaic of multiple coastal habitats can be a resilient and adaptive coastal protection alternative to conventional engineered structures. The success of an oyster reef living shoreline depends on the ...</description>
      <dc:title>Reefense: Living shoreline mosaics can achieve ecological and engineering outcomes with interdisciplinary design</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516197123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-03T07:00:00Z</dc:date>
      <dc:creator>Rebecca L. MorrisJaden E. AkersSandra CasasJustin GeldardAlex GoadMarco GhisalbertiXiming GuoReid HollandHongyue JinKelly M. KiblerDanielle KreegerBrendan S. LanhamJerome F. La PeyreRyan J. LoweCynthia E. M. LuptonHani NassifWilliam MatherAndrew W. M. PomeroyElla RothermelMichael RuszalaMadhuwanthi RupasingheF. Scott RikardRichard E. RimanRackel San NicolasJenny P. ShinnPrashansa ShresthaEric L. SparksStephen E. SwearerJyotismita TayeNigel A. TempleManisha N. ThenuwaraPeter B. VienZhenwei WangMason L. WilliamsDavid BushekaSchool of BioSciences, Faculty of Science, The University of Melbourne, Parkville, VIC 3010, AustraliabCoastal Research and Extension Center, Mississippi State University, Biloxi, MS 39532cSchool of Animal Sciences, Louisiana State University Agricultural Center, Baton Rouge, LA 70803dSchool of Earth and Oceans, Oceans Institute, The University of Western Australia, Crawley, WA 6009, AustraliaeReef Design Lab, Mentone, VIC 3194, AustraliafSchool of Engineering, Oceans Institute, The University of Western Australia, Crawley, WA 6009, AustraliagDepartment of Marine and Coastal Sciences, Haskin Shellfish Research Laboratory, Rutgers University, Port Norris, NJ 08349hRutgers Infrastructure Monitoring and Evaluation Group, Department of Civil and Environmental Engineering, Rutgers University, Piscataway, NJ 08854iDepartment of Systems and Industrial Engineering, University of Arizona, Tucson, AZ 85721jDepartment of Civil, Environmental and Construction Engineering, University of Central Florida, Orlando, FL 32816kWSP Climate, Resiliency and Sustainability, Tallahassee, FL 32301lPartnership for the Delaware Estuary, Wilmington, DE 19801mDepartment of Infrastructure Engineering, The University of Melbourne, Melbourne, VIC 3010, AustralianAuburn University Shellfish Lab, School of Fisheries, Aquaculture and Aquatic Science, Auburn University, Dauphin Island, AL 36528oDepartment of Materials Science and Engineering, Rutgers University, Piscataway, NJ 08854pMississippi-Alabama Sea Grant Consortium, Ocean Springs, MS 39564qMississippi Sound Estuary Program, Biloxi, MS 39532rOceans Institute, The University of Western Australia, Crawley, WA 6009, Australia.sDepartment of Civil, Coastal, and Environmental Engineering, The University of South Alabama, Mobile, AL 36688</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516197123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516197123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524258123?af=R">
      <title>Cerebellar contributions to action and cognition: Prediction, timescale, and continuity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524258123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;The cerebellum is implicated in nearly every domain of human cognition, yet our understanding of how this subcortical structure contributes to cognition remains elusive. Efforts on this front have tended to fall into one of two camps. On one side are ...</description>
      <dc:title>Cerebellar contributions to action and cognition: Prediction, timescale, and continuity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524258123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-03T07:00:00Z</dc:date>
      <dc:creator>Jonathan S. TsayRichard B. IvryaDepartment of Psychology, Carnegie Mellon University, Pittsburgh, PA 15213bDepartment of Psychology, University of California, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524258123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524258123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603593123?af=R">
      <title>How do RNA molecules distinguish self from non-self?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603593123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceRNA molecules frequently assemble into clusters inside cells. In organisms including fruit flies, zebrafish, and nematodes, certain RNA clusters are found to be homotypic, comprising multiple copies of the same RNA sequence. Homotypic ...</description>
      <dc:title>How do RNA molecules distinguish self from non-self?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603593123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-03T07:00:00Z</dc:date>
      <dc:creator>Ofer KimchiKira MitchelAndrew G. T. PyoNed S. WingreenElizabeth R. GavisaDepartment of Mathematics, Courant Institute School of Mathematics, Computing, and Data Science, New York University, New York, NY 10012bLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544cDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544dDepartment of Physics, Princeton University, Princeton, NJ 08544</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603593123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603593123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531777123?af=R">
      <title>Phage display–mediated immuno-PCR to detect low-abundance secreted proteins in Drosophila</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531777123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHormones and other secreted factors orchestrate organism-wide physiology, yet their routine quantification inDrosophilahas been limited by the limited volume of hemolymph available for assays like enzyme-linked immunosorbent assay. Here, we ...</description>
      <dc:title>Phage display–mediated immuno-PCR to detect low-abundance secreted proteins in Drosophila</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531777123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Myeonghoon HanBaolong XiaAh-Ram KimElizabeth FilineEmily StoneburnerTing MiaoYing LiuJonathan ZirinNorbert PerrimonaDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, MA 02115bHHMI, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531777123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531777123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516807123?af=R">
      <title>AI-derived therapeutic development of a serotonin receptor–targeting drug for the treatment of opioid use disorder</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516807123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe premise of these studies was to develop and validate a therapeutic for opioid use disorder. Using an AI-based platform aimed at polypharmacy-focused drug discovery, two compounds were synthesized and tested, GATC-021 and GATC-1021. We ...</description>
      <dc:title>AI-derived therapeutic development of a serotonin receptor–targeting drug for the treatment of opioid use disorder</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516807123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Valeria LallaiSamuel KhoA. C. MartinJames P. FowlerMadison L. RoachKevin WangKendyl N. LaumannTyler G. MorrisonMina PalaniappanMalia BautistaAllison S. MogulJinjutha E. CheepluesakBijay ShresthaDhanaji M. LadeJulia E. LagomarsinoVaishnavi NarayanJayson UffensWaldemar LernhardtSaman MirzaeiIan JenkinsArturo R. ZavalaJonathan R. T. LakeyRobert TinderChristie D. FowleraDepartment of Neurobiology and Behavior, University of California, Irvine, CA 92697bGATC Health, Irvine, CA 92614cC. Eugene Bennett Department of Chemistry, West Virginia University, Morgantown, WV 26506dDepartment of Psychology, California State University, Long Beach, CA 90840eDepartment of Surgery, University of California, Irvine, CA 92697fDepartment of Cardiovascular and Thoracic Research, West Virginia University, Morgantown, WV 26506</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516807123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516807123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521857123?af=R">
      <title>Building courage, strength, and knowledge: Mindfulness training reduces psychological threat and increases engagement in college physics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521857123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMany college students experience introductory physics courses as psychologically threatening contexts. Yet, succeeding in these high-stakes gateway courses is necessary to declare majors in engineering and physical sciences. We tested whether ...</description>
      <dc:title>Building courage, strength, and knowledge: Mindfulness training reduces psychological threat and increases engagement in college physics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521857123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Tessa M. Benson-GreenwaldAvital PelakhMichael J. TumminiaSara JahanianMichael S. DiamondEric KuoMelanie GoodTimothy J. Nokes-MalachBrian M. GallaaLearning Research and Development Center, University of Pittsburgh, Pittsburgh, PA 15260bDepartment of Physics, University of Illinois Urbana-Champaign, Urbana, IL 61801cDepartment of Physics &amp; Astronomy, University of Pittsburgh, Pittsburgh, PA 15260</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521857123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521857123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530482123?af=R">
      <title>The detection of episodic memory in others biases social choice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530482123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSharing personal past experiences is central to human social interaction, yet the social function of remembering remains poorly understood. We show that people can detect the contextual richness of others’ memories and use this information to ...</description>
      <dc:title>The detection of episodic memory in others biases social choice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530482123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Elisa CiaramelliAnna WaismanDebora StendardiMorris MoscovitchaDipartimento di Psicologia “Renzo Canestrari”, University of Bologna, Bologna 40126, ItalybDepartment of Psychology, University of Toronto, Toronto, ON M5S 3G3, CanadacRotman Research Institute, Baycrest Health Centre, Toronto, ON M6A 1W1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530482123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530482123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2515768123?af=R">
      <title>Proton-activated chloride channel 1 is essential for innate host defense against bacterial sepsis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2515768123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceBacterial sepsis remains a major global health burden. Here, we report an essential role for the recently discovered acid-sensitive chloride channel, Proton-activated chloride channel 1 (PACC1) (PAC/ASOR/TMEM206), in protective host defense ...</description>
      <dc:title>Proton-activated chloride channel 1 is essential for innate host defense against bacterial sepsis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515768123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Lucien P. GaroKevin BrueckSarah WalachowskiArchana JayaramanMarcel StrueveShuang XuHulbert YangMatthew HelmkampSeung Hoan ChoiChristoph ReinhardtMarkus BosmannaPulmonary Center, Department of Medicine, Boston University Chobanian and Avedisian School of Medicine, Boston, MA 02119bCenter for Thrombosis and Hemostasis, University Medical Center of the Johannes Gutenberg-University Mainz, Mainz 55131, GermanycDepartment of Biostatistics, Boston University School of Public Health, Boston, MA 02119dGerman Center for Cardiovascular Research, Partner Site Rhine-Main, Mainz 55131, GermanyeResearch Center for Immunotherapy, University Medical Center of the Johannes Gutenberg-University Mainz, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515768123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2515768123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531951123?af=R">
      <title>Single-cell insights: Mosquito Toll activation enhances granulocyte differentiation and immune surveillance via Notch suppression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531951123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMosquito immune cells (hemocytes) mediate defenses that can eliminatePlasmodiumparasites. Understanding the development and function of hemocytes is essential for defining natural barriers to malaria transmission. This study provides a ...</description>
      <dc:title>Single-cell insights: Mosquito Toll activation enhances granulocyte differentiation and immune surveillance via Notch suppression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531951123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Banhisikha SahaColton M. McNinchStephanie Serafim De CarvalhoAna Beatriz Barletta FerreiraCarolina Barillas-MuryaLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852bBioinformatics and Computational Biosciences Branch, Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531951123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531951123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527879123?af=R">
      <title>The influence of electrical charge on plasmodesma conductivity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527879123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFor decades, it was believed that the hydrodynamic radius of a molecule is the defining factor for diffusion or convection through plasmodesmata between plant cells. Here, we show that positively charged molecules are excluded from narrow ...</description>
      <dc:title>The influence of electrical charge on plasmodesma conductivity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527879123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Alexander H. HowellVincent JamesAnneline H. ChristensenViktoriya V. VasinaKaare H. JensenJames FoleyJames E. EvansHoward A. StoneWinfried S. PetersMichael KnoblauchaSchool of Biological Sciences, Washington State University, Pullman, WA 99164bDepartment of Physics, Technical University of Denmark, Lyngby DK-2800 Kgs., DenmarkcRowland Institute, Harvard University, Cambridge, MA 02142dEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352eDepartment of Mechanical and Aerospace Engineering, Princeton University, Princeton, NJ 08544fDepartment of Biological Sciences, Purdue University Fort Wayne, Fort Wayne, IN 46805gDepartment of Marine Zoology, Senckenberg Research Institute and Natural History Museum, Frankfurt a.M. 60325, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527879123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527879123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533973123?af=R">
      <title>Niche-dependent modular regulation of the stem cell transcriptome separates cell identity and potential</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533973123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceDedifferentiation is a mechanism by which differentiating cells revert back to stem cell identity to compensate for the loss of stem cells, allowing for long-term tissue homeostasis. It remains poorly understood how stem cells and progeny ...</description>
      <dc:title>Niche-dependent modular regulation of the stem cell transcriptome separates cell identity and potential</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533973123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Amelie RazHafidh HassanYukiko M. YamashitaaWhitehead Institute for Biomedical Research, Cambridge, MA 02142bDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142cHHMI, Cambridge, MA 02142</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533973123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533973123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537754123?af=R">
      <title>Semiochemicals and odorant receptors underlying potato cultivar susceptibility and resistance to potato tuber moth</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537754123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceInsect pests cause substantial losses in global food production, and their control often relies on chemical insecticides with environmental costs. Environmentally friendly alternatives, such as push–pull strategies that exploit plant-derived ...</description>
      <dc:title>Semiochemicals and odorant receptors underlying potato cultivar susceptibility and resistance to potato tuber moth</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537754123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Ruipeng ChenWangtao HuQin HuJunjie YanJiao YinFathiya M. KhamisYulin GaoWalter S. LealaState Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinabInternational Center of Insect Physiology and Ecology, Nairobi 30772-00100, KenyacDepartment of Zoology and Entomology, University of Pretoria, Hatfield 0028, South AfricadInstitute of Bast Fiber Crops and Center of Southern Economic Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, ChinaeDepartment of Molecular and Cellular Biology, University of California, Davis, CA 95616</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537754123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537754123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520064123?af=R">
      <title>Configuration of circum-Antarctic circulation at the last green- to icehouse climate transition</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520064123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceAround 34 Ma, during the Eocene–Oligocene Transition, Earth transitioned from a warm “greenhouse” to our current “icehouse” climate. While the opening of ocean gateways around Antarctica is often credited with enabling the Antarctic ...</description>
      <dc:title>Configuration of circum-Antarctic circulation at the last green- to icehouse climate transition</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520064123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Hanna S. KnahlJohann P. KlagesLars AckermannKatharina HochmuthLu NiuNicholas R. GolledgeGerrit LohmannaAlfred Wegener Institute, Helmholtz Centre for Polar and Marine Research, Bremerhaven 27570, GermanybAustralian Centre of Excellence in Antarctic Science, Institute for Marine and Antarctic Studies, University of Tasmania, Hobart, Tasmania 7001, AustraliacAntarctic Research Centre, Victoria University of Wellington, Wellington 6140, New ZealanddDepartment of Environmental Physics, University of Bremen, Bremen 28359, GermanyeMARUM - Center for Marine Environmental Sciences, Bremen 28359, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520064123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520064123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R">
      <title>A rare glycoalkaloid biosynthetic pathway from wild potato unlocks genetic routes to Colorado potato beetle resistance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSolanaceous crops such as potato produce steroidal glycoalkaloids, compounds that are toxic to humans and animals yet provide protection against pests. The Colorado potato beetle (CPB) is a destructive pest that quickly evolves insecticide ...</description>
      <dc:title>A rare glycoalkaloid biosynthetic pathway from wild potato unlocks genetic routes to Colorado potato beetle resistance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537847123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Ryota AkiyamaYuki IkeyamaHyoung Jae LeeNaoyuki UmemotoKenji AsanoTetsuya MoriToshiya MuranakaKazuki SaitoYukihiro SugimotoMasaharu MizutaniaDepartment of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Hyogo 657-8501, JapanbMetabolomics Research Group, RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa 230-0045, JapancNational Agricultural Research Center for Hokkaido Region, National Agriculture and Food Research Organization, Hokkaido 082-0081, JapandDepartment of Biotechnology, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537847123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523574123?af=R">
      <title>A swarm intelligence approach to density function reconstruction from moments using entropy optimization</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523574123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis paper presents an application of swarm intelligence to a hundred-year-old problem in mathematics, the Hausdorff moment problem (HMP), where one reconstructs a density function from its moments. The problem is notoriously difficult to ...</description>
      <dc:title>A swarm intelligence approach to density function reconstruction from moments using entropy optimization</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523574123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Parthapratim BiswasStephen R. ElliottaTrinity College, University of Cambridge, Cambridge CB2 1TQ, United KingdombDepartment of Physics and Astronomy, The University of Southern Mississippi, Hattiesburg, MS 39406cDepartment of Chemistry, University of Cambridge, Cambridge CB2 1EW, United KingdomdPhysical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523574123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523574123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2510914123?af=R">
      <title>Microvesicle release drives cycles of mitophagy flux disruption and inflammatory amplification in sepsis-induced myocardial dysfunction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2510914123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSepsis-induced myocardial dysfunction remains a leading contributor to sepsis-related mortality; however, its molecular underpinnings are not completely understood. This study uncovers a previously unrecognized dual vicious cycle in which DRP1-...</description>
      <dc:title>Microvesicle release drives cycles of mitophagy flux disruption and inflammatory amplification in sepsis-induced myocardial dysfunction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2510914123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Rui SongYinrui MaJunfang WanShuai HaoBing ChenYichen LiaoYingjiao LiaoYuzhou XiaoXi ZhangZhaocai ZhangShuang RenXuxin TanJiahe TanHe HuangMilad AshrafizadehGautam SethiJoão CondeLiangming LiuChenyang DuanaDepartment of Critical Care Medicine and Anesthesiology, The Second Affiliated Hospital of Chongqing Medical University, Chongqing 400010, People’s Republic of ChinabDepartment of General Surgery, Research Institute of General Surgery, Jinling Hospital, Affiliated Hospital of Medical School, Nanjing University, Nanjing 210002, People’s Republic of ChinacDepartment of Critical Care Medicine, The Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, People’s Republic of ChinadDepartment of Neurosurgery, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, People’s Republic of ChinaeDepartment of Radiation Oncology, Shandong Provincial Key Laboratory of Radiation Oncology, Shandong Cancer Hospital and Institute, Shandong First Medical University, Shandong Academy of Medical Sciences, Jinan 250000, People’s Republic of ChinafDepartment of Pharmacology and National University of Singapore Centre for Cancer Research, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, SingaporegDivision of Comprehensive Health Research Centre, NOVA Medical School, Faculdade de Ciências Médicas, NOVA Medical School|Faculdade de Ciências Médicas, Universidade NOVA de Lisboa, Lisboa 1169-056, PortugalhState Key Laboratory of Trauma and Chemical Poisoning, Department of Shock and Transfusion, Army Medical Center, Army Medical University, Chongqing 400042, People’s Republic of China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2510914123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2510914123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527957123?af=R">
      <title>Proteome-wide prediction of interactions between structured domains and peptide motifs reveals functionally coherent subnetworks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527957123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificancePRD–SLiM interactions are essential for cellular signaling and regulation yet remain underrepresented in current interactome maps owing to their transient nature and limited structural characterization. Our PrePPI-SLiM pipeline makes proteome-...</description>
      <dc:title>Proteome-wide prediction of interactions between structured domains and peptide motifs reveals functionally coherent subnetworks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527957123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Aakash SahaChristopher L. TangDiana MurrayBarry HonigaDepartment of Systems Biology, Columbia University Irving Medical Center, New York, NY 10032bDepartment of Biochemistry and Molecular Biophysics, Columbia University Irving Medical Center, New York, NY 10032cDepartment of Medicine, Columbia University Irving Medical Center, New York, NY 10032dZuckerman Mind Brain and Behavior Institute, Columbia University, New York, NY 10027</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527957123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527957123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528666123?af=R">
      <title>Extracellular matrix chemistry tunes bacterial biofilm metabolism and optimizes fitness</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528666123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceBiofilms are ubiquitous, capable of thriving in diverse and often hostile environments. Yet, the mechanisms behind their success remain poorly understood. To gain a foundational understanding of biofilm survival, we show that tuning matrix ...</description>
      <dc:title>Extracellular matrix chemistry tunes bacterial biofilm metabolism and optimizes fitness</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528666123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Jinyang LiGeorgia R. SquyresKathy DuongCourtney ReichhardtMatthew R. ParsekDianne K. NewmanaDivision of Biology and Biological Engineering, Caltech, Pasadena, CA 91125bDepartment of Chemistry, Washington University, St. Louis, MO 63130cDepartment of Microbiology, University of Washington, Seattle, WA 98195dDivision of Geological and Planetary Sciences, Caltech, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528666123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528666123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522978123?af=R">
      <title>Structural insights into measles virus RNA synthesis regulation and pan-paramyxoviral polymerase inhibition by ERDRP-0519</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522978123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceNonsegmented negative-sense RNA viruses (nsNSVs), including measles and Nipah viruses, pose major health threats yet lack effective antivirals. These pathogens rely on a large RNA-dependent RNA polymerase (RdRP) complex to replicate and ...</description>
      <dc:title>Structural insights into measles virus RNA synthesis regulation and pan-paramyxoviral polymerase inhibition by ERDRP-0519</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522978123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Tianjiao DuJiening WangChengji YangRubing XueYing ChenKaiyue JieXiaokang ZhangLong ZhangGaojie SongQiansen ZhangShan WuHeng RuaLife Sciences Institute, Second Affiliated Hospital of Zhejiang University School of Medicine, Zhejiang Key Laboratory of Molecular Cancer Biology, Zhejiang University, Hangzhou 310058, ChinabState Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Collaborative Innovation Center for Green Transformation of Bio-Resources, Hubei Key Laboratory of Industrial Biotechnology, School of Life Sciences, Hubei University, Wuhan 430062, ChinacShanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, ChinadInterdisciplinary Center for Brain Information, The Brain Cognition and Brain Disease Institute, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522978123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522978123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520276123?af=R">
      <title>Oocyte-inspired universal whole-cell vaccines against tumor heterogeneity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520276123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceTumor heterogeneity undermines cancer-vaccine efficacy by presenting a complex and patient-specific antigenic landscape. Inspired by the zona pellucida, an extracellular armor that safeguards the oocyte, we engineered a biomimetic whole-tumor-...</description>
      <dc:title>Oocyte-inspired universal whole-cell vaccines against tumor heterogeneity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520276123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Sishi GuoQi LeiYun ChenJunxian YangJiangguo LinC. Jeffrey BrinkerJimin GuoWei ZhuaMOE International Joint Research Laboratory on Synthetic Biology and Medicines, School of Biology and Biological Engineering, South China University of Technology, Guangzhou 510006, People’s Republic of ChinabThe Second Affiliated Hospital, Provincial Key Laboratory of Allergy &amp; Clinical Immunology, Guangzhou Medical University, Guangzhou 510260, People’s Republic of ChinacSchool of Chemistry, Chemical Engineering and Biotechnology, Nanyang Technological University, Nanyang 637371, SingaporedResearch Department of Medical Sciences, Guangdong Provincial People’s Hospital, Guangdong Academy of Medical Sciences, Guangzhou 510080, People’s Republic of ChinaeCenter for Micro-Engineered Materials and the Department of Chemical and Biological Engineering, The University of New Mexico, Albuquerque, NM 87131fState Key Laboratory of Organic-Inorganic Composites, Key Lab of Biomedical Materials of Natural Macromolecules (Beijing University of Chemical Technology, Ministry of Education), Beijing Laboratory of Biomedical Materials, and College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, People’s Republic of ChinagInstitute of Emergent Elastomers, School of Materials Science and Engineering, South China University of Technology, Guangzhou, Guangdong 510640, People’s Republic of China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520276123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R">
      <title>BpFLC coordinates seasonal and age-related flowering in Betula platyphylla through environmental cues and epigenetic regulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis study addresses the prolonged juvenile phase inBetulaplatyphylla(white birch) breeding by identifyingBpFLCas a central flowering-time regulator.BpFLCdelays flowering and promotes vegetative growth, thereby influencing carbon ...</description>
      <dc:title>BpFLC coordinates seasonal and age-related flowering in Betula platyphylla through environmental cues and epigenetic regulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518761123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Yi LiuSui WangTangchun ZhengHuiying SuoDi XiaoDong ZengXiangling YouHeike W. SederoffVincent L. ChiangXiyang ZhaoRonald R. SederoffGuanzheng QuaState Key Laboratory of Tree Genetics and Breeding, School of Forestry, Northeast Forestry University, Harbin 150040, ChinabJilin Provincial Key Laboratory of Tree and Grass Genetics and Breeding, College of Forestry and Grassland Science, Jilin Agricultural University, Changchun 130118, ChinacNational Key Laboratory of Smart Farm Technologies and Systems, Northeast Agricultural University, Harbin 150030, ChinadKey Laboratory of Soybean Biology of Chinese Education Ministry, College of Agriculture, Northeast Agricultural University, Harbin 150030, ChinaeNational Engineering Research Center for Floriculture, School of Landscape Architecture, Beijing Forestry University, Beijing 100083, ChinafCollege of Life Science, Northeast Forestry University, Harbin 150040, ChinagKey Laboratory of Horticulture Crop Genomics and Genetic Improvement in Xinjiang, Institute of Fruits and Vegetables, Xinjiang Academy of Agricultural Sciences, Urumqi 830091, ChinahDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695iForest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518761123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2510928123?af=R">
      <title>Reconsideration of Secure Communities rollout reveals preemptive local-federal cooperation in immigration enforcement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2510928123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceArrests by local police result in the transfer of many noncitizens into federal custody for possible deportation. From 2008 to 2013, the federal government rolled out the Secure Communities program to expand these local-federal collaborations. ...</description>
      <dc:title>Reconsideration of Secure Communities rollout reveals preemptive local-federal cooperation in immigration enforcement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2510928123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Cesar D. Vargas NunezSakshina BhattBasil F. SeifFernando S. MendozaDavid D. LaitinAsad L. AsadaImmigration Policy Lab, Stanford University, Stanford, CA 94305bDepartment of Government, Claremont McKenna College, Claremont, CA 91711cDepartment of Pediatrics, School of Medicine, Stanford University, Stanford, CA 94305dDepartment of Political Science, Stanford University, Stanford, CA 94305eDepartment of Sociology, Stanford University, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2510928123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526822123?af=R">
      <title>Mycoviruses confer hypovirulence but enhance antifungal volatile organic compound production in a phytopathogenic fungus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526822123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceWe identified an evolutionary lineage of RNA viruses within the proposed family Shuviridae, revealing an unexpected connection to animal viruses. Using a transfection system, we demonstrated that SsAShV1 confers hypovirulence, attenuating ...</description>
      <dc:title>Mycoviruses confer hypovirulence but enhance antifungal volatile organic compound production in a phytopathogenic fungus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526822123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Zhijun LiuQiangqiang PanHuang HuangLixia GaoZhi ZhouDan ZhengXueqiong XiaoYanping FuJiasen ChengQing CaiBo LiTao ChenXiao YuYang LinXueliang LyuTom HsiangJiatao XieDaohong JiangaNational Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, ChinabHubei Provincial Key Laboratory of Plant Pathology, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, ChinacHubei Hongshan Laboratory, Wuhan 430070, ChinadSchool of Environmental Sciences, University of Guelph, Guelph, ON N1G 2W1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526822123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526822123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534451123?af=R">
      <title>Hyperactive Rac converts sublethal to lethal trogocytosis in vivo</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534451123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceRac is a key protein in the cellular eating process called phagocytosis. Rac hyperactivity enhances the consumption of tumor cells by chimeric antigen receptor-macrophages (CAR-M), a promising type of cellular immunotherapy. Elucidating the ...</description>
      <dc:title>Hyperactive Rac converts sublethal to lethal trogocytosis in vivo</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534451123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Lauren PenfieldAbhinava K. MishraMorgan SmithDenise J. MontellaMolecular, Cellular, and Developmental Biology Department, University of California, Santa Barbara, CA 93106bDepartment of Biology, University of Louisville, Louisville, KY 40292</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534451123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534451123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2506647123?af=R">
      <title>Hypoxia inducible factors regulate pneumovirus replication by enhancing innate immune sensing</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2506647123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis study explores the role of the hypoxic inducible factor (HIF) signaling pathway in limiting pneumoviral infections, such as respiratory syncytial virus (hRSV) and pneumonia virus of mice (PVM). Using daprodustat, a clinically approved ...</description>
      <dc:title>Hypoxia inducible factors regulate pneumovirus replication by enhancing innate immune sensing</dc:title>
      <dc:identifier>doi:10.1073/pnas.2506647123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Jiyeon HaParul SharmaSammi TaSenko TsukudaJames M. HarrisRebekah Penrice-RandalEleanor BentleyAdam KirbyDaniele F. MegaDavid A. MatthewsPeter BalfeJan RehwinkelAnja KiparJames P. StewartJane A. McKeatingPeter A. C. WingaCAMS Oxford Institute, Chinese Academy of Medical Sciences &amp; Peking Union Medical College, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7BN, United KingdombDepartment of Infection Biology and Microbiomes, Institute of Infection, Veterinary and Ecological Sciences, University of Liverpool, Liverpool L3 5RF, United KingdomcNuffield Department of Medicine, University of Oxford, Oxford OX3 7FZ, United KingdomdSchool of Cellular and Molecular Medicine, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, United KingdomeMedical Research Council Translational Immune Discovery Unit, Medical Research Council Weatherall Institute of Molecular Medicine, Radcliffe Department of Medicine, University of Oxford, Oxford OX3 9DS, United KingdomfLaboratory for Animal Model Pathology, Institute of Veterinary Pathology, Vetsuisse Faculty, University of Zurich, Zurich 8057, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2506647123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2506647123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520356123?af=R">
      <title>RIPK1 ubiquitination regulates its kinase-independent function in development and inflammation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520356123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceReceptor-interacting protein kinase 1 (RIPK1) is a central regulator of apoptosis, necroptosis, and inflammation, with distinct functions determined by its scaffold role and kinase activity. Posttranslational modifications of RIPK1-...</description>
      <dc:title>RIPK1 ubiquitination regulates its kinase-independent function in development and inflammation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520356123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Ming LiJianling LiuMingyan XingHan LiuLingxia WangXiaoxia WuYangjing OuXiaoming ZhaoYangYang WangYangYang XieHanwen ZhangZhuyang WuJincheng HaoHong LiYu LiHaibing ZhangaChinese Academy of Sciences Key Laboratory of Nutrition, Metabolism and Food Safety, Shanghai Institute of Nutrition and Health, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai 200031, ChinabChinese Academy of Sciences Key Laboratory of Computational Biology, Shanghai Institute of Nutrition and Health, Chinese Academy of Sciences, Shanghai 200031, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520356123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520356123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605594123?af=R">
      <title>A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605594123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe Arg/N-degron pathway of the yeastSaccharomyces cerevisiaetargets proteins for degradation via its targeting complex that contains the Ubr1/Ufd4 E3 ubiquitin ligases. Ubr1 E3 recognizes destabilizing N-terminal residues (N-degrons) of ...</description>
      <dc:title>A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605594123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Jang-Hyun OhJu-Yeon HyunShun-Jia ChenAlexander VarshavskyaDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605594123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605594123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530328123?af=R">
      <title>Heat- and PIP2-dependent TRPM4 activity underlies mutually exclusive human diseases</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530328123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceOur study uncovered a signaling network that connects four universal and powerful cellular signaling systems—intracellular Ca2+, membrane potential, phosphatidylinositol 4,5-bisphosphate (PIP2), and temperature—linked together by TRPM4, a ...</description>
      <dc:title>Heat- and PIP2-dependent TRPM4 activity underlies mutually exclusive human diseases</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530328123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Yuhua TianSoohyeon BaeXuesong WuKyle C. RouenAdriana Hernández-GonzalezYanxiao HanAbdullah Al TekreetiSimon VuIrene ChenEllen LiIgor VorobyovVladimir Yarov-YarovoyByung-Chang SuhSamuel T. HwangJie ZhengaDepartment of Pharmacology, School of Pharmacy, Qingdao University, Qingdao 266071, ChinabDepartment of Physiology and Membrane Biology, School of Medicine, University of California, Davis, CA 95616cDepartment of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 42988, KoreadDepartment of Dermatology, University of California Davis, Sacramento, CA 95816eDepartment of Biological Sciences, University of North Texas, Denton, TX 76203fDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720gCarlmont High School, Belmont, CA 94002</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530328123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530328123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517498123?af=R">
      <title>Meiotic prophase I disruption as a strategy for nonhormonal male contraception using small-molecule inhibitor JQ1</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517498123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFew reversible male contraceptives have advanced toward clinical translation, largely because the optimal biological stage for safe intervention remains undefined. Meiosis represents a natural checkpoint in sperm production where transient ...</description>
      <dc:title>Meiotic prophase I disruption as a strategy for nonhormonal male contraception using small-molecule inhibitor JQ1</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517498123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Stephanie TanisLeah E. SimonAdriana K. AlexanderTegan S. HoranMaria de las Mercedes CarroSamantha Jane BonnettAudrey XieRoni Ben-ShlomoConnor E. OwensCharles G. DankoJelena LujicPaula E. CohenaDepartment of Biomedical Sciences and Cornell Reproductive Sciences Center, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853bBaker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14850</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517498123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517498123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526386123?af=R">
      <title>Multimetric analysis uncovers time-dependent climate forcings from China’s 2.3-fold cropland reactive nitrogen emissions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526386123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFood production for people and animals requires nitrogen fertilizers. A major 21st-century challenge is to reduce nitrogen fertilizers while meeting the food and nutritional demands of humanity. By comprehensively analyzing cropland Ngr ...</description>
      <dc:title>Multimetric analysis uncovers time-dependent climate forcings from China’s 2.3-fold cropland reactive nitrogen emissions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526386123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Peng XuZhenzhong ZengHuizhong ShenMin HuMingxu LiuCheng GongYilin ChenChaopu TiGeng LiXuejing WangYi ZhengSi-Liang LiCong-Qiang LiuBenjamin Z. HoultonaInstitute of Surface-Earth System Science, School of Earth System Science, Tianjin University, Tianjin 300072, ChinabSchool of Environmental Science and Engineering, Southern University of Science and Technology, Shenzhen 518055, ChinacState Joint Key Laboratory of Environmental Simulation and Pollution Control, College of Environmental Sciences and Engineering, Peking University, Beijing 100871, ChinadMax Planck Institute for Biogeochemistry, Jena 07745, GermanyeSchool of Urban Planning and Design, Peking University, Shenzhen Graduate School, Shenzhen 518055, ChinafState Key Laboratory of Soil and Sustainable Agriculture, Changshu National Agro-Ecosystem Observation and Research Station, Institute of Soil Science, Chinese Academy of Sciences, Nanjing 210008, ChinagDivision of Environment and Sustainability, the Hong Kong University of Science and Technology, Hong Kong 999077, ChinahDepartment of Ecology and Evolutionary Biology, Cornell University, Ithaca, NY 14850iDepartment of Global Development, Cornell University, Ithaca NY 14850</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526386123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526386123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528851123?af=R">
      <title>Sender–receiver subdivisions of the default mode network in perceptual and memory-guided cognition</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528851123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHuman cognition depends on flexibly shifting between perception and memory-based thought. These modes place opposing demands on neural systems, consistent with opposite directions of information flow. We show that this flexibility is ...</description>
      <dc:title>Sender–receiver subdivisions of the default mode network in perceptual and memory-guided cognition</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528851123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Meichao ZhangCasey PaquolaKatya Krieger-RedwoodBrontë MckeownCharlotte MurphyChang LiuDaniel S. MarguliesRobert LeechJonathan SmallwoodElizabeth JefferiesaState Key Laboratory of Cognitive Science and Mental Health, Institute of Psychology, Chinese Academy of Sciences, Beijing 100101, ChinabDepartment of Psychology, University of Chinese Academy of Sciences, Beijing 100049, ChinacDepartment of Psychology, University of York, Heslington, York YO10 5DD, United KingdomdInstitute for Neuroscience and Medicine, Forschungszentrum Juelich, Juelich 52425, GermanyeDepartment of Psychology, Queen’s University, Kingston, ON K7L 3N6, CanadafIntegrative Neuroscience and Cognition Centre, Centre National de la Recherche Scientifique and Université de Paris, Paris 75006, FrancegInstitute of Psychiatry, Psychology &amp; Neuroscience, King‘s College London, London SE5 8AF, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528851123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528851123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516485123?af=R">
      <title>Antagonism by the type VI secretion system of Bacteroides fragilis is controlled by a TetR family regulator and released small molecule</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516485123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThere are numerous external and intrinsic signals that dictate when bacteria become aggressive and when they activate their defensive systems. Here,Bacteroides fragilisstrains with a GA3 T6SS are shown to release a small molecule that acts ...</description>
      <dc:title>Antagonism by the type VI secretion system of Bacteroides fragilis is controlled by a TetR family regulator and released small molecule</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516485123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Leila TuzlakTéa E. PappasMichael J. CoyneMadeline L. SheahanVictoria BurgoPhoebe A. RiceLaurie E. ComstockaDuchossois Family Institute University of Chicago, Chicago, IL 60637bDepartment of Microbiology, University of Chicago, Chicago, IL 60637cCommittee on Microbiology, University of Chicago, Chicago, IL 60637dDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516485123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516485123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537810123?af=R">
      <title>Tanycyte-derived lactate activates astrocytic HCAR1 to modulate glutamatergic signaling and POMC neuron excitability</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537810123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHow local metabolic signals in the brain are translated into adaptive feeding behavior remains a fundamental question in physiology. Here, we identify a glial metabolic relay in the hypothalamus, in which lactate produced by tanycytes ...</description>
      <dc:title>Tanycyte-derived lactate activates astrocytic HCAR1 to modulate glutamatergic signaling and POMC neuron excitability</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537810123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Sergio LópezRoberto Elizondo-VegaVinka AzócarVania SepúlvedaValentina Opazo-MelladoWalter VásquezJuan C. SáezRicardo C. AranedaMaría de los Ángeles García-RoblesaLaboratorio de Biología Celular, Departamento de Biología Celular, Facultad de Ciencias Biológicas, Universidad de Concepción, Concepción 4030000, ChilebInstituto de Neurociencias, Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2340000, ChilecDepartment of Biology, University of Maryland, College Park, MD 20742</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537810123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537810123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525724123?af=R">
      <title>Spatial and semantic memory reorganize a hippocampal long-axis gradient</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525724123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceEpisodic memory requires linking events with the places where they occur. A central question has been how the hippocampus, one of the brain’s key memory structures, organizes such different kinds of information at the same time. We demonstrate ...</description>
      <dc:title>Spatial and semantic memory reorganize a hippocampal long-axis gradient</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525724123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Anikka G. JordanJoel L. VossJames E. KragelaDepartment of Neurology, University of Chicago, Chicago, IL 60637</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525724123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525724123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2511080123?af=R">
      <title>Chemputer and chemputation—A universal chemical compound synthesis machine</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2511080123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceChemical synthesis is still performed today much like bespoke craftsmanship where each target molecule demands specialized equipment, ad hoc protocols, and labor intensive trial and error. We demonstrate that this is not a fundamental ...</description>
      <dc:title>Chemputer and chemputation—A universal chemical compound synthesis machine</dc:title>
      <dc:identifier>doi:10.1073/pnas.2511080123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Leroy CroninSebastian PagelAbhishek SharmaaSchool of Chemistry, Advanced Research Centre, University of Glasgow, Glasgow G11 6EW, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2511080123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2511080123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520128123?af=R">
      <title>Targeted degradation of c-Myc through the midnolin–proteasome pathway</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520128123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceAlthough PROTACs have revolutionized drug discovery, they face limitations regarding E3 ligase reliance and resistance, while emerging lysosomal strategies are often unsuitable for intranuclear targets. Addressing the challenge of degrading ...</description>
      <dc:title>Targeted degradation of c-Myc through the midnolin–proteasome pathway</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520128123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Jingyuan ZhaoHuanhuan WuHan YuChenyu LiYuling MaoHong YuanShuai LiaClinical Laboratory Center, Central Hospital of Dalian University of Technology, Dalian 116011, ChinabLaboratory Medicine College of Dalian Medical University, Dalian 116044, ChinacThe First Affiliated Hospital of Dalian Medical University, Dalian 116011, ChinadSchool of Pharmacy, Shenyang Pharmaceutical University, Shenyang 110016, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520128123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520128123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525726123?af=R">
      <title>Humanized extracellular vesicles for efficient RNA delivery</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525726123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceWe developed engineered extracellular vesicles (EVs) as RNA delivery vehicles to address limitations of virus-like particles (VLPs) and lipid nanoparticles (LNPs) in gene therapies and vaccines. We first developed an assay for individual ...</description>
      <dc:title>Humanized extracellular vesicles for efficient RNA delivery</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525726123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Xiang MaSophia R. ZhaoConstance L. CepkoaDepartment of Genetics, Harvard Medical School, Boston, MA 02115bHHMI, Chevy Chase, MD 20815</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525726123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525726123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527693123?af=R">
      <title>Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527693123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceIons are essential for RNA and ribosome function, though the mechanisms by which they control large-scale conformational motions have remained elusive. Characterizing their roles is challenging because ions interact with RNA molecules through ...</description>
      <dc:title>Transient ion-mediated interactions regulate subunit rotation in a eukaryotic ribosome</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527693123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>George WanesUdayan MohantyPaul C. WhitfordaCenter for Theoretical Biological Physics, Northeastern University, Boston, MA 02115bDepartment of Physics, Northeastern University, Boston, MA 02115cDepartment of Chemistry, Boston College, Chestnut Hill, MA 02467dDepartment of Chemical Engineering, Northeastern University, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527693123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527693123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R">
      <title>A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHuanglongbing (HLB) is the most devastating disease of citrus with no resistance having been identified in commercial cultivars. Previous work implicated papain-like cysteine proteases (PLCPs) as an important hub of defense in citrus; however, ...</description>
      <dc:title>A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528641123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Alexander J. McClellandBin HuYuantao XuXiaodong FangChunxia WangBenjamin L. KochAmelia H. LovelaceEva HawaraYuanchun WangZhiqian PangAgustina De FrancescoSuzanne P. van WierAndrew M. BeekmanAmit LevyNian WangRenier A. L. van der HoornQiang XuWenbo MaaThe Sainsbury Laboratory, University of East Anglia, Norwich NR4 7UH, United KingdombNational Key Laboratory for Germplasm Innovation and Utilization of Horticultural Crops, Huazhong Agricultural University, Wuhan 430070, ChinacCitrus Research and Education Center, Department of Plant Pathology, Microbiology and Cell Science, University of Florida/Institute of Food and Agricultural Sciences, Lake Alfred, FL 33850dDepartment of Microbiology and Plant Pathology, University of California Riverside, Riverside, CA 92521eSchool of Chemistry, Pharmacy and Pharmacology, University of East Anglia, Norwich NR4 7TJ, United KingdomfPlant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford OX1 3RB, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528641123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519742123?af=R">
      <title>A regulatory axis for tonotopic MYO7A expression in cochlear hair cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519742123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceCochlear hair cells rely on the molecular motor MYO7A for mechanosensory function. Our previous study revealed thatMyo7aisoforms are differentially expressed in auditory hair cells, however, the mechanisms regulating this isoform-specific ...</description>
      <dc:title>A regulatory axis for tonotopic MYO7A expression in cochlear hair cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519742123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Sihan LiSujin JunYe-Ri KimAyathi GogineniFranklin LeeChul Hoon KimUn-Kyung KimAnthony W. PengJung-Bum ShinaDepartment of Neuroscience, School of Medicine, University of Virginia, Charlottesville, VA 22903bDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045cDepartment of Biology, College of Natural Sciences, Kyungpook National University, Daegu 41566, Republic of KoreadSchool of Life Sciences, BK21 plus KNU Kyungpook National University Creative BioResearch Group, Kyungpook National University, Daegu 41566, Republic of KoreaeAdvanced Bio-Resource Research Center, Kyungpook National University, Daegu 41566, Republic of KoreafDepartment of Immunology, School of Medicine, Kyungpook National University, Daegu 41944, Republic of KoreagDepartment of Pharmacology, BK21 PLUS Project for Medical Science, Brain Research Institute, Yonsei University College of Medicine, Seoul 03722, KoreahDepartment of Cell Biology, School of Medicine, University of Virginia, Charlottesville, VA 22903iDepartment of Membrane and Cell Physiology, School of Medicine, University of Virginia, Charlottesville, VA 22903jDepartment of Otolaryngology, School of Medicine, University of Virginia, Charlottesville, VA 22903kDepartment of Biochemistry and Molecular Genetics, School of Medicine, University of Virginia, Charlottesville, VA 22903</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519742123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519742123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529572123?af=R">
      <title>Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529572123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceOur study reveals that the recruitment of Munc13-1 into RIM1/RIM-BP2 biomolecular condensates is not merely a localization event but a fundamental mechanism that confers transformative new functions. Within the condensate, Munc13-1 evolves ...</description>
      <dc:title>Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529572123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Hong ZhangYu ZhangZhifei ZhaoZelin CaoKexu ZhaoMengshi LeiShen WangCong MaaKey Laboratory of Molecular Biophysics of the Ministry of Education, Hubei Provincial Research Center for Basic Biological Sciences, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, ChinabKey Laboratory of Neurogenetics and Channelopathies of the Ministry of Education, The Second Affiliated Hospital, Guangzhou Medical University, Guangzhou 510260, ChinacDepartment of Rheumatology and Immunology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430022, ChinadTongji-Rongcheng Center for Biomedicine, Huazhong University of Science and Technology, Wuhan 430022, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529572123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529572123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527695123?af=R">
      <title>Whole-genome combinatorial gene fusions generate novel genes for advanced microbial trait development</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527695123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceGeneration of phenotypic diversity is a key challenge in biotechnology and the improvement of microbes, plants, and animals cultivated by humans. Traditional diversity generation relies heavily on mutagenesis and homologous recombination which,...</description>
      <dc:title>Whole-genome combinatorial gene fusions generate novel genes for advanced microbial trait development</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527695123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Melody M. McNaySabrina BaffertAlan GreenerChristopher R. SchvarczB. Greg MitchellHelge ZieleraPrimrose Bio, Inc., San Diego, CA 92121bScripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92037</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527695123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527695123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521914123?af=R">
      <title>Deep learning–enabled scaffolding of spatial arrays of PfCSP epitopes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521914123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMalaria is a leading cause of disease in developing countries. Monoclonal antibody L9 has been shown to provide potent protection against malaria in humans. L9 binds to NPNV motifs within the circumsporozoite protein (CSP), with three L9 Fabs ...</description>
      <dc:title>Deep learning–enabled scaffolding of spatial arrays of PfCSP epitopes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521914123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Nelson R. WuKarla M. CastroNathan BeutlerWen-Hsin LeeSai S. R. RaghavanGregory M. MartinMonika JainSashank AgrawalAlessia LiguoriOleksandr KalyuzhniyPatrick D. SkogSierra TeradaYen-Chung LaiJustin NdihokubwayoDanny LuSaman EskandarzadehNushin AlaviNicole PhelpsRyan TingleJohn E. YouhannaSonya AmirzehniThomas F. RogersDennis R. BurtonIan A. WilsonAndrew B. WardBruno E. CorreiaWilliam R. SchiefaDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037bInstitute of Bioengineering, École Polytechnique Fédérale de Lausanne, Lausanne 1015, SwitzerlandcDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037dIAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037eDivision of Infectious Diseases, Department of Medicine, University of California, San Diego, CA 92037fThe Ragon Institute of Mass General Brigham, Massachusetts Institute of Technology and Harvard University, Cambridge, MA 02139gThe Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037hModerna, Inc., Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521914123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521914123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518381123?af=R">
      <title>Shift current anomalous photovoltaics in a double perovskite ferroelectric</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518381123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFerroelectric anomalous photovoltaic (APV) effect holds a great promise in the new optoelectronic application fields. Nevertheless, the limited understanding of ferroelectric APV effect mechanism hinders the exploration of new APV-active ...</description>
      <dc:title>Shift current anomalous photovoltaics in a double perovskite ferroelectric</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518381123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Linjie WeiFu LiYi LiuHongbin ZhangJunhua LuoZhihua SunaState Key Laboratory of Functional Crystals and Devices, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian 350002, People’s Republic of ChinabUniversity of Chinese Academy of Sciences, Chinese Academy of Sciences, Beijing 100039, People’s Republic of ChinacDepartment of Materials and Earth Sciences, Technical University of Darmstadt, Darmstadt 64287, GermanydFujian Science &amp; Technology Innovation Laboratory for Optoelectronic Information of China, Fuzhou, Fujian 350108, People’s Republic of China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518381123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518381123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528620123?af=R">
      <title>Typical development of the human fetal subplate: Regional heterogeneity, growth, and asymmetry assessed by in vivo T2-weighted MRI</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528620123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe subplate (SP) is a transient fetal brain compartment that provides an early foundation for downstream cerebral development. Using fetal MRI, we show that SP morphology is regionally heterogeneous and that its growth follows distinct ...</description>
      <dc:title>Typical development of the human fetal subplate: Regional heterogeneity, growth, and asymmetry assessed by in vivo T2-weighted MRI</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528620123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Andrea GondováJennings ZhangSungmin YouSeungyoon JeongMilton Osiel Candela-LealCaitlin Kantrowitz RollinsPatricia Ellen GrantHyuk Jin YunKiho ImaFetal Neonatal Neuroimaging and Developmental Science Center, Division of Newborn Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115bDivision of Newborn Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115cDepartment of Neurology, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115dDepartment of Radiology, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115eDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528620123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528620123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530673123?af=R">
      <title>Pathogen hijacks focal adhesion signaling by a T3SS effector CteX</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530673123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMany bacterial pathogens utilize type III secretion systems to inject effector proteins that manipulate host cell signaling. We identified CteX, a cysteine protease effector fromChromobacterium violaceumthat exhibits no sequence homology to ...</description>
      <dc:title>Pathogen hijacks focal adhesion signaling by a T3SS effector CteX</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530673123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Xing PanYanbo ZhaoJiwei LuoLili DingLina MaYanxin LiJuan XueXinyuan TaoSongying OuyangShan LiaState Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, College of Biomedicine and Health, Huazhong Agricultural University, Wuhan, Hubei 430070, ChinabInstitute of Infection and Immunity, Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei 442000, ChinacDepartment of Biochemistry, Homeostatic Medicine Institute, School of Medicine, Southern University of Science and Technology, Shenzhen, Guangdong 518055, ChinadKey Laboratory of Microbial Pathogenesis and Interventions of Fujian Province University, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, Fujian 350117, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530673123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530673123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600482123?af=R">
      <title>Aging alters DNA structure–induced genetic instability in mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600482123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceGenetic instability is a hallmark of aging and disease. Z-DNA has been implicated in the etiology of age-related diseases such as Alzheimer’s and cancer. We have previously shown that Z-DNA can stimulate DNA double-strand breaks, resulting in ...</description>
      <dc:title>Aging alters DNA structure–induced genetic instability in mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600482123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Tonia T. LiGuliang WangAlexandra M. D’AmicoLaura A. ChristensenKaren M. VasquezaDivision of Pharmacology and Toxicology, Dell Pediatric Research Institute, College of Pharmacy, The University of Texas at Austin, Austin, TX 78723</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600482123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600482123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522686123?af=R">
      <title>Elucidation of the aragonite nanofiber formation mechanism of LICP contained in the hinge ligament of Pinctada fucata</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522686123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceUnderstanding how proteins control crystal growth on solid surfaces is essential in biomineralization, materials science and protein sciences. Ligament intracrystalline peptide (LICP) controls the crystal orientation and growth in the ...</description>
      <dc:title>Elucidation of the aragonite nanofiber formation mechanism of LICP contained in the hinge ligament of Pinctada fucata</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522686123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Kei FutagawaYuto NamikawaTaichi MoriokaHaruki MeguroAkira ShidaYuki NaganoKazuo FurihataHiroyuki WatanabeFabio NudelmanTaiga OkumuraToshihiro KogureTeppei IkeyaYutaka ItoHidekazu KatayamaKoji NagataMichio SuzukiaDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, JapanbSchool of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, United KingdomcDepartment of Earth Sciences, School of Education, Faculty of Education and Integrated Arts and Sciences, Waseda University, Shinjuku-ku, Tokyo 169-8050, JapandDepartment of Earth and Planetary Science, Graduate School of Science, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, JapaneDepartment of Chemistry, Graduate School of Science, Tokyo Metropolitan University, Hachioji, Tokyo 192-0397, JapanfLiberal Arts Center, Teikyo University, Utsunomiya, Tochigi 320-8551, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522686123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522686123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2505125123?af=R">
      <title>Spatial multiomics profiling reveals ZFP36-mediated immunometabolic reprogramming in bladder cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2505125123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceOur findings pinpoint ZFP36 as both an immunosuppressive driver and a powerful therapeutic target. Moreover, this study provides a robust methodological framework for integrating spatially resolved transcriptomic and metabolic data, paving the ...</description>
      <dc:title>Spatial multiomics profiling reveals ZFP36-mediated immunometabolic reprogramming in bladder cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2505125123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Fangdie YeXuedan HanWeijian LiLei HuangZiang ChenYu LuHang HuangHaowen JiangLufeng ZhengaDepartment of Urology, Huashan Hospital, Fudan University, Shanghai 200040, ChinabFudan Institute of Urology, Huashan Hospital, Fudan University, Shanghai 200040, ChinacDepartment of Biopharmaceuticals, School of Life Science and Technology, China Pharmaceutical University, Nanjing, Jiangsu Province 211198, ChinadDepartment of Molecular Cell and Cancer Biology, University of Massachusetts Chan Medical School, Worcester, MA 01605eDepartment of Urology, The First Affiliated Hospital of Wenzhou Medical University, Wenzhou City 325000, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2505125123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2505125123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528772123?af=R">
      <title>Negative design enables cell-free expression and folding of designed transmembrane β-barrels</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528772123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMembrane proteins (MPs) are essential to biology and biotechnology yet designing them from scratch remains challenging. Using synthetic transmembrane β-barrels and a cell-free expression system with lipid vesicles, we show that conventional ...</description>
      <dc:title>Negative design enables cell-free expression and folding of designed transmembrane β-barrels</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528772123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Giacomo PedrelliMarvelous ChikeremaAndrei SokolovskiiTamas LazarAlexander V. ShkumatovAlexander N. VolkovAnastassia A. VorobievaaStructural Biology Brussels, Department for Bio-engineering Sciences, Vrije Universiteit Brussel (VUB), Brussels 1050, BelgiumbVlaams Instituut voor Biotechnology (VIB) Center for Structural Biology, Brussels 1050, BelgiumcJean Jeener Nuclear Magnetic Resonance Centre, Vrije Universiteit Brussel, Brussels 1050, Belgium</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528772123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528772123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528925123?af=R">
      <title>Chromosome-specific drift under stabilizing selection generates polygenic barriers to sex chromosome turnover</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528925123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSex-determining mechanisms show striking evolutionary contrasts across the tree of life. In some clades they change frequently, while in others they remain unchanged for millions of years. Here, I show that stabilizing selection on polygenic ...</description>
      <dc:title>Chromosome-specific drift under stabilizing selection generates polygenic barriers to sex chromosome turnover</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528925123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Pavitra MuralidharaDepartment of Ecology &amp; Evolution, University of Chicago, Chicago, IL 60637bNational Institute for Theory and Mathematics in Biology, Northwestern University and University of Chicago, Chicago, IL 60611</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528925123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528925123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520079123?af=R">
      <title>Structure basis for C-C chemokine receptor 4 modulation by orthosteric and allosteric antagonists</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520079123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceC-C chemokine receptor 4 (CCR4) guides immune cells to sites of inflammation and tumors and plays a central role in certain leukemias and lymphomas. It has emerged as a promising target for cancer immunotherapy and the treatment of immune ...</description>
      <dc:title>Structure basis for C-C chemokine receptor 4 modulation by orthosteric and allosteric antagonists</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520079123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Ning ZhouRong WangBaozhi ChenXiaofeng QiaDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390bDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390cHarold C. Simmons Comprehensive Cancer Center, University of Texas Southwestern Medical Center, Dallas, TX 75390</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520079123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520079123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601363123?af=R">
      <title>Nocturnal hydration prepares desert cyanobacteria for dawn-light harvesting by inducing phycoerythrin synthesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601363123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceDesert cyanobacteria exhibit remarkable resilience under extreme aridity, where the overlap between photosynthetically active radiation and hydration is restricted to a narrow temporal window around dawn. Chromatic acclimation promotes the ...</description>
      <dc:title>Nocturnal hydration prepares desert cyanobacteria for dawn-light harvesting by inducing phycoerythrin synthesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601363123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Yang BaiHai-Feng XuRen-Han LiAi-Wei ZuoGe-Yan LiuChen YuJin ZhangKe LiuGuo-Zheng DaiAaron KaplanBao-Sheng QiuaSchool of Life Sciences, Key Laboratory of Pesticide and Chemical Biology of Ministry of Education, Hubei Key Laboratory of Genetic Regulation and Integrative Biology, Central China Normal University, Wuhan 430079, Hubei, ChinabDepartment of Plant and Environmental Sciences, Edmond J. Safra Campus, The Hebrew University of Jerusalem, Jerusalem 9190401, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601363123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601363123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528625123?af=R">
      <title>From female to female: Communication via chemosignals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528625123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHuman female social behavior balances cooperation and competition, yet the cues that guide these interactions remain poorly understood. We show that women’s brains respond selectively to the chemosignals of other women depending on both the ...</description>
      <dc:title>From female to female: Communication via chemosignals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528625123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Susanne NehlsElena LosseIssa Salloum SleibiMaya ArminUte HabelNatalia ChechkoaDepartment of Psychiatry, Psychotherapy and Psychosomatics, Medical Faculty, Rheinisch-Westfälische Technische Hochschule Aachen, Aachen 52074, GermanybInstitute of Neuroscience and Medicine 10: Translational Neuroscience, Research Center Jülich, Jülich 52425, GermanycInstitute of Translational Neuroscience and Clinical Psychology, Medical Faculty, Rheinisch-Westfälische Technische Hochschule Aachen, Aachen 52047, GermanydInstitute of Neuroscience and Medicine 7: Brain and Behavior, Research Center Jülich, Jülich 52545, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528625123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528625123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516511123?af=R">
      <title>Reconstruction of human metabolic models with large language models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516511123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHuman metabolic models are essential tools for understanding how the body processes nutrients, enabling the identification of disease mechanisms and potential therapeutic strategies. However, building and curating these models has ...</description>
      <dc:title>Reconstruction of human metabolic models with large language models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516511123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Jiahao LuoHao WangDevlin MoyerZhetao GuoJonathan L. RobinsonJohan GustafssonMihail AntonYu ChenEduard J. KerkhovenJens NielsenFeiran LiaInstitute of Biopharmaceutical and Health Engineering, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen 518055, ChinabKey Laboratory for Industrial Biocatalysis, Ministry of Education, Institute of Biochemical Engineering, Department of Chemical Engineering, Tsinghua University, Beijing 100084, ChinacDepartment of Life Sciences, Chalmers University of Technology, Gothenburg SE-412 96, SwedendDepartment of Biology, Boston University, Boston, MA 02215eBioinformatics Program, Boston University, Boston, MA 02215fBioInnovation Institute, Copenhagen N DK2200, DenmarkgBroad Institute of Massachusetts Institute of Technology and Harvard, Cambridge, MA 02142hDepartment of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg SE-405 30, SwedeniELIXIR, Wellcome Genome Campus, Hinxton, Cambridgeshire CB10 1SD, United KingdomjKey Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, ChinakNovo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Lyngby DK2800, DenmarklSciLifeLab, Chalmers University of Technology, Gothenburg SE-412 96, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516511123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516511123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600210123?af=R">
      <title>Dopamine D1 and D2 receptors differentially control strength and dynamics of abstract decision codes in the primate prefrontal cortex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600210123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHow dopamine shapes abstract decision-making in the prefrontal cortex remains a central unresolved problem in neuroscience. Using causal, receptor-specific manipulations combined with single-neuron recordings in behaving primates, we show that ...</description>
      <dc:title>Dopamine D1 and D2 receptors differentially control strength and dynamics of abstract decision codes in the primate prefrontal cortex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600210123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Esther F. KutterPooja ViswanathanAndreas NiederaAnimal Physiology, Institute of Neurobiology, Department of Biology, University of Tuebingen, Tuebingen 72076, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600210123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600210123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600036123?af=R">
      <title>Loss of FoxO in skeletal muscle leads to disrupted muscle metabolism and exacerbates starvation-induced hepatic steatosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600036123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis study demonstrates that skeletal muscle FoxO transcription factors play a critical role in coordinating systemic lipid homeostasis during starvation. We show that loss of skeletal muscle FoxOs prevents muscle wasting but exacerbates ...</description>
      <dc:title>Loss of FoxO in skeletal muscle leads to disrupted muscle metabolism and exacerbates starvation-induced hepatic steatosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600036123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Mamoru OyabuManato SakaueAtsushi KuboKiyoshi YoshiokaRuna KawaguchiHaruki YamamotoYuzuka KinjoJungin KwonHiroki NishiDaisuke YamanakaTomoki SatoDaiki MoriTakahiro EguchiNaoki ItoSo-ichiro FukadaTakayoshi SuganamiShinji MiuraYusuke OnoFumihiko HakunoShin-ichiro TakahashiTsuyoshi GotoYasutomi KameiaLaboratory of Molecular Nutrition, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Kyoto 606-8522, JapanbBrain-Skeletal Muscle Connection in Aging Project Team, Geroscience Research Center, National Center for Geriatrics and Gerontology, Obu, Aichi 474-8511, JapancLaboratory of Stem Cell Regeneration and Adaptation, Graduate School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, JapandInstitute for Research on Productive Aging, Tokyo 108-0075, JapaneDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, JapanfDepartment of Animal Resource Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, JapangDepartment of Science and Engineering, Saitama University, Saitama City, Saitama 338-8570, JapanhDepartment of Veterinary Medical Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo 113-8657, JapaniLaboratory of Nutritional Biochemistry, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka, Shizuoka 422-8526, JapanjDepartment of Molecular Medicine and Metabolism, Research Institute of Environmental Medicine, Nagoya University, Nagoya 464-8601, JapankDepartment of Immunometabolism, Nagoya University Graduate School of Medicine, Nagoya 466-8550, JapanlDepartment of Muscle Development and Regeneration, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, JapanmMuscle Biology Laboratory, Tokyo Metropolitan Institute for Geriatrics and Gerontology, Tokyo 173-0015, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600036123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600036123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2427192123?af=R">
      <title>Selective depletion of virus-specific CD8 T cells from the liver after PD-1 therapy with Fc-intact antibody during chronic infection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2427192123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe role of the Fc region in programmed cell death 1 (PD-1)-directed immunotherapy is pivotal yet underexplored. We show that Fc-intact anti-PD-1 antibodies depleted PD-1+ CD8 T cells from the liver during chronic lymphocytic choriomeningitis ...</description>
      <dc:title>Selective depletion of virus-specific CD8 T cells from the liver after PD-1 therapy with Fc-intact antibody during chronic infection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2427192123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Masao HashimotoTahseen H. NastiHyun-Tak JinMelissa BuKoichi ArakiJunghwa LeeRajesh M. ValanparambilAkil AkhtarMohammad Affan KhanZhipeng PengYinghong HuDaniel T. McManusIlham BahharAndreas WielandCarl W. DavisSuresh S. RamalingamArlene H. SharpeJeffrey V. RavetchGordon J. FreemanRafi AhmedaEmory Vaccine Center, Emory University School of Medicine, Atlanta, GA 30322bDepartment of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322cCHA Biotech, CHA Bio Complex, Seongnam-si, Gyeonggi-do 13488, Republic of KoreadDepartment of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02215eDepartment of Medicine, Harvard Medical School, Boston, MA 02115fMedical Scientist Training Program, UCSF Graduate Division, School of Medicine, University of California, San Francisco, CA 94143gDivision of Infectious Diseases, Center for Inflammation and Tolerance, Cincinnati Children’s Hospital Medical Center, Cincinnati, OH 45229hDepartment of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45229iViral Immunology Laboratory, Institut Pasteur Korea, Seongnam 13488, Republic of KoreajImmunology Laboratory, Department of Biomedical Engineering, Indian Institute of Technology Ropar, Rupnagar 140001, IndiakDepartment of Otolaryngology, Pelotonia Institute for Immuno-Oncology, The Ohio State University Comprehensive Cancer Center, College of Medicine, The Ohio State University Wexner Medical Center, Columbus, OH 43210lWinship Cancer Institute, Emory University School of Medicine, Atlanta, GA 30322mDepartment of Hematology and Medical Oncology, Emory University School of Medicine, Atlanta, GA 30322nDepartment of Immunology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115oGene Lay Institute of Immunology and Inflammation of Brigham and Women‘s Hospital, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02115pLaboratory of Molecular Genetics and Immunology, The Rockefeller University, New York, NY 10065</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2427192123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2427192123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537049123?af=R">
      <title>Estimating returns to education using the genetic lottery</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537049123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe extent to which education increases earnings is widely debated. We use genetic variation linked to schooling as a natural experiment to estimate the causal effect of an additional year of education on earnings. We find that an extra year ...</description>
      <dc:title>Estimating returns to education using the genetic lottery</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537049123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Tarjei Widding-HavneraasPerline A. DemangeHenrik Daae ZachrissonNicolai BorgenEivind YstromFelix ElwertaCentre for Research on Equality in Education, University of Oslo, Oslo 0318, NorwaybDepartment of Special Needs Education, University of Oslo, Oslo 0318, NorwaycPROMENTA Research Center, Department of Psychology, University of Oslo, Oslo 0317, NorwaydDepartment of Child Health and Development, Norwegian Institute of Public Health, Oslo 0473, NorwayeDepartment of Sociology, University of Wisconsin-Madison, Madison, WI 53705fDepartment of Biostatistics and Medical Informatics, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53705gDepartment of Population Health Sciences, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53705</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537049123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537049123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537425123?af=R">
      <title>STAG2 loss amplifies EWS-FLI1-driven microsatellite enhancer activity promoting Ewing sarcoma aggressiveness</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537425123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceEwing sarcoma is driven by the EWS-FLI1 fusion transcription factor, which activates cancer-promoting genes through GGAA microsatellite enhancers. Loss of the cohesin subunit STAG2 is a recurrent alteration in aggressive Ewing sarcoma, but its ...</description>
      <dc:title>STAG2 loss amplifies EWS-FLI1-driven microsatellite enhancer activity promoting Ewing sarcoma aggressiveness</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537425123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Sanjana EyunniShih-Chun ChuMary L. GuanMichaela LouwEleanor YoungSandra E. CarsonJianhui GongMarcin CieslikArul M. ChinnaiyanAbhijit ParoliaaDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109bMichigan Center for Translational Pathology, University of Michigan, Ann Arbor, MI 48109cDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109dRogel Cancer Center, University of Michigan, Ann Arbor, MI 48109eHHMI, University of Michigan, Ann Arbor, MI 48109fDepartment of Urology, University of Michigan, Ann Arbor, MI 48109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537425123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537425123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524305123?af=R">
      <title>Lysosome-related organelles orchestrate guanine crystal formation in pigment cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524305123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceTo form patterns, coloration, communicate, and enable vision, many organisms utilize guanine crystals formed within iridosomes, specialized crystal-forming organelles. Yet the biogenesis and maturation of iridosomes have remained poorly ...</description>
      <dc:title>Lysosome-related organelles orchestrate guanine crystal formation in pigment cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524305123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Anna Gorelick-AshkenaziYuval BarzilayTali Lerer-GoldshteinTsviya OlenderZohar EyalMay GlaserYonatan BroderNadav MisholRachael DeisMerav KedmiDvir GuraDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, IsraelbDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, IsraelcDepartment of Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot 7610001, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524305123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524305123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2515310123?af=R">
      <title>Alternative microexon splicing code for a four-amino acid peptide of PTPRD governs behavioral development</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2515310123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHow animal behavior develops is still a mystery. It is presumably determined to some extent by genes and modulated by environment and experience. We here find both genetic and environment-dependent splicing regulatory elements for the ...</description>
      <dc:title>Alternative microexon splicing code for a four-amino acid peptide of PTPRD governs behavioral development</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515310123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Ayako ImaiHironori IzumiNagomi ItoHina OgisoYuki KitajimaShuhei KawaseMizuki SendoKenji AzechiToshihide TabataYumie KoshidakaShuya FukaiKeizo TakaoHisashi MoriTomoyuki YoshidaaDepartment of Molecular Neuroscience, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, JapanbResearch Center for Idling Brain Science, University of Toyama, Toyama 930-0194, JapancDepartment of Veterinary Nursing and Health Science, School of Veterinary Medicine, Azabu University, Kanagawa 252-5201, JapandDepartment of Molecular Neuroscience, Interdisciplinary Graduate School of Medicine, Pharmacy, Sciences and Engineering, University of Toyama, Toyama 930-0194, JapaneDepartment of Biofunctional Molecular Chemistry, Faculty of Engineering, University of Toyama, Toyama 930-8555, JapanfDepartment of Biological Information Processing, Graduate School of Science and Engineering, University of Toyama, Toyama 930-8555, JapangLife Science Research Center, University of Toyama, Toyama 930-0194, JapanhDepartment of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515310123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2515310123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535453123?af=R">
      <title>A scalable embryonic stem cell–based platform for efficient generation of mitochondrial DNA mutant mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535453123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMitochondrial DNA (mtDNA) accumulates mutations at a high rate, and more than 260 pathogenic germline mtDNA mutations have been identified in humans, producing diverse and often tissue-specific disorders. In addition, numerous population-...</description>
      <dc:title>A scalable embryonic stem cell–based platform for efficient generation of mitochondrial DNA mutant mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535453123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Weiwei FanTae Gyu OhLillian CrossleyHunter RobbinsMingxiao HeYang DaiMorgan L. TruittAnnette R. AtkinsMichael DownesRonald M. EvansaGene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037bDepartment of Oncology Science, Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535453123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535453123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526665123?af=R">
      <title>Nanocondensate bioadhesive delivery via metal–halogenated catechol coordination in tunicate rhizoid holdfasts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526665123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceProtein-based marine adhesives produced by biological organisms are an important source of inspiration for design of underwater and biomedical glues. However, this requires a deep understanding of relationships between their composition, ...</description>
      <dc:title>Nanocondensate bioadhesive delivery via metal–halogenated catechol coordination in tunicate rhizoid holdfasts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Hyungbin KimSeunghyeon LeeSamantha JeeGeonho SongDorian SchoenaersJérôme DelroissePatrick FlammangMatthew J. HarringtonDong Soo HwangaSchool of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreabDivision of Environmental Science and Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreacDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, CanadadDepartment of Chemical Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreaeDepartment of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam14424, GermanyfBiology of Marine Organisms and Biomimetics Unit, Research Institute for Biosciences, University of Mons, Mons 7000, Belgium</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526665123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526665123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532906123?af=R">
      <title>China’s demographic dividend has moved from age-based labor supply to skill-based productivity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532906123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceGlobal population aging is reducing the age-based demographic dividend that has long supported economic growth. This study identifies the skill-based dividend as the pivotal driver of future growth and highlights a mechanism where the economic ...</description>
      <dc:title>China’s demographic dividend has moved from age-based labor supply to skill-based productivity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532906123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Hengyu GuYingju WuGuillaume MaroisWolfgang LutzTianlong NiuaSchool of Geography and Ocean Science, Nanjing University, Nanjing 210023, ChinabAsian Demographic Research Institute, Shanghai University, Shanghai 200444, ChinacWittgenstein Centre for Demography and Global Human Capital (University of Vienna, International Institute for Applied Systems Analysis, Vienna Institute of Demography/Austrian Academy of Sciences), International Institute for Applied Systems Analysis, Laxenburg 2361, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532906123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532906123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526776123?af=R">
      <title>Offspring chemical control of adult reproductive transitions in a social insect</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526776123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceParental care enhances offspring survival but induces profound physiological changes in caregivers. A common feature across animals is that adults temporarily suppress their own reproduction while caring for the young. The offspring cues ...</description>
      <dc:title>Offspring chemical control of adult reproductive transitions in a social insect</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526776123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Baptiste PiqueretJerrit WeissflogSandra TretterTim ZetzscheDaniel VeitStefan BartramRayko HalitschkeYuko UlrichaLise Meitner Research Group Social Behaviour, Max Planck Institute for Chemical Ecology, Jena 07745, GermanybMass Spectrometry and Metabolomics, Max Planck Institute for Chemical Ecology, Jena 07745, GermanycFaculty of Biological Sciences, Friedrich Schiller University, Jena 07743, GermanydMax Planck Institute for Chemical Ecology, Jena 07745, GermanyeDepartment of Natural Product Biosynthesis, Max Planck Institute for Chemical Ecology, Jena 07745, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526776123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526776123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524516123?af=R">
      <title>Selective reuse of prior ensemble data improves the latest air temperature forecast over North America</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524516123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSubseasonal to seasonal (S2S) weather prediction—spanning the critical range of 2 to 5 wk—remains one of the hardest problems in atmospheric science. Forecast skill often collapses at these lead times because initial atmospheric information ...</description>
      <dc:title>Selective reuse of prior ensemble data improves the latest air temperature forecast over North America</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524516123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Daisuke TokudaPaul A. DirmeyeraInstitute of Industrial Science, The University of Tokyo, Kashiwanoha, Chiba 277-8574, JapanbGeorge Mason University, Fairfax, VA 22030cCenter for Ocean-Land-Atmosphere Studies, George Mason University, Fairfax, VA 22030</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524516123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524516123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536296123?af=R">
      <title>SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536296123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceCoronaviruses cause disease across a wide range of animal species and the human coronaviruses SARS-CoV-2 and MERS-CoV have caused epidemics of severe respiratory illness. Thus, it is imperative to understand how these viruses antagonize host ...</description>
      <dc:title>SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536296123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Nicholas A. ParentiRenee CusicDavid M. RennerNathaniel JacksonChengjin YeLi Hui TanJessica J. PfannenstielAnthony R. FehrNoam A. CohenLuis Martinez-SobridoJames M. BurkeSusan R. WeissaDepartment of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104bPenn Center for Research on Emerging Viruses, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104cDepartment of Molecular Medicine, The Herbert Wertheim University of Florida Scripps Institute for Biomedical Innovation and Technology, Jupiter, FL 33458dDepartment of Immunology and Microbiology, The Herbert Wertheim University of Florida Scripps Institute for Biomedical Innovation and Technology, Jupiter, FL 33458eSkaggs Graduate School of Chemical and Biological Sciences, The Scripps Research Institute, Jupiter, FL 33458fDisease Intervention and Prevention, Texas Biomedical Research Institute, San Antonio, TX 78227gDepartment of Otorhinolaryngology-Head and Neck Surgery, Division of Rhinology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104hDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045iDepartment of Surgery, Corporal Michael J. Crescenz Veterans Administration Medical Center, Philadelphia, PA 19104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536296123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536296123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517309123?af=R">
      <title>Simulation-based inference captures non-Markovian effects as exemplified in protein production kinetics through cell division</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517309123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceLearning parameters from biological data can be intractable when the likelihood cannot be calculated. One example is protein production during cell division, where molecule counts depend not only on synthesis within a cell but also on ...</description>
      <dc:title>Simulation-based inference captures non-Markovian effects as exemplified in protein production kinetics through cell division</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517309123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-08T07:00:00Z</dc:date>
      <dc:creator>Pedro PessoaJuan Andres MartinezVincent VandenbrouckeFrank DelvigneSteve PresséaCenter for Biological Physics, Arizona State University, Tempe, AZ 85281bDepartment of Physics, Arizona State University, Tempe, AZ 85281cTerra Research and Teaching Centre, Microbial Processes and Interactions, Gembloux Agro-Bio Tech, University of Liège, Gembloux B-5030, BelgiumdSchool of Molecular Sciences, Arizona State University, Tempe, AZ 85281</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517309123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517309123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530071123?af=R">
      <title>MDFIC2 is a sensory neuron–specific PIEZO channel auxiliary subunit</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530071123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificancePIEZO1 and PIEZO2 channels play critical roles in sensory processes including touch, blood pressure regulation, and proprioception. We previously identified MyoD-family inhibitor proteins (MDFIC and MDFI) as auxiliary subunits of PIEZO1. Here, ...</description>
      <dc:title>MDFIC2 is a sensory neuron–specific PIEZO channel auxiliary subunit</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530071123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Zijing ZhouFei DaiDelfine ChengXiaonuo MaSeyedeh Farzaneh OmidkhodaJack ClarkeHuijing ZhangMichael LadenYang GuoJinyuan Vero LiRenjing LiuEmily S. WongYixiao ZhangCharles D. CoxaMolecular Cardiology and Biophysics, Victor Chang Cardiac Research Institute, Sydney, NSW 2010, AustraliabSchool of Clinical Medicine, Faculty of Medicine and Health, University of New South Wales, Sydney, NSW 2052, AustraliacInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, ChinadSchool of Biotechnology and Biomolecular Sciences, Faculty of Medicine and Health, University of New South Wales, Sydney, NSW 2052, AustraliaeShanghai Key Laboratory of Aging Studies, Shanghai 201210, ChinafState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, ChinagSchool of Biomedical Sciences, Faculty of Medicine and Health, University of New South Wales, Sydney, Kensington, NSW 2052, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530071123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530071123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531899123?af=R">
      <title>Maternal IntS11 primes embryonic totipotency by organizing early zygotic transcription initiation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531899123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceAs the first transcriptional milestone in life, zygotic genome activation (ZGA) driven by pioneer factors is a hallmark of totipotency, enabling embryos to transition from maternal to zygotic control. Yet, the mechanisms governing the ...</description>
      <dc:title>Maternal IntS11 primes embryonic totipotency by organizing early zygotic transcription initiation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531899123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Liangliang WangYiru WangYaqi MiaoYuan SongJialiang ZhouYuanxiang ZhuYing ChengWenxin ZhangQinmiao SunFan LaiGuoqiang ZhangDahua ChenaInstitute of Biomedical Research, Yunnan University, Kunming 650500, ChinabState Key Laboratory of Organ Regeneration and Reconstruction, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, ChinacBeijing Institute for Stem Cell and Regenerative Medicine, Beijing 100101, ChinadSchool of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, ChinaeSouthwest United Graduate School, Kunming 650500, ChinafSchool of Life Sciences, Yunnan University, Kunming 650500, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531899123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531899123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R">
      <title>An acetyltransferase family required for biosynthesis of diverse marine carotenoids</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceApproximately half of global photosynthesis occurs in oceans. Marine eukaryotic algae synthesize specialized carotenoids to facilitate efficient light capture underwater. While the multistep biosynthesis of these pigments has been partially ...</description>
      <dc:title>An acetyltransferase family required for biosynthesis of diverse marine carotenoids</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525772123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Tianjun CaoXuechun BaiTingting YouYanyou JiangMartin LohrXiaobo LiaState Key Laboratory of Gene Expression, School of Life Sciences, Westlake University, Hangzhou 310030, ChinabInstitute of Biology, Westlake Institute for Advanced Study, Hangzhou 310030, ChinacWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou 310024, ChinadInstitut für Molekulare Physiologie, Johannes Gutenberg University, 55099 Mainz, GermanyeZhejiang Key Laboratory of Low-Carbon Intelligent Synthetic Biology, Westlake University, Hangzhou 310030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525772123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602434123?af=R">
      <title>Probing rock rupture with naturally occurring nuclide signals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602434123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe idea of hydrogeochemical precursors for geological hazards such as earthquakes, volcanic eruptions, and landslides has been proposed over half a century. Numerous lab experiments and field observations, especially on naturally occurring ...</description>
      <dc:title>Probing rock rupture with naturally occurring nuclide signals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602434123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Jia-Qing ZhouRong MaoXin LuoM. Bayani CardenasYi-Feng ChenFu-Shuo GanChuang-Bing ZhouChangdong LiHuiming TangRan HuZhibing YangMichael MangaaState Key Laboratory of Water Resources Engineering and Management, Wuhan University, Wuhan 430072, ChinabLaboratory for Sea Space Agent, Department of Earth and Planetary Sciences, The University of Hong Kong, Hong Kong 999077, ChinacKey Laboratory of Rock Mechanics in Hydraulic Structural Engineering of the Ministry of Education, Wuhan University, Wuhan 430072, ChinadCenter for Natural Resources, Department of Civil and Environmental Engineering, New Jersey Institute of Technology, Newark, NY 07102eDepartment of Earth and Planetary Sciences, The University of Texas at Austin, Austin, TX 787812fFaculty of Engineering, China University of Geosciences, Wuhan 430074, ChinagDepartment of Earth and Planetary Science, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602434123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602434123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528146123?af=R">
      <title>The rhythm of aging: Stability and drift in the individual rate of senescence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528146123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificancePeople are living longer than ever, but is it because we age more slowly, or because the onset of aging is later? This study addresses this question by distinguishing the individual rate at which mortality risk accelerates with age from the ...</description>
      <dc:title>The rhythm of aging: Stability and drift in the individual rate of senescence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528146123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Silvio C. PatricioaInterdisciplinary Centre on Population Dynamics, Department of Economics, University of Southern Denmark, Odense 5230, Denmark</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528146123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528146123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526136123?af=R">
      <title>mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526136123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHeat shock proteins 70 (Hsp70) are central hubs of cellular proteostasis networks. Their biological functions are enabled by the large conformational changes these chaperones undergo as they hydrolyze ATP in their nucleotide-binding domain and ...</description>
      <dc:title>mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526136123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Rupa BanerjeeVanessa TrauschkeNils BertramIna AretzChristof OsmanDon C. LambDejana MokranjacaBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Martinsried 82152, GermanybPhysical Chemistry, Department of Chemistry and Center for NanoScience, Ludwig-Maximilians-Universität München, Munich 81377, GermanycBiozentrum, Cell Biology, Ludwig-Maximilians-Universität München, Martinsried 82152, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526136123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526136123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536219123?af=R">
      <title>Extended Rice–Thomson analysis and atomistic simulations revealing grain boundary effects on fracture in refractory high-entropy alloys</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536219123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis work serves to extend the fundamental ductile vs. brittle fracture theory, specifically the Rice–Thomson criterion, by introducing a grain boundary ahead of an initiating crack which propagates at an oblique angle to impinge the boundary. ...</description>
      <dc:title>Extended Rice–Thomson analysis and atomistic simulations revealing grain boundary effects on fracture in refractory high-entropy alloys</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536219123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Wenqing WangDavid H. CookXiaoyu ChenPunit KumarAndrew M. MinorSatish I. RaoMark AstaRobert O. RitchieDiana FarkasaMaterials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720bDepartment of Materials Science and Engineering, University of California, Berkeley, CA 94720cDepartment of Materials Science and Engineering, Virginia Polytechnic Institute, Computer Simulation Laboratory, Blacksburg, VA 24061-0237</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536219123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536219123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528064123?af=R">
      <title>Resolving competing evolutionary histories in joint ancestral state reconstruction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528064123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceUnderstanding the evolutionary trajectories of complex traits, such as antibiotic resistance, is a critical challenge. Traditional methods characterize individual ancestors in isolation, but they do not necessarily identify the most probable ...</description>
      <dc:title>Resolving competing evolutionary histories in joint ancestral state reconstruction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528064123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>James D. BoykoKyle J. GontjesEvan S. SnitkinStephen A. SmithaDepartment of Ecology and Evolutionary Biology, University of Michigan, Ann Arbor, MI 48109bDepartment of Microbiology and Immunology, University of Michigan, Medical School, Ann Arbor, MI 48109cDepartment of Internal Medicine, Division of Infectious Disease, University of Michigan Medical School, Ann Arbor, MI 48109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528064123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528064123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523913123?af=R">
      <title>Diffusive spreading across dynamic mitochondrial network architectures</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523913123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMitochondria form dynamic networks of interconnected tubules, with network structure varying across nutrient condition, disease state, and cell type. Numerous cellular functions rely on the sharing of ions, proteins, lipids, and RNAs ...</description>
      <dc:title>Diffusive spreading across dynamic mitochondrial network architectures</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523913123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Keaton B. HoltCamryn ZuritaLizzy TeryoshinSamantha C. LewisElena F. KosloveraDepartment of Physics, University of California, San Diego, La Jolla, CA 92093bDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720cInnovative Genomics Institute, Berkeley, CA 94720dHelen Wills Neuroscience Institute, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523913123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523913123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527863123?af=R">
      <title>Metabolite mimicry identifies butyrate analogs with select protective functions in the intestinal mucosa</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527863123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceButyrate is a well-studied microbial short-chain fatty acid that regulates a number of mucosal pathways and is paramount in maintaining intestinal integrity. In health, it is a major source of energy for colonocytes and regulates gene ...</description>
      <dc:title>Metabolite mimicry identifies butyrate analogs with select protective functions in the intestinal mucosa</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527863123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Alfredo OrnelasJacob A. CountessJi Yeon KimRachel H. CohenBrittany D. GomezRebecca L. RoerFaiz MinhajuddinKiranmayee Yenugudhati Vijaya SaiLiheng ZhouJulia L. M. DunnCaleb ChandlerPhilip ReiganIan M. CartwrightCaroline H. T. HallGeetha BhagavatulaJoseph C. OnyiahAlexander S. DowdellSean P. ColganaMucosal Inflammation Program and Division of Gastroenterology and Hepatology, Department of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045bMedical Scientist Training Program, Department of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045cDivision of Gastroenterology, Hepatology, and Nutrition, Department of Pediatrics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045dDigestive Health Institute, Children’s Hospital Colorado, Aurora, CO 80045eDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045fDepartment of Medicine, Rocky Mountain Veterans Regional Veterans Affairs Medical Center, Aurora, CO 80045</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527863123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527863123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525442123?af=R">
      <title>Variability in alluvial river width driven by intermittent bank collapse</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525442123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceRiver width variability influences floodplain dynamics, ecosystem structure, and human activities. We identify three distinct spatial patterns of river width variability, driven by meander bends, mid-channel bars, and bank-line irregularities ...</description>
      <dc:title>Variability in alluvial river width driven by intermittent bank collapse</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525442123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Kun ZhaoStefano LanzoniGiovanni CocoFan XuKaili ZhangZheng GongaState Key Laboratory of Water Disaster Prevention, Hohai University, Nanjing 210098, ChinabDepartment of Civil, Environmental and Architectural Engineering, University of Padua, Padua 35122, ItalycInstitut de Ciències del Mar, Consejo Superior de Investigaciones Científicas, Barcelona 08003, SpaindState Key Laboratory of Estuarine and Coastal Research, East China Normal University, Shanghai 3663, ChinaeState Key Laboratory of Water Disaster Prevention, Nanjing Hydraulic Research Institute, Nanjing 210029, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525442123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525442123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532472123?af=R">
      <title>Structure-guided design of 7-azaindole DNMT1 inhibitors active against hypomethylating agent–resistant acute myeloid leukemia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532472123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceAberrant DNA hypermethylation silences tumor suppressor genes (TSGs) and contributes to the progression of both hematologic and solid cancers, yet current DNA hypomethylating therapies are limited by toxicity and resistance. We introduce DMI46,...</description>
      <dc:title>Structure-guided design of 7-azaindole DNMT1 inhibitors active against hypomethylating agent–resistant acute myeloid leukemia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532472123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Shibing TangLiangyi ZongShuyuan MaYini ShangJiale WeiJianguang LiuYing CuiHuahui GuoKang ZouKezhi WangHongkun LiFei YeJing HuangCheng LuoZhihai LiStephen B. BaylinXiangqian KongaInstitute of Drug Discovery, Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, China-New Zealand Joint Laboratory on Biomedicine and Health, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, ChinabUniversity of Chinese Academy of Sciences, Beijing 100049, ChinacKey Laboratory of Glyco-drug Research of Zhejiang Province, School of Pharmaceutical Science and Technology, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, ChinadDepartment of Oncology, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, The Johns Hopkins University School of Medicine, Baltimore, MD 21287eCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, ChinafState Key Laboratory of Oncology in South China, Guangdong Key Laboratory of Nasopharyngeal Carcinoma Diagnosis and Therapy, Sun Yat-sen University Cancer Center, Guangzhou 510060, ChinagState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, ChinahDepartment of Epigenetics, Van Andel Institute, Grand Rapids, MI 49503</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532472123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532472123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530860123?af=R">
      <title>Light-activated cAMP signaling controls sodium-driven motility in Vibrio cholerae</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530860123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceBacteria use second messengers to couple environmental cues to behavior, but how light regulates motility inVibrio choleraeis not well defined. We show that in strain AJ10, a photoresponsive adenylyl cyclase (CyaA) elevates intracellular ...</description>
      <dc:title>Light-activated cAMP signaling controls sodium-driven motility in Vibrio cholerae</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530860123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Jun XuShuichi NakamuraSuzuna TomoyoseReika ShimabukuRintaro TomiokaTetsu YamashiroaDepartment of Bacteriology, Graduate School of Medicine, University of the Ryukyus, Ginowan, Okinawa 901-2720, JapanbDepartment of Applied Physics, Graduate School of Engineering, Tohoku University, Sendai, Miyagi 980-8579, JapancDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo 113-8656, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530860123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530860123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531389123?af=R">
      <title>Reciprocal regulation of TNF receptor 1–mediated signaling and inflammatory damages by MARCH2 and USP22</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531389123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceTNF is a secreted protein that binds to TNF-R1 to trigger systemic or local inflammatory responses and diseases. TNF inhibitors have been clinically proven effectively for inflammatory and autoimmune diseases. Here, we reveal that the level of ...</description>
      <dc:title>Reciprocal regulation of TNF receptor 1–mediated signaling and inflammatory damages by MARCH2 and USP22</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531389123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Hui-Fang LiRui LiuPeng RenHong-Bing ShuShu LiaDepartment of Infectious Diseases, State Key Laboratory of Virology and Biosafety, Frontier Science Center for Immunology and Metabolism, Medical Research Institute, Zhongnan Hospital of Wuhan University, Taikang Center for Life and Medical Sciences, Wuhan University, Wuhan 430071, ChinabHubei Provincial Research Center for Basic Biological Sciences, Wuhan University, Wuhan 430071, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531389123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531389123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525769123?af=R">
      <title>Brain–computer interface–based neurofeedback training enables transferable control of cortical state switching in humans</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525769123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHumans can flexibly control actions. Although closed-loop regulation of sensorimotor activity has been demonstrated since the 1960s, whether these volitional transitions can be rapidly controlled to improve behavior was unknown. Here, we ...</description>
      <dc:title>Brain–computer interface–based neurofeedback training enables transferable control of cortical state switching in humans</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525769123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Seitaro IwamaAtsuya MatsuokaJunichi UshibaaDepartment of Biosciences and Informatics, Faculty of Science and Technology, Keio University, Kanagawa, JapanbSchool of Fundamental Science and Technology, Graduate School of Science and Technology, Keio University, Kanagawa, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525769123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525769123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537651123?af=R">
      <title>Energetics of biomolecular shells in core–shell nanocomplexes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537651123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThe drug delivery efficiency of engineered nanocarriers depends critically on their stability in biological media. Here, we introduce the stabilization enthalpy concept to describe experimentally determined thermodynamic stability relations of ...</description>
      <dc:title>Energetics of biomolecular shells in core–shell nanocomplexes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537651123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Kristina LilovaTamilarasan SubramaniIsabella MontiniAnne HarrisonManuel ScharrerHongwu XuAlexandra NavrotskyaCenter for Materials of the Universe, Arizona State University, Tempe, AZ 85281bSchool of Molecular Sciences, Arizona State University, Tempe, AZ 85281cBiochemistry and Biophysics Department, Oregon State University, Corvallis, OR 97331dSchool of Biological and Health Systems Engineering, Ira A. Fulton School of Engineering, Tempe, AZ 85281eEarth, Environment, and Planetary Sciences, University of Tennessee, Knoxville, TN 37916</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537651123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537651123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520717123?af=R">
      <title>Amoeboid–mesenchymal transition and the proteolytic control of cancer invasion plasticity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520717123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceIn vivo, cancer cells exhibit invasion plasticity as they traverse extracellular matrix (ECM) barriers in collective or single-cell fashion while displaying either mesenchymal or amoeboid phenotypes. Current dogma holds that invasion ...</description>
      <dc:title>Amoeboid–mesenchymal transition and the proteolytic control of cancer invasion plasticity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520717123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Adam W. OlsonJonathan LiXiao-Yan LiLana KingLong JiangKalins BanerjeeAtticus J. McCoyMahnoor N. GondalArul M. ChinnaiyanDorraya El-AshryEvan T. KellerAndrew J. PutnamStephen J. WeissaCancer Biology Department, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109bDepartment of Urology, Single Cell Spatial Analysis Program and Biointerfaces Institute, University of Michigan Medical School, Ann Arbor, MI 48109cDepartment of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109dDepartment of Computational Medicine &amp; Bioinformatics, University of Michigan, Ann Arbor, MI 48109eMichigan Center for Translational Pathology, Department of Computational Medicine &amp; Bioinformatics, University of Michigan, Ann Arbor, MI 48109fDepartment of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109gMichigan Center for Translational Pathology, Department of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109hDepartment of Urology, University of Michigan Medical School, Ann Arbor, MI 48109iRogel Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109jHHMI, University of Michigan Medical School, Ann Arbor, MI 48109kBreast Cancer Research Foundation, New York, NY 10036</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520717123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520717123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537315123?af=R">
      <title>Many paths to destruction: Family-specific turnover and stress responses for tRNA introns</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537315123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceMost eukaryotic genome sequences are transcribed into noncoding RNAs such as transfer RNAs (tRNAs). A subset of tRNA genes contain introns which must be excised from precursor tRNAs to enable tRNAs to function in protein synthesis. Freed tRNA ...</description>
      <dc:title>Many paths to destruction: Family-specific turnover and stress responses for tRNA introns</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537315123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Sara MetcalfRegina T. NostramoAlicia BaoKatherine ClarkPaolo L. SinopoliAnita K. HopperaDepartment of Molecular Genetics, The Ohio State University, Columbus, OH 43210bCenter for RNA Biology, The Ohio State University, Columbus, OH 43210cComprehensive Cancer Center, The Ohio State University, Columbus, OH 43210</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537315123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537315123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600197123?af=R">
      <title>Use of a cytochrome P450 humanized mouse model to refine schistosomiasis drug discovery</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600197123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSchistosomiasis remains a major global health burden and is treated almost exclusively with praziquantel, despite evidence of emerging resistance and a sparse pipeline of new anti-schistosomals. A key barrier to drug discovery is the poor ...</description>
      <dc:title>Use of a cytochrome P450 humanized mouse model to refine schistosomiasis drug discovery</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600197123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Sarah D. DaveyJosephine E. Forde-ThomasBenjamin J. HulmeKristin LeesAlice H. CostainMary EvansGabriel RinaldiLaura FrameLaste StojanovskiFrederick R. C. SimeonsAmy TavendaleA. Kenneth MacLeodRemi PichonYi-Hsuan LeeOktawia PolakIain W. ChalmersBismark DankwaBrenda Kisia OdhiamboVictor Hugo GuimaraesMatthew HegartyMartin T. SwainWayne AubreyNicola CaldwellAndrew S. MacDonaldIan H. GilbertBeatriz BaragañaKevin D. ReadKarl F. HoffmannaDepartment of Life Sciences, Aberystwyth University, Wales, Aberystwyth SY23 3DA, United KingdombLydia Becker Institute of Immunology and Inflammation, Division of Immunology, Immunity to Infection and Respiratory Medicine, School of Biological Sciences, The University of Manchester, England, Manchester M13 9NT, United KingdomcDivision of Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, United KingdomdDepartment of Computer Science, Aberystwyth University, Wales, Aberystwyth SY23 3DA, United KingdomeLaboratory of Inflammation and Infectious Diseases, Department of Morphology and Pathology, Federal University of São Carlos, São Carlos CEP 13565-905, Brazil</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600197123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600197123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530440123?af=R">
      <title>Fast automated adjoints for spectral PDE solvers</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530440123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceScientific computing increasingly requires both accurate simulations of physical systems as well as optimizing them over many parameters for tasks such as inverse modeling, system control, and variational data assimilation. Adjoint methods ...</description>
      <dc:title>Fast automated adjoints for spectral PDE solvers</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530440123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Calum S. SkeneKeaton J. BurnsaDepartment of Applied Mathematics, University of Leeds, Leeds LS2 9JT, United KingdombSchool of Physics and Astronomy, The University of Edinburgh, Edinburgh EH9 3FD, United KingdomcDepartment of Mathematics, Massachusetts Institute of Technology, Cambridge, MA 02139dCenter for Computational Astrophysics, Flatiron Institute, New York, NY 10010</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530440123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530440123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531771123?af=R">
      <title>Infants use helping to infer the existence and strength of caring relationships</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531771123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceDecades of work suggest that human infants distinguish prosocial and antisocial behavior. However, less is known about what infants infer from such behaviors. People can behave prosocially for at least two different reasons: Their actions may ...</description>
      <dc:title>Infants use helping to infer the existence and strength of caring relationships</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531771123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Bill PepeBrandon M. WooAshley J. ThomasLindsey J. PowellaDepartment of Psychology, University of California San Diego, La Jolla, CA 92093bDepartment of Psychological and Brain Sciences, University of California Santa Barbara, Santa Barbara, CA 93106cDepartment of Psychology, Harvard University, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531771123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531771123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526262123?af=R">
      <title>Snooping helices: The elastic path finding algorithm of growing hyphae</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526262123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceProprioception is the integrated sense of self-movement and body position in complex organisms. Here, we describe a mechanical form of proprioception driving directional choice making in tip-growing helical organisms. We show thatC. albicans...</description>
      <dc:title>Snooping helices: The elastic path finding algorithm of growing hyphae</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526262123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Antoine RittaudElodie CouttenierSophie Bachellier-BassiChristophe d’EnfertIgor M. KulićCatherine VillardaInstitut Charles Sadron, Université de Strasbourg, CNRS, 23 rue du Loess, BP 84047, Strasbourg 67034, FrancebUniversité Paris Cité, CNRS, Laboratoire Interdisciplinaire des Energies de Demain, Paris F-75013, FrancecInstitut Curie, Université Paris Sciences et Lettres, Sorbonne Université, CNRS, Physics of Cells and Cancer, Paris F-75005, FrancedInstitut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris F-75015, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2526262123</prism:doi>
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      <title>Conformational equilibria in the activation of cystine-knot hormone receptors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536028123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceCystine-knot hormones such as thyroid-stimulating hormone (TSH) act through cognate receptors (TSHR here) to effect responses (cyclic AMP production here). Despite substantial evidence that TSHR acts as a dimer in cells, it is monomeric as ...</description>
      <dc:title>Conformational equilibria in the activation of cystine-knot hormone receptors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536028123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Zhen GongWayne A. HendricksonaDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032bDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536028123</prism:doi>
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      <title>Coalescence and translation: A language model for population genetics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518956123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;Significancecxt is a language model for population genetics which introduces next-coalescence prediction as translation from observed mutations to coalescence times by modeling the coalescent with recombination as a conditional stochastic process. It ...</description>
      <dc:title>Coalescence and translation: A language model for population genetics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518956123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Kevin KorfmannNathaniel S. PopeMelinda MeleghyAurélien TellierAndrew D. KernaInstitute of Ecology and Evolution, University of Oregon, Eugene, OR 97403bDepartment of Biology, University of Pennsylvania, Philadelphia, PA 19104cDepartment of Life Science Systems, Technical University of Munich, Freising 85354, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518956123</prism:doi>
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      <title>Predicting and controlling laser-induced breakup and multidirectional propulsion of liquid droplets</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526933123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceShort laser pulses can push and fragment microscopic liquid droplets, but the motion is difficult to control because the first laser-triggered plasma spark can form at varying locations in or near the droplet. We show that two measurable ...</description>
      <dc:title>Predicting and controlling laser-induced breakup and multidirectional propulsion of liquid droplets</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526933123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Awanish Pratap SinghD. Chaitanya Kumar RaoMaik RahlvesAlfred VogelSaptarshi BasuaInstitute of Biomedical Optics, University of Lübeck, Lübeck 23562, GermanybDepartment of Aerospace Engineering, Indian Institute of Technology Kanpur, Kanpur 208016, IndiacDepartment of Mechanical Engineering, Indian Institute of Science, Bangalore 560012, India</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526933123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528175123?af=R">
      <title>Large infinities and definable sets</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528175123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;Large cardinal axioms extend the standard set of axioms for mathematics by asserting that very large infinite sets exist. A prominent line of current research in mathematical logic is identifying ever stronger principles of this kind; this serves as an ...</description>
      <dc:title>Large infinities and definable sets</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528175123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>J. P. AguileraJ. BagariaP. LückeaInstitut für diskrete Mathematik und Geometrie, Technische Universität Wien, Vienna 1040, AustriabInstitució Catalana de Recerca i Estudis Avançats, Barcelona 08010, SpaincDepartament de Matemàtiques i Informàtica, Universitat de Barcelona, Barcelona, Catalonia 08007 SpaindFachbereich Mathematik, Universität Hamburg, Hamburg 20146, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528175123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528175123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536055123?af=R">
      <title>The fitness costs of reproductive specialization scale inversely with organismal size</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536055123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;The evolution of reproductive specialization, in which somatic cells forfeit reproduction, represents a fundamental innovation in complex multicellular life. This specialization imposes a fitness cost: because somatic cells do not produce offspring, ...</description>
      <dc:title>The fitness costs of reproductive specialization scale inversely with organismal size</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536055123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Christopher ZhangEric LibbyAnthony BurnettiMatthew D. HerronWilliam C. RatcliffaSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332bInterdisciplinary Graduate Program in Quantitative Biosciences, Georgia Institute of Technology, Atlanta, GA 30332cDepartment of Mathematics and Mathematical Statistics, Integrated Science Lab, Umeå Centre for Microbial Research, Umeå University, Umeå 90187, SwedendNational Science Foundation, Alexandria, VA 22314</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536055123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536055123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536291123?af=R">
      <title>B cells enable autoreactive T cells to avoid suppression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536291123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;Clinical trials and experimental observations have shown that B cells are essential for development of T cell–mediated organ-specific autoimmunity, although their exact contribution is not clear. As antigen presentation by B cells is focused on antigens ...</description>
      <dc:title>B cells enable autoreactive T cells to avoid suppression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536291123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Matthew FunstenRenee de PooterVineeth VaranasiMichael BurrowsKatharine BlockAndrey KuznetsovDavid SerrezeHaochu HuangAlexander ChervonskyaDepartment of Pathology, The University of Chicago, Chicago, IL 60637bCommittee on Immunology, Biological Sciences Division, The University of Chicago, Chicago, IL 60637cThe Jackson Laboratory, Bar Harbor, ME 04609</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536291123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536291123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535986123?af=R">
      <title>The colors of images preferred by individual voxels can be used to delineate functionally distinct visually responsive brain areas</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535986123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;We exploited co-occurrences between color and other properties of natural scenes to identify and visualize functionally distinct brain regions. For each voxel in the Natural Scenes Dataset (NSD), we computed a scaled response-weighted average of the ...</description>
      <dc:title>The colors of images preferred by individual voxels can be used to delineate functionally distinct visually responsive brain areas</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535986123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Ian M. L. PennockChris RaceyKendrick KayAnna FranklinJenny M. BostenaSchool of Psychology, Sussex Neuroscience, University of Sussex, Falmer BN1 9QH, United KingdombCenter for Magnetic Resonance Research, Department of Radiology, University of Minnesota, Minneapolis, Minnesota, MN 55455</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535986123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R">
      <title>Structural innovation and flexibility in plant chemical defenses</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Structural innovation and flexibility in plant chemical defenses</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606250123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Martin VolfaBiology Centre, Institute of Entomology, Czech Academy of Sciences, Ceske Budejovice 370 05, Czech RepublicbFaculty of Science, Department of Zoology, University of South Bohemia, Ceske Budejovice 370 05, Czech Republic</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606250123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604049123?af=R">
      <title>Timing the decline: Cellular circadian rhythms and Alzheimer’s disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604049123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Timing the decline: Cellular circadian rhythms and Alzheimer’s disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604049123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Christopher S. ColwellaDepartment of Psychiatry and Biobehavioral Sciences, Semel Institute, University of California Los Angeles, Los Angeles, CA</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604049123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604888123?af=R">
      <title>The central dogma in reverse</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604888123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>The central dogma in reverse</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604888123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Natalia MrnjavacWilliam F. MartinaInstitute for Molecular Evolution, Heinrich Heine University Düsseldorf, Düsseldorf 40225, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604888123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605413123?af=R">
      <title>An insect that cooperates like bacteria</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605413123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>An insect that cooperates like bacteria</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605413123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Stuart A. WestAshleigh S. GriffinaDepartment of Biology, University of Oxford, Oxford OX1 3SZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605413123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536826123?af=R">
      <title>Standard EF tasks can still have predictive validity within diverse cultural contexts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536826123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Standard EF tasks can still have predictive validity within diverse cultural contexts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536826123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Jesse C. NiebaumaCenter for Mind and Brain, Department of Psychology, Davis, CA 95616</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536826123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533899123?af=R">
      <title>The case for contextually grounded executive function measurement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533899123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>The case for contextually grounded executive function measurement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533899123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Mateus M. MazzaferroJelena ObradovićSabine DoebelSharon WolfYuko MunakataLisa B. ThorellMichael WilloughbySteven J. HowardaGraduate School of Education, Stanford University, Stanford, CA 94305bDepartment of Psychology, George Mason University, Fairfax, VA 22030cGraduate School of Education, University of Pennsylvania, Philadelphia, PA 19104dDepartment of Psychology, University of California, Davis, Davis, CA 95616eDepartment of Clinical Neuroscience, Karolinska Institutet, Stockholm 17165, SwedenfRTI International, Durham, NC 27713gDepartment of Education, University of Oxford, Oxford OX2 6PY, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533899123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R">
      <title>Expanded applicability of the triple oxygen isotope composition of phytoliths as an indicator of atmospheric relative humidity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Expanded applicability of the triple oxygen isotope composition of phytoliths as an indicator of atmospheric relative humidity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534827123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Anne AlexandreJulie AlemanMinger GuoDavid Au YangRobin HavasElizabeth WebbaCentre Européen de Recherche et d’Enseignement des Géosciences de l’Environnement (CEREGE), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université, Institut de Recherche pour le Développement (IRD), Institut National de la Recherche Agronomique (INRA), Collège de France, Aix-en-Provence 13580, FrancebTrent School of the Environment, Trent University, Peterborough, ON K9L 0G2, CanadacEarth Sciences, University of Western Ontario, London, ON N6A 5B7, Canada</dc:creator>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
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      <title>Correction for Lazzaroni et al., Wolves respond differently to human cues as they expand into urban landscapes</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
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      <dc:identifier>doi:10.1073/pnas.2609972123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <title>Correction for Anand et al., Convolutional neural networks outperform other presence-only species distribution modeling algorithms</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609030123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Anand et al., Convolutional neural networks outperform other presence-only species distribution modeling algorithms</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
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      <title>Reply to Mazzaferro et al. and Niebaum: The limits of alignment: Grounding executive functions without assuming special contexts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603106123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Mazzaferro et al. and Niebaum: The limits of alignment: Grounding executive functions without assuming special contexts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603106123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Ivan KroupinHelen Elizabeth DavisEmily BurdettJoseph HenrichaDepartment of Comparative Cultural Psychology, Max Planck Institute for Evolutionary Anthropology, Deutscher Platz 6, Leipzig 04103, GermanybDepartment of Psychological and Behavioral Science, London School of Economics and Political Science, Clement House, 99–101 Aldwych, London WC2B 4JF, United KingdomcDepartment of Human Evolutionary Biology, Harvard University, 11 Divinity Avenue, Cambridge, MA 02138dSchool of Human Evolution and Social Change, Arizona State University, 900 Cady Mall, Tempe, AZ 85287eInstitute of Human Origins, Arizona State University, Institute of Human Origins, Arizona State University, 777 East University Drive, Tempe, AZ 85287fDepartment of Psychology, Nottingham University, School of Psychology, University of Nottingham, University Park, Nottingham NG7 2RD, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
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      <title>Reply to Godin-Beekmann et al.: Quantitative agreement between the CRE theory and spatiotemporal ozone observations is well founded</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537183123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Godin-Beekmann et al.: Quantitative agreement between the CRE theory and spatiotemporal ozone observations is well founded</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537183123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Qing-Bin LuaDepartment of Physics and Astronomy, University of Waterloo, Waterloo, ON N2L 3G1, CanadabDepartment of Biology and Chemistry, University of Waterloo, Waterloo, ON N2L 3G1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <title>Reply to Alexandre et al.: Insensitivity of the Δ′17O value of equisetum to atmospheric relative humidity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604539123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Alexandre et al.: Insensitivity of the Δ′17O value of equisetum to atmospheric relative humidity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604539123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Zachary SharpAnthony GarganoVincent HareJordan WostbrockaDepartment of Earth and Planetary Sciences, University of New Mexico, Albuquerque, NM 87122bDepartment of Archaeology, University of Cape Town, Rondebosch 7701, South AfricacEarth and Planetary Sciences, Yale University, New Haven, CT 06511</dc:creator>
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      <title>QnAs with Yukiko Yamashita</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>QnAs with Yukiko Yamashita</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Sandeep Ravindran</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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