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      <dc:title>In This Issue</dc:title>
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      <title>Distinct evolutionary patterns of endemic and emerging parvoviruses and the origin of a new pandemic virus</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceComparing the evolution of a virus in its reservoir host with that seen in a new host will reveal the special circumstances that allow epidemic emergence. A feline parvovirus (FPV) that jumped to dogs in the mid-1970s formed canine parvovirus (...</description>
      <dc:title>Distinct evolutionary patterns of endemic and emerging parvoviruses and the origin of a new pandemic virus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515274123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Robert A. López-AstacioBrian R. WasikHyunwook LeeIan E. H. VoorheesWendy S. WeichertOluwafemi F. AduLaura B. GoodmanSusan L. HafensteinUwe TruyenColin R. ParrishaBaker Institute for Animal Health, Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853bThe Hormel Institute, Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Medical Research Center, Austin, MN 55912cBaker Institute for Animal Health, Department of Public and Ecosystems Health, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853dDepartment of Biochemistry, Biophysics and Molecular Biology, University of Minnesota, Minneapolis, MN 55455eDepartment of Infectious Diseases, Mayo Clinic, Rochester, MN 55905fInstitut für Tierhygiene und Öffentliches Veterinärwesen, Abteilung für Biochemie, Universität Leipzig, Leipzig 04103, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515274123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2515274123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524709123?af=R">
      <title>Epigenetic constraints and enhancer innovation link neuronal plasticity to evolutionary adaptation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524709123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceHow do nervous systems evolve new cell types while maintaining core functions? This study reveals that small changes in gene regulation can enable neurons to adopt new roles, influencing behavior and evolution. Using nematodes, we show that ...</description>
      <dc:title>Epigenetic constraints and enhancer innovation link neuronal plasticity to evolutionary adaptation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524709123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Andrea Millán-TrejoCarlos Mora-MartínezAdrián Tarazona-SánchezCarla Lloret-FernándezRafael AlisAntonio Jordán-PlaArantza BarriosNuria FlamesaDevelopmental Neurobiology Unit, Instituto de Biomedicina de Valencia Instituto de Biomedicina de Valencia. Consejo Superior de Investigaciones Científicas, Valencia 46010, SpainbAssociated Unit Instituto de Biomedicina de Valencia and Valencia Biomedical Research Foundation, Centro de Investigación Príncipe, Valencia 46012, SpaincDepartment of Cell and Developmental Biology, University College London, London WC1E 7JE, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524709123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524709123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537987123?af=R">
      <title>A plasma-based DNA test for quantification of disease burden in acute myeloid leukemia patients undergoing bone marrow transplantation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537987123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceWe report a blood test that tracks up to 96 patient-specific mutations and applied it to patients with acute myeloid leukemia (AML) who had undergone bone marrow transplantation. Using this test to evaluate cell-free plasma DNA, we found ...</description>
      <dc:title>A plasma-based DNA test for quantification of disease burden in acute myeloid leukemia patients undergoing bone marrow transplantation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537987123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Yuxuan WangJiajun XieSergiu PascaMaria PopoliJanine PtakLisa DobbynNatalie SillimanSuman PaulRichard J. JonesMark J. LevisSamuel D. CurtisChristopher DouvilleCynthia ShamsMatthew Z. GuoShirley MoChristopher D. GockeSami N. MalekCatherine M. BollardChetan BettegowdaKenneth W. KinzlerBert VogelsteinNickolas PapadopoulosLukasz P. GondekaDepartment of Oncology, Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine, Baltimore, MD 21287bThe Ludwig Center for Cancer Genetics and Therapeutics, Johns Hopkins University School of Medicine, Baltimore, MD 21287cDepartment of Oncology, The Sol Goldman Pancreatic Cancer Research Center, Johns Hopkins University School of Medicine, Baltimore, MD 21287dDivision of Hematologic Malignancies, Johns Hopkins University School of Medicine, Baltimore, MD 21287eThe HHMI, Baltimore, MD 21287fDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21287gDivision of Quantitative Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21287hDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21287iDepartment of Internal Medicine, Division of Hematology and Oncology, University of Michigan, Ann Arbor, MI 48109jCenter for Cancer and Immunology Research, Children’s National Research Institute, Children’s National Hospital, Washington, DC 20010kDepartment of Neurosurgery, Johns Hopkins University School of Medicine, Baltimore, MD 21287lDepartment of Neurosurgery, Khatib Brain Tumor Center, Johns Hopkins School of Medicine, MD 21287</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537987123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537987123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533681123?af=R">
      <title>Southern Ocean seabird population shifts over the Holocene revealed by peat sequestration of mercury from guano</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533681123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe Southern Ocean is home to vast seabird populations and threatened species. To understand the wider impact of the catastrophic decline in many seabird populations over recent decades, we need knowledge of their long-term population dynamics ...</description>
      <dc:title>Southern Ocean seabird population shifts over the Holocene revealed by peat sequestration of mercury from guano</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533681123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Chuxian LiStephen J. RobertsMartin GrosjeanAdrien MestrotMartin WilleRichard A. PhillipsMaxime EnricoKevin BishopUlf SkyllbergDmitri MauquoyClemens von SchefferThomas TheurerDavid MuirheadAlex WhittleAngela Gallego-SalaJeroen E. SonkeFrançois De VleeschouwerNathalie Van der PuttenPascale BraconnotOlivier MartiStefan OsterwalderNina BuchmannThomas FrölicherEva AnthamattenAurea C. Chiaia-HernándezPetra ZahajskáCatherine JeandelKrystyna M. SaundersSae Yun KwonDingyong WangRichard BindlerLouise SimeDominic A. HodgsonaInstitute of Geography and Oeschger Center for Climate Change Research, University of Bern, Bern 3012, SwitzerlandbDepartment of Aquatic Sciences and Assessment, Swedish University of Agricultural Sciences, Uppsala 75007, SwedencBritish Antarctic Survey, Natural Environment Research Council, Cambridge CB3 0ET, United KingdomdInstitute of Geological Sciences, University of Bern, Bern 3012, SwitzerlandeUniversité de Pau et des Pays de l’Adour, LFCR, E2S UPPA, CNRS, Pau 64000, FrancefDepartment of Forest Ecology and Management, Swedish University of Agricultural Sciences, Umeå 901 83, SwedengSchool of Geosciences, University of Aberdeen, Scotland, Aberdeen AB24 3U, United KingdomhGeography Department, University of Exeter, Exeter EX4 4RJ, United KingdomiGéosciences Environnement Toulouse, Université de Toulouse, CNRS, IRD, Toulouse 31400, FrancejInstituto Franco-Argentino para el Estudio del Clima y sus Impactos (IRL3351 IFAECI/CNRS-CONICET-IRD-UBA), Universidad de Buenos Aires, Buenos Aires C1428EGA, ArgentinakDepartment of Earth Sciences, Vrije Universiteit Amsterdam, Amsterdam 1081, The NetherlandslLaboratoire des Sciences du Climat et de l’Environnement, LSCE/IPSL, CEA-CNRS-UVSQ, Université Paris-Saclay, Gif-sur-Yvette 91191, FrancemDepartment of Geography, Hydrology and Climate, University of Zurich, Zurich 8057, SwitzerlandnGrassland Sciences, Institute of Agricultural Sciences, ETH Zurich, Zurich 8092, SwitzerlandoClimate and Environmental Physics, Physics Institute, University of Bern, Bern 3012, SwitzerlandpLEGOS, Université de Toulouse, CNES, CNRS, IRD, Toulouse 31400, FranceqInstitute for Antarctic and Marine Studies, University of Tasmania, Hobart, Tasmania 7004, AustraliarDivision of Environmental Science and Engineering, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of KoreasCollege of Resources and Environment, Southwest University, Chongqing 400715, ChinatDepartment of Ecology and Environmental Science, Umeå University, Umeå 901 87, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533681123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533681123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533019123?af=R">
      <title>Cell wall remodeling–dependent morphotype switch in Mycobacterium avium differentially regulates colonization and tissue persistence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533019123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceMycobacterium aviumcan switch between two primary colony morphologies—smooth transparent (SmT) and smooth opaque (SmO)—where SmT is associated with human disease while the avirulent SmO morphotype might represent an environmental form of the ...</description>
      <dc:title>Cell wall remodeling–dependent morphotype switch in Mycobacterium avium differentially regulates colonization and tissue persistence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533019123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Katie LaschanzkyGiulia Magri RibeiroRodrigo SequeiraSacha CancadeFredric CarlssonJulia LienardaDepartment of Biology, Lund University, Lund 22362, SwedenbDepartment of Biological Sciences, Smith College, Northampton 01063, MAcDepartment of Medical Biotechnology, University of Siena, Siena 53100, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533019123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533019123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520755123?af=R">
      <title>Sulfated polysaccharide reprograms arterialized angiogenesis of endochondral ossification to rescue defective osteonecrosis therapy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520755123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificancePersistent arteriogenesis during the repair process is critical for the treatment of glucocorticoid-induced osteonecrosis. Conventional proangiogenic agents remain suboptimal in efficacy, and the intrinsically chronic inflammatory further ...</description>
      <dc:title>Sulfated polysaccharide reprograms arterialized angiogenesis of endochondral ossification to rescue defective osteonecrosis therapy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520755123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Shuang ZhangYang LiuShunshu DengZehua GaoJing WangChangsheng LiuaSchool of Materials Science and Engineering, The State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai 200237, People’s Republic of ChinabSchool of Materials Science and Engineering, Engineering Research Center for Biomedical Materials of the Ministry of Education, East China University of Science and Technology, Shanghai 200237, People’s Republic of ChinacDepartment of Cardiovascular Surgery, Shanghai East Hospital, Tongji University School of Medicine, Shanghai 200092, People’s Republic of ChinadSchool of Materials Science and Engineering, Frontiers Science Center for Materiobiology and Dynamic Chemistry, East China University of Science and Technology, Shanghai 200237, 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>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520755123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520755123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531564123?af=R">
      <title>Alternative splicing of the Rbm24 gene is essential for cochlear hair cell stereocilia integrity and hearing function in mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531564123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceMechanotransduction of cochlear hair cells relies on stereocilia, the F-actin-filled cell protrusions at their apical surface. Previously, we reported that RNA-binding protein RBM24 plays pivotal roles in stereocilia development and hearing ...</description>
      <dc:title>Alternative splicing of the Rbm24 gene is essential for cochlear hair cell stereocilia integrity and hearing function in mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531564123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Chunjiao SunJingshuang ZhaoNana LiXuebo YaoYanfei WangChul Hoon KimJinwoong BokAnthony W. PengZhigang XuaShandong Provincial Key Laboratory of Development and Regeneration and Key Laboratory for Experimental Teratology of the Ministry of Education, School of Life Sciences, Shandong University, Qingdao 266237, Shandong, ChinabDepartment of Pharmacology, Yonsei University College of Medicine, Seoul 03722, KoreacBrain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul 03722, KoreadDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, KoreaeDepartment of Physiology and Biophysics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045fAdvanced Medical Research Institute, Cheeloo College of Medicine, Shandong University, Jinan 250012, Shandong, ChinagDepartment of Otolaryngology Head and Neck Surgery, The First Hospital of Lanzhou University, Lanzhou 730000, Gansu, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531564123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531564123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2504211123?af=R">
      <title>Space-based observation of global increase in urban methane emissions from 2019–2023</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2504211123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceCities are large emitters of methane, a potent greenhouse gas and precursor for tropospheric ozone. We use space-based observations to study nearly 100 cities with a total population of 1.18 billion people, and find emissions from these cities ...</description>
      <dc:title>Space-based observation of global increase in urban methane emissions from 2019–2023</dc:title>
      <dc:identifier>doi:10.1073/pnas.2504211123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Erica WhitingGenevieve PlantEric A. KortIlse AbenKira J. BienerGijs LeguijtJoannes D. MaasakkersaClimate and Space Sciences and Engineering, University of Michigan, Ann Arbor, MI 48109bAtmospheric Chemistry Department, Max Planck Institute for Chemistry, Mainz 55128, GermanycNetherlands Institute for Space Research, Leiden 2333 CA, The NetherlandsdEarth and Planetary Sciences, Yale University, New Haven, CT 06511eDepartment of Climate, Air and Sustainability, Netherlands Organisation for Applied Scientific Research, Utrecht 3584 CB, The Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2504211123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2504211123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533611123?af=R">
      <title>Habitat-specific temporal variation in the pace of fish diversification</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533611123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceAquatic habitats vary in their biotic and abiotic properties. In this study, we demonstrate that these differences have modulated the pace of species diversification through time for ray-finned fishes, which represent over half of extant ...</description>
      <dc:title>Habitat-specific temporal variation in the pace of fish diversification</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533611123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Nick PeoplesMichalis MihalitsisPeter C. WainwrightaDepartment of Evolution and Ecology, University of California, Davis, Davis, CA 95616bMarine Laboratory, University of Guam, Mangilao, Guam 96923</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533611123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533611123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518250123?af=R">
      <title>mRNA m6A modifications and the RNA-binding protein YTHDF1 affect translational control in both normal and pathological learning</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518250123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceNeural plasticity is essential for learning and adaptation to environmental changes. However, maladaptive plasticity leads to neurological and psychiatric disorders. It is known that long-term plasticity requires new protein synthesis. By ...</description>
      <dc:title>mRNA m6A modifications and the RNA-binding protein YTHDF1 affect translational control in both normal and pathological learning</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518250123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Zhuoyue ShiKailong WenWenqin FuZhongyu ZouKathryn GuoNabilah H. SammudinMeera J. PatelXiangbin RuanShivang SullereShuai WangXiaochang ZhangGopal ThinakaranChuan HeXiaoxi ZhuangaDepartment of Neurobiology, The University of Chicago, Chicago, IL 60637bCommittee on Neurobiology, Biological Sciences Division, The University of Chicago, Chicago, IL 60637cDepartment of Chemistry, The University of Chicago, Chicago, IL 60637dDepartment of Human Genetics, The University of Chicago, Chicago, IL 60637eByrd Alzheimer’s Center and Research Institute, The University of South Florida, Tampa, FL 33613fNeuroscience Institute, Biological Sciences Division, The University of Chicago, Chicago, IL 60637gDepartment of Molecular Medicine, Morsani College of Medicine, The University of South Florida, Tampa, FL 33612hHHMI, Department of Chemistry, The 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>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518250123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518250123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523372123?af=R">
      <title>Weather forecasts become more important for reducing mortality as the climate warms</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523372123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificancePeople use weather forecasts to avoid deadly consequences of extreme weather, but the usefulness of forecasts depends on their accuracy. We find that accurate temperature forecasts already save lives, particularly during periods of extreme ...</description>
      <dc:title>Weather forecasts become more important for reducing mortality as the climate warms</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523372123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Jeffrey G. ShraderStephan ThiesLaura BakkensenManuel LinsenmeierDerek LemoineaSchool of International and Public Affairs, Columbia University, New York, NY 10027bDepartment of Economics, University of Oregon, Eugene, OR 97403cCenter for Critical Computational Studies, Goethe University, Frankfurt am Main 60322, GermanydHigh Meadows Environmental Institute, Princeton University, Princeton, NJ 08544eDepartment of Economics, University of Arizona, Tucson, AZ 85721fNational Bureau of Economic Research, Cambridge, MA 02138gCentre for Economic Policy Research, Paris 75007, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523372123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523372123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528108123?af=R">
      <title>Glassy interphases reinforce elastomeric nanocomposites by enhancing volume expansion under strain</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528108123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceBy adding nanoparticles to elastomers, engineers turn materials with the compliance of rubber bands into composites strong enough to support a Boeing 747 on just a few tire patches. The physics driving this transformation has remained elusive ...</description>
      <dc:title>Glassy interphases reinforce elastomeric nanocomposites by enhancing volume expansion under strain</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528108123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Pierre KawakHarshad BhapkarDavid S. SimmonsaDepartment of Chemical, Biological, and Materials Engineering, University of South Florida, Tampa, FL 33612</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2528108123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532223123?af=R">
      <title>Deep learning framework for quantifying self-organization in Myxococcus xanthus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532223123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceMulticellular self-organization, such as the formation of fruiting bodies inMyxococcus xanthus, involves complex dynamics that are hard to quantify, hindering our ability to link genetic variation to emergent behaviors. We present an ...</description>
      <dc:title>Deep learning framework for quantifying self-organization in Myxococcus xanthus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532223123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Jiangguo ZhangEduardo A. CaroPeiying ChenTrosporsha Tasnim KhanPatrick A. MurphyLawrence J. ShimketsAnkit B. PatelRoy D. WelchOleg A. IgoshinaDepartment of Bioengineering, Rice University, Houston, TX 77005bDepartment of Biology, Syracuse University, Syracuse, NY 13244cDepartment of Mathematics, San José State University, San Jose, CA 95192dDepartment of Microbiology, University of Georgia, Athens, GA 30602eDepartment of Electrical and Computer Engineering, Rice University, Houston, TX 77005fDepartment of Neuroscience, Baylor College of Medicine, Houston, TX 77005gDepartment of Biosciences, Rice University, Houston, TX 77005hDepartment of Chemistry, Rice University, Houston, TX 77005iCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532223123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517953123?af=R">
      <title>A modified CRISPR/Cas9 approach in silencing the triplication in Down syndrome: A treatment path XISTs</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517953123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceDown syndrome (DS) results from trisomy 21 and remains without a molecularly targeted therapy. Prior work demonstrated that ectopic expression of the long noncoding RNA XIST could epigenetically silence the extra chromosome 21, but technical ...</description>
      <dc:title>A modified CRISPR/Cas9 approach in silencing the triplication in Down syndrome: A treatment path XISTs</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517953123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Gewei LianAbdalla KhabazehVolney SheenaDepartment of Neurology, Beth Israel Deaconess Medical Center and 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>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517953123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527944123?af=R">
      <title>Ancient environmental genome reveals a migratory brown bear individual in Early Holocene Scandinavia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527944123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceAncient brown bear genomes from Scandinavia are rare due to a scarce bone fossil record. Using an alternative source of ancient genomic information—lake sediments—we present a 9,600-y-old ancient brown bear environmental genome from ...</description>
      <dc:title>Ancient environmental genome reveals a migratory brown bear individual in Early Holocene Scandinavia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527944123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Ernst JohnsonIsabelle Sofie FeinauerCarl RegnéllChenyu JinJ. Camilo Chacón-DuqueGonzalo Oteo-GarcíaRichard GyllencreutzSarah L. GreenwoodLove DalénPeter D. HeintzmanAnna LinderholmaCentre for Palaeogenetics, Stockholm SE-106 91, SwedenbDepartment of Geological Sciences, Stockholm University, Stockholm SE-106 91, SwedencBolin Centre for Climate Research, Stockholm University, Stockholm SE-106 91, SwedendDepartment of Zoology, Stockholm University, Stockholm SE-106 91, SwedeneDepartment of Bioinformatics and Genetics, Swedish Museum of Natural History, Stockholm SE-104 05, SwedenfDepartment of Environmental Science, Kristianstad University, Kristianstad SE-291 88, SwedengAncient DNA Unit, Science for Life Laboratory, Uppsala SE-752 36, SwedenhDepartment of Organismal Biology, Uppsala University, Uppsala SE-752 36, SwedeniDepartment of Archaeology and Classical Studies, Stockholm University, Stockholm SE-106 91, SwedenjDipartamento di Biologia Ambientale, Sapienza Università di Roma, Rome 00185, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527944123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532451123?af=R">
      <title>Tree growth after a major hurricane reflects predisturbance vigor rather than canopy damage</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532451123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceSevere storms are expected to intensify with climate change, yet the long-term impacts of hurricane damage on tropical tree growth remain a subject of debate. By integrating airborne Light Detection and Ranging (LiDAR) with repeated field ...</description>
      <dc:title>Tree growth after a major hurricane reflects predisturbance vigor rather than canopy damage</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532451123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Laura E. BoeschotenRoi Ankori-KarlinskyGabriel ArellanoAlyssa J. BrownDingyi FangVeronika LeitoldDouglas MortonGan YuanTian ZhengJess K. ZimmermanMaría UriarteaDepartment of Ecology, Evolution and Environmental Biology, Columbia University, New York, NY 10027bQ-ForestLab, Department of Environment, Faculty of Bioscience Engineering, Ghent University, Ghent 9000, BelgiumcDepartment of Ecology and Evolutionary Biology, University of Michigan, Ann Arbor, MI 48109dOikobit Limited Liability Company (LLC), Albuquerque, NM 87120eDepartment of Statistics, Columbia University, New York, NY 10032fDepartment of Geographical Sciences, University of Maryland, College Park, MD 20742gBiospheric Sciences Laboratory, NASA Goddard Space Flight Center, Greenbelt, MD 20771hDepartment of Biostatistics, City University of Hong Kong, Kowloon, Hong KongiDepartment of Environmental Sciences, Universidad de Puerto Rico, San Juan, PR 00925</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532451123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532451123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523589123?af=R">
      <title>Industrialization increases the estrogen-recycling capacity of the gut microbiome</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523589123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceEstrogens are essential regulators of human biology, influencing reproduction, physiology, and risk for sex hormone-associated diseases. Gut microbes can recycle estrogens by breaking down their inactivated forms in the intestine, which allows ...</description>
      <dc:title>Industrialization increases the estrogen-recycling capacity of the gut microbiome</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523589123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Rebecca S. A. BrittainRichard G. BribiescasGrazyna JasienskaaDepartment of Anthropology, Yale University, New Haven, CT 06520bDepartment of Environmental Health, Faculty of Health Sciences, Jagiellonian University Medical College, Kraków 31-066, Poland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523589123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523589123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521977123?af=R">
      <title>Voltage-gated proton channel Hv1/VSOP regulates reciprocal interactions between F-actin and endosomes in microglia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521977123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceVoltage-gated proton channels are classically viewed as plasma membrane proteins that regulate pH homeostasis. Our study uncovers an intracellular pool of voltage-gated proton channel 1 (Hv1)/VSOP on endosomal membranes in microglia and ...</description>
      <dc:title>Voltage-gated proton channel Hv1/VSOP regulates reciprocal interactions between F-actin and endosomes in microglia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521977123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Takafumi KawaiDaisuke YoshiokaPattama WiriyasermkulRisa Mori-KreinerRizki Tsari AndrianiMegumi KobayashiManabu AbeKenji SakimuraKazuki NagayasuShushi NagamoriYasushi OkamuraaDepartment of Integrative Physiology, Graduate School of Medicine, The University of Osaka, Osaka 565-0871, JapanbDepartment of Molecular and Cellular Physiology, Graduate School of Medicine, Ehime University, Ehime 791-0295, JapancCenter for Systemic Intelligence in Biomedicine, The Jikei University School of Medicine, Tokyo 105-8461, JapandDepartment of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, JapaneLaboratory of Molecular Neuropharmacology, Graduate School of Pharmaceutical Sciences, The University of Osaka, Osaka 565-0871, JapanfDivision of Multiscale Nutritional Biochemistry, Research Center for Medical Sciences, The Jikei University School of Medicine, Tokyo 105-8461, JapangDepartment of Integrative Physiology, Graduate School of Frontier Biosciences, The University of Osaka, Osaka 565-0871, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521977123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521977123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528843123?af=R">
      <title>SCD1 licenses STING signaling through fatty acid desaturation–mediated membrane remodeling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528843123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceSTING is a central adaptor in innate antiviral immunity, and its activity must be tightly regulated to prevent immunopathology. Our work establishes SCD1 as a metabolic checkpoint that licenses STING activation through biophysical control of ...</description>
      <dc:title>SCD1 licenses STING signaling through fatty acid desaturation–mediated membrane remodeling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528843123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Danhui QinYanjie GaoHaojia JiangXintong MengYing QinHui SongYue FuChengjiang GaoMutian JiaChunyuan ZhaoWei ZhaoaDepartment of Pathogenic Biology, Key Laboratory of Infection Immunity and Disease Intervention of Shandong Province, and Key Laboratory for Experimental Teratology of the Chinese Ministry of Education, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, ChinabState Key Laboratory for Innovation and Transformation of Luobing Theory, Department of Cardiology, Qilu Hospital of Shandong University, Jinan 250012, ChinacKey Laboratory of Cardiovascular Remodeling and Function Research of Chinese Ministry of Education, Chinese National Health Commission, Chinese Academy of Medical Sciences and Shandong Province, Department of Cardiology, Qilu Hospital of Shandong University, Jinan 250012, ChinadDepartment of Physiology and Pathophysiology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, ChinaeDepartment of Immunology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, ChinafDepartment of Cell Biology, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, Shandong 250012, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528843123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528843123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523148123?af=R">
      <title>Trem2 exacerbates ischemic brain injury through Gpnmb in a photothrombotic stroke model</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523148123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceStroke is a leading cause of death and disability, with microglia-driven inflammation as a key contributor to brain injury. The microglial receptor Trem2 has shown inconsistent roles: protective in a classic stroke model but associated with ...</description>
      <dc:title>Trem2 exacerbates ischemic brain injury through Gpnmb in a photothrombotic stroke model</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523148123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Xuezhen ChenKunyu LiSiyu LiuJunyi ZhaoSagun TiwariFan ZengYue ZhaoPingping ZhangHan TangHong ZhaoHelmut KettenmannXianyuan XiangXinzhou ZhuaThe Brain Cognition and Brain Disease Institute, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, ChinabBio-X international institute, Faculty of Life and Health Sciences, Shenzhen University of Advanced Technology, Shenzhen 518107, ChinacMinistry of Education Key Laboratory of Gene Function and Regulation, Guangdong Province Key Laboratory of Pharmaceutical Functional Genes, State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, ChinadShenzhen Key Laboratory of Neuroimmunomodulation for Neurological Diseases, Shenzhen 518055, ChinaeUniversity of Chinese Academy of Sciences, Beijing 100049, ChinafShenzhen Hospital of Shanghai University of Traditional Chinese Medicine, Shenzhen 518001, ChinagLuohu District Hospital of Traditional Chinese Medicine, Shenzhen 518001, ChinahMax-Delbrück Center for Molecular Medicine, Berlin 13125, GermanyiShenzhen-Hong Kong Institute of Brain Science-Shenzhen Fundamental Research Institutions, Shenzhen 518055, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523148123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523148123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534025123?af=R">
      <title>Quinones operate as proton-collecting antennas in energy-transducing membranes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534025123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceQuinones are central carriers of redox energy in biological membranes. Here, we show that ubiquinone Q10, the main lipophilic redox carrier in respiratory chains, strongly influences the protonation reactions at the membrane surface. Our ...</description>
      <dc:title>Quinones operate as proton-collecting antennas in energy-transducing membranes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534025123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Adel BeghiahNiusha BagheriSofia BadolatoHyunho KimTimir Baran SilMaximilian C. PöverleinJerker WidengrenVille R. I. KailaaDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm 10691, SwedenbExperimental Biomolecular Physics, Department of Applied Physics, Royal Institute of Technology (Kungliga Tekniska högskolan), Albanova University Center, Stockholm 106 91, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534025123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534025123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526252123?af=R">
      <title>CHK2-USP37 axis stabilizes FOXO4 to sustain senescence and evade apoptosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526252123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceCellular senescence is a key driver of aging and age-related diseases, largely due to the accumulation of apoptosis-resistant senescent cells. While the transcription factor FOXO4 is known to promote senescent cell survival, the mechanisms ...</description>
      <dc:title>CHK2-USP37 axis stabilizes FOXO4 to sustain senescence and evade apoptosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526252123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Jiahui SunAnke GengZhiwei SongLingjiang ChenZhen-Ning ZhangYing JiangZhiyong MaoaShanghai Key Laboratory of Maternal Fetal Medicine, Clinical and Translational Research Center of Shanghai First Maternity and Infant Hospital, Frontier Science Center for Stem Cell Research, School of Life Sciences and Technology, Tongji University, Shanghai 200092, ChinabInstitute for Regenerative Medicine, State Key Laboratory of Cardiology and Medical Innovation Center, Shanghai East Hospital, Frontier Science Center for Stem Cell Research, Shanghai Key Laboratory of Signaling and Disease Research, School of Life Sciences and Technology, Tongji University, Shanghai 200092, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526252123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526252123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529741123?af=R">
      <title>Evidence for strong purifying selection of human 47S ribosomal RNA genes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529741123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe rRNA genes are the most highly expressed genes in the human genome but there are almost no known diseases linked to sequence variants in the rRNA. We describe over 14,000 sequence variants that coexist within and between individuals and ...</description>
      <dc:title>Evidence for strong purifying selection of human 47S ribosomal RNA genes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529741123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Xufan MaFiona ChowBuz GalbraithDaniel SultanovEli K. BeharAndreas HochwagenaDepartment of Biology, New York University, New York, NY 10003bGraduate Program in Data Science, Center for Data Science, New York University, New York, NY 10003</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529741123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529741123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602266123?af=R">
      <title>Structural basis of transcription-coupled RNA damage by incorporation of oxidized ribonucleotides</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602266123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceCells are continuously exposed to oxidative stress, which lead to oxidation damage on DNA, RNA as well as nucleotide pools. However, the formation of oxidative RNA damage and the impact of an oxidized ribonucleotide pool on transcription ...</description>
      <dc:title>Structural basis of transcription-coupled RNA damage by incorporation of oxidized ribonucleotides</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602266123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Peini HouChanjoo LeeJenny ChongJuntaek OhDong WangaDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, CA 92093bDepartment of Regulatory Science, Graduate School, Kyung Hee University, Seoul 02447, Republic of KoreacInstitute of Regulatory Innovation through Science, Kyung Hee University, Seoul 02447, Republic of KoreadInstitute of Integrated Pharmaceutical Sciences, Kyung Hee University, Seoul 02447, Republic of KoreaeDepartment of Cellular and Molecular Medicine, University of California, San Diego, CA 92093fDepartment of Chemistry and Biochemistry, University of California, San Diego, CA 92093</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602266123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602266123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524705123?af=R">
      <title>Immune modulation promotes heart regeneration through macrophage and Granulin functions in medaka</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524705123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceOur work highlights the importance of sensitized damage-associated molecular patterns (DAMPs) signaling in shaping acute inflammatory responses that favor regenerative healing rather than fibrosis. We show that immune modulation enhances ...</description>
      <dc:title>Immune modulation promotes heart regeneration through macrophage and Granulin functions in medaka</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524705123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Kaushik ChowdhuryChia-Lin HuangI-Ting LinYu-Jen HungKhai Lone LimHsing-Wei LiuKe-Hsuan WeiKai-Chien YangYao-Ming ChangBen Shih-Lei LaiaInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, TaiwanbTaiwan International Graduate Program in Molecular Medicine, National Yang Ming Chiao Tung University and Academia Sinica, Taipei 11529, TaiwancDepartment and Graduate Institute of Pharmacology, National Taiwan University College of Medicine, Taipei 10051, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524705123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524705123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523345123?af=R">
      <title>Medial temporal lobe encodes cognitive maps of real-world social networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523345123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceNavigating everyday social life—from strategic gossiping to building influence—depends on a representation of the hundreds of ties that link people in the community to one another. We uncover the precise format of these neural representations ...</description>
      <dc:title>Medial temporal lobe encodes cognitive maps of real-world social networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523345123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Yi Yang TeohJae-Young SonAlice XiaApoorva BhandariOriel FeldmanHallaDepartment of Cognitive and Psychological Sciences, Brown University, Providence, RI 02912bRobert J. and Nancy D. Carney Institute for Brain Science, Brown University, Providence, RI 02912</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523345123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523345123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517403123?af=R">
      <title>Selective octopaminergic tuning of mushroom body circuits during memory formation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517403123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceAnimals adapt their behavior by integrating past experiences with current conditions. Our study uncovers how octopamine signaling adds an additional layer of complexity to the neuronal circuits essential for learning and memory inDrosophila. ...</description>
      <dc:title>Selective octopaminergic tuning of mushroom body circuits during memory formation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517403123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Ulrike S. FrankeAlexandra GroßjohannSamantha AurichInes KöhlerMarius LambertySara GranatoAlice FallahaJana BreitfeldPeter KovacsMareike SelchoRobert J. KittelAndreas S. ThumDennis PaulsaDepartment of Animal Physiology, Institute of Biology, Leipzig University, Leipzig 04103, GermanybDepartment of Genetics, Institute of Biology, Leipzig University, Leipzig 04103, GermanycDivision of Endocrinology, Nephrology and Rheumatology, Department of Medicine III, Leipzig University, Leipzig 04103, GermanydGerman Centre for Integrative Biodiversity Research (iDiv) Halle-Jena-Leipzig, Leipzig 04103, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517403123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517403123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524021123?af=R">
      <title>Recurrent mutations drive rapid HIV escape from two broadly neutralizing antibodies in vivo</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524021123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceUsing recently developed techniques that capture viral genetic diversity and associations between mutations at depth, we deeply sequenced HIV from two clinical trials of broadly neutralizing antibody (bNAb) monotherapies, 3BNC117 and 10-1074. ...</description>
      <dc:title>Recurrent mutations drive rapid HIV escape from two broadly neutralizing antibodies in vivo</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524021123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Elena V. RomeroAbigail E. ClydeElena E. GiorgiDylan H. WestfallWalker AzamMegan L. TaylorMarina CaskeyAlison F. FederLillian B. CohnaDepartment of Genome Sciences, University of Washington, Seattle, WA 98105bHHMI, Seattle, WA 98105cVaccine and Infectious Diseases Division, Fred Hutchinson Cancer Center, Seattle, WA 98109dMedical Scientist Training Program, University of Washington, Seattle, WA 98195eLaboratory of Molecular Immunology, The Rockefeller University, New York, NY 10065fDivision of Public Health Sciences, Fred Hutch Cancer Center, Seattle, WA 98109gDepartment of Global Health, University of Washington, Seattle, WA 98105</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524021123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524021123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516376123?af=R">
      <title>Quantifying and combating zoonotic viruses poised for emergence: Using multiplex receptor screening and decoy engineering technologies</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516376123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;Viral discovery efforts have uncovered millions of zoonotic viruses across multiple continents, listed on the World Health Organization’s pandemic risk register. Over two-thirds of these zoonotic viruses pose significant risks, are poised to infect humans,...</description>
      <dc:title>Quantifying and combating zoonotic viruses poised for emergence: Using multiplex receptor screening and decoy engineering technologies</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516376123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Alex OdoomEugene M. ObengChristian K. O. DzuvoraDepartment of Medical Microbiology, University of Ghana Medical School, Accra KB 4236, GhanabSchool of Medical Sciences, Faculty of Medicine and Health, University of Sydney, Camperdown, NSW 2006, AustraliacSydney Nano Institute, University of Sydney, Camperdown, NSW 2006, AustraliadSydney Biomanufacturing Incubator, University of Sydney, Sydney, NSW 2006, AustraliaeDepartment of Immunology and Infectious Diseases, Harvard T.H. Chan School of Public Health, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516376123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516376123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524893123?af=R">
      <title>Podocin oligomers regulate the ordering of nephrin chains, providing the molecular basis of NPHS2 interallelic interactions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524893123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe kidney filters blood through a specialized barrier formed by proteins such as nephrin, whose precise spacing determines the size of filtration pores. Inherited kidney diseases that disrupt this barrier cause massive protein leakage into ...</description>
      <dc:title>Podocin oligomers regulate the ordering of nephrin chains, providing the molecular basis of NPHS2 interallelic interactions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524893123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Violetta Antal-KónyaGusztáv SchayMáté KétszeriEszter BaloghÁgnes MikóDániel SeidlTália Magdolna KeszthelyiMária BernáthAnita Ungvári-VeresGuillaume DorvalMoin A. SaleemAbhijit DixitCorinne AntignacKatalin PásztyMiklós KellermayerDóra K. MenyhárdKálmán ToryaMagyar Tudományos Akadémia-Semmelweis Egyetem Lendület Nephrogenetic Laboratory, Budapest H-1083, HungarybSemmelweis University, Pediatric Center, MTA Center of Excellence, Budapest H-1083, HungarycDepartment of Biophysics and Radiation Biology, Semmelweis University, Budapest H-1094, HungarydLaboratory of Hereditary Kidney Diseases, INSERM, UMR 1163, Imagine Institute, Université Paris Cité, Paris F-75015, FranceeDépartement de Génétique, Assistance Publique–Hôpitaux de Paris, Hôpital Necker-Enfants Malades, Paris F-75015, FrancefBristol Renal, Bristol Medical School, University of Bristol, Bristol BS1 3NY, United KingdomgNottingham Regional Genetics Service, Nottingham City Hospital Campus, Nottingham NG5 1PB, United KingdomhHungarian Research Network-Eötvös Loránd University Protein Modeling Research Group, Eötvös Loránd University, Budapest H-1117, HungaryiMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Budapest H-1117, Hungary</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524893123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524893123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524579123?af=R">
      <title>YTHDC1 recognizes METTL16-dependent m6A on caRNAs and coordinates cotranscriptional splicing</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524579123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe presence of multiple m6A writers and readers strongly suggests undiscovered layers of functional specialization and unique modes of action, yet how these diverse components achieve precise, cell-type, or developmental stage-specific ...</description>
      <dc:title>YTHDC1 recognizes METTL16-dependent m6A on caRNAs and coordinates cotranscriptional splicing</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524579123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-14T07:00:00Z</dc:date>
      <dc:creator>Zhong ZhangQi YinWeimin LinQiwen LiRui ShengShuang JiangKexin LeiLinfeng LiuLanxin ZhangChunlin QianJunru WenZirui WangChong ChenQuan YuanaDepartment of Implantology, State Key Laboratory of Oral Diseases and National Center for Stomatology and National Clinical Research Center for Oral Diseases, West China Hospital of Stomatology, Sichuan University, Chengdu, Sichuan 610041, ChinabDepartment of Implantology, The Affiliated Stomatological Hospital of Nanjing Medical University, Jiangsu Province Key Laboratory of Oral Diseases, Nanjing Medical University, Nanjing, Jiangsu 210008, ChinacState Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, ChinadDepartment of Implantology, Stomatology Hospital, Zhejiang University School of Medicine, Hangzhou 310016, ChinaeDaniel J. Epstein Department of Industrial &amp; Systems Engineering, University of Southern California, Los Angeles, CA 90089</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524579123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524579123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R">
      <title>Small subunit isoform diversity underlies structural heterogeneity in native plant Rubisco</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceRibulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the key enzyme in photosynthetic CO2fixation, has long challenged efforts to understand its assembly, regulation, and potential for enhancement. Here, we show that multiple small ...</description>
      <dc:title>Small subunit isoform diversity underlies structural heterogeneity in native plant Rubisco</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519949123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Thomas ReynoldsZhemin ZhangDušan ŽivkovićSteven KellyJani R. BollaaDepartment of Biology, Univeristy of Oxford, Oxford OX1 3RB, United KingdombDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH 44106cDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519949123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R">
      <title>Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificancePlants survive drought by sensing the hormone abscisic acid (ABA), but how receptor structure converts hormone levels into precise stress responses has remained unclear. Here, we uncover a minimal five-amino acid “code” that determines whether ...</description>
      <dc:title>Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534140123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Maria Rivera-MorenoMar BonoLourdes InfantesPedro L. RodriguezArmando AlbertaInstituto de Química-Física “Blas Cabrera”, Consejo Superior de Investigaciones Científicas, Madrid ES-28006, SpainbInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, Valencia ES-46022, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534140123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534844123?af=R">
      <title>WWOX maintains epidermal identity and suppresses EMT to prevent aggressive cutaneous squamous cell carcinoma</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534844123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceCutaneous squamous cell carcinoma (cSCC) is an increasingly common cancer whose aggressive forms remain poorly understood. We identify WW domain–containing oxidoreductase (WWOX) as a central guardian of epidermal identity, stabilizing p63-...</description>
      <dc:title>WWOX maintains epidermal identity and suppresses EMT to prevent aggressive cutaneous squamous cell carcinoma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534844123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Tirza Bidany-MizrahiKian MarounMara ManciniOsama HidmiIhab AnsariJonathan MoninTal Keidar HaranAlexander MalyGerry MelinoEleonora CandiRami I. AqeilanaThe Concern Foundation Laboratories, The Lautenberg Center for Immunology and Cancer Research, Department of Immunology and Cancer Research, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 91120, IsraelbDepartment of Experimental Medicine and Surgery, University of Rome “Tor Vergata”, Rome 00133, ItalycBiochemistry Laboratory, Istituto di Ricovero e Cura a Carattere Scientifico-Istituto Dermopatico Immacolata, Rome 00133, ItalydDepartment of Developmental Biology and Cancer Research, Institute for Medical Research Israel-Canada, Hebrew University Medical School, Jerusalem 91120eDepartment of Pathology, Hadassah University Hospital, Jerusalem 91120, IsraelfCyprus Cancer Research Institute, Nicosia 2109, Cyprus</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534844123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534844123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537522123?af=R">
      <title>Compositional memory matters for early molecular systems</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537522123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceTransient compartmentalization is thought to be essential for preventing parasites (short nonfunctional RNA sequences) from invading replicases (self-replicating RNA), but how compartmentalization behaviors specifically affect replicase-...</description>
      <dc:title>Compositional memory matters for early molecular systems</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537522123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Barnabe LedouxRyoka KuwabaraNorikazu IchihashiRyo MizuuchiDavid LacosteaGulliver Laboratory, UMR CNRS 7083, Paris Sciences et Lettres Research University, Ecole SupÃ©rieure de Physique et Chimie Industrielles, Paris F-75231, FrancebDepartment of Electrical Engineering and Bioscience, Faculty of Science and Engineering, Waseda University, Shinjuku, Tokyo 162-8480, JapancDepartment of Life Science, Graduate School of Arts and Science, The University of Tokyo, Meguro, Tokyo 153-8902, JapandKomaba Institute for Sciences, The University of Tokyo, Meguro, Tokyo 153-8902, JapaneResearch Center for Complex Systems Biology, Universal Biology Institute, The University of Tokyo, Meguro, Tokyo 153-8902, JapanfJapan Science and Technology Agency, Fusion Oriented Research for disruptive Science and Technology, Kawaguchi, Saitama 332-0012, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537522123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523130123?af=R">
      <title>FABP7 controls radial glial scaffold stability during human cortical development</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523130123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceRadial glial (RG) cells are the principal neural progenitors of the developing cortex and form the structural scaffold that guides neuronal migration and cortical lamination. Here, we reveal that FABP7 is a functional regulator of RG scaffold ...</description>
      <dc:title>FABP7 controls radial glial scaffold stability during human cortical development</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523130123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Yuanhao WangXu ZhangRu BaYimin ZhuHanwen YuDa WangChu ChuXinyue ZhangYuan HongShanshan WuWanying ZhuMin XuQing ChengChunjie ZhaoXiao HanYan LiuaInstitute of Stem Cell and Neural Regeneration, School of Pharmacy, Nanjing Medical University, Nanjing 211166, ChinabInterdisciplinary InnoCenter for Organoids, State Key Laboratory of Reproductive Medicine and Offspring Health, Nanjing Medical University, Nanjing 211166, ChinacDepartment of histology and embryology, School of Medicine, Southeast University, Nanjing 210009, ChinadState Key Laboratory of Reproductive Medicine (Suzhou Centre), The Affiliated Suzhou Hospital of Nanjing Medical University, Suzhou Municipal Hospital, Gusu School, Innovation Center of Suzhou, Nanjing Medical University, Suzhou 215000, China;eDepartment of Obstetrics and Gynecology, Women’s Hospital of Nanjing Medical University, Nanjing Women and Children’s Healthcare Hospital, Nanjing Medical University, Nanjing 210004, ChinafDepartment of Anesthesiology, Surgery and Pain Management and Key Laboratory of Clinical Science and Research, Zhongda Hospital, Southeast University, Nanjing 210009, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523130123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523130123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R">
      <title>Rubisco kinetic acclimation at the holoenzyme level</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceKinetic acclimation enables proteins to adjust their activity in response to environmental perturbations. For the CO2-fixing enzyme Rubisco, kinetic acclimation may be conferred by its small subunits. Plants express multiple small subunits and ...</description>
      <dc:title>Rubisco kinetic acclimation at the holoenzyme level</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519914123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Bryce AskeyMaddie CeminskyElena ScottYongsheng WangZhen Guo OhStavros AzinasArthur LaganowskyLaura Helen GunnaPlant Biology Section, School of Integrated Plant Science, Cornell University, Ithaca, NY 14853bDepartment of Chemistry, Texas A&amp;M University, College Station, TX 77843cDepartment of Molecular Medicine, Cornell University, Ithaca, NY 14853dDepartment of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Solna 171 65, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519914123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536956123?af=R">
      <title>Constrained evolutionary funnels shape viral immune escape</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536956123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceViruses evolve to evade our immune defenses, but with constraints. Like navigating a high-dimensional minefield, each step toward immune escape comes at the potential cost of structural stability and functionality. We show that despite the ...</description>
      <dc:title>Constrained evolutionary funnels shape viral immune escape</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536956123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Marian HuotDianzhuo WangEugene ShakhnovichRémi MonassonSimona CoccoaLaboratory of Physics of the Ecole Normale Supérieure, Department of Physics, CNRS UMR 8023 and Paris Sciences and Lettres Research, Sorbonne Université, Paris 75005, FrancebDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138cJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536956123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536956123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524135123?af=R">
      <title>Sister chromatid separation determines the proliferative properties upon whole-genome duplication via homologous chromosome arrangement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524135123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceWhole-genome duplication (WGD), doubling of cellular content through skipping cell division after DNA synthesis, drives cellular diversification in development, aging, tumorigenesis, or evolution. While various mechanisms of WGD are featured ...</description>
      <dc:title>Sister chromatid separation determines the proliferative properties upon whole-genome duplication via homologous chromosome arrangement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524135123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Masaya InokoGuang YangYuki TsukadaRyota UeharaaDivision of Life Science, Graduate School of Life Science, Hokkaido University, Kita-Ku, Sapporo 001-0021, JapanbDepartment of Biosciences and Informatics, Keio University, Kouhoku-ku, Yokohama 223-8522, JapancFaculty of Advanced Life Science, Hokkaido University, Kita-Ku, Sapporo 001-0021, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524135123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524135123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529161123?af=R">
      <title>In situ and real-time monitoring of intracellular activities in single live cells using a nanopore probe</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529161123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceUnderstanding molecular dynamics within single live cells is essential for elucidating how cellular heterogeneity drives physiology and disease. Yet, existing single-cell methods cannot continuously track multiple biomolecules in situ and in ...</description>
      <dc:title>In situ and real-time monitoring of intracellular activities in single live cells using a nanopore probe</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529161123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Xiaobin HuangZiyi LiYanling HuangKe ZhouLei LiuHai-Chen WuaBeijing National Laboratory for Molecular Sciences, Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, ChinabSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 100049, ChinacLaboratory of Bio-inspired Materials and Interfacial Science, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, ChinadCollege of Food and Bioengineering, Xihua University, Chengdu 610039, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529161123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529161123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534385123?af=R">
      <title>A universal polymer signature in Hi-C resolves cohesin loop density and supports monomeric extrusion</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534385123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceLoop extrusion is believed to dynamically fold meter-long DNA inside a micrometer-sized nucleus, yet the density of these loops has remained unknown. A central obstacle is that Hi-C contact maps encode chromatin structure through a biochemical ...</description>
      <dc:title>A universal polymer signature in Hi-C resolves cohesin loop density and supports monomeric extrusion</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534385123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Kirill PolovnikovDmitry StarkovaAI Center, Skolkovo Institute of Science and Technology, Moscow 121205, Russian FederationbInstitute for Physics &amp; Astronomy, University of Potsdam, Potsdam-Golm 14476, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534385123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534385123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600755123?af=R">
      <title>Comparative analysis of naked mole-rat thermogenesis and its potential to maintain euthermia in response to cold</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600755123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThis study provides critical insights into the thermal biology of naked mole-rats (NMRs), resolving long-standing controversies regarding their thermoregulatory strategies. We highlight the unique adaptations and limitations of NMR physiology ...</description>
      <dc:title>Comparative analysis of naked mole-rat thermogenesis and its potential to maintain euthermia in response to cold</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600755123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Aleksei MikhalchenkoJune K. CorriganYuchen HeZalan PeterfiSun Hee YimSang-Goo LeeZhaoming DengVince G. AmorosoVera GorbunovaAndrei SeluanovThomas J. ParkAlexander S. BanksVadim N. GladyshevaDivision of Genetics, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115bDivision of Endocrinology, Diabetes and Metabolism, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215cDepartment of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607dDepartment of Biology, University of Rochester, Rochester, NY 14627</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600755123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600755123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2504976123?af=R">
      <title>Self-adjuvanting α-helical polypeptide simultaneously delivers neoantigen mRNAs and activates dendritic cells to eradicate tumors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2504976123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceMessenger RNA (mRNA)-based cancer vaccines have long been sought, but are limited by the modest therapeutic efficacy. One central challenge lies in the development of mRNA carriers that not only facilitate the expression of mRNA-encoded tumor ...</description>
      <dc:title>Self-adjuvanting α-helical polypeptide simultaneously delivers neoantigen mRNAs and activates dendritic cells to eradicate tumors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2504976123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Joonsu HanJiadiao ZhouAbhisek DwivedyTianrui XueRimsha BhattaYusheng LiuDaniel NguyenYang BoYueji WangXin WangMeng XuMatthew BerryKeith BaileyJoseph IrudayarajJian LiuQian ChenShuming NieXing WangHua WangaDepartment of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801bDepartment of Bioengineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801cDepartment of Veterinary Clinical Medicine, University of Illinois at Urbana-Champaign, Urbana, IL 61801dAlnylam Pharmaceuticals, Inc., Cambridge, MA 02142eCancer Center at Illinois, Urbana, IL 61801fCarle College of Medicine, University of Illinois at Urbana-Champaign, Urbana, IL 61801gZhejiang University-University of Edinburgh Institute, Zhejiang University School of Medicine, International Campus, Zhejiang University, Haining 314400, ChinahDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801iBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801jMaterials Research Laboratory, University of Illinois at Urbana-Champaign, Urbana, IL 61801kDepartment of Electrical and Computer Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801lInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2504976123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2504976123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2504764123?af=R">
      <title>Uncovering mitochondrial defects in photoreceptors opens therapeutic opportunities for Stargardt disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2504764123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceStargardt disease type 1 (STGD1) is a progressive retinal disorder with no effective treatments. Our research reveals that mitochondrial defects in photoreceptors, driven by OPA1, a crucial regulator of mitochondria, significantly contribute ...</description>
      <dc:title>Uncovering mitochondrial defects in photoreceptors opens therapeutic opportunities for Stargardt disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2504764123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Simona BrillanteMariagrazia VolpeAnna DianaSantiago NegueruelaMarta MolinariRosa SaurinoEva CipollaroElena PolishchukErika TenderiniCarla DamianoPatrizia TornabeneRoman PolishchukGiancarlo ParentiAntonietta TaralloSandro BanfiIvana TrapaniSabrina CarrellaAlessia IndrieriaTelethon Institute of Genetics and Medicine, Pozzuoli 80078, ItalybInstitute for Genetic and Biomedical Research, National Research Council, Milan 20090, ItalycEuropean School of Molecular Medicine, Milan 20122, ItalydDepartment of Translational Medical Sciences, University of Naples Federico II, Naples 80131, ItalyeSantobono-Pausilipon, Laboratori di Ricerca e Biobanca, Naples 80122, ItalyfMedical Genetics, Department of Precision Medicine, University of Campania “Luigi Vanvitelli”, Naples 80138, ItalygDepartment of Advanced Biomedical Sciences, University of Naples Federico II, Naples 80131, ItalyhBiology and Evolution of Marine Organisms Department, Stazione Zoologica Anton Dohrn, Naples 80121, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2504764123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2504764123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531352123?af=R">
      <title>Structure making and breaking in electrolyte solutions explained by water energetics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531352123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceA prevailing dogma categorizes salts as structure-makers or structure-breakers to explain transport properties, but this classification lacks a clear molecular origin. Hydrogen bonds (HBs) are lost in the first hydration shell of ions but ...</description>
      <dc:title>Structure making and breaking in electrolyte solutions explained by water energetics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531352123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Lucia F. SedanoLuis Carlos PardoGustavo MadrigalEva G. NoyaCarlos VegaaDepartamento de Química Física, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid 28040, SpainbGroup of Characterization of Materials, Department of Physics, Engineering School of Barcelona, Universitat Politecnica de Catalunya, Barcelona 08019, SpaincDepartment of Physics and Barcelona Research Center in Multiscale Science and Engineering, Universitat Politecnica de Catalunya, Barcelona 08019, SpaindInstituto de Química Física Blas Cabrera, Consejo Superior de Investigaciones Científicas, Madrid 28006, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531352123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531352123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603301123?af=R">
      <title>PPP1R3G–RIPK1–ZBP1 axis activates early-stage apoptosis and late-stage necroptosis to promote doxorubicin-induced cardiotoxicity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603301123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThis study identifies Protein Phosphatase 1 Regulatory Subunit 3G (PPP1R3G) as a key driver of doxorubicin-induced cardiotoxicity, acting by removing a protective molecular brake on cell death. We define a PPP1R3G–RIPK1–ZBP1 signaling axis ...</description>
      <dc:title>PPP1R3G–RIPK1–ZBP1 axis activates early-stage apoptosis and late-stage necroptosis to promote doxorubicin-induced cardiotoxicity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603301123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Xueling MaKen ChenZhigao WangaCenter for Regenerative Medicine, Heart Institute, Department of Internal Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33602</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603301123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603301123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2509165123?af=R">
      <title>Rhesus macaques with an OPA1 mutation demonstrate features of autosomal dominant optic atrophy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2509165123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceOptic neuropathies due to heritable diseases are a common cause of blindness in humans, but limited therapies currently exist for the vision loss that occurs from them. One such condition is autosomal dominant optic atrophy (ADOA), an ...</description>
      <dc:title>Rhesus macaques with an OPA1 mutation demonstrate features of autosomal dominant optic atrophy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2509165123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Tracy N. JaggersAna Ripolles-GarciaAla MoshiriBrett D. StoryJun WangRui ChenLucy G. MooreLeandro B. C. TeixeiraJaeho ShimAna C. RaposoMaria Isabel CasanovaSophie M. LeSangwan ParkLaura J. YoungSoohyun KimKarolina P. RoszakVanessa UrenoPaige M. KarpinenNayeli EcheverriaMonica ArdonBrian C. LeonardMarguerite KnipeEliza Bliss-MoreauBrad FortuneJ. Timothy StoutJeffrey RogersNicholas Marsh-ArmstrongSara M. ThomasyaDepartment of Surgical and Radiological Sciences, School of Veterinary Medicine, University of California, Davis, Davis, CA 95616bDepartment of Ophthalmology and Vision Science, School of Medicine, University of California, Davis, Sacramento, CA 95817cDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030dHuman Genome Sequencing Center, Baylor College of Medicine, Houston, TX 77030eComparative Ocular Pathology Laboratory of Wisconsin, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI 53706fDepartment of Psychology, California National Primate Research Center, University of California, Davis, Davis, CA 95616gLegacy Devers Eye Institute, Portland, OR 97210hCullen Eye Institute, Baylor College of Medicine, Houston, TX 77030</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2509165123</prism:doi>
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   </item>
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      <title>Initiation of swarming in Bacillus subtilis as a resolution for the sorites paradox in bacteria</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534573123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe sorites paradox shows how tricky it is to define when something changes—like a heap of sand losing grains one by one. Biology has a similar puzzle: When does a single bacterial cell become a swarm? We followed individualBacillus subtilis...</description>
      <dc:title>Initiation of swarming in Bacillus subtilis as a resolution for the sorites paradox in bacteria</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534573123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Ajesh JoseShira Omer BendoriAvigdor EldarDaniel B. KearnsGil ArielAvraham Be’eraThe Albert Katz International School for Desert Studies, The Jacob Blaustein Institutes for Desert Research, Ben-Gurion University of the Negev, Sede Boqer Campus, Midreshet Ben-Gurion 84990, IsraelbThe Shmunis School of Biomedicine and Cancer Research, Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, IsraelcDepartment of Biology, Indiana University, Bloomington, IN 47405dDepartment of Mathematics, Bar-Ilan University, Ramat Gan 52900, IsraeleZuckerberg Institute for Water Research, The Jacob Blaustein Institutes for Desert Research, Midreshet Ben-Gurion 84990, IsraelfDepartment of Physics, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534573123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534573123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524346123?af=R">
      <title>Phase separation induced by active polymerization makes protocells robust against environmental changes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524346123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe discovery of biomolecular condensates within cells suggests the hypothesis that phase separation, in conjunction with spontaneous polymerization processes, could have played a central role for the origin of life. However, such ...</description>
      <dc:title>Phase separation induced by active polymerization makes protocells robust against environmental changes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524346123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Xi ChenJens-Uwe SommerTyler S. HarmonaDivision Theory of Polymers, Leibniz Institute of Polymer Research, Dresden 01069, GermanybCluster of Excellence ‘Physics of Life’, Dresden University of Technology, Dresden 01062, GermanycInstitute for Theoretical Physics, Faculty of Physics, Dresden University of Technology, Dresden 01069, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524346123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524346123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531938123?af=R">
      <title>The role of interfacial excess charge in the reversibility of proton and hydroxide solvation in electrocatalysis and bipolar membranes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531938123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe desolvation and recombination of protons and hydroxides in bulk water is one of the fastest reactions known to mankind. The very existence of an increased activation barrier at heterogenous interfaces reflects a key component of ...</description>
      <dc:title>The role of interfacial excess charge in the reversibility of proton and hydroxide solvation in electrocatalysis and bipolar membranes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531938123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Carlos Gomez RodellarJody DruceJosé Maria Gisbert-GonzálezFrancisco SarabiaBeatriz Roldan CuenyaSebastian Z. OeneraDepartment of Interface Science, Fritz-Haber Institute of the Max Planck Society, Berlin 14195, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531938123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531938123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525757123?af=R">
      <title>Vagal nerve TRPV3 regulates sedative-mediated appeasement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525757123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThis study identifies transient receptor potential vanilloid 3 (TRPV3) in the nodose ganglion as an effective molecular target that regulates cardiopulmonary function and stress-related behaviors. We demonstrate that citronellal and ...</description>
      <dc:title>Vagal nerve TRPV3 regulates sedative-mediated appeasement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525757123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Peiyu WangJinpiao ZhuXuteng LuChang ChenBomin GaoWanjiang TaoKeyu XiaYang SongQiong ShiHongcun GaiPanhao XiaoFeng LiuPeiyuan PangYang LiXiaoyi MoXiao-Dong WangChang XieDongdong LiZongze ZhangJing YaoaState Key Laboratory of Virology and Biosafety, Hubei Provincial Research Center for Basic Biological Sciences, TaiKang Center for Life and Medical Sciences, College of Life Sciences, Hubei Key Laboratory of Cell Homeostasis, Frontier Science Center for Immunology and Metabolism, Department of Psychiatry, Renmin Hospital of Wuhan University, Wuhan University, Wuhan, Hubei 430072, ChinabDepartment of Anesthesiology, Zhongnan Hospital, Wuhan University, Wuhan, Hubei 430072, ChinacSchool of Brain Science and Brain Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310058, ChinadSorbonne Université, CNRS, INSERM, Center for Neuroscience at Sorbonne Université, Paris F-75005, FranceeSorbonne Université, CNRS, INSERM, Institut de Biologie Paris-Seine, Paris F-75005, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525757123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525757123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533391123?af=R">
      <title>Molten iron at extreme conditions reveals compositional inhomogeneity in Earth’s lower outer core</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533391123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceEarth’s magnetic field is sustained by convection in the liquid iron outer core, yet the thermoelastic behavior of molten iron under core conditions remains poorly constrained. By extending high-precision temperature measurements of shock-...</description>
      <dc:title>Molten iron at extreme conditions reveals compositional inhomogeneity in Earth’s lower outer core</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533391123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Bo GanJun LiHeli MaLong HaoZhipeng GaoXiang WuQiang WuYoujun ZhangaInstitute of Atomic and Molecular Physics, Sichuan University, Chengdu 610065, ChinabNational Key Laboratory for Shock Wave and Detonation Physics, Institute of Fluid Physics, China Academy of Engineering Physics, Mianyang 621900, ChinacState Key Laboratory of Geological Processes and Mineral Resources, School of Earth Sciences, China University of Geosciences, Wuhan 430074, ChinadState Key Laboratory of Intelligent Construction and Healthy Operation and Maintenance of Deep Underground Engineering, Sichuan University, Chengdu 610065, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533391123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533391123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604818123?af=R">
      <title>When sexual selection through mate choice depletes versus exaggerates genetic variation: Unraveling the lek paradox</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604818123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe “lek paradox”—the dissonance between a hypothesized loss of variation in sexual display traits due to mate choice, leading to the subsequent cessation of sexual selection, and evidence of high variation in such traits and the persistence ...</description>
      <dc:title>When sexual selection through mate choice depletes versus exaggerates genetic variation: Unraveling the lek paradox</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604818123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Kuangyi XuMaria R. ServedioaDepartment of Ecology and Evolutionary Biology, University of Toronto, Toronto, ON M5S 3B2, CanadabDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604818123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604818123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600386123?af=R">
      <title>Plant pathogenic nematode exosomes remodel vector tracheae to enhance pathogen transmission</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600386123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificancePathogen-driven manipulation of vector physiology represents a fundamental yet understudied survival strategy for optimizing transmission efficiency. This study reveals a sophisticated mechanism whereby the pinewood nematode utilizes exosome-...</description>
      <dc:title>Plant pathogenic nematode exosomes remodel vector tracheae to enhance pathogen transmission</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600386123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Yue ChangJiao ZhouFangyuan YeHongxia ZhangJianghua SunLilin ZhaoaState Key Laboratory of Animal Biodiversity Conservation and Integrated Pest Management, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, ChinabUniversity of Chinese Academy of Sciences, Beijing 100101, ChinacCollege of Life Sciences/Hebei Basic Science Center for Biotic Interactions, Institute of Life Science and Green Development, Hebei University, Baoding 071002, ChinadShanxi Fen River Plain Farmland Shelterbelt Ecosystem National Observation Research Station, Jinzhong 030801, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600386123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600386123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524741123?af=R">
      <title>Temperature controls the episodic dynamics of deep slow slip</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524741123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceEpisodic slow slip at the root of tectonic plate boundaries is a common mechanism by which plate motion is accommodated within the transition between shallow frictional earthquake slip and deep viscous creep. We use swarms of low-frequency ...</description>
      <dc:title>Temperature controls the episodic dynamics of deep slow slip</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524741123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Zaccaria El YousfiBaptiste RoussetMathilde RadiguetWilliam B. FrankaInstitut des Sciences de La Terre (ISTerre), Univ. Grenoble Alpes, Univ. Savoie Mont Blanc, CNRS, Institut de recherche pour le développement, Univ. Gustave Eiffel, Grenoble 38000, FrancebInstitut Terre &amp; Environnement de Strasbourg, Université de Strasbourg, Strasbourg 67084, FrancecDepartment of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524741123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524741123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535716123?af=R">
      <title>Mecp2 deficiency induces dysphagia in a preclinical model of Rett syndrome</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535716123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceDifficulty swallowing (dysphagia) arises from dysfunction of swallow muscles and/or impaired coordination with breathing, increasing the risk of aspiration pneumonia, one of the top three causes of mortality among individuals with Rett ...</description>
      <dc:title>Mecp2 deficiency induces dysphagia in a preclinical model of Rett syndrome</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535716123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Luiz Marcelo OliveiraMaryam Saeed AslamJan-Marino RamirezAlyssa D. HuffaNorcliffe Foundation Center for Integrative Brain Research, Seattle Children’s Research Institute, Seattle, WA 98101bDepartment of Neurological Surgery, University of Washington School of Medicine, Seattle, WA 98108cDepartment of Anesthesiology and Critical Care Medicine, The George Washington University, Washington, DC 20052</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535716123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535716123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528910123?af=R">
      <title>The identification of potent nonopioid analgesics and their potential for perioperative use</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528910123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceSodium channel has been considered as one of the most promising nonopioid analgesic targets in both academic and industrial worlds to address the opioid-related crisis. The prevailing strategy is to develop subtype-specific sodium channel ...</description>
      <dc:title>The identification of potent nonopioid analgesics and their potential for perioperative use</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528910123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Chaoyi DengYu DengXudong LuoJunyu LuChenyang LiPeiwen GaoXiaoyu XieBingbing XiangSicheng LiuXingxing LiuXiaoxiao LiPan ChangXia WuGuoyan ZhaoDeying GongJing WangCheng ZhouJin LiuTao ZhuFengming LuoWensheng ZhangaDepartment of Anesthesiology, West China Hospital, Sichuan University, Chengdu 610041, ChinabLaboratory of Anesthesia and Critical Care Medicine, National-Local Joint Engineering Research Centre of Translational Medicine of Anesthesiology, West China Hospital, Sichuan University, Chengdu 610041, ChinacDepartment of Pharmacy, West China Hospital, Sichuan University, Chengdu 610041, ChinadDepartment of Pharmacy, West China Tianfu Hospital, Sichuan University, Chengdu 610213, ChinaeDepartment of Anesthesiology, Affiliated Hospital of Zunyi Medical University, Zunyi 563000, ChinafDepartment of Respiratory and Critical Care Medicine, West China Hospital, Sichuan University, Chengdu 610041, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528910123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528910123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518776123?af=R">
      <title>Eye of the beholder: Pupillary response reflects how subjective prior beliefs shape reinforcement learning with fake news</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518776123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceIn an age where misinformation spreads rapidly and online environments favor belief-consistent information, understanding how people learn from and act upon misleading content is a scientific and societal priority. This study integrates fake ...</description>
      <dc:title>Eye of the beholder: Pupillary response reflects how subjective prior beliefs shape reinforcement learning with fake news</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518776123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-16T07:00:00Z</dc:date>
      <dc:creator>Silvana LozitoValentina PigaSara Lo PrestiAngelica ScuderiFabrizio DoricchiMassimo SilvettiStefano LasaponaraaDepartment of Psychology, “Sapienza” University of Rome, Rome 00185, ItalybPhD Programme in Behavioural Neuroscience, Department of Psychology, “Sapienza” University of Rome, Rome 00185, ItalycIRCCS Fondazione Santa Lucia, Rome 00179, ItalydComputational and Translational Neuroscience Lab, Institute of Cognitive Sciences and Technologies, National Research Council, Rome 00196, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518776123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518776123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2508144123?af=R">
      <title>Sparse identification of nonlinear dynamics and Koopman operators with Shallow Recurrent Decoder Networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2508144123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceWe present sparse identification of nonlinear dynamics with shallow recurrent decoders (SINDy-SHRED), which jointly solves the sensing, model reduction and model identification problem with simple implementation, efficient computation, and ...</description>
      <dc:title>Sparse identification of nonlinear dynamics and Koopman operators with Shallow Recurrent Decoder Networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2508144123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-17T07:00:00Z</dc:date>
      <dc:creator>Mars Liyao GaoJan P. WilliamsJ. Nathan KutzaPaul G. Allen School of Computer Science &amp; Engineering, University of Washington, Seattle, WA 98195bDepartment of Mechanical Engineering, University of Washington, Seattle, WA 98195cDepartment of Applied Mathematics, University of Washington, Seattle, WA 98195dDepartment of Electrical and Computer Engineering, University of Washington, Seattle, WA 98195</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2508144123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2412919123?af=R">
      <title>Type I interferons induced upon respiratory viral infection impair lung metastatic initiation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2412919123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe lungs are a metastatic site for cancers such as breast cancer. In addition, the lungs are constantly exposed to viruses, such as coronavirus, respiratory syncytial virus (RSV), and influenza virus. Thus, breast cancer and respiratory virus ...</description>
      <dc:title>Type I interferons induced upon respiratory viral infection impair lung metastatic initiation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2412919123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-17T07:00:00Z</dc:date>
      <dc:creator>Ana FariasVictoria L. BridgemanFelipe S. RodriguesFranz PutturAmber OwenStefanie RuhlandRute M. M. FerreiraMatthias MackIlaria MalanchiCecilia JohanssonaRespiratory Infections Section, National Heart and Lung Institute, Imperial College London, London W12 0NN, United KingdombTumor-Host Interaction Laboratory, The Francis Crick Institute, London NW1 1AT, United KingdomcInflammation Repair and Development, National Heart and Lung Institute, Imperial College London, London W12 0NN, United KingdomdDepartment of Nephrology, University Hospital Regensburg, Regensburg 93053, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2412919123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2412919123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2500343123?af=R">
      <title>The institutional dynamics of inequality for women inventors who break with conventional thinking</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2500343123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceThe gender innovation gap—where women’s inventions are less likely to be patented or pursued—raises concerns about its potential to slow scientific progress. Our analysis of millions of patent applications reveals that the gender gap in ...</description>
      <dc:title>The institutional dynamics of inequality for women inventors who break with conventional thinking</dc:title>
      <dc:identifier>doi:10.1073/pnas.2500343123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-17T07:00:00Z</dc:date>
      <dc:creator>Tara SowrirajanRyan WhalenBrian UzziaKellogg School of Management, Northwestern University, Evanston, IL 60208bNorthwestern Institute on Complex Systems, Northwestern University, Evanston, IL 60208cFaculty of Law, University of Hong Kong, Hong Kong Special Administrative RegiondRyan Institute of Complexity, Kellogg School of Management, Northwestern University, Evanston, IL 60208</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2500343123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2500343123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537014123?af=R">
      <title>Making invisible excited-state structures of pro-interleukin-18 visible by combining NMR and machine learning</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537014123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceIn many cases accurate models of the low energy, most populated form of a protein’s three-dimensional structure can be rapidly determined using machine learning (ML) programs, such as AlphaFold. However, biomolecular function is often ...</description>
      <dc:title>Making invisible excited-state structures of pro-interleukin-18 visible by combining NMR and machine learning</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537014123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-17T07:00:00Z</dc:date>
      <dc:creator>Jeffrey P. BoninJin Sub LeeZi Hao LiuPhilip M. KimLewis E. KayaDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, CanadabDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, CanadacDepartment of Chemistry, University of Toronto, Toronto, ON M5S 3H6, CanadadDonnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON M5S 3E1, CanadaeProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON M5G 0A4, CanadafDepartment of Computer Science, University of Toronto, Toronto, ON M5S 3E1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537014123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537014123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537999123?af=R">
      <title>Extensive heterozygosity and genetic exchange among natural populations of Leishmania species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537999123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceHybridization is increasingly recognized as a powerful evolutionary force, yet the extent to which it impacts the population genetics ofLeishmaniaremains enigmatic. Previous work suggested thatLeishmaniapropagation is predominantly by ...</description>
      <dc:title>Extensive heterozygosity and genetic exchange among natural populations of Leishmania species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537999123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-17T07:00:00Z</dc:date>
      <dc:creator>Eliza V. C. Alves-FerreiraMourad BarhoumiTiago R. FerreiraMatthew W. BrownPetr VolfYusr Saadi-BenAounImmen KhammariIhcen KherachiAkila Fathallah MiliZoubir HarratIkram GuizaniDavid L. SacksJulius LukešMichael E. GriggaMolecular Parasitology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892bLaboratory of Molecular Epidemiology and Experimental Pathology, Institut Pasteur de Tunis, and University of Tunis El Manar, Tunis 1002, TunisiacIntracellular Parasite Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892dDepartment of Biological Sciences, Mississippi State University, Starkville, MS 39762eDepartment of Parasitology, Faculty of Sciences, Charles University, Prague 12800, CzechiafDepartment of Parasitology, Faculty of Medicine, University of Sousse, Sousse 4000, TunisiagInstitut Pasteur d’Algérie, Algiers 16047, AlgeriahInstitute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice 37005, CzechiaiFaculty of Science, University of South Bohemia, České Budějovice 37005, Czechia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537999123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537999123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532091123?af=R">
      <title>Cellular remodeling of ovarian follicular epithelial cells transmits an obligate nutritional endosymbiont in a scale insect</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532091123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceMany insects have evolved specialized mechanisms for vertical transmission of their microbial symbionts. Here, we report that the scale insectInsignorthezia insignisshows unique exaptation of the oocyte’s follicular cells into tubular ...</description>
      <dc:title>Cellular remodeling of ovarian follicular epithelial cells transmits an obligate nutritional endosymbiont in a scale insect</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532091123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Ojaswini Sourajyoti PalAranya DhibarKailash ChandraAnnapoorni RangarajanShantanu P. ShuklaaDepartment of Developmental Biology and Genetics, Indian Institute of Science, Bengaluru 560012, India</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532091123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532091123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536005123?af=R">
      <title>Municipal water fluoridation, adolescent IQ, and cognition across the life course: Evidence from the Wisconsin Longitudinal Study</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536005123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;We investigate associations between community water fluoridation (CWF), adolescent IQ, and cognition across the life course using representative data from the US state of Wisconsin. Exposure is inferred from historical records on community water ...</description>
      <dc:title>Municipal water fluoridation, adolescent IQ, and cognition across the life course: Evidence from the Wisconsin Longitudinal Study</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536005123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>John Robert WarrenGina RumoreKamil SicinskiPamela HerdMichal EngelmanaInstitute for Social Research and Data Innovation, University of Minnesota, Minneapolis, MN 55455bCenter for Demography of Health and Aging, University of Wisconsin, Madison, WI 53706cGerald Ford School of Public Policy, 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>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536005123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536005123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605026123?af=R">
      <title>A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605026123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605026123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Mengqi XuE. Michael OstapaDepartment of Physiology, Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104bCenter for Engineering Mechanobiology, University of Pennsylvania, Philadelphia, PA 19104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605026123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605026123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605415123?af=R">
      <title>Cooperative traits maintain bacterial niche breadth</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605415123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Cooperative traits maintain bacterial niche breadth</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605415123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Shryli K. ShreekarChristian KostaDivision of Ecology, School of Biology/Chemistry, Osnabrück University, Osnabrück 49076, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605415123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605415123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602950123?af=R">
      <title>The hourglass of high acuity vision: Cone plasticity at the intersection of time and space shapes the foveola</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602950123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>The hourglass of high acuity vision: Cone plasticity at the intersection of time and space shapes the foveola</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602950123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Michael HoussetMichel CayouetteaCellular Neurobiology Research Unit, Montreal Clinical Research Institute, Montreal, QC H2W 1R7, CanadabDepartment of Medicine, Université de Montréal, Montreal, QC H3T 1J4, CanadacDepartment of Anatomy and Cell Biology, McGill University, Montreal, QC H3A 0C7, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602950123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602950123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605414123?af=R">
      <title>Combining process-based models with machine learning ensemble improves soil nitrous oxide estimates</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605414123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Combining process-based models with machine learning ensemble improves soil nitrous oxide estimates</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605414123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Stephen Del GrossoStephen OgleaNatural Resource Ecology Laboratory, Colorado State University, Fort Collins, CO 80523</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605414123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605414123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R">
      <title>The next frontier: Exploring plant hypoxia sensing and response mechanisms through synthetic biology</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>The next frontier: Exploring plant hypoxia sensing and response mechanisms through synthetic biology</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606254123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Emmanuelle GracietaBiology Department, Maynooth University, Maynooth Co. Kildare W23 XY3X, Ireland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606254123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605166123?af=R">
      <title>Electrostatic interactions constrain generalization of porous-media models for intracellular diffusion in mammalian cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605166123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Electrostatic interactions constrain generalization of porous-media models for intracellular diffusion in mammalian cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605166123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Debabrata DeyGideon SchreiberaAmity Institute of Click Chemistry Research and Studies, Amity University, Noida, Uttar Pradesh 201313, IndiabDepartment of Biomolecular Sciences, 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>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605166123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605166123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605698123?af=R">
      <title>Polygyny’s marriage squeeze is real but temporary</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605698123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Polygyny’s marriage squeeze is real but temporary</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605698123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Jingyuan DengaDepartment of Economics, University of Oxford, Oxford OX1 3UQ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605698123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605698123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610805123?af=R">
      <title>Correction for Brodsky and Farge, How earthquakes organize stress</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610805123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Brodsky and Farge, How earthquakes organize stress</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610805123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Deng: Polygyny’s marriage squeeze has little power to explain violence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607580123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Hampton GaddyRebecca SearLaura FortunatoaDepartment of Economic History, London School of Economics, London WC2A 3LZ, United KingdombLeverhulme Centre for Demographic Science, University of Oxford, Oxford OX1 1JD, United KingdomcCentre for Culture and Evolution, Brunel University, London UB8 3PH, United KingdomdInstitute of Human Sciences, University of Oxford, Oxford OX2 6QS, United KingdomeSanta Fe Institute, Santa Fe, NM 87501</dc:creator>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Dey and Schreiber: Porous media framework of intracellular diffusion is not limited to inert molecules</dc:title>
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      <dc:date>2026-04-10T07:00:00Z</dc:date>
      <dc:creator>Olivier DestrianRené-Marc MègeBenoît LadouxBenoît GoyeauMorgan ChabanonaUniversité Paris-Saclay, CNRS, CentraleSupélec, Laboratoire d’Energétique Moleculaire et Macroscopique, Combustion (EM2C), Gif-sur-Yvette 91190, FrancebUniversité Paris-Cité, CNRS, Institut Jacques Monod, Paris 75013, FrancecDepartment of Physics, Friedrich-Alexander Universität Erlangen-Nürnberg, Erlangen 91058, GermanydMax-Planck-Zentrum für Physik und Medizin and Max Planck Institute for the Science of Light, Erlangen 91054, Germany</dc:creator>
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