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      <title>Proceedings of the National Academy of Sciences</title>
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      <title>In This Issue</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
      <dc:identifier>doi:10.1073/iti3726123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <title>One mechanism, two diseases: Involvement of enzyme–substrate complexes in the pathogenesis of celiac disease and rheumatoid arthritis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600933123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;Celiac disease (CeD) and rheumatoid arthritis (RA) share several key features. In both diseases HLA class II allotypes are the major genetic determinants, in both diseases there are antibodies to posttranslationally modified peptides (i.e., deamidated ...</description>
      <dc:title>One mechanism, two diseases: Involvement of enzyme–substrate complexes in the pathogenesis of celiac disease and rheumatoid arthritis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600933123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-04T07:00:00Z</dc:date>
      <dc:creator>Ludvig M. Sollidahttps://ror.org/01xtthb56KG Jebsen Center for Specific Autoimmune Therapy and Norwegian Coeliac Disease Research Centre, Institute of Clinical Medicine, University of Oslo, Oslo N-0372, Norwaybhttps://ror.org/00j9c2840Department of Immunology, Oslo University Hospital-Rikshospitalet, Oslo N-0372, Norway</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
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      <title>Heritability and social interaction in labor market outcomes: Evidence from the population of twins in the United States</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620927123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceWhy do families matter so much for the labor market success of their children? One explanation is shared hereditary factors; another is family resources and family-related preferences. We use data for twins to measure the share of the ...</description>
      <dc:title>Heritability and social interaction in labor market outcomes: Evidence from the population of twins in the United States</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620927123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>David CardJesse RothsteinMoises Yiahttps://ror.org/01an7q238Department of Economics, University of California, Berkeley, CA 94720-3880bhttps://ror.org/01qn7cs15Center for Economic Studies, US Census Bureau, Suitland, MD 20746</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614496123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;Many groundbreaking works in art and science owe their origins to the creative spark ignited by reimagination—the process whereby artists and scientists reinterpret and reframe past and existing knowledge, envisioning it in a new context that reveals new ...</description>
      <dc:title>Reimagination in art and science: Seeing the familiar in a new light and creating new things that didn’t exist before</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614496123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Joseph L. Goldsteinahttps://ror.org/05fcw6535Chair, Lasker Awards Jury, Lasker Foundation, New York City, NY 10174bhttps://ror.org/05byvp690Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9046</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <prism:doi>10.1073/pnas.2614496123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622460123?af=R">
      <title>Lasker~Bloomberg Public Service Award to Michael J. Fox: The challenge of Parkinson’s disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622460123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;This year’s Lasker~Bloomberg Public Service Award honors the singular achievement of Michael J. Fox, who has devoted much of his life to a philanthropic effort to conquer Parkinson’s Disease (PD), a progressive neurodegenerative disorder that afflicts ...</description>
      <dc:title>Lasker~Bloomberg Public Service Award to Michael J. Fox: The challenge of Parkinson’s disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622460123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Randy Schekmanahttps://ror.org/01an7q238HHMI, University of California Berkeley, Berkeley, CA 94720bhttps://ror.org/01an7q238Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2622460123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622459123?af=R">
      <title>Discovery and development of a bispecific antibody for the treatment of hemophilia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622459123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;The 2026 Lasker~DeBakey Clinical Medical Research Award has been awarded to Kunihiro Hattori, Takehisa Kitazawa, and Tomoyuki Igawa (Chugai Pharmaceuticals, Tokyo, Japan) for invention of a bispecific antibody that joins blood clotting Factors IXa (FIXa) ...</description>
      <dc:title>Discovery and development of a bispecific antibody for the treatment of hemophilia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622459123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>William PaoaRevelio Therapeutics Inc, New York, NY 10016</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <title>To sleep and dream: Unraveling narcolepsy</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;In an extraordinary convergence, Emmanuel Mignot and Masashi Yanagisawa employed two entirely different approaches to establish the pathogenesis of narcolepsy, a devastating sleep disorder associated with overwhelming sleep attacks, cataplexy, episodes ...</description>
      <dc:title>To sleep and dream: Unraveling narcolepsy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622458123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Jeffrey M. Friedmanahttps://ror.org/0420db125HHMI at Rockefeller University, New York, NY 10065</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622458123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621115123?af=R">
      <title>End-functionalized ions promote stability of highly frustrated phases in diblock copolymers</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621115123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceBlock copolymers spontaneously assemble into ordered nanostructures with tunable geometry, but topologically complex “frustrated” phases are largely inaccessible in conventional neutral systems. We show that ionic interactions localized at ...</description>
      <dc:title>End-functionalized ions promote stability of highly frustrated phases in diblock copolymers</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621115123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Chao DuanZhen-Gang Wangahttps://ror.org/05dxps055Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2621115123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603289123?af=R">
      <title>The “synthetic validity” problem in AI-generated science</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603289123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>The “synthetic validity” problem in AI-generated science</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603289123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Jacob D. TeenyAndrew LuttrellDongchan LeeaMarketing Department, Kellogg School of Management, Northwestern University, Evanston, IL 60208bhttps://ror.org/00k6tx165Psychology Department, Ball State University, Muncie, IN 47306</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603289123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536563123?af=R">
      <title>Temporally structured motor and auditory representations in covert syllable production</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536563123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSpeaking silently in one’s mind is a pervasive feature of human cognition, yet its neural basis remains unclear. Using magnetoencephalography, we show that covert syllable production unfolds through a coordinated sequence of motor and auditory ...</description>
      <dc:title>Temporally structured motor and auditory representations in covert syllable production</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536563123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-31T07:00:00Z</dc:date>
      <dc:creator>Joan OrpellaFrancesco MantegnaChantal OderbolzM. Florencia AssaneoDavid Poeppelahttps://ror.org/00hjz7x27Department of Neuroscience, Georgetown University Medical Center, Washington, DC 20057bhttps://ror.org/0190ak572Department of Psychology, New York University, New York, NY 10003chttps://ror.org/052gg0110Department of Engineering Science, Oxford University, Oxford OX1 3PJ, Oxfordshire, United Kingdomdhttps://ror.org/01tmp8f25Institute of Neurobiology, National Autonomous University of Mexico, Juriquilla 76230, Querétaro, Mexicoehttps://ror.org/0190ak572Center for Language, Music and Emotion, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536563123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604868123?af=R">
      <title>A three-decade-long analysis shows rising threatened species and responsibility gaps in global supply chains</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604868123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceBiodiversity threats driven by global supply chains are escalating across space and time, resulting in higher extinction rates of species. Yet the causal links between species-specific threats and both local and telecoupled human activities ...</description>
      <dc:title>A three-decade-long analysis shows rising threatened species and responsibility gaps in global supply chains</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604868123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-31T07:00:00Z</dc:date>
      <dc:creator>Ling ZhangQuanliang YeAli KharraziQingxu HuangJiansheng WuBrian FathaKey Laboratory for Urban Habitat Environmental Science and Technology, School of Urban Planning and Design, Peking University, Shenzhen 518055, Chinabhttps://ror.org/02v51f717Urban and Environmental Sciences, Laboratory for Earth Surface Processes, Ministry of Education, Peking University, Beijing 100871, Chinachttps://ror.org/02wfhk785International Institute for Applied Systems Analysis, Laxenburg 2361, Austriadhttps://ror.org/012tb2g32School of Public Administration, College of Management and Economics, Tianjin University, Tianjin 300072, Chinaehttps://ror.org/022k4wk35State Key Laboratory of Earth Surface Processes and Disaster Risk Reduction, Beijing Normal University, Beijing 100875, Chinafhttps://ror.org/022k4wk35School of Natural Resources, Faculty of Geographical Science, Beijing Normal University, Beijing 100875, Chinaghttps://ror.org/044w7a341Department of Biological Sciences, Towson University, Towson, MD 21252</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604868123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604868123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611373123?af=R">
      <title>Evidence for endemism and local adaptation in Antarctic soil bacteria</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611373123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceAntarctic soils are among the most extreme environments on Earth, yet they host diverse microbial communities whose adaptations are poorly understood. To test whether Antarctic microbes are distinct from those found elsewhere, we examined...</description>
      <dc:title>Evidence for endemism and local adaptation in Antarctic soil bacteria</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611373123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-31T07:00:00Z</dc:date>
      <dc:creator>Nicholas B. DragoneMary K. ChildressNoah MendezJordan GallettaCaihong VanderburghClifton P. Bueno de MesquitaKristen M. DeAngelisC. Alisha QuandtPok Man LeungChris GreeningByron J. AdamsNoah Fiererahttps://ror.org/02ttsq026Cooperative Institute for Research in Environmental Sciences, University of Colorado, Boulder, CO 80309bhttps://ror.org/02ttsq026Department of Ecology and Evolutionary Biology, University of Colorado Boulder, Boulder, CO 80309chttps://ror.org/0072zz521Department of Microbiology, University of Massachusetts Amherst, Amherst, MA 01003dhttps://ror.org/02bfwt286Department of Microbiology, Biomedicine Discovery Institute, Monash University, Melbourne, VIC 3800, Australiaehttps://ror.org/02bfwt286Securing Antarctica’s Environmental Future, Monash University, Melbourne, VIC 3800, Australiafhttps://ror.org/047rhhm47Department of Biology, Evolutionary Ecology Laboratories, and Monte L. Bean Museum, Brigham Young University, Provo, UT 84602</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611373123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611373123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621054123?af=R">
      <title>The genomic origins and evolutionary path to a key innovation in the world’s most venomous snakes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621054123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThis study investigates how an entirely new blood-clotting venom type evolved during the recent radiation of Australia’s iconic venomous snakes. We traced the key genetic events that occurred on the evolutionary path to one of the world’s most ...</description>
      <dc:title>The genomic origins and evolutionary path to a key innovation in the world’s most venomous snakes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621054123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-04T07:00:00Z</dc:date>
      <dc:creator>Jory van ThielNoah L. DowellCara F. SmithElda E. SanchezSean B. Carrollahttps://ror.org/047s2c258HHMI, University of Maryland, College Park, MD 20742bhttps://ror.org/047s2c258Department of Biology, University of Maryland, College Park, MD 20742chttps://ror.org/03svjbs84Centre for Snakebite Research and Interventions, Department of Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool L35QA, United KingdomdNational Natural Toxins Research Center, Texas Agricultural and Mechanical University-Kingsville, Kingsville, TX 78363eDepartment of Chemistry, Texas Agricultural and Mechanical University-Kingsville, Kingsville, TX 78363</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621054123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621054123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618039123?af=R">
      <title>Peptides adopt stable omega-loop structures in concentrated sulfuric acid</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618039123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceConcentrated sulfuric acid is widely regarded as destructive to Earth-like biochemistry. Recent studies, however, show that an increasing number of biomolecules, including nucleic acid bases, amino acids, and lipids, remain stable in this ...</description>
      <dc:title>Peptides adopt stable omega-loop structures in concentrated sulfuric acid</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618039123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-04T07:00:00Z</dc:date>
      <dc:creator>Jia Yi ZhangAurelio J. DregniJanusz J. PetkowskiSara SeagerMei Hongahttps://ror.org/042nb2s44Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/008fyn775Faculty of Environmental Engineering, Wroclaw University of Science and Technology, Wroclaw 50-370, PolandcJJ Scientific, Warsaw, Mazowieckie 02-792, Polanddhttps://ror.org/042nb2s44Department of Earth, Atmospheric and Planetary Sciences, Massachusetts Institute of Technology Cambridge, MA 02139ehttps://ror.org/042nb2s44Department of Physics, Massachusetts Institute of Technology, Cambridge, MA 02139fhttps://ror.org/042nb2s44Department of Aeronautics and Astronautics, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618039123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618039123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521821123?af=R">
      <title>Myosin II–independent contraction of actin filaments in membrane nanotubes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521821123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceForce generation by actin filaments is a fundamental property of Eukaryotic cells. These filaments can generate pushing forces via polymerization, pulling forces via the action of molecular motor proteins, and can generate filament sliding ...</description>
      <dc:title>Myosin II–independent contraction of actin filaments in membrane nanotubes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521821123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Md Arsalan AshrafTapas SinghaSusav PradhanSerene Rose DavidPierre SensPramod Pullarkatahttps://ror.org/01qdav448Raman Research Institute, Bengaluru 560080, Indiabhttps://ror.org/04t0gwh46Institut Curie, Paris Science and Letters Research University, CNRS UMR 168, Paris F-75005, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521821123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521821123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536532123?af=R">
      <title>Transthyretin can denature by an alternative pathway</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536532123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceIt is surprising that transthyretin (TTR) has an aggregation pathway leading to organ system deterioration in humans, because it denatures very slowly in circulation at physiological pH, and denaturation is required for aggregation. A ...</description>
      <dc:title>Transthyretin can denature by an alternative pathway</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536532123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Marcus JägerJan-Hannes SchäferGabriel C. LanderEvan T. PowersMartin GruebeleJeffery W. Kellyahttps://ror.org/02dxx6824Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037bhttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037chttps://ror.org/047426m28Department of Chemistry, University of Illinois Urbana-Champaign, Champaign, IL 61801dhttps://ror.org/047426m28Department of Physics, University of Illinois Urbana-Champaign, Champaign, IL 61801ehttps://ror.org/047426m28Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Champaign, IL 61801fhttps://ror.org/047426m28Carle-Illinois College of Medicine, University of Illinois Urbana-Champaign, Champaign, IL 61801</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536532123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619143123?af=R">
      <title>Cell-type-specific circadian and light-responsive transcriptional dynamics in adult Drosophila neurons</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619143123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThis current single-nuclei RNA sequencing study (snRNA-seq) uses theDrosophilaGenetic Reference Panel (DGRP) multiplexing strategy, which profiles together multiple time points and eliminates troublesome batch effects. It also introduces EL-...</description>
      <dc:title>Cell-type-specific circadian and light-responsive transcriptional dynamics in adult Drosophila neurons</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619143123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Gillian BerglundPranav OjhaMaria IvanovaMelina Pérez TorresMichael Rosbashahttps://ror.org/05abbep66HHMI, Brandeis University, Waltham, MA 02454bhttps://ror.org/05abbep66Department of Biology, Brandeis University, Waltham, MA 02454</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619143123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615890123?af=R">
      <title>A host-encoded prophage targets a Candidate Phyla Radiation bacterium and shapes episymbiotic interactions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615890123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceCandidate Phyla Radiation (CPR) bacteria constitute a major fraction of microbial diversity, yet their interactions with bacteriophages (phages) have remained largely speculative due to a lack of experimentally tractable systems. Using the ...</description>
      <dc:title>A host-encoded prophage targets a Candidate Phyla Radiation bacterium and shapes episymbiotic interactions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615890123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Ajay KumarNusrat NaharDeepak ChouhanJeffrey S. McLeanBatbileg BorPu-Ting DongXuesong Heahttps://ror.org/00cb9nn43Department of Microbiology, American Dental Association Forsyth Institute, Somerville, MA 02143bhttps://ror.org/00cvxb145Department of Periodontics, University of Washington, Seattle, WA 98195chttps://ror.org/00cvxb145Department of Oral Health Sciences, University of Washington, Seattle, WA 98195dhttps://ror.org/00cvxb145Department of Microbiology, University of Washington, Seattle, WA 98195ehttps://ror.org/05qghxh33Department of Biomedical Engineering, Stony Brook University, Stony Brook, NY 11794fhttps://ror.org/05qghxh33Department of Microbiology and Immunology, Stony Brook University, Stony Brook, NY 11794</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615890123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615890123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620995123?af=R">
      <title>A structure–function neuronal network model of the rat nervous system</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620995123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceA systems science approach clarified the basic architecture of the neuronal network of the rat nervous system, revealing a projected 81,582 axonal connections between 924 region nodes, equating to a connection density of 9.6%. Cluster analysis ...</description>
      <dc:title>A structure–function neuronal network model of the rat nervous system</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620995123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Larry W. SwansonJoel D. HahnOlaf Spornsahttps://ror.org/03taz7m60Department of Neurobiology, University of Southern California, Los Angeles, CA 90089bDepartment of Psychological and Brain Sciences, Indiana University, Bloomington, IN 47405</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620995123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620995123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619771123?af=R">
      <title>Decoupling proton reactivity from Zn2+ interfacial electrochemistry through solvent isotope substitution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619771123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceTo meet the global energy demand, new chemistries are required to access grid-level energy storage devices. Aqueous metal batteries, including those made of zinc, are rising as promising candidates owing to their intrinsic safety, high ...</description>
      <dc:title>Decoupling proton reactivity from Zn2+ interfacial electrochemistry through solvent isotope substitution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619771123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Taizhe LiuMd. Arif FaisalAshutosh RanaAshutosh BhadouriaJames H. NguyenSaptarshi PaulBrian M. TackettJeffrey E. Dickahttps://ror.org/02dqehb95Department of Chemistry, Purdue University, West Lafayette, IN 47907bhttps://ror.org/02dqehb95Davidson School of Chemical Engineering, Purdue University, West Lafayette, IN 47907chttps://ror.org/02dqehb95Elmore Family School of Electrical and Computer Engineering, Purdue University, West Lafayette, IN 47907</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619771123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619771123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613091123?af=R">
      <title>Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613091123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceAntibody discovery typically operates on the “same epitope, same function” paradigm. However, for dynamic proteins like immunoglobulin E (IgE), the primary mediator of allergic disease, this approach is overly simplistic. By characterizing ...</description>
      <dc:title>Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613091123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Anna M. DaviesNyssa DrinkwaterAndrew J. BeavilVictoria O’DowdDaniel LightwoodTom CeskaAlistair J. HenryBrian J. SuttonJames M. McDonnellahttps://ror.org/0220mzb33Randall Centre for Cell and Molecular Biophysics, King’s College London, New Hunt’s House, London SE1 1UL, United KingdombUCB, Slough SL1 3WE, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613091123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613091123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616799123?af=R">
      <title>Fibronectin inhibition restores myelination in endothelial TNFR2–dependent nonremitting experimental autoimmune encephalomyelitis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616799123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceIn multiple sclerosis (MS), spontaneous remyelination occurs early in disease, but becomes inefficient over time leading to neurodegeneration and clinical decline. Global TNFR2 deletion in experimental autoimmune encephalomyelitis, the mouse ...</description>
      <dc:title>Fibronectin inhibition restores myelination in endothelial TNFR2–dependent nonremitting experimental autoimmune encephalomyelitis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616799123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Aikaterini NanouKonstantinos Apostolou-KarampelisVasiliki TriantafyllidouMaria SakkouFani RoumeliotiMaria C. DenisGeorge KolliasaInstitute for Bioinnovation, Biomedical Sciences Research Center “Alexander Fleming”, Athens 16672, Greecebhttps://ror.org/04gnjpq42Center of New Biotechnologies and Precision Medicine, School of Medicine, National and Kapodistrian University of Athens, Athens 11527, Greecechttps://ror.org/04gnjpq42Department of Physiology, Medical School, National and Kapodistrian University of Athens, Athens 11527, Greece</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616799123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616799123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608675123?af=R">
      <title>Sexual selection purges mutation load, but not overall genetic diversity, decreasing vulnerability to extinction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608675123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceA long standing prediction is that sexual selection can improve population health by biasing reproduction away from individuals with high deleterious mutation load. However, direct genomic evidence is scarce, and the indirect data available ...</description>
      <dc:title>Sexual selection purges mutation load, but not overall genetic diversity, decreasing vulnerability to extinction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608675123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Michael D. PointerWill J. NashMatthew J. G. GageTracey ChapmanAlexei A. MaklakovDavid S. Richardsonahttps://ror.org/026k5mg93Department of Biological Sciences, Department of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, United Kingdombhttps://ror.org/0062dz060Earlham Institute, Norwich Research Park, Norwich NR4 7UZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608675123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608675123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614163123?af=R">
      <title>Increased receptor binding and spike glycosylation, remodeled immune escape of surging SARS-CoV-2 subvariant BA.3.2.2/RE.2.2/Cicada</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614163123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSARS-CoV-2 evolved into distinct phylogenetic clades, generating a series of mutant strains. Notably, variants such as BA.1, BA.2.86, and BA.3.2 deserve special attention as they emerged abruptly at high detection frequencies during specific ...</description>
      <dc:title>Increased receptor binding and spike glycosylation, remodeled immune escape of surging SARS-CoV-2 subvariant BA.3.2.2/RE.2.2/Cicada</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614163123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Linjie LiLinh NguyenHao QuQile WuPengyue GaoDedong LiXinyu LiXueyuan LiuQiuyao JiangKefang LiuCatherine C. L. WongGeorge Fu GaoaChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, Chinabhttps://ror.org/05qbk4x57College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100049, Chinachttps://ror.org/04c4dkn09Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, Chinadhttps://ror.org/03xpwj629School of Life Sciences, Liaoning University, Shenyang 110036, ChinaeSchool of Public Health, Cheeloo College of Medicine, Shandong University, Jinan 250012, Chinafhttps://ror.org/05jb9pq57Medical Science and Technology Innovation Center, Shandong First Medical University and Shandong Academy of Medical Sciences, Jinan 250000, ChinagXYnZ Biologics Co. Ltd., Beijing 100176, ChinahBeijing Life Science Academy, Beijing 102206, Chinaihttps://ror.org/02drdmm93State Key Laboratory of Complex, Severe and Rare Diseases Peking Union Medical College Hospital Chinese Academy of Medical Sciences, Beijing 100730, Chinajhttps://ror.org/03cve4549Tsinghua-Peking Center for Life Sciences, School of Medicine, Tsinghua University, Beijing 100084, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614163123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614163123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617633123?af=R">
      <title>Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617633123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe translation of mRNAs into protein relies on tRNAs to deliver amino acids to ribosomes that incorporate these building blocks into the growing polypeptide chain. By monitoring ribosomes as they progress from one codon to the next, we ...</description>
      <dc:title>Ribosome stalling position, spacing, and A-site occupancy impact translation and cotranslational mRNA decay in plants</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617633123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Sjors van der HorstJoseph L. GageJulia Bailey-Serresahttps://ror.org/03nawhv43Department of Botany and Plant Sciences, University of California, Riverside, CA 92521bhttps://ror.org/03nawhv43Center for Plant Cell Biology, University of California, Riverside, CA 92521cWageningen Seed Science Centre, Laboratory of Plant Physiology, Wageningen University, Wageningen 6708 PB, The Netherlandsdhttps://ror.org/04tj63d06Department of Crop and Soil Sciences, North Carolina State University, Raleigh, NC 27695ehttps://ror.org/04tj63d06North Carolina Plant Sciences Initiative, North Carolina State University, Raleigh, NC 27606</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617633123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617633123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618090123?af=R">
      <title>The 4EHP/GIGYF2 translation repressor complex is co-opted by the vaccinia virus K3L protein as a potential mechanism of immunoevasion</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618090123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePoxviruses are adept at evading the host immune response by encoding several dozen proteins that counteract antiviral defenses. We report that the 4EHP/GIGYF2 mRNA translation repressor complex, which is implicated in immunosuppression ...</description>
      <dc:title>The 4EHP/GIGYF2 translation repressor complex is co-opted by the vaccinia virus K3L protein as a potential mechanism of immunoevasion</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618090123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Reese Jalal LadakAdrian PelinHaotian ZhuangChelsea AbboudNiaz MahmoodJonathan BlanchetChenyue WuHuy-Dung HoangTom McGirrAndia MoshariMohamed Moustafa-KamalPatric Harris SnellStefan DüsterhöftAlbert M. BerghuisJean-François TrempeMichel L. TremblayJose G. TeodoroArkady KhoutorskyTommy AlainNevan J. KroganJung-Hyun ChoiSeyed Mehdi JafarnejadNahum Sonenbergahttps://ror.org/01pxwe438Department of Biochemistry, McGill University, Montreal, QC H3A 1A3, Canadabhttps://ror.org/01pxwe438Rosalind and Morris Goodman Cancer Institute, McGill University, Montreal, QC H3A 1A3, Canadachttps://ror.org/043mz5j54Quantitative Biosciences Institute, University of California, San Francisco, San Francisco, CA 94158dhttps://ror.org/038321296Gladstone Institute of Data Science and Biotechnology and Gladstone Infectious Disease Institute, J. David Gladstone Institutes, San Francisco, CA 94158ehttps://ror.org/043mz5j54Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158fhttps://ror.org/01pxwe438Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC H3G 0B1, Canadaghttps://ror.org/01pxwe438Department of Microbiology and Immunology, McGill University, Montreal, QC H3A 1A3, Canadahhttps://ror.org/03c4mmv16Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8L1, Canadaihttps://ror.org/03c4mmv16Children’s Hospital of Eastern Ontario Research Institute, University of Ottawa, Ottawa, ON K1H 8L1, Canadajhttps://ror.org/00hswnk62Johnston Cancer Research Centre, Queen’s University Belfast, Belfast BT9 7AE, United Kingdomkhttps://ror.org/04xfq0f34Institute of Molecular Pharmacology, Medical Faculty, Rheinisch-Westfälische Technische Hochschule Aachen University, Aachen 52074, Germanylhttps://ror.org/01pxwe438Department of Pharmacology and Therapeutics, McGill University, Montreal, QC H3G 0B1, Canadamhttps://ror.org/01pxwe438Department of Anesthesia and Faculty of Dental Medicine and Oral Health Sciences, McGill University, Montréal, QC H4A 3J1, Canadanhttps://ror.org/01pxwe438Alan Edwards Centre for Research on Pain, McGill University, Montréal, QC H3A 2B4, Canadaohttps://ror.org/043mz5j54Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, CA 94158phttps://ror.org/02wnxgj78Department of Biochemistry, Chungbuk National University, Cheongju 28644, South Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618090123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618090123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612170123?af=R">
      <title>The native structure of the Trichonympha centriole cartwheel reveals a zigzag stacking pattern</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612170123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceCentrioles are fundamental for cell division, cilia formation, and human health, yet the molecular principles governing their earliest assembly remain incompletely understood. By resolving the native architecture of the cartwheel in situ from ...</description>
      <dc:title>The native structure of the Trichonympha centriole cartwheel reveals a zigzag stacking pattern</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612170123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Carlee M. RowsellShintaroh KuboAsuva ArinThibault LegalMolly Yining YuKhanh Huy Buiahttps://ror.org/01pxwe438Department of Biochemistry, McGill University, Montreal, QC H3G 0B1, Canadabhttps://ror.org/057zh3y96Department of Applied Chemistry, Graduate School of Engineering, the University of Tokyo, Tokyo 113-0033, Japanchttps://ror.org/01pxwe438Department of Anatomy and Cell Biology, McGill University, Montreal, QC H3A 0C7, Canadadhttps://ror.org/01pxwe438Centre for Structural Biology Research, McGill University, Montreal, QC H3G 0B1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612170123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612170123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604252123?af=R">
      <title>Integration of Semaphorin/Plexin activation and amplification by a Neuropilin-like coreceptor ensures robust homeostatic plasticity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604252123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceNeural circuits must rapidly stabilize their activity when synaptic function is perturbed, yet how weak extracellular signals trigger fast and robust compensatory responses has remained unclear. Here, we identify a conserved signaling module ...</description>
      <dc:title>Integration of Semaphorin/Plexin activation and amplification by a Neuropilin-like coreceptor ensures robust homeostatic plasticity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604252123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Rosario VicidominiTae Hee HanWen-Chieh HsiehPeter NguyenJiefu LiEdward GinigerMihaela SerpeaSection on Cellular Communication, Eunice Kennedy Shiver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892bhttps://ror.org/013sk6x84Janelia Research Campus, HHMI, Ashburn, VA 20147chttps://ror.org/01s5ya894Axon Guidance and Neural Connectivity Section, National Institute of Neurological Disorders and Stroke, NIH, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604252123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604252123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611584123?af=R">
      <title>The structural dynamics of music drive acute stress recovery through functional reorganization of stress-regulation networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611584123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceStress is a pervasive threat to global mental and physical health. While music is universally used to promote relaxation, the neurobiological mechanisms that translate acoustic patterns into physiological relief have remained elusive. By ...</description>
      <dc:title>The structural dynamics of music drive acute stress recovery through functional reorganization of stress-regulation networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611584123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Siqi YouLei ZhangGuowei WuYi Duahttps://ror.org/03j7v5j15State Key Laboratory of Cognitive Science and Mental Health, Institute of Psychology, Chinese Academy of Sciences, Beijing 100101, Chinabhttps://ror.org/001fxzj49Rotman Research Institute, Baycrest Academy for Research and Education, Toronto, ON M6A 2E1, Canadachttps://ror.org/05qbk4x57Department of Psychology, University of Chinese Academy of Sciences, Beijing 100049, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611584123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611584123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607937123?af=R">
      <title>Cryo-EM structure of TGFBIp fibrils driven by a corneal dystrophy–linked mutation enables design of peptide inhibitors of aggregation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607937123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceUnderstanding the molecular basis of protein aggregation disorders is essential to developing treatments. One such disease is corneal dystrophy, genetically and pathologically associated with transforming growth factor β–induced protein (...</description>
      <dc:title>Cryo-EM structure of TGFBIp fibrils driven by a corneal dystrophy–linked mutation enables design of peptide inhibitors of aggregation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607937123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Yi Xiao JiangLukasz SalwinskiMichael R. SawayaPeng GeLiisa LutterXinyi ChengCarolyn J. HuHillary HernandezDavid R. BoyerConrad WangFilipe A. MeloDuilio CascioDavid S. Eisenbergahttps://ror.org/046rm7j60Department of Biological Chemistry, University of California, Los Angeles, CA 90095bhttps://ror.org/046rm7j60Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095chttps://ror.org/046rm7j60Department of Energy Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095dhttps://ror.org/046rm7j60Molecular Biology Institute, University of California, Los Angeles, CA 90095ehttps://ror.org/046rm7j60Institute for Quantitative and Computational Biosciences, University of California, Los Angeles, CA 90095</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607937123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607937123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611941123?af=R">
      <title>Quantum-enhanced coherent Raman spectroscopy with broadband squeezed-light detection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611941123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceCoherent Raman spectroscopy enables label-free chemical imaging and the study of ultrafast molecular dynamics, but its performance is fundamentally limited by nonresonant backgrounds that can obscure weak vibrational signals. Quantum ...</description>
      <dc:title>Quantum-enhanced coherent Raman spectroscopy with broadband squeezed-light detection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611941123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Konstantin E. DorfmanVladislav V. YakovlevShaul MukamelaCenter for Theoretical Physics and School of Physics and Optoelectronic Engineering, Hainan University, Haikou 570228, ChinabHimalayan Institute for Advanced Study, Unit of Gopinath Seva Foundation, Rishikesh, Uttarakhand 249201, Indiachttps://ror.org/01f5ytq51Institute for Quantum Science and Engineering, Texas A&amp;M University, College Station, TX 77843dhttps://ror.org/01f5ytq51Department of Physics and Astronomy, Texas A&amp;M University, College Station, TX 77843ehttps://ror.org/01f5ytq51Department of Electrical and Computer Engineering, Texas A&amp;M University, College Station, TX 77843fhttps://ror.org/04gyf1771Department of Chemistry, University of California, Irvine, CA 92697-2025ghttps://ror.org/04gyf1771Department of Physics and Astronomy, University of California, Irvine, CA 92697-2025</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611941123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611941123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2538135123?af=R">
      <title>Flow-driven lumen remodeling and valve opening in the vas deferens</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2538135123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceMale reproductive ducts must rapidly propel sperm-containing fluids forward, yet how they do so in living animals has remained unclear due to a lack of imaging studies. By combining real-time in vivo imaging and molecular activity reporters, ...</description>
      <dc:title>Flow-driven lumen remodeling and valve opening in the vas deferens</dc:title>
      <dc:identifier>doi:10.1073/pnas.2538135123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Nicole Ng Shu YingQin Ying LimGen YamadaTsuyoshi Hirashimaahttps://ror.org/01tgyzw49Mechanobiology Institute, National University of Singapore, Singapore 117411, Singaporebhttps://ror.org/005qv5373Department of Developmental Genetics, Wakayama Medical University, Wakayama City, Wakayama 641-8509, Japanchttps://ror.org/01tgyzw49Department of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117593, Singaporedhttps://ror.org/02kpeqv85The Hakubi Center, Graduate School of Biostudies, Kyoto University, Kyoto 606-8501, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2538135123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2538135123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600754123?af=R">
      <title>Redox state of Protein Kinase A RIα coordinates lysosomal calcium signaling and mitochondrial homeostasis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600754123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceMitochondrial quality control is essential for cellular energy balance, yet how redox signaling regulates this process remains poorly understood. We show that the cysteine redox state of the Protein Kinase A (PKA) regulatory subunit RIα is ...</description>
      <dc:title>Redox state of Protein Kinase A RIα coordinates lysosomal calcium signaling and mitochondrial homeostasis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600754123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Lorena Fernandez-MosqueraPhilip Eatonahttps://ror.org/026zzn846William Harvey Research Institute, Faculty of Medicine and Dentistry, Queen Mary University of London, London EC1M 6BQ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600754123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600754123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514037123?af=R">
      <title>LINE-1 repeats are a defining feature of the Xce</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514037123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceWhich X chromosome becomes inactivated in females is determined randomly but can be skewed by the mysterious “X chromosome controlling element(s)” (Xce). Here, we provide evidence that LINE-1 repeats of the L1Tf subfamily play a role in ...</description>
      <dc:title>LINE-1 repeats are a defining feature of the Xce</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514037123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Yesu JeonFei JiPriyojit DasPeggy I. WangUri WeissbeinLieselot L. G. CarretteBarry KesnerRuslan SadreyevJeannie T. Leeahttps://ror.org/002pd6e78Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114bDepartment of Genetics, Harvard Medical School, Boston, MA 02114</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514037123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514037123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533918123?af=R">
      <title>Heel-strike mechanics reveal evolutionary trade-offs in hominin bipedalism</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533918123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe “heel-strike” that initiates the typical human walking step has been observed in very few species outside our closest living relatives, the African apes, but the evolutionary origin and functional consequences of this unusual gait feature ...</description>
      <dc:title>Heel-strike mechanics reveal evolutionary trade-offs in hominin bipedalism</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533918123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Nicholas B. HolowkaMatthew C. O’NeillVincent BhandalOtto LamZacchariah M. ApolitoCaleb A. MassimiKevin G. PalmisanoSteven WorthingtonBrigitte DemesNathan E. Thompsonahttps://ror.org/04p491231Department of Anthropology, The Pennsylvania State University, University Park, PA 16803bhttps://ror.org/04p491231Huck Institute of Life Sciences, The Pennsylvania State University, University Park, PA 16803cDepartment of Anthropology, University at Buffalo, Buffalo, NY 14261dDepartment of Anatomy, Midwestern University, Glendale, AZ 85308ehttps://ror.org/05qghxh33Department of Anatomical Sciences, Renaissance School of Medicine at Stony Brook University, Stony Brook, NY 11794fhttps://ror.org/04a9tmd77Icahn School of Medicine at Mount Sinai, New York, NY 10029ghttps://ror.org/03vek6s52Institute for Quantitative Social Sciences, Harvard University, Cambridge, MA 02138hDepartment of Anatomy, College of Osteopathic Medicine, New York Institute of Technology, Old Westbury, NY 11568</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533918123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533918123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603034123?af=R">
      <title>Size-tailored nanoparticle–antibody conjugates overcome hepatic sequestration in Alzheimer’s disease treatment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603034123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe clinical efficacy of anti–amyloid-β (Aβ) immunotherapy is constrained by rapid hepatic sequestration, immune-related adverse events, and limited long-term safety, particularly among patients with impaired hepatic function. We demonstrate ...</description>
      <dc:title>Size-tailored nanoparticle–antibody conjugates overcome hepatic sequestration in Alzheimer’s disease treatment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603034123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Xuewei DuNi LiuTaoping ZhangChangwen YangHaiming Luoahttps://ror.org/03ab0at74State Key Laboratory of Digital Medical Engineering, Key Laboratory of Biomedical Engineering of Hainan Province, School of Biomedical Engineering, Hainan University, Haikou 570228, Chinabhttps://ror.org/00p991c53Ministry of Education Key Laboratory for Biomedical Photonics, Wuhan National Laboratory for Optoelectronics, Huazhong University of Science and Technology, Wuhan 430074, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603034123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603034123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604933123?af=R">
      <title>Neuromotor modules revealed by direct electrical stimulation of the human primary motor cortex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604933123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThis study has advanced our understanding of the origin of muscle synergies in humans by utilizing direct electrophysiological evidence obtained from cortical stimulation in patients undergoing glioma resection. Beyond demonstrating the neural ...</description>
      <dc:title>Neuromotor modules revealed by direct electrical stimulation of the human primary motor cortex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604933123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Jodie J. XieSubing HuangKelvin Y. S. LauAmy H. S. KongRosa H. M. ChanPeter Y. M. WooVincent C. K. Cheungahttps://ror.org/00t33hh48School of Biomedical Sciences, and The Gerald Choa Neuroscience Institute, The Chinese University of Hong Kong, Hong Kong, Chinabhttps://ror.org/03q8dnn23Department of Electrical Engineering, City University of Hong Kong, Hong Kong, Chinachttps://ror.org/03s9jrm13Department of Anaesthesiology and Operating Theatre Services, Kwong Wah Hospital, Hong Kong, ChinadDepartment of Neurosurgery, Prince of Wales Hospital, Hong Kong, Chinaehttps://ror.org/03s9jrm13Department of Neurosurgery, Kwong Wah Hospital, Hong Kong, Chinafhttps://ror.org/03m0vk445Joint Laboratory of Bioresources and Molecular Research of Common Diseases, The Chinese University of Hong Kong and Kunming Institute of Zoology of the Chinese Academy of Sciences, Hong Kong, Chinaghttps://ror.org/00t33hh48The Gerald Choa Neuroscience Institute–Oujiang Laboratory Joint Laboratory for Neuroscience and Neurology, The Chinese University of Hong Kong, Hong Kong, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604933123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604933123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530363123?af=R">
      <title>Increasing risk of vapor pressure deficit exceeding critical thresholds for tree growth</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530363123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceRising atmospheric vapor pressure deficit (VPD), a measure of atmospheric dryness, is increasingly recognized as a major threat to terrestrial ecosystems. Using global tree-ring records, we quantify growth-related VPD thresholds beyond which ...</description>
      <dc:title>Increasing risk of vapor pressure deficit exceeding critical thresholds for tree growth</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530363123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Tiewei LiHans W. ChenDeliang ChenJingfeng XiaoLanlan GuoLianyou LiuFeng ShiWenping YuanZiqian ZhongHuan ZhengBin Heahttps://ror.org/03cve4549Department of Earth System Science, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/040wg7k59Department of Environmental and Energy Sciences, Chalmers University of Technology, Gothenburg SE-412 96, Swedenchttps://ror.org/03cve4549Institute for Carbon Neutrality, Tsinghua University, Beijing 100084, ChinadEarth Systems Research Center, Institute for the Study of Earth, Oceans, and Space, University of New Hampshire, Durham, NH 03824ehttps://ror.org/022k4wk35Faculty of Geographical Science, Beijing Normal University, Beijing 100875, Chinafhttps://ror.org/034t30j35State Key Laboratory of Lithospheric and Environmental Coevolution, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, Chinaghttps://ror.org/02v51f717Institute of Carbon Neutrality, Sino-French Institute for Earth System Science, College of Urban and Environmental Sciences, Peking University, Beijing 100871, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530363123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530363123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532469123?af=R">
      <title>Scale-dependent effects of species richness and asynchrony regulate the temporal stability of consumer-mediated nutrient dynamics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532469123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe stability of ecosystem function is often regulated by biodiversity, yet research has focused largely on plants, leaving a gap in understanding how consumer diversity influences nutrient cycling stability. Synthesizing ~25 y of fish ...</description>
      <dc:title>Scale-dependent effects of species richness and asynchrony regulate the temporal stability of consumer-mediated nutrient dynamics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532469123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Mack WhiteW. Ryan JamesNathan P. LemoineJoseph R. PetersAdrian C. StierKyle A. EmeryMax C. N. CastoraniDante A. CaponeAnya ŠtajnerLauren N. EnrightShalanda R. GrierGrace F. CawleyAmanda C. SpivakJames A. NelsonRussell R. HopcroftAngel ChenNicholas J. LyonLi KuiJennifer E. CaselleBradley A. StricklandJacob E. AllgeierJennifer S. RehageDeron E. Burkepileahttps://ror.org/02gz6gg07Department of Earth and Environment, Florida International University, Miami, FL 33199bhttps://ror.org/02gz6gg07Institute of Environment, Florida International University, Miami, FL 33199chttps://ror.org/04gr4te78Department of Biological Sciences, Marquette University, Milwaukee, WI 53233dhttps://ror.org/02t274463Marine Science Institute, University of California, Santa Barbara, Santa Barbara, CA 93106ehttps://ror.org/02t274463Department of Ecology, Evolution, and Marine Biology, University of California, Santa Barbara, Santa Barbara, CA 93106fhttps://ror.org/0153tk833Department of Environmental Sciences, University of Virginia, Charlottesville, VA 22903ghttps://ror.org/0168r3w48Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92037hDepartment of Marine Sciences, University of Georgia, Athens, GA 30602ihttps://ror.org/01j7nq853Department of Oceanography, University of Alaska, Fairbanks, AK 99775jhttps://ror.org/02t274463National Center for Ecological Analysis and Synthesis, University of California, Santa Barbara, CA 93101khttps://ror.org/044zqqy65South Florida Natural Resources Center, National Park Service, Homestead, FL 33034lhttps://ror.org/00jmfr291Department of Ecology and Evolutionary Biology, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532469123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532469123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534362123?af=R">
      <title>In vivo genome-wide CRISPR screens identify FOXR1 as a suppressor of CD8+ T cell antitumor immunity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534362123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceT cell dysfunction compromises T cell antitumor functions and limits the efficacy of CAR T therapy. In this study, we performed an in vivo genome-wide CRISPR screen and identified the transcription factor Forkhead Box R1 (FOXR1) as a key ...</description>
      <dc:title>In vivo genome-wide CRISPR screens identify FOXR1 as a suppressor of CD8+ T cell antitumor immunity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534362123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Xue YangHan OuyangHenan XuLingxiao PengJianzhou CuiBin ZhangBo HuangChunmei WangGuideng LiXuetao Caoahttps://ror.org/02drdmm93Department of Immunology, Center for Immunotherapy, Institute of Basic Medical Sciences &amp; School of Basic Medicine, Chinese Academy of Medical Sciences &amp; Peking Union Medical College, Beijing 100005, Chinabhttps://ror.org/02drdmm93National Key Laboratory of Immunity and Inflammation, Suzhou Institute of Systems Medicine, Chinese Academy of Medical Sciences, Suzhou 215123, Chinachttps://ror.org/032p70522State Key Laboratory of Medicinal Chemical Biology, Institute of Immunology, College of Life Sciences, Nankai University, Tianjin 300071, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534362123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534362123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537797123?af=R">
      <title>Mitochondrial depolarization stabilizes the vitamin B12 chaperone MMADHC in the cytosol to increase MTR activity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537797123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceHumans have only two vitamin B12-dependent enzymes—mitochondrial methylmalonyl-CoA mutase and cytosolic 5-methyltetrahydrofolate-homocysteine methyltransferase (MTR)—and both require a common B12chaperone MMADHC. We show that MMADHC is a low ...</description>
      <dc:title>Mitochondrial depolarization stabilizes the vitamin B12 chaperone MMADHC in the cytosol to increase MTR activity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537797123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Sneha P. RathZhu LiArkajit GuhaFangcong DongRuma BanerjeeVamsi K. Moothaahttps://ror.org/002pd6e78Department of Molecular Biology, Mass General Hospital, Boston, MA 02114bDepartment of Systems Biology and Medicine, Harvard Medical School, Boston, MA 02115chttps://ror.org/042nb2s44Broad Institute of Massachusetts Institute of Technology and Harvard, Cambridge, MA 02142dhttps://ror.org/00jmfr291Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109eHHMI, Boston, MA 02114</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2537797123</prism:doi>
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      <title>Evolution of maize recombination landscape during domestication</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534336123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSelection by early farmers during the domestication of maize resulted in radical changes in the physical appearance of the plant. These changes were enabled by alterations in many genetic processes, including meiotic recombination. Meiotic ...</description>
      <dc:title>Evolution of maize recombination landscape during domestication</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534336123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Ruth EpsteinJ. J. WheelerMelissa J. HubiszJingjing ZhaiWei-Yun LaiRegina A. FairbanksQi SunEdward S. BucklerWojciech P. Pawlowskiahttps://ror.org/05bnh6r87School of Integrative Plant Science, Cornell University, Ithaca, NY 14853bhttps://ror.org/05bnh6r87Bioinformatics Facility, Cornell University, Ithaca, NY 14853chttps://ror.org/05rrcem69Department of Evolution and Ecology, University of California Davis, Davis, CA 95616dhttps://ror.org/05rrcem69Center for Population Biology, University of California Davis, Davis, CA 95616ehttps://ror.org/01na82s61Agricultural Research Service, United States Department of Agriculture, Ithaca, NY 14853</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2534336123</prism:doi>
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      <title>Negative feedback regulation of karrikin signaling in Arabidopsis thaliana by an antagonistic paralog of karrikin receptors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525145123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePlants use hormones—small, mobile, chemical or peptide signals—to regulate developmental and physiological responses to environmental and biotic cues. Karrikins (KARs) are chemicals found in smoke that affect the growth of many plants, but are ...</description>
      <dc:title>Negative feedback regulation of karrikin signaling in Arabidopsis thaliana by an antagonistic paralog of karrikin receptors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525145123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Qingtian LiSun Hyun ChangAndrew TuckeyClaudia SepulvedaKartikye VarshneyDan LiCaroline GutjahrMark T. WatersDavid C. Nelsonahttps://ror.org/03nawhv43Department of Botany and Plant Sciences, University of California, Riverside, CA 92521bYazhouwan National Laboratory, Sanya 572025, Chinachttps://ror.org/047272k79School of Molecular Sciences, University of Western Australia, Perth, WA 6009, Australiadhttps://ror.org/01fbde567Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm 14476, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2525145123</prism:doi>
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      <title>eIF5A and polyamines restrict mRNA levels in response to ribosome stalls</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533876123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceCells synthesize a diversity of proteins, and allow for variation in protein synthesis rates while also recognizing and eliminating proteins that take an interminable length of time. Precisely how cells accomplish both tasks is unclear. In ...</description>
      <dc:title>eIF5A and polyamines restrict mRNA levels in response to ribosome stalls</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533876123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Chloe M. WohlenbergParissa C. MonemNatalia BarbosaJudith FrydmanJoshua A. Arribereahttps://ror.org/03s65by71Department of Molecular, Cell, and Developmental Biology, University of California Santa Cruz, Santa Cruz, CA 95064bhttps://ror.org/00f54p054Department of Biology, Stanford University, Stanford, CA 94305chttps://ror.org/00f54p054Department of Genetics, Stanford University, Stanford, CA 94305dhttps://ror.org/03s65by71RNA Center, University of California Santa Cruz, Santa Cruz, CA 95064ehttps://ror.org/03s65by71Genomics Institute, University of California Santa Cruz, Santa Cruz, CA 95064</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2533876123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530056123?af=R">
      <title>Coordinated regulation of diverse F-actin organizations orchestrates F-actin pulses in the actomyosin network</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530056123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceActomyosin pulsation is a fundamental mechanism driving morphogenesis, but how actin networks generate and coordinate such dynamics remains unclear. UsingDrosophilaoogenesis, we show that basal actomyosin networks consist of two F-actin ...</description>
      <dc:title>Coordinated regulation of diverse F-actin organizations orchestrates F-actin pulses in the actomyosin network</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530056123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Hao LiBing LiuJiaying LiuThomas MangeatKarine BelguiseShi-Lei XueXiaobo Wangahttps://ror.org/01ahyrz84CNRS, Centre de Biologie Integrative, Molecular Cellular and Developmental Biology Unit, University of Toulouse, Toulouse 31062, Francebhttps://ror.org/05hfa4n20Department of Materials Science and Engineering, School of Engineering, Westlake University, Hangzhou 310030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530056123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530056123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621342123?af=R">
      <title>Exosome trafficking is a key regulator of adipocyte thermogenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621342123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThermogenic adipocytes, including beige and brown fat cells, help maintain energy balance by converting excess nutrients into heat, thereby reducing fat storage and supporting metabolic health. Although these cells are known to increase energy ...</description>
      <dc:title>Exosome trafficking is a key regulator of adipocyte thermogenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621342123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Devesh KesharwaniMichele KarolakChad DoucetteRachelle MendolaSummer PrayRaghu BhardwajSu SuAnne HarringtonVictoria DeMambroClifford RosenLucy LiawAaron C. BrownaCenter for Molecular Medicine, MaineHealth Institute for Research, Scarborough, ME 04074bhttps://ror.org/01adr0w49Graduate School of Biomedical Science and Engineering, The University of Maine, Orono, ME 04469chttps://ror.org/05wvpxv85Tufts University School of Medicine, Boston, MA 02111</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621342123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621342123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610659123?af=R">
      <title>Alternative genetic codes in bacteria and archaea identified with a fast k-mer–based algorithm</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610659123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe genetic code is nearly universal in all living organisms yet the extent of exceptions to this rule is not well understood. Recent developments in DNA sequencing technologies have led to identification of hundreds of thousands of new ...</description>
      <dc:title>Alternative genetic codes in bacteria and archaea identified with a fast k-mer–based algorithm</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610659123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Artem V. MelnykovaIndependent Scholar, Belleville, IL 62220</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610659123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610659123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612002123?af=R">
      <title>Integrative modeling of the genome structure and dynamics in fission yeast</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612002123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceBuilding quantitative models that connect genome structure to chromatin dynamics is essential for predicting chromosome motion and genome function in living cells. Using genome-wide live-cell imaging and Hi-C data-constrained polymer modeling ...</description>
      <dc:title>Integrative modeling of the genome structure and dynamics in fission yeast</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612002123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Soya ShinkaiToshinori NambaTakeshi SugawaraSoya HagiwaraShuichi OnamiTokuko HaraguchiYasushi HiraokaAkinori AwazuMasaru UenoShin-ichi TateaLaboratory for Developmental Dynamics, Center for Biosystems Dynamics Research, RIKEN, Kobe 650-0047, Japanbhttps://ror.org/03t78wx29Research Center for the Mathematics on Chromatin Live Dynamics, Hiroshima University, Higashi-Hiroshima 739-8530, Japanchttps://ror.org/035t8zc32Graduate School of Frontier Biosciences, University of Osaka, Suita 565-0871, Japandhttps://ror.org/03t78wx29Graduate School of Integrated Sciences for Life, Hiroshima University, Higashi-Hiroshima 739-8530, Japanehttps://ror.org/03t78wx29International Institute for Sustainability with Knotted Chiral Meta Matter, Hiroshima University, Higashi-Hiroshima 739-0046, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612002123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612002123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614077123?af=R">
      <title>Resolving cell lineages and gene functions in the developing mouse gastrointestinal tract using in utero transduction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614077123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe gastrointestinal tract comprises diverse cell types originating from all three germ layers and includes the neural crest-derived enteric nervous system (ENS). Progress in defining these lineages and their gene regulation is challenged by ...</description>
      <dc:title>Resolving cell lineages and gene functions in the developing mouse gastrointestinal tract using in utero transduction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614077123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Ziwei LiuKrishnanand PadmanabhanJingyan HeKatrin HectorBettina SemschJia SunViktoria KnoflachSarantis GiatrellisJohan LorentzKhachatur DallakyanChristian GöritzEmma Rachel AnderssonUlrika Marklundahttps://ror.org/056d84691Department of Medical Biochemistry and Biophysics, Unit of Molecular Neurobiology, Karolinska Institutet SE-171 77, Stockholm, Swedenbhttps://ror.org/056d84691Department of Cell and Molecular Biology, Karolinska Institutet SE-171 77, Stockholm, Swedenchttps://ror.org/056d84691Comparative Medicine, Karolinska Institutet SE-171 77, Stockholm, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614077123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614077123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605103123?af=R">
      <title>Gating crosstalk in potassium channels</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605103123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePotassium channels regulate electrical signaling by transporting K+across cell membranes. This activity is controlled by multiple gates, yet how these gates interact remains not entirely understood. We identify a conserved gating crosstalk ...</description>
      <dc:title>Gating crosstalk in potassium channels</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605103123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Lyubin HuBert L. de GrootRuo-Xu Guahttps://ror.org/0220qvk04Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, Chinabhttps://ror.org/03av75f26Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605103123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605103123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617905123?af=R">
      <title>Coadapting but not static predators facilitate prey adaptation to a fluctuating environment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617905123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSpecies in the wild face the dual challenge of adapting to their changing physical environment and coping with detrimental interactions with other species, including predators. While evolution by natural selection may jointly overcome both ...</description>
      <dc:title>Coadapting but not static predators facilitate prey adaptation to a fluctuating environment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617905123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Lou GuyotAryan RamachandranLuis-Miguel Chevinahttps://ror.org/051escj72Centre d’Ecologie Fonctionnelle et Evolutive, CNRS, Ecole Pratique des Hautes Etudes, Institut de Recherche pour le Développement, Université de Montpellier, Montpellier 34293, Francebhttps://ror.org/03xjwb503Ecologie, Société et Evolution, CNRS, Universite Paris-Saclay, AgroParisTech, Gif-sur-Yvette 91190, Francechttps://ror.org/01rk35k63Ecole Normale Supérieure de Lyon, Département de biologie, Universite de Lyon, Lyon Cedex 07 69342, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617905123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617905123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617902123?af=R">
      <title>FERONIA phosphorylates the amino-terminal extension of phytochrome B to modulate plant light and temperature responses</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617902123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePhytochrome B (phyB) is a prominent light and temperature sensor that optimizes plant growth and development in response to environmental light and temperature changes. PhyB N-terminal Extension (NTE, amino acid 1 to 90) is essential for phyB ...</description>
      <dc:title>FERONIA phosphorylates the amino-terminal extension of phytochrome B to modulate plant light and temperature responses</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617902123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Ping WangJuan DuJiangman HeZhi LiJustin W. WalleyMeng ChenHongqing Guoahttps://ror.org/04rswrd78Department of Genetics, Development and Cell Biology, Iowa State University, Ames, IA 50011bhttps://ror.org/03nawhv43Department of Botany and Plant Sciences, University of California, Riverside, CA 92521chttps://ror.org/04rswrd78Department of Plant Pathology, Entomology &amp; Microbiology, Iowa State University, Ames, IA 50011dhttps://ror.org/04rswrd78Plant Sciences Institute, Iowa State University, Ames, IA 50011</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617902123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617902123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608466123?af=R">
      <title>Seasonally asymmetric warming reshapes grassland stability across timescales</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608466123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSeasonally asymmetric climate change is reshaping our understanding of ecosystem stability. Evidence from two multiyear field experiments in Tibetan alpine grasslands demonstrated that spring warming exerted a more substantial influence on ...</description>
      <dc:title>Seasonally asymmetric warming reshapes grassland stability across timescales</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608466123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Chunyan LuHuiying LiuYixuan HuangJingya ZhangJuanjuan ZhangSiyuan GaoZhenhua ZhangHao WangJin-Sheng HeMadhav P. Thakurahttps://ror.org/02n96ep67Zhejiang Tiantong Forest Ecosystem National Observation and Research Station, Institute of Eco-Chongming, Zhejiang Zhoushan Island Ecosystem Observation and Research Station, School of Ecological and Environmental Sciences, East China Normal University, Shanghai 200241, Chinabhttps://ror.org/02k7v4d05Institute of Ecology and Evolution, University of Bern, Bern 3012, Switzerlandchttps://ror.org/034t30j35Qinghai Haibei National Field Research Station of Alpine Grassland Ecosystem, Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining 810008, Chinadhttps://ror.org/01mkqqe32State Key Laboratory of Herbage Improvement and Grassland Agro-Ecosystems, College of Ecology, Lanzhou University, Lanzhou 730000, Chinaehttps://ror.org/01mkqqe32State Key Laboratory of Herbage Improvement and Grassland Agro-Ecosystems, College of Pastoral Agriculture Science and Technology, Lanzhou University, Lanzhou 730020, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608466123</prism:doi>
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   </item>
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      <title>Plausible nonsense and deliberative reasoning: Benchmarking LLMs against human judgment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600126123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceLarge Language Models (LLMs) are increasingly used to generate arguments and support decision-making in policy contexts. This use raises a democratic concern: by shaping which arguments are visible and how choices are framed, AI systems can ...</description>
      <dc:title>Plausible nonsense and deliberative reasoning: Benchmarking LLMs against human judgment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600126123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Francesco VeriGustavo Kreia Umbelinoahttps://ror.org/02crff812Centre for Democracy Studies Aarau, University of Zurich, Aarau 5000, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600126123</prism:doi>
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      <title>Targeting cholesterol-dependent Piezo1 activation impairs amoeboid migration in melanoma cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607369123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThis study builds on a phenotypic drug screen that identified statins as inhibitors of bleb-based migration, a key mode of cancer cell movement through confined spaces. We show that statins reduce membrane cholesterol, disrupting the function ...</description>
      <dc:title>Targeting cholesterol-dependent Piezo1 activation impairs amoeboid migration in melanoma cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607369123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Sylvia H. KuangAlleah G. AbrenicaNeelakshi KarJeremy S. Logueahttps://ror.org/03g66yt05Department of Regenerative and Cancer Cell Biology, Albany Medical College, Albany, NY 12208</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607369123</prism:doi>
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      <title>Minimal-length CAG repeats in AR define a hyperactive AR–LSD1 axis driving metabolic reprogramming in prostate cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534152123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePrevious studies have suggested that shorter CAG repeat lengths may increase androgen receptor (AR) protein stability, but the biological and clinical significance of this observation has remained unclear. This study demonstrates that ARs with ...</description>
      <dc:title>Minimal-length CAG repeats in AR define a hyperactive AR–LSD1 axis driving metabolic reprogramming in prostate cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534152123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Songqi ZhangMuqing LiMingyu LiuNolan D. PattenMaryam LabafJaeweon JeongHyeonYeong SunJared LourieKai ZouSusan PatalanoMichaela J. MulhearnJill A. MacoskaShuai GaoRoberta AndreottiMaria PennutoDong HanSteven P. BalkChangmeng Caiahttps://ror.org/04ydmy275Center for Personalized Cancer Therapy, University of Massachusetts Boston, Boston, MA 02125bhttps://ror.org/04ydmy275Department of Biology, University of Massachusetts Boston, Boston, MA 02125chttps://ror.org/04b6nzv94Department of Urology, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115dhttps://ror.org/04ydmy275Department of Mathematics, University of Massachusetts Boston, Boston, MA 02125ehttps://ror.org/04drvxt59Hematology-Oncology Division, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215fhttps://ror.org/04ydmy275Department of Exercise and Health Sciences, University of Massachusetts Boston, Boston, MA 02125ghttps://ror.org/03dkvy735Department of Cell and Molecular Physiology, New York Medical College, Valhalla, NY 10595hhttps://ror.org/00240q980Department of Biomedical Sciences, University of Padova, Padova 35131, Italyihttps://ror.org/0048jxt15Veneto Institute of Molecular Medicine, Padova 35129, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534152123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534152123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600311123?af=R">
      <title>A role for self-regulatory control in the absence of ingroup preference</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600311123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceWhile humans generally exhibit a robust preference for their own social groups, members of lower-status groups frequently lack this preference on implicit measures, a pattern with consequences for how social hierarchies are maintained. To ...</description>
      <dc:title>A role for self-regulatory control in the absence of ingroup preference</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600311123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Samuel A. W. KleinTessa E. S. CharlesworthDaniel W. HeckMahzarin R. BanajiJeffrey W. Shermanahttps://ror.org/00hj8s172Department of Psychology, Columbia University, New York, NY 10027bKellogg School of Management, Northwestern University, Evanston, IL 60208cDepartment of Psychology, University of Marburg, Marburg 35032, Germanydhttps://ror.org/03vek6s52Department of Psychology, Harvard University, Cambridge, MA 02138ehttps://ror.org/05rrcem69Department of Psychology, University of California, Davis, CA 95616</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600311123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600311123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613134123?af=R">
      <title>Harmonizing amplification and cleavage kinetics through crRNA scaffold mutation enables robust one-pot CRISPR–Cas12 diagnostics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613134123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceRapid and accurate pathogen detection is essential for public health response. Current one-pot CRISPR diagnostics, however, often sacrifice sensitivity because uncontrolled Cas enzyme activity interferes with upstream amplification. We ...</description>
      <dc:title>Harmonizing amplification and cleavage kinetics through crRNA scaffold mutation enables robust one-pot CRISPR–Cas12 diagnostics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613134123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Qingyang JiangRuiquan XuZhixin LinChenyu SunFeidi YeYanyan YeDuoming LinZhen LiJingwen MaiZhihong LinJiuxin QuXiaoyan DengChenchen GeDou Wangahttps://ror.org/00zat6v61KingMed School of Laboratory Medicine, Guangzhou Medical University, Guangzhou, Guangdong 511436, People’s Republic of ChinabGuangdong Provincial Engineering Research Center for Early Warning and Diagnosis of Respiratory Infectious Diseases, Guangzhou, Guangdong 511436, People’s Republic of Chinachttps://ror.org/049tv2d57Department of Clinical Laboratory, Shenzhen Third People’s Hospital, Second Hospital Affiliated to Southern University of Science and Technology, National Clinical Research Center for Infectious Diseases, Guangdong 518055, People’s Republic of Chinadhttps://ror.org/04qzpec27College of Health Science and Environmental Engineering, Shenzhen Technology University, Shenzhen 518118, Guangdong, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613134123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613134123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611577123?af=R">
      <title>A multifaceted role for synaptic ribbons in sensory circuit assembly and computation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611577123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceRibbons are specialized structures of sensory synapses in the visual, auditory, and vestibular systems, long thought to function primarily as scaffolds that dock and prime synaptic vesicles for rapid neurotransmitter release. We extend this ...</description>
      <dc:title>A multifaceted role for synaptic ribbons in sensory circuit assembly and computation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611577123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Andrew SchultzHaoshen ZhaiYunwei ChuPranav VenkitMrinalini HoonRaunak SinhaaDepartment of Neuroscience, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53705bMolecular and Cellular Pharmacology Training Program, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53705chttps://ror.org/05783y657McPherson Eye Research Institute, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53705dDepartment of Ophthalmology and Visual Sciences, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53705</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611577123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611577123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612849123?af=R">
      <title>MAVS undergoes aggregation under hypoxia to enhance the hypoxia signaling pathway by promoting the generation of mitochondrial ROS</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612849123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThis study reveals an unexpected function of MAVS, which is mostly regarded as a key mediator of antiviral response in cells. We found that MAVS also helps cells survive in low-oxygen environments by activating protective mechanisms. Using ...</description>
      <dc:title>MAVS undergoes aggregation under hypoxia to enhance the hypoxia signaling pathway by promoting the generation of mitochondrial ROS</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612849123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Xueyi SunChunchun ZhuWen LiuZixuan WangHongyan DengShuke JiaShuai ShiYuhan XiangYiman LuoJian-Fang GuiXing LiuWuhan Xiaoahttps://ror.org/034t30j35State Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, People’s Republic of ChinabHubei Hongshan Laboratory, Wuhan 430070, People’s Republic of ChinacLaboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266237, People’s Republic of Chinadhttps://ror.org/05qbk4x57College of Advanced Agricultural Sciences, University of Chinese Academy of Sciences, Beijing 100049, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612849123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612849123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533522123?af=R">
      <title>Methyl indole-3-acetate contributes to strain-specific anti-inflammatory effects of Lactiplantibacillus plantarum</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533522123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceLactiplantibacillus plantarumhas attracted considerable interest as a probiotic, owing to its beneficial impact on gut health and its capacity to alleviate gastrointestinal inflammation. However, its anti-inflammatory efficacy varies among ...</description>
      <dc:title>Methyl indole-3-acetate contributes to strain-specific anti-inflammatory effects of Lactiplantibacillus plantarum</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533522123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Kailin LiuMeng WangXinyi ZhuLibin PanLichao WangWu BaoBingqing HangXianjiong ChenGuifang LiDaqian XuDong GuoYinan ShenGaopeng LiYuan DingHonglin AnYanan ZhangShu Jeffrey ZhuJuan DuQiming LiangWangyun XuBin HuangJiaxin ChenPing LiYuhao Wangahttps://ror.org/00a2xv884Zhejiang Provincial Key Laboratory of Pancreatic Disease of The First Affiliated Hospital, Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, Chinabhttps://ror.org/04vs9wp72Department of Pharmacy, Zhejiang Cancer Hospital, Hangzhou Institute of Medicine, Chinese Academy of Sciences, Hangzhou, Zhejiang 310022, ChinacDepartment of Colorectal Surgery and Oncology of the Second Affiliated Hospital, Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, Chinadhttps://ror.org/00a2xv884Department of Hepatobiliary and Pancreatic Surgery, The Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, Chinaehttps://ror.org/05n0qbd70Academy of Integrative Medicine, Affiliated People’s Hospital, Fujian-Hong Kong-Macau-Taiwan Collaborative Laboratory for the Inheritance and Innovation of Traditional Chinese Medicine, Fujian University of Traditional Chinese Medicine, Fuzhou 350122, Chinafhttps://ror.org/00a2xv884Department of Veterinary Medicine, College of Animal Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, Chinaghttps://ror.org/00a2xv884Department of Gastroenterology, First Affiliated Hospital of Zhejiang University School of Medicine, Hangzhou, Zhejiang 310006, Chinahhttps://ror.org/0220qvk04Department of Immunology and Microbiology, Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, ChinaiHangzhou Puyuan Biotechnology Company Limited, Hangzhou, Zhejiang 310030, Chinajhttps://ror.org/00a2xv884Department of Breast Surgery and Key Laboratory of Tumor Microenvironment and Immune Therapy of Zhejiang Province, The Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, Chinakhttps://ror.org/0569mkk41School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, Chinalhttps://ror.org/00a2xv884Cancer Center, Zhejiang University, Hangzhou, Zhejiang 310029, Chinamhttps://ror.org/00a2xv884Institute of Fundamental and Transdisciplinary Research, Zhejiang University, Hangzhou, Zhejiang 310029, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533522123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533522123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615468123?af=R">
      <title>Programming sequential deployment of origami via kinematic transition fronts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615468123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificancePropagating transition fronts—where local changes trigger sequential responses—are common in nature and engineered systems, but are typically driven by stored energy and instability. Here, we focus on designing propagation that arises purely ...</description>
      <dc:title>Programming sequential deployment of origami via kinematic transition fronts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615468123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Rinki ImadaTomohiro Tachiahttps://ror.org/059yhyy33Department of Space Flight Systems, Institute of Space and Astronautical Science, Japan Aerospace Exploration Agency, Sagamihara-shi, Kanagawa 252-5210, Japanbhttps://ror.org/057zh3y96Department of General Systems Studies, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo 153-8902, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615468123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615468123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614238123?af=R">
      <title>Starvation suppression in dense scale-free metabolic networks: Dynamical mean-field analysis of catalytic reaction networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614238123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceLiving cells maintain their functions through complex networks of chemical reactions. Despite their diversity, metabolic networks share a scale-free structure across species, with highly heterogeneous connectivity. However, how this ...</description>
      <dc:title>Starvation suppression in dense scale-free metabolic networks: Dynamical mean-field analysis of catalytic reaction networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614238123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Kota MitsumotoShuji Ishiharaahttps://ror.org/057zh3y96Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo 153-8902, Japanbhttps://ror.org/057zh3y96Research Center for Complex Systems Biology, Universal Biology Institute, The University of Tokyo, Meguro-ku, Tokyo 153-8902, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614238123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614238123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600520123?af=R">
      <title>Differentiation of frontolimbic functional connectivity from birth to early adulthood links with adversity exposure and cognition</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600520123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe frontolimbic circuit, especially the fronto-hippocampus and fronto-amygdala circuitry, is integral for cognitive and affective processes. Yet its maturation has been challenging to characterize due to variable connectivity growth across ...</description>
      <dc:title>Differentiation of frontolimbic functional connectivity from birth to early adulthood links with adversity exposure and cognition</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600520123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Wonyoung KimSarah WhittleAndrew ZaleskyYe Ella Tianahttps://ror.org/01ej9dk98Department of Psychiatry, University of Melbourne, Melbourne, VIC 3010postal-code&gt;, Australiabhttps://ror.org/02czsnj07Faculty of Health, Faculty of Health, School of Psychology, Deakin University, Melbourne, VIC 3125, Australiachttps://ror.org/01ej9dk98Department of Biomedical Engineering, University of Melbourne, Melbourne, VIC 3010, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600520123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600520123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614500123?af=R">
      <title>Two-dimensional billiards are Turing complete</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614500123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceBilliards are a textbook model of deterministic motion: A particle moves freely and reflects specularly from rigid walls. We show that, even in two dimensions, billiard trajectories can simulate arbitrary Turing machines. This universality ...</description>
      <dc:title>Two-dimensional billiards are Turing complete</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614500123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Eva MirandaIsaac Ramosahttps://ror.org/03mb6wj31Department of Mathematics, Institute of mathematics of UPC-BarcelonaTech, Laboratory of Geometry and Dynamical Systems, SYMCREA research unit, Universitat Politècnica de Catalunya, Barcelona 08028, Spainbhttps://ror.org/020s51w82Centre de Recerca Matemàtica, Barcelona 08193, Spainchttps://ror.org/05a28rw58Department of Mathematics, ETH Zürich, Zürich 8006, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614500123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614500123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613408123?af=R">
      <title>Built-in electric field leverages synergistic thermodynamic–kinetic enhancement for superior fixed-bed oxyanion adsorption</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613408123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceTraditional adsorbent design primarily enhances static performance—such as selectivity and capacity—by tuning adsorption thermodynamics, for instance, through strengthening affinity toward target species. In fixed-bed adsorption, the most ...</description>
      <dc:title>Built-in electric field leverages synergistic thermodynamic–kinetic enhancement for superior fixed-bed oxyanion adsorption</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613408123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Pengfei ShenYidong ZhangHuai WangXiaolin ZhangBingcai Panahttps://ror.org/01rxvg760State Key Laboratory of Water Pollution Control and Green Resource Recycling, School of Environment, Nanjing University, Nanjing 210023, Chinabhttps://ror.org/01rxvg760Research Center for Environmental Nanotechnology, Nanjing University, Nanjing 210023, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613408123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613408123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602259123?af=R">
      <title>Confinement controls the stochastic onset of single-cell rotation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602259123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceA cascade of symmetry-breaking events transforms a single cell into a complex organism. Here, at the single-cell level, we investigate how confined cells can spontaneously break their symmetry and rotate persistently despite intrinsic noise. ...</description>
      <dc:title>Confinement controls the stochastic onset of single-cell rotation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602259123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Sebastián Echeverría-AlarBadri Narayanan NarasimhanStephanie I. FraleyWouter-Jan Rappelahttps://ror.org/0168r3w48Department of Physics, University of California, San Diego, CA 92093bhttps://ror.org/0168r3w48Department of Bioengineering, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602259123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602259123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614167123?af=R">
      <title>Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614167123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceGenetic code expansion enables the incorporation of diverse chemical functionalities into proteins, yet its utility is often limited by the availability of noncanonical amino acids (ncAAs). While in-cell ncAA biosynthesis can address this ...</description>
      <dc:title>Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614167123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>James S. AndonAbhijit BeheraDebashrito DebAmy M. WeeksAndrew R. BullerTina Wangahttps://ror.org/01y2jtd41Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706bhttps://ror.org/01y2jtd41Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706chttps://ror.org/027m9bs27Department of Chemistry, University of Manchester, Manchester M13 9PL, United Kingdomdhttps://ror.org/027m9bs27Manchester Institute of Biotechnology, University of Manchester, Manchester M1 7DN, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614167123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614167123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602861123?af=R">
      <title>Actuation of CRP activating region 3 by formylation modulates the Vibrio cholerae response to oxidative DNA damage</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602861123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceAs a model in the field of bacterial transcription, the structure and function of the cyclic adenosine monophosphate receptor protein (CRP), a global transcription regulator, has been exhaustively investigated. These studies have established ...</description>
      <dc:title>Actuation of CRP activating region 3 by formylation modulates the Vibrio cholerae response to oxidative DNA damage</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602861123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Renato E. R. S. SantosPallabi BasuBrendan J. O’HaraJacob A. GibsonMichael J. GebhardtChris AkutWilliam P. RobinsJohn J. MekalanosSimon L. DovePaula I. Watnickahttps://ror.org/00dvg7y05Division of Infectious Diseases, Boston Children’s Hospital, Boston, MA 02115bDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115cBiological and Biomedical Sciences Program, Harvard Medical School, Boston, MA 02115dhttps://ror.org/036jqmy94Department of Microbiology and Immunobiology, University of Iowa, Iowa City, IA 52242eDepartment of Microbiology, 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>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602861123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602861123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615477123?af=R">
      <title>Tmem216 deficiency induces hydrocephalus via impaired ciliogenesis and disrupted ependymal planar polarity in mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615477123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceMulticiliated ependymal cells (ECs) lining the walls of brain ventricles exhibit location-specific polarity and asymmetric positioning of their cilia and generate unidirectional cerebrospinal fluid (CSF) flow through coordinated ciliary ...</description>
      <dc:title>Tmem216 deficiency induces hydrocephalus via impaired ciliogenesis and disrupted ependymal planar polarity in mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615477123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Qianqian GongZhuowen LvZhilin DouSen WangKeyi ZhangYuyu GuoYingying WangMing ShaoLing SuXiangguo LiuXiaoyang Sunahttps://ror.org/0207yh398Shandong Provincial Key Laboratory of Development and Regeneration, School of Life Sciences, Shandong University, Qingdao 266237, ChinabKey Laboratory for Experimental Teratology of the Ministry of Education and Department of Medical Genetics, School of Basic Medical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinacState Key Laboratory of Microbial Technology, Institute of Microbial Technology, Shandong University, Qingdao 266237, Chinadhttps://ror.org/0207yh398Shandong University Taishan College, 266237, Chinaehttps://ror.org/0207yh398Shandong University-Yuanchen Joint Biomedical Technology Laboratory, Qingdao 266237, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615477123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615477123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534899123?af=R">
      <title>A refined phylochronology of the second plague pandemic in Western Eurasia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534899123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceTo date, over one hundred genomes of the plague pathogenYersinia pestishave been reconstructed from ancient DNA and attributed to the second plague pandemic (14th to 18th centuries). However, for a large proportion of those genomes, we rely ...</description>
      <dc:title>A refined phylochronology of the second plague pandemic in Western Eurasia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534899123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Marcel KellerMeriam GuellilPhilip SlavinLehti SaagKadri IrdtHelja KabralAnu SolnikMartin MalveHeiki ValkAivar KriiskaCraig CessfordSarah A. InskipJohn E. RobbChristine CooperConradin von PlantaMathias SeifertThomas ReitmaierWillem A. BaetsenDon WalkerSandra LöschSönke SzidatMait MetspaluToomas KivisildKristiina TambetsChristiana L. Scheibahttps://ror.org/03z77qz90Estonian Biocentre, Institute of Genomics, University of Tartu, Tartu 51010, Estoniabhttps://ror.org/02s6k3f65Integrative Prehistory and Archaeological Sciences Unit, Department of Environmental Sciences, University of Basel, Basel 4055, Switzerlandchttps://ror.org/02k7v4d05Department of Physical Anthropology, Institute of Forensic Medicine, University of Bern, Bern 3008, Switzerlanddhttps://ror.org/03prydq77Department of Evolutionary Anthropology, University of Vienna, Vienna 1030, Austriaehttps://ror.org/03prydq77Human Evolution and Archaeological Sciences, University of Vienna, Vienna 1030, Austriafhttps://ror.org/045wgfr59Division of History, Heritage and Politics, University of Stirling, Stirling FK9 4LA, United Kingdomghttps://ror.org/03z77qz90Core Facility of Genomics, Institute of Genomics, University of Tartu, Tartu 51010, Estoniahhttps://ror.org/03z77qz90Institute of History and Archaeology, University of Tartu, Tartu 51005, Estoniaihttps://ror.org/013meh722McDonald Institute for Archaeological Research, University of Cambridge, Cambridge CB2 3ER, United Kingdomjhttps://ror.org/013meh722Cambridge Archaeological Unit, University of Cambridge, Cambridge CB3 0DT, United Kingdomkhttps://ror.org/04h699437School of Archaeology and Ancient History, University of Leicester, Leicester LE1 7RH, United Kingdomlhttps://ror.org/013meh722Department of Archaeology, University of Cambridge, Cambridge CB2 3DZ, United KingdommArchaeological Service of the Canton of Grisons, Chur 7001, SwitzerlandnDepartment of Archaeology, Office of Culture, Triesen 9495, Principality of Liechtensteinohttps://ror.org/02s52y897Institut für Kulturforschung Graubünden, Chur 7000, SwitzerlandpRAAP Archeologisch Adviesbureau B.V., Leiden 2314 XT, The Netherlandsqhttps://ror.org/01qedwh63Museum of London Archaeology, London N1 7ED, United Kingdomrhttps://ror.org/02k7v4d05Department of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Bern 3012, Switzerlandshttps://ror.org/02k7v4d05Oeschger Centre for Climate Change Research, University of Bern, Bern 3012, Switzerlandthttps://ror.org/05f950310Department of Human Genetics, Katholieke Universiteit Leuven, Leuven 3000, Belgiumuhttps://ror.org/013meh722St. John’s College, University of Cambridge, Cambridge CB2 1TP, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534899123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534899123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617140123?af=R">
      <title>Structural and mechanistic insights into the fungal glycosylphosphatidylinositol mannosyltransferase I complex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617140123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceGPI mannosyltransferase I (GPI-MT-I) catalyzes the first committed mannosylation step of the GlcN-(acyl)PI acceptor during GPI anchor biosynthesis. This process is essential for fungal viability and virulence, positioning GPI-MT-I as a ...</description>
      <dc:title>Structural and mechanistic insights into the fungal glycosylphosphatidylinositol mannosyltransferase I complex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617140123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Jia LiuYizheng YangYi TanZhengkang HuaXinlin HuXuyang DingPing YangYan KeZhentao ZhangTianlu LiPeng PengMin ZhangHongjun Yuahttps://ror.org/00p991c53Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Huazhong University of Science and Technology, Wuhan 430030, Chinabhttps://ror.org/00p991c53Department of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan 430030, Chinachttps://ror.org/0207yh398National Glycoengineering Research Center, Shandong University, Qingdao 266237, Shandong, Chinadhttps://ror.org/00p991c53Cell Architecture Research Center, Huazhong University of Science and Technology, Wuhan 430030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617140123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617140123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2512284123?af=R">
      <title>Multicellular rosette formation guides epithelial tissue assembly in pancreatic ductal adenocarcinoma cell organoids</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2512284123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe organization of cells from a disordered aggregate to an ordered columnar tissue is crucial for functional organ formation. A key step in this process is the formation of rosettes—clusters of wedge-shaped cells. While previous studies have ...</description>
      <dc:title>Multicellular rosette formation guides epithelial tissue assembly in pancreatic ductal adenocarcinoma cell organoids</dc:title>
      <dc:identifier>doi:10.1073/pnas.2512284123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Marion K. RaichFridtjof BraunsTamara MüllerMaximilian ReichertAndreas R. Bauschahttps://ror.org/02kkvpp62Department for Bioscience, Heinz Nixdorf Chair in Biophysical Engineering of Living Matter, TUM School of Natural Sciences, Technical University of Munich, Garching 85748, Germanybhttps://ror.org/02kkvpp62Center for Functional Protein Assemblies, Technical University of Munich, Garching 85748, Germanychttps://ror.org/02kkvpp62Center for Organoid Systems, Technical University of Munich, Garching 85748, Germanydhttps://ror.org/01bf9rw71Max Planck Institute for the Physics of Complex Systems, Dresden 01187, Germanyehttps://ror.org/05b8d3w18Max Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germanyfhttps://ror.org/05hrn3e05Center for Systems Biology Dresden, Dresden 01307, GermanygKlinik und Poliklinik für Innere Medizin II, Klinikum Rechts der Isar der Technischen Universität München, Munich 81675, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2512284123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2512284123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613665123?af=R">
      <title>Evolution of flowering phenology over 44 years of climate change</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613665123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe ability of species to rapidly adapt to changing climates is vital for predicting future climate change responses, but evolution in response to contemporary climate change has rarely been observed directly. In a combined space-for-time, ...</description>
      <dc:title>Evolution of flowering phenology over 44 years of climate change</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Samantha Van DeursSimone FiorAlon SingerEinav Mayzlish-GatiJake M. Alexanderahttps://ror.org/01kwjhv40Institute of Integrative Biology, Swiss Federal Institute of Technology Zurich, Zurich CH-8092, Switzerlandbhttps://ror.org/05hbrxp80Israel Gene Bank, Agricultural Research Organization, Volcani Institute, Rishon LeZion 7505101, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-15T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613665123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613665123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620112123?af=R">
      <title>Direct activation of SARM1 by dsDNA is not supported by biochemical and cellular evidence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620112123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceSterile alpha and Toll/interleukin-1 receptor motif–containing protein 1 (SARM1) activation is sufficient to trigger the genetic axon degeneration program, making its upstream regulatory mechanisms a major focus of neurodegeneration research ...</description>
      <dc:title>Direct activation of SARM1 by dsDNA is not supported by biochemical and cellular evidence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620112123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Allison H. KaoBiswa P. MishraMitchell SorbelloWenbin ZhangQinyi ZhouYuefeng JiangVeronika MasicPaige HartenWeixi GuJian Yuan YangA. Joseph BloomRobi D. MitraZhe ZhangYong Juan ZhaoGiuseppe OrsomandoXiaodong WangJeffrey MilbrandtBostjan KobeThomas VeAaron DiAntonioaDepartment of Developmental Biology, Washington University School of Medicine, St. Louis, MO 63110bDepartment of Genetics, Washington University School of Medicine, St. Louis, MO 63110chttps://ror.org/02sc3r913Institute for Biomedicine and Glycomics, Griffith University, Gold Coast, QLD 4222, Australiadhttps://ror.org/018kjjj71School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland, Brisbane, QLD 4072, Australiaehttps://ror.org/00wksha49National Institute of Biological Sciences, Beijing 102206, Chinafhttps://ror.org/05kje8j93State Key Laboratory of Natural and Biomimetic Drugs, Department of Molecular and Cellular Pharmacology, Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, School of Pharmaceutical Sciences, Peking University, Beijing 100191, Chinaghttps://ror.org/02d5ks197Division of Biomedical Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, ChinahNeedleman Center for Neurometabolism and Axonal Therapeutics, St. Louis, MO 63110iDepartment of Clinical Sciences, Section of Biochemistry, Polytechnic University of Marche, Ancona 60131, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <title>Facial palsy reveals the sensorimotor contribution to facial-emotion recognition</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceHow do we recognize emotions from other people’s faces? A long-standing debate opposes two answers: that we match faces to learned visual patterns, or that we covertly draw on our own facial movements. Facial palsy provides a natural ...</description>
      <dc:title>Facial palsy reveals the sensorimotor contribution to facial-emotion recognition</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <dc:creator>Paola SessaArianna Schiano LomorielloThomas QuettierAntonio MaffeiSara CostaMarta NichelePier Francesco Ferrariahttps://ror.org/00240q980Department of Developmental Psychology and Socialisation, University of Padova, Padova 35131, Italybhttps://ror.org/00240q980Padova Neuroscience Center, Department of Developmental Psychology and Socialisation, University of Padova, Padova 35129, Italychttps://ror.org/02k7wn190Department of Medicine and Surgery, University of Parma, Parma 43126, ItalydIndependent Physiotherapist, Padova 35143, Italyehttps://ror.org/029brtt94Social Neuroscience and Comparative Development, Social Neuroscience and Comparative Development, Institut des Sciences Cognitives Marc Jeannerod, CNRS/Université Claude Bernard Lyon 1, Bron Cedex 69675, France</dc:creator>
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      <title>Identifiability of Bayesian models of perception</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceBayesian models represent an important class of models in cognitive science and neuroscience. The model components (prior, likelihood function, loss function) play important roles in understanding perceptual and cognitive processing. So far, ...</description>
      <dc:title>Identifiability of Bayesian models of perception</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Michael HahnEntang WangXue-Xin Weiahttps://ror.org/01jdpyv68Department of Language Science and Technology, Saarland Informatics Campus, Saarland University, Saarbrücken 66123, Germanybhttps://ror.org/00hj54h04Department of Neuroscience, The University of Texas at Austin, Austin, TX 78712chttps://ror.org/00hj54h04Department of Psychology, The University of Texas at Austin, Austin, TX 78712dhttps://ror.org/00hj54h04Center for Perceptual Systems, The University of Texas at Austin, Austin, TX 78712ehttps://ror.org/00hj54h04Center for Learning and Memory, The University of Texas at Austin, Austin, TX 78712fhttps://ror.org/00hj54h04Center for Theoretical and Computational Neuroscience, The University of Texas at Austin, Austin, TX 78712</dc:creator>
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      <title>Imaging the Meissner effect in lanthanum hydride using diamond quantum sensors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536915123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceNear-room-temperature superconductivity in hydrogen-rich materials has attracted considerable interest in recent years. However, its characterization is often hindered by the requirement for ultrahigh pressure conditions. This study extends ...</description>
      <dc:title>Imaging the Meissner effect in lanthanum hydride using diamond quantum sensors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536915123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Yang ChenJunyan WenZe-Xu HeJing-Wei FanXin-Yu PanCheng JiHuiyang GouXiaohui YuLiucheng ChenGang-Qin Liuahttps://ror.org/034t30j35Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, Chinabhttps://ror.org/05qbk4x57School of Physical Sciences, University of Chinese Academy of Sciences, Beijing 100049, Chinachttps://ror.org/02czkny70Department of Physics, Hefei University of Technology, Hefei 230601, Chinadhttps://ror.org/03wcck081Shanghai Key Laboratory of MFree, Shanghai Advanced Research in Physical Science, Shanghai 201203, ChinaeCenter for High Pressure Science and Technology Advanced Research, Beijing 100193, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <prism:doi>10.1073/pnas.2536915123</prism:doi>
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      <title>Formin-1 maintains cochlear microtubule architecture required for hearing in humans and mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622920123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceFormin proteins are critical to normal cell structures. Mutations in formin genes lead to neurologic, renal, reproductive, and cardiac disorders, but the consequences in humans of mutations in formin-1 were previously unknown. In an extended ...</description>
      <dc:title>Formin-1 maintains cochlear microtubule architecture required for hearing in humans and mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622920123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Lara KamalAmal AburayyanRoni HahnShahar TaiberSuleyman GulsunerMoien N. KanaanMary-Claire KingKaren B. Avrahamahttps://ror.org/04mhzgx49Department of Human Genetics and Computational Medicine, Gray Faculty of Medical and Health Sciences and Sagol School of Neuroscience, Tel Aviv University, Tel Aviv 6997801, Israelbhttps://ror.org/047cjg072Department of Applied Sciences, Hereditary Research Laboratory, Bethlehem University, Bethlehem P1520468, Palestinechttps://ror.org/00cvxb145Department of Medicine, University of Washington, Seattle, WA 98195-7720dhttps://ror.org/00cvxb145Department of Genome Sciences, University of Washington, Seattle, WA 98195-5065</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <prism:doi>10.1073/pnas.2622920123</prism:doi>
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      <title>IID432, a parasite-selective topoisomerase II inhibitor, achieves rapid single-dose parasite clearance in a murine chronic Chagas model</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620085123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceChagas disease remains one of the most neglected parasitic infections of the Americas, with current treatments requiring months of dosing and frequently abandoned due to side effects. Patients have long needed a shorter, safer cure. Here, we ...</description>
      <dc:title>IID432, a parasite-selective topoisomerase II inhibitor, achieves rapid single-dose parasite clearance in a murine chronic Chagas model</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620085123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-09T07:00:00Z</dc:date>
      <dc:creator>Manuel SaldiviaRajiv S. JumaniBryanna ThomasGrace M. BaxleyJayant SanchetiDomenico BullaraJean-Rene GalarneauHarry CheungYen-Liang ChenReginara Souza DeAsisDebjani PatraOlivier RenéJonas NoeskeAndreas D. SchenkColin DenistonSamarth ThakoreCatherine LuuCharles WartchowDennis C. KoesterAmanda Fortes FranciscoJohanne BlaisJan JiricekScott A. HollingsworthJonathan E. GableJohn M. KellyNatasha HochbergCharlie G. KnutsonSuresh B. LakshminarayanaChristopher SarkoUjjini H. ManjunathaColin S. OsborneThierry T. DiaganaSrinivasa P. S. RaoaGlobal Health, Biomedical Research, Novartis, Emeryville, CA 94608bPharmacokinetic Sciences, Novartis Healthcare Private Limited, Hyderabad 500081, IndiacModeling and Simulation, Biomedical Research, Novartis, Cambridge, MA 02139dPreclinical Safety, Biomedical Research, Novartis, Cambridge, MA 02139eGlobal Discovery Chemistry, Biomedical Research, Novartis Pharma AG, Emeryville, CA 94608fMolecular Discovery Science, Biomedical Research, Novartis, Emeryville, CA 94608gProtein Sciences, Biomedical Research, Novartis, Basel CH 4056, SwitzerlandhStructural Biologics, Biomedical Research, Novartis, La Jolla, CA 92121ihttps://ror.org/00a0jsq62London School of Hygiene and Tropical Medicine, London WC1E 7HT, United KingdomjComputational Chemistry, Biomedical Research, Novartis, Emeryville, CA 94608kTranslational Medicine, Discovery and Profiling, Biomedical Research, Novartis, Cambridge, MA 02139lPharmacokinetic Sciences, Biomedical Research, Novartis, Cambridge, MA 02139mPharmacokinetic Sciences, Biomedical Research, Novartis, Emeryville, CA 94608</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <prism:doi>10.1073/pnas.2620085123</prism:doi>
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      <title>Integrating tumor–immune mechanistic modeling with transcriptomics reveals pattern-driven prognostic biomarkers in tumors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532976123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;SignificanceThe spatial interplay between tumor and immune cells in the tumor microenvironment is a critical yet poorly understood determinant of cancer progression and treatment response. This study bridges a key gap in cancer systems biology by ...</description>
      <dc:title>Integrating tumor–immune mechanistic modeling with transcriptomics reveals pattern-driven prognostic biomarkers in tumors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532976123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Ke QiSuoqin JinHan MaTengfei WangYijun LouQing NieXiufen Zouahttps://ror.org/033vjfk17School of Mathematics and Statistics, Wuhan University, Wuhan 430072, Chinabhttps://ror.org/0030zas98Department of Applied Mathematics, Hong Kong Polytechnic University, Hong Kong 999077, Chinachttps://ror.org/04gyf1771National Science Foundation–Simons Center for Multiscale Cell Fate Research, University of California, Irvine, CA 92697dhttps://ror.org/04gyf1771Department of Developmental and Cell Biology, University of California, Irvine, CA 92697ehttps://ror.org/04gyf1771Department of Mathematics, University of California, Irvine, CA 92697</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <prism:doi>10.1073/pnas.2532976123</prism:doi>
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      <title>Illusory early-warning signals of Greenland Ice Sheet destabilization</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2623190123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;Interannual variability of surface mass balance over the Greenland Ice Sheet has been increasing, which has been cited as an early-warning signal of ice sheet destabilization under current climatic conditions. A destabilized ice sheet would continue to ...</description>
      <dc:title>Illusory early-warning signals of Greenland Ice Sheet destabilization</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623190123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Alexander A. RobelGrant HollyAminat A. Ambelorunahttps://ror.org/01zkghx44School of Earth and Atmospheric Sciences, Georgia Institute of Technology, Atlanta, GA 30318</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
      <prism:coverDate>2026-09-15T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2623190123</prism:doi>
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      <title>Reading the ribosome critically: A palindrome hypothesis and the limits of molecular inference</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624727123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>Reading the ribosome critically: A palindrome hypothesis and the limits of molecular inference</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624727123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Anton S. Petrovahttps://ror.org/01zkghx44National Aeronautics and Space Administration, Center for Integration of the Origins of Life, Georgia Institute of Technology, Atlanta, GA 30332bhttps://ror.org/01zkghx44School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <prism:doi>10.1073/pnas.2624727123</prism:doi>
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      <title>Exploring the unseen dimensions of olfaction via human perception and AI</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625648123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>Exploring the unseen dimensions of olfaction via human perception and AI</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625648123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Pritish Kumar VaradwajaCentre for Cognitive Computing, Department of Applied Sciences, Indian Institute of Information Technology, Allahabad 211012, India</dc:creator>
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      <prism:number>37</prism:number>
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      <title>Structural coloration in the red seaweed, Chondrus crispus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624731123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>Structural coloration in the red seaweed, Chondrus crispus</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>David S. Domozychahttps://ror.org/04nzrzs08Department of Biology, Skidmore College, Saratoga Springs, NY 12866</dc:creator>
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      <prism:number>37</prism:number>
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      <title>Disproportionality analysis to investigate fatal adverse events with immune checkpoint inhibitors: Proceed with extreme caution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608648123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>Disproportionality analysis to investigate fatal adverse events with immune checkpoint inhibitors: Proceed with extreme caution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608648123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Bruno RevolCharles KhouriEmanuel Raschiahttps://ror.org/02rx3b187Pharmacovigilance Department, Centre Hospitalier Universitaire Grenoble Alpes, Université Grenoble Alpes, Grenoble 38043, Francebhttps://ror.org/02rx3b187Inserm U1300, Hypoxie Physiopathologie Lab, Université Grenoble Alpes, Grenoble 38700, Francechttps://ror.org/01111rn36Department of Medical and Surgical Sciences, Alma Mater Studiorum–University of Bologna, Bologna 40126, Italy</dc:creator>
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      <prism:volume>123</prism:volume>
      <prism:number>37</prism:number>
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      <title>PFAS-defined liquid crystal monomers: An overlooked class of organofluorine contaminants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625255123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. &lt;br/&gt;</description>
      <dc:title>PFAS-defined liquid crystal monomers: An overlooked class of organofluorine contaminants</dc:title>
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