<?xml version="1.0" encoding="UTF-8" standalone="no"?><rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns="http://purl.org/rss/1.0/" xmlns:cc="http://web.resource.org/cc/" xmlns:content="http://purl.org/rss/1.0/modules/content/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:prism="http://prismstandard.org/namespaces/basic/2.0/">
   <channel rdf:about="https://www.pnas.org/loi/pnas?af=R">
      <title>Proceedings of the National Academy of Sciences Most-Read Full-Text Articles</title>
      <description></description>
      <link>https://www.pnas.org/loi/pnas?af=R</link>
      <dc:title>Proceedings of the National Academy of Sciences: Proceedings of the National Academy of Sciences: Table of Contents</dc:title>
      <dc:publisher>Proceedings of the National Academy of Sciences</dc:publisher>
      <dc:language>en-US</dc:language>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <items>
         <rdf:Seq>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/iti3426123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2616897123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2624553123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601685123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604191123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537942123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603552123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2532739123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2522360123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603458123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536892123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605816123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2611580123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607702123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2600647123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2616584123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604725123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610235123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2600215123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617912123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2615884123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603905123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2503559123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2613782123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2618057123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534361123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610907123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2527702123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605305123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602410123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2527860123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536343123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528342123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528506123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2600891123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2614472123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617943123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537388123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612072123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605763123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536998123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610136123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531697123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534903123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610782123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603853123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2533429123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2533465123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607117123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2522958123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2527470123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612884123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2504068123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535939123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607072123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2611013123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607561123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2614314123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2622262123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606216123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606983123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604642123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2533109123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2619778123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610398123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612355123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601204123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2523784123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537018123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2608091123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2616934123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2608998123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612340123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2530122123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617376123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606669123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602779123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607359123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2611441123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2520063123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601643123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617990123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2610388123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2621879123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2622914123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2620768123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612932123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2627119123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2625637123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2626818123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2627895123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2626420123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2626815123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2627297123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617958123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2626100123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2627721123?af=R"/>
         </rdf:Seq>
      </items>
   </channel>
   <image rdf:about="https://www.pnas.org/cms/asset/433b8ee2-291a-4032-a821-9a689e8fcaa8/default_cover.png">
      <title>Proceedings of the National Academy of Sciences</title>
      <url>https://www.pnas.org/cms/asset/433b8ee2-291a-4032-a821-9a689e8fcaa8/default_cover.png</url>
      <link>https://www.pnas.org/loi/pnas?af=R</link>
   </image>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/iti3426123?af=R">
      <title>In This Issue</title>
      <link>https://www.pnas.org/doi/abs/10.1073/iti3426123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
      <dc:identifier>doi:10.1073/iti3426123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-25T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/iti3426123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/iti3426123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616897123?af=R">
      <title>Autoantibodies neutralizing type I interferons underlie a third of cases of Chikungunya virus encephalitis or myelitis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616897123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceChikungunya virus (CHIKV) infection results in life-threatening central nervous system (CNS) complications in rare cases. We found that autoantibodies neutralizing type I interferons underlie severe CNS CHIKV infection in 35% of the patients ...</description>
      <dc:title>Autoantibodies neutralizing type I interferons underlie a third of cases of Chikungunya virus encephalitis or myelitis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616897123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Vu L. TranAdrian GervaisMarie-Mechtilde ChampeauxMaria Paula de Souza SampaioSylvie AbelIsabelle CalmontMateus Santana do RosarioLaire SchidlowskiJordan D. SimionePedro Augusto AlvesAnne PuelPaul BastardLaurent AbelCarolina PrandoRafael Freitas de Oliveira FrancaIsadora Cristina de SiqueiraAndré CabiéAurélie CobatShen-Ying ZhangJean-Laurent Casanovaahttps://ror.org/0420db125St. Giles Laboratory of Human Genetics of Infectious Diseases, The Rockefeller University, New York, NY 10065bLaboratory of Human Genetics of Infectious Diseases, Necker Branch, INSERM U1163, Necker Hospital for Sick Children, Paris 75015, Francechttps://ror.org/05rq3rb55Imagine Institute, Paris Cité University, Paris 75015, FrancedLaboratório de Investigação em Saúde Global e Doenças Negligenciadas, Instituto Gonçalo Moniz, Fiocruz-Bahia, Salvador 40296-710, BrazileCaribbean Clinical Investigation Center, INSERM 2504, University Hospital of Martinique, Fort-de-France 97200, FrancefInfectious Diseases and Tropical Medicine Unit, University Hospital of Martinique, Martinique 97200, Franceghttps://ror.org/051escj72Pathogenesis and Control of Chronic and Emerging Infections, University of Montpellier, INSERM, University of the Antilles, Fort-de-France 97200, FrancehFaculdades Pequeno Príncipe, Rebouças, Curitiba, Paraná 80230-020, BraziliInstituto de Pesquisa Pelé Pequeno Príncipe, Água Verde, Curitiba, Paraná 80250-060, BraziljLaboratório de Imunologia de Doenças Virais, Instituto René Rachou, Fiocruz Minas, Belo Horizonte, Minas Gerais 30190-002, BrazilkPediatric Hematology-Immunology and Rheumatology Unit, Necker Hospital for Sick Children, Assistance Publique-Hôpitaux de Paris, Paris 75015, FrancelHospital Pequeno Príncipe, Água Verde, Curitiba, Paraná 80250-060, Brazilmhttps://ror.org/04jhswv08Plataforma de Pesquisa em Medicina Translacional, Fundação Oswaldo Cruz-Fiocruz São Paulo, Ribeirão Preto, São Paulo 14049-900, BrazilnHHMI, New York, NY 10065</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616897123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616897123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2624553123?af=R">
      <title>Peter H. Raven: Botanist, evolutionary biologist, and biodiversity champion</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624553123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;Peter H. Raven was a transformative leader whose influence extended far beyond his own research. From a precocious childhood passion for natural history to landmark contributions to coevolution, ecological speciation, biogeography, and botanical ...</description>
      <dc:title>Peter H. Raven: Botanist, evolutionary biologist, and biodiversity champion</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624553123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Jonathan B. LososGeorge B. JohnsonBarbara A. SchaalaDepartment of Biology, Washington University, Saint Louis, MO 63130</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2624553123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2624553123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601685123?af=R">
      <title>Hydrogen-ready infrastructure risks new carbon lock-in</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601685123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Hydrogen-ready infrastructure risks new carbon lock-in</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601685123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Hongfang LuTong GuoZhenhua RuiY. Frank Chengahttps://ror.org/05nqg3g04State Key Laboratory of Advanced Marine Materials, Ningbo Institute of Materials Technology and Engineering, Chinese Academy of Sciences, Ningbo 315201, ChinabSchool of Civil Engineering, Southeast University, Nanjing 210096, ChinacCollege of Geophysics, China University of Petroleum (Beijing), Beijing 102249, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601685123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601685123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604191123?af=R">
      <title>White-matter functional connectivity uniquely predicts brain age, cognition, and psychopathology beyond gray-matter connectivity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604191123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAlthough functional signals have been detected in human white matter (WM), whether functional connectivity (FC) involving WM contributes information beyond gray-matter FC remains unclear. Across multiple independent cohorts, we show that white-...</description>
      <dc:title>White-matter functional connectivity uniquely predicts brain age, cognition, and psychopathology beyond gray-matter connectivity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604191123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-10T07:00:00Z</dc:date>
      <dc:creator>Jing CongShaoling ZhaoHaoshu XuXiaoyu XuChao LiHongming LiTing XuYang LiHang YangZaixu Cuiahttps://ror.org/022k4wk35State Key Laboratory of Cognitive Neuroscience and Learning, Beijing Normal University, Beijing 100875, Chinabhttps://ror.org/02drdmm93Beijing Institute for Brain Research, Chinese Academy of Medical Sciences &amp; Peking Union Medical College, Beijing 102206, Chinachttps://ror.org/029819q61Chinese Institute for Brain Research, Beijing 102206, Chinadhttps://ror.org/0220qvk04School of Nursing, Shanghai Jiao Tong University, Shanghai 200025, Chinaehttps://ror.org/02v51f717Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, Chinafhttps://ror.org/013meh722Department of Applied Mathematics and Theoretical Physics, University of Cambridge, Cambridge CB3 0WA, United Kingdomghttps://ror.org/013meh722Department of Clinical Neurosciences, University of Cambridge, Cambridge CB3 0WA, United Kingdomhhttps://ror.org/00b30xv10Department of Radiology, University of Pennsylvania, Philadelphia, PA 19104ihttps://ror.org/01bfgxw09Center for the Integrative Developmental Neuroscience, Child Mind Institute, New York, NY 10022</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604191123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604191123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537942123?af=R">
      <title>Genomic signatures of dairy adaptation in Saccharomyces cerevisiae from traditional Yaghnob goat-cheese fermentation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537942123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe yeastSaccharomyces cerevisiae, known for its role in wine, bread, and beer fermentation, has also been found to participate in cheese fermentation. Genomic sequencing and assembly of a set of strains isolated from traditional goat ...</description>
      <dc:title>Genomic signatures of dairy adaptation in Saccharomyces cerevisiae from traditional Yaghnob goat-cheese fermentation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537942123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-10T07:00:00Z</dc:date>
      <dc:creator>Marina BambiAhmed El GoutbiMonica Di PaolaMatilda BelliniBenedetta CerasuoloMaria Angela DiromaPaola MattarelliStefano NenciariniChiara NataliAntonio Clemente Domenico PanainoMatteo RamazzottiIrene StefaniniDuccio Cavalieriahttps://ror.org/048tbm396Department of Life Sciences and Systems Biology, University of Turin, 10123 Turin, Italybhttps://ror.org/04jr1s763Department of Biology, University of Florence, Sesto Fiorentino, Florence 50019, Italychttps://ror.org/01111rn36Department of Agricultural and Food Sciences, University of Bologna, 40127 Bologna, Italydhttps://ror.org/01111rn36Department of Cultural Heritage, University of Bologna, 48121 Bologna, Italyehttps://ror.org/04jr1s763Department of Experimental and Clinical Biomedical Sciences, University of Florence, Florence 501340, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537942123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537942123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603552123?af=R">
      <title>Structural rearrangements of PDGFRβ in the membrane upon activation by the viral oncoprotein E5</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603552123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThis work uncovers the molecular details by which the short viral oncoprotein, E5 from bovine papillomavirus, hijacks the platelet-derived growth factor receptor β (PDGFRβ) without any ligand. Using solid-state15N-NMR spectroscopy we ...</description>
      <dc:title>Structural rearrangements of PDGFRβ in the membrane upon activation by the viral oncoprotein E5</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603552123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Sebastian OtteniDirk WindischColin ZieglerStephan L. GrageParvesh WadhwaniSergii AfoninNermin KaraVioletta SchneiderThilo MastTorsten H. WaltherAnne S. Ulrichahttps://ror.org/04t3en479Institute of Organic Chemistry, Karlsruhe Institute of Technology, Karlsruhe 76131, Germanybhttps://ror.org/04t3en479Institute of Biological Interfaces-2, Karlsruhe Institute of Technology, Karlsruhe 76021, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603552123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603552123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532739123?af=R">
      <title>Brassinosteroid-regulated transcription factors confer epigenetic changes that repress plant immunity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532739123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceSteroid hormones are powerful regulators of growth but also act as potent suppressors of immunity, with well-established clinical applications, for example in treating autoimmune diseases in humans. In plants, the steroid hormones ...</description>
      <dc:title>Brassinosteroid-regulated transcription factors confer epigenetic changes that repress plant immunity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532739123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Veronica E. RamirezHaiwei ShuaiFang-Yu HwuRashmi R. HazarikaChia-Nan TaoSera ChoiRobert S. PiecykSusanne I. WudyMichael GiglJohannes W. BagnoliSarah BrajkovicPablo AlbertosYuanyuan LiangAndreas KeymerCorinna DawidWolfgang EnardA. Corina VlotCaroline GutjahrMartin ParniskeBernhard KusterTobias SiebererChristina LudwigCyril ZipfelJurriaan TonFrank JohannesBrigitte Poppenbergerahttps://ror.org/02kkvpp62Biotechnology of Horticultural Crops, School of Life Sciences, Technical University of Munich, Freising 85354, Germanybhttps://ror.org/05591te55Faculty of Biology-Genetics, Ludwig-Maximilians-Universität-München, Martinsried 82152, Germanychttps://ror.org/02kkvpp62Plant Epigenomics, School of Life Sciences, Technical University of Munich, Freising 85354, Germanydhttps://ror.org/05krs5044School of Biosciences, Plants, Photosynthesis and Soil Cluster, University of Sheffield, Sheffield S10 2TN, United Kingdomehttps://ror.org/02crff812Department of Plant and Microbial Biology, University of Zurich, Zurich 8008, Switzerlandfhttps://ror.org/02kkvpp62Bavarian Center for Biomolecular Mass Spectrometry, School of Life Sciences, Technical University of Munich, Freising 85354, Germanyghttps://ror.org/02kkvpp62Chemosensory Food Systems, School of Life Sciences, Technical University of Munich, Freising 85354, Germanyhhttps://ror.org/05591te55Anthropology and Human Genomics, Faculty of Biology, Ludwig-Maximilians-Universität-München, Martinsried 82152, Germanyihttps://ror.org/02kkvpp62Chair of Proteomics and Bioanalytics, School of Life Sciences, Technical University of Munich, Freising 85354, Germanyjhttps://ror.org/02kkvpp62Plant Genetics, School of Life Sciences, Technical University of Munich, Freising 85354, Germanykhttps://ror.org/02kkvpp62Leibniz Institute for Food Systems Biology at the Technical University of Munich, Freising 85354, Germanylhttps://ror.org/0234wmv40Crop Plant Genetics, Faculty of Life Sciences: Food, Nutrition and Health, University of Bayreuth, Kulmbach 95326, Germanymhttps://ror.org/01fbde567Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm 14476, Germanynhttps://ror.org/02kkvpp62Plant Growth Regulation, School of Life Sciences, Technical University of Munich, Freising 85354, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532739123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532739123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522360123?af=R">
      <title>Exploiting the CXCR3/CXCL10 axis overrides tumor immune suppression by enhancing immune trafficking and effector cell priming in HNSCC</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522360123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceIntratumoral (IT) delivery of CXCL10 suppresses tumor growth and recurrence in murine models of head and neck squamous cell carcinoma by boosting recruitment of CD8+T, CD4+T, and NK cells into the tumor microenvironment. However, it does ...</description>
      <dc:title>Exploiting the CXCR3/CXCL10 axis overrides tumor immune suppression by enhancing immune trafficking and effector cell priming in HNSCC</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522360123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Cheyanne K. ShinnRobert Saddawi-KonefkaCatherina L. SalangaShiruyeh SchokrpurJ. Silvio GutkindTracy M. Handelahttps://ror.org/0168r3w48Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, CA 92093bhttps://ror.org/0168r3w48Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093chttps://ror.org/0168r3w48Moores Cancer Center, University of California, San Diego, La Jolla, CA 92093dhttps://ror.org/0168r3w48Department of Otolaryngology-Head and Neck Surgery, University of California, San Diego, La Jolla, CA 92093ehttps://ror.org/0168r3w48Gleiberman Head and Neck Cancer Center, University of California, San Diego, La Jolla, CA 92093</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522360123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522360123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603458123?af=R">
      <title>Neonatal diethylstilbestrol exposure disrupts uterine epithelial apical–basal polarity and partial EMT state</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603458123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceUterine development is strongly impacted by brief exposure to estrogenic endocrine disruptors, but it is unclear what mechanisms explain why development is such a sensitive time point. This study employed multiomic analysis to identify cell ...</description>
      <dc:title>Neonatal diethylstilbestrol exposure disrupts uterine epithelial apical–basal polarity and partial EMT state</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603458123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Rachel E. BainbridgeWendy N. JeffersonTianyuan WangSara A. GrimmCarmen J. Williamsahttps://ror.org/00j4k1h63Reproductive and Developmental Biology Laboratory, National Institute of Environmental Health Sciences, NIH, Durham, NC 27709bhttps://ror.org/00j4k1h63Biostatistics and Computational Biology Branch, National Institute of Environmental Health Sciences, NIH, Durham, NC 27709</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603458123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603458123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536892123?af=R">
      <title>The 1820 Mallorca plague was not a classic bubonic outbreak</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536892123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceUnderstanding how plague spread in the centuries before bacteriology requires integrating historical evidence with modern analytical tools. This study reevaluates the 1820 Mallorca outbreak using historical daily data and Bayesian ...</description>
      <dc:title>The 1820 Mallorca plague was not a classic bubonic outbreak</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536892123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Pedro PuigJoana Maria Pujadas-Moraahttps://ror.org/052g8jq94Departament de Matemàtiques, Universitat Autònoma de Barcelona, Cerdanyola del Vallés 08193, Spainbhttps://ror.org/020s51w82Centre de Recerca Matemàtica, Cerdanyola del Vallés 08193, Spainchttps://ror.org/01f5wp925Departament d’Arts i Humanitats, Universitat Oberta de Catalunya, Barcelona 08018, Spaindhttps://ror.org/02dm87055Historical Demography Unit, Centre d’Estudis Demogràfics, Cerdanyola del Vallés 08193, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536892123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536892123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605816123?af=R">
      <title>VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605816123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAll organisms performing oxygenic photosynthesis rely on thylakoid membranes to capture light and produce oxygen. Yet these membranes are highly susceptible to environmental stress, particularly excess light, which causes oxidative damage to ...</description>
      <dc:title>VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605816123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Pamela VetranoKelsey KrallLaura MartinezEleonora TraversoTomas MorosinottoNicholas A. T. IrwinYuval MazorSilvia Ramundoahttps://ror.org/03anc3s24Gregor Mendel Institute, Austrian Academy of Sciences, Vienna BioCenter, Vienna 1030, Austriabhttps://ror.org/05n3x4p02Vienna BioCenter PhD Program, Doctoral School of the University of Vienna and Medical University of Vienna, Vienna 1030, AustriacBiodesign Institute, https://ror.org/03efmqc40School of Molecular Sciences, Arizona State University, Tempe, AZ 85281dhttps://ror.org/00240q980Dipartimento di Biologia, Università di Padova, Padova 35131, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605816123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605816123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611580123?af=R">
      <title>4000-year-old painted plaque from Southeast Indonesia reveals Austronesian Painting Tradition preceded Neolithic pottery</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611580123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe dispersal of the Austronesian language family was the most widespread human migration in prehistory. Excavations on Wetar island in southern Indonesia reveal a 4000-y-old plaque painted with a sun-ray motif, showing the early establishment ...</description>
      <dc:title>4000-year-old painted plaque from Southeast Indonesia reveals Austronesian Painting Tradition preceded Neolithic pottery</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611580123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Sue O’ConnorShimona KealyHendri A. F. KaharudinEmily NutmanLucas WattimenaMuhammad Lanang AdiyatmaDevi Mustika SariYuni SuniartiMahirta Marlon N. R. RirimasseSofia C. Samper CarroCeri ShiptonaDepartment of Archaeology and Natural History, School of Culture, History, and Language, College of Asia and the Pacific, The Australian National University, Canberra, ACT 2601, AustraliabRijang Research Indonesia, Sleman, Yogyakarta 55581, Indonesiachttps://ror.org/02hmjzt55Pusat Riset Arkeologi Lingkungan, Maritim, dan Budaya Berkelanjutan, Organisasi Riset Arkeologi, Bahasa, dan Sastra, Badan Riset dan Inovasi Nasional, Jakarta 10340, Indonesiadhttps://ror.org/03ke6d638Departmen Arkeologi, Fakultas Ilmu Budaya, Universitas Gadjah Mada, Yogyakarta 55281, Indonesiaehttps://ror.org/02jx3x895Institute of Archaeology, University College London, London WC1H 0PY, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611580123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611580123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607702123?af=R">
      <title>A peripheral carboxysome component regulates cyanobacterial glycogen deposition</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607702123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCarboxysomes are among the best-studied bacterial microcompartments with well-defined roles in specifying a subcellular microenvironment to promote the carbon-fixation reactions of photosynthesis. Here, we provide evidence that a previously ...</description>
      <dc:title>A peripheral carboxysome component regulates cyanobacterial glycogen deposition</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607702123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Joshua S. MacCreadyDuncan M. BorenMaría Santos-MerinoLuke A. SharpeSigal Lechno-YossefJosh V. VermaasDaniel C. Ducatahttps://ror.org/05hs6h993Michigan State University - Department of Energy, Plant Research Laboratory, Michigan State University, East Lansing, MI 48824bhttps://ror.org/05hs6h993Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607702123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607702123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600647123?af=R">
      <title>The role of small Heat Shock Proteins in Trypanosoma cruzi infection and intestinal homeostasis in a Chagas disease vector</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600647123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThis study demonstrates that small Heat Shock Proteins (sHSPs) serve as critical regulators of digestive physiology and intestinal homeostasis in a Chagas disease vector. These proteins orchestrate key processes including reactive oxygen ...</description>
      <dc:title>The role of small Heat Shock Proteins in Trypanosoma cruzi infection and intestinal homeostasis in a Chagas disease vector</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600647123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Tainan C. Guedes-SilvaAna B. Walter-NunoJéssica C. T. PereiraMarianna R. FrançaFelipe A. DiasHugo D. PerdomoIsabela RamosGabriela O. Paiva-SilvaRafael D. MesquitaPedro L. Oliveiraahttps://ror.org/03490as77Laboratório de Bioquímica de Artrópodes Hematófagos, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazilbhttps://ror.org/03490as77Laboratório de Bioquímica de Insetos, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-902, Brazilchttps://ror.org/03490as77Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600647123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600647123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616584123?af=R">
      <title>Manipulation of localized excitons in CrPS4 by temperature and magnetic field</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616584123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceIn van der Waals antiferromagnets, electrons occupyingd-orbitals of transition metal ions contribute concurrently to the macroscopic spin ordering and formation of many-body electronic states. This creates complex physical systems in which ...</description>
      <dc:title>Manipulation of localized excitons in CrPS4 by temperature and magnetic field</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616584123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Dipankar JanaSwagata AcharyaAmit PawbakeDmitrii LitvinovAljoscha SollZdenek SoferClement FaugerasDimitar PashovMark van SchilfgaardeKostya S. NovoselovMarek PotemskiMaciej Koperskiahttps://ror.org/01tgyzw49Institute for Functional Intelligent Materials, National University of Singapore, Singapore 117544, Singaporebhttps://ror.org/036266993Materials, Chemical, and Computational Science Directorate, National Laboratory of the Rockies, Golden, CO 80401chttps://ror.org/02rx3b187Laboratoire National des Champs Magnetiques Intenses, UPR 3228, Centre National de la Recherche Scientifique, European Magnetic Field Laboratory, Université Grenoble Alpes, 38000 Grenoble, Francedhttps://ror.org/01tgyzw49Department of Materials Science and Engineering, National University of Singapore, Singapore 117575, Singaporeehttps://ror.org/05ggn0a85Department of Inorganic Chemistry, University of Chemistry and Technology Prague, Prague 16628, Czech Republicfhttps://ror.org/0220mzb33King’s College London, Theory and Simulation of Condensed Matter, The Strand, London WC2R 2LS, United Kingdomghttps://ror.org/00y0xnp53Center for Terahertz Research and Applications, Center for Advanced Materials and Technologies, Warsaw University of Technology, Warsaw 02-822, Polandhhttps://ror.org/01dr6c206Institute of High Pressure Physics Polish Academy of Sciences, Warsaw PL-01-142, Poland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616584123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616584123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604725123?af=R">
      <title>Unitary currents through K+ selective channelrhodopsins reveal multiple conductance states within an activated state complex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604725123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceUnderstanding the molecular function of brain neurons is a key challenge of present neuroscience with the aim to cure multiple neurological and psychiatric maladies. The methodology of optogenetics has significantly advanced the control of the ...</description>
      <dc:title>Unitary currents through K+ selective channelrhodopsins reveal multiple conductance states within an activated state complex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604725123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Klaus BenndorfRalf SchmauderPeter Hegemannahttps://ror.org/05qpz1x62Institut für Physiologie II, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Jena 07740, Germanybhttps://ror.org/01hcx6992Institute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin 10115, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604725123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604725123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610235123?af=R">
      <title>Architecture and mechanism of the human p24 cargo receptor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610235123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;Significancep24 proteins are major cargo receptors in the early secretory pathway, but how ten members of the four p24 subfamilies assemble and mediate cargo transport has remained elusive. Using structural, biochemical, and cellular analyses of the human ...</description>
      <dc:title>Architecture and mechanism of the human p24 cargo receptor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610235123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Zhengkang HuaDi ZhangMin ZhangXinlin HuChengtao KangHuanhuan SunPing YangChu QiXinyuan LinJiameng LiHongjun Yuahttps://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, Chinabhttps://ror.org/00p991c53Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Chinachttps://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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610235123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610235123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600215123?af=R">
      <title>CXCR4-targeted dual softener for inducing senescence therapy in hepatic fibrosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600215123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceLiver fibrosis is sustained by the dense extracellular matrix (ECM) produced by persistently activated hepatic stellate cells (aHSCs), which limits antifibrotic efficacy. Senescence-inducing therapy activates endogenous immune surveillance to ...</description>
      <dc:title>CXCR4-targeted dual softener for inducing senescence therapy in hepatic fibrosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600215123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Junmei MuJingwen DongJiahui ChenPanle SimaYinuo FanXunyi GongJunjie ZhouXue YangZhanwei ZhouMinjie Sunahttps://ror.org/01sfm2718Department of Pharmaceutics, National Medical Products Administration Key Laboratory for Research and Evaluation of Pharmaceutical Preparations and Excipients, State Key Laboratory of Natural Medicines, School of Pharmacy, China Pharmaceutical University, Nanjing 210009, ChinabDepartment of Radiology, Nurturing Center of Jiangsu Province for State Laboratory of Artificial Intelligence Imaging and Interventional Radiology Zhongda Hospital, Medical School, Southeast University, Nanjing 210009, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600215123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600215123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617912123?af=R">
      <title>Direct dating of 3.5 Ga biogenic carbon in a microbial mat remnant, Singhbhum Craton, India</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617912123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceKerogen, insoluble organic matter preserved in sediments, represents some of the earliest known terrestrial biosignatures which have provided important insights into the origin of life and planetary habitability. Direct dating of these ...</description>
      <dc:title>Direct dating of 3.5 Ga biogenic carbon in a microbial mat remnant, Singhbhum Craton, India</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617912123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Trisrota ChaudhuriT. Mark HarrisonElizabeth A. BellMark Van ZuilenLéna ThomasNouf Al AlawiRajat MazumderStefan V. Lalondeahttps://ror.org/00nthx533Secondary Ion Mass Spectrometer (SIMS) Laboratory, Geological Survey of India, Kolkata 700091, Indiabhttps://ror.org/046rm7j60Department of Earth, Planetary, and Space Sciences, University of California, Los Angeles, CA 90095chttps://ror.org/0566bfb96Earth, Life, Time Group, Naturalis Biodiversity Center, Leiden 2333 CR, The NetherlandsdIfremer, Research and Technological Development Unit (RDT), Plouzané F-29280, Franceehttps://ror.org/055hq4920Department of Applied Geosciences, German University of Technology in Oman, Athaibah 130, Sultanate of OmanfSchool of Natural Sciences and Engineering, Natural Institute of Advanced Studies, Indian Institute of Science Campus, Bengaluru 560012, Indiaghttps://ror.org/04pfr1b11European Institute for Marine Studies, CNRS-UMR6538 Laboratoire Géo-Océan, Plouzané 29280, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617912123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617912123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615884123?af=R">
      <title>Coreless exoplanets induced by metal–silicate miscibility</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615884123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceRocky exoplanets are generally assumed to differentiate into a silicate mantle and an iron core. Here we provide direct computational evidence that, under the extreme pressures and temperatures of exoplanet interiors, iron and silicate can ...</description>
      <dc:title>Coreless exoplanets induced by metal–silicate miscibility</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615884123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Haiyang LuoDonghao ZhengCaroline DornJie Dengahttps://ror.org/01rxvg760School of Earth Sciences and Engineering, International Center for Isotope Effects Research, State Key Laboratory of Critical Earth Material Cycling and Mineral Deposits, Nanjing University, Nanjing 210023, Chinabhttps://ror.org/00hx57361Department of Geosciences, Princeton University, Princeton, NJ 08544chttps://ror.org/01cgmpb23Institute for Particle Physics and Astrophysics, ETH Zürich, Zürich 8093, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615884123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615884123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603905123?af=R">
      <title>Serum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603905123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMultiple human challenge studies have shown that serum IgA titers to norovirus correlate with protection against norovirus-associated gastroenteritis; however, the molecular and structural basis of polyclonal serum IgA responses remains poorly ...</description>
      <dc:title>Serum IgA proteomics reveals clonal composition and neutralization of dimeric and monomeric IgA repertoires against human norovirus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603905123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Juyeon ParkGyunghee JoYaoska ReyesWhitney PickensDae Sung KimAlexandra BeaverVerónica P. CostantiniChang LiuDaeun KimDaechan ParkVictoria LongoPaul D. Brewer-JensenMichael L. MalloryEd SatterwhiteRocio Zapata-BustosJeffrey MarchioniMark R. ZweigartBecca A. FlitterJan VinjéJulianna HanTed M. RossJiwon LeeJason J. LavinderSean N. TuckerZunlong KeAndrew B. WardLisa C. LindesmithRalph S. BaricGeorge Georgiouahttps://ror.org/00hj54h04Department of Chemical Engineering, The University of Texas at Austin, Austin, TX 78712bhttps://ror.org/00hj54h04Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712chttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037dhttps://ror.org/0130frc33Department of Epidemiology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599ehttps://ror.org/00hj54h04Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712fDivision of Viral Diseases, Centers for Disease Control and Prevention, Atlanta, GA 30329ghttps://ror.org/04h9pn542Institute of Chemical Processes, Seoul National University, Seoul 08826, South Koreahhttps://ror.org/03tzb2h73Ajou Energy Science Research Center, Ajou University, Suwon 16499, South Koreaihttps://ror.org/03tzb2h73Department of Molecular Science and Technology, Advanced College of Bio-Convergence Engineering, Ajou University, Suwon 16499, South KoreajVaxart, Inc., South San Francisco, CA 94080kCenter for Vaccines and Immunology, The University of Georgia, Athens, GA 30602lhttps://ror.org/03xjacd83Florida Research and Innovation Center, Cleveland Clinic, Port Saint Lucie, FL 34987mDepartment of Infectious Diseases, The University of Georgia, Athens, GA 30602nhttps://ror.org/03xjacd83Department of Infection Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44106ohttps://ror.org/049s0rh22Thayer School of Engineering, Dartmouth College, Hanover, NH 03755pDepartment of Convergence Medicine, Korea University College of Medicine, Seoul 02841, Republic of KoreaqVaccine Innovation Center, Korea University College of Medicine, Seoul 02841, Republic of Korearhttps://ror.org/00hj54h04LaMontagne Center for Infectious Diseases, The University of Texas at Austin, Austin, TX 78712</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603905123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603905123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2503559123?af=R">
      <title>Electromechanical activation and recovery wave imaging for pediatric mitral valve disease characterization</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2503559123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceSudden cardiac death is a major risk in mitral valve (MV) disease, often driven by abnormal electrical activity. Arrhythmogenic MV disease remains challenging to diagnose and treat due to a limited understanding of how valvular mechanics ...</description>
      <dc:title>Electromechanical activation and recovery wave imaging for pediatric mitral valve disease characterization</dc:title>
      <dc:identifier>doi:10.1073/pnas.2503559123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Melina TourniChristina ProestakiSeungyeon Julia HanJohanna B. TonkoMary KucinskiRachel WeberRosalia MinyetyYaffa WolickiYoussef A. ElnabawiAikaterini AfentouliJad El HarakeCagla OzsoyHannah SchleiferLeonardo LibermanAlexandra ChanningElisa E. Konofagouahttps://ror.org/00hj8s172Department of Biomedical Engineering, Columbia University, New York, NY 10027bhttps://ror.org/02jx3x895Institute for Cardiovascular Science, University College London, London WC1E 6DD, United Kingdomchttps://ror.org/00hj8s172Department of Radiology, Columbia University, New York, NY 10032dhttps://ror.org/01esghr10Division of Cardiology, Columbia University Irving Medical Center, New York, NY 10032ehttps://ror.org/01esghr10Department of Pediatric Cardiology, Columbia University Irving Medical Center, New York, NY 10032fhttps://ror.org/00hj8s172Department of Neurological surgery, Columbia University, New York, NY 10032</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2503559123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2503559123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613782123?af=R">
      <title>Ingested plastics reduce recruitment and survival of an Australian seabird</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613782123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceEstablishing the relationship between the ingestion of plastics by marine wildlife and population-level impacts is a priority but has proven challenging due to the complex data requirements. Using a globally unique, long-term dataset, we ...</description>
      <dc:title>Ingested plastics reduce recruitment and survival of an Australian seabird</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613782123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Jennifer L. LaversHannah WorthingtonAlexander L. Bondahttps://ror.org/00wfvh315Gulbali Institute, Charles Sturt University, Wagga Wagga, NSW 2678, AustraliabBird Group, The Natural History Museum, Tring HP23 6AP, United KingdomcAdrift Lab, Underwood, TAS 7268, Australiadhttps://ror.org/02wn5qz54School of Mathematics and Statistics, University of St Andrews, St Andrews KY16 9SS, United Kingdomehttps://ror.org/02wn5qz54Centre for Research into Ecological and Environmental Modelling, University of St Andrews, St Andrews KY16 9LZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613782123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613782123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618057123?af=R">
      <title>Host DNA repair factors empower a mechanism of antiviral nucleoside analog resistance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618057123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceNucleoside analogues, such as ganciclovir, a leading drug for preventing and treating human cytomegalovirus, are a critical defense against viral diseases. However, antiviral resistance often results in treatment failures. This study reveals a ...</description>
      <dc:title>Host DNA repair factors empower a mechanism of antiviral nucleoside analog resistance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618057123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Pierce LongmireHan ChenDavid R. McKinzeyMamata SavanagouderNoelle N. KosarekJean M. PesolaCarly A. BobakGiovanni BoscoFelicia GoodrumDonald M. Coenahttps://ror.org/03m2x1q45Department of Immunobiology, BIO5 Institute, University of Arizona, Tucson, AZ 85721bhttps://ror.org/03m2x1q45Department of Immunobiology, University of Arizona, Tucson, AZ 85721cDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115dDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, NH 03756ehttps://ror.org/049s0rh22Research Computing and Data, Information, Technology, and Consulting, Dartmouth College, Hanover, NH 03755fDepartment of Molecular and Systems Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618057123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618057123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534361123?af=R">
      <title>A flat-band perspective on the boson peak in amorphous solids</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534361123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;The boson peak is a characteristic anomaly of amorphous solids broadly defined as a low-energy excess in the density of states and heat capacity compared to the textbook predictions of Debye theory. The origin of this anomaly has long been the subject of ...</description>
      <dc:title>A flat-band perspective on the boson peak in amorphous solids</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534361123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Shivam MahajanLong-Zhou HuangCunyuan JiangYun-Jiang WangMassimo Pica CiamarraJie ZhangMatteo Baggioliahttps://ror.org/02e7b5302Division of Physics and Applied Physics, School of Physical and Mathematical Sciences, Nanyang Technological University 50 Nanyang Avenue, Singapore 639798bhttps://ror.org/034t30j35State Key Laboratory of Nonlinear Mechanics, Institute of Mechanics, Chinese Academy of Sciences, Beijing 100190, Chinachttps://ror.org/05qbk4x57School of Engineering Science, University of Chinese Academy of Sciences, Beijing 100049, Chinadhttps://ror.org/0220qvk04School of Physics and Astronomy, Shanghai Jiao Tong University, Shanghai 200240, Chinaehttps://ror.org/0220qvk04School of Physics and Astronomy, Wilczek Quantum Center, Shanghai Jiao Tong University, Shanghai 200240, ChinafDipartimento di Scienze Fisiche, CNR–SuPerconductors, oxides and other INnovative materials and devices, Università di Napoli Federico II, Napoli I-80126, Italyghttps://ror.org/0220qvk04Institute of Natural Sciences, Shanghai Jiao Tong University, Shanghai 200240, Chinahhttps://ror.org/023hj5876State Key Laboratory of Structural Analysis, Optimization and CAE Software for Industrial Equipment, Dalian University of Technology, Dalian 116023, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534361123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534361123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610907123?af=R">
      <title>The ecology of Lyme disease: Long-term data, surprises, and a synthesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610907123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceLong-term study of ticks, pathogens, hosts, and weather in an area with endemic Lyme disease reveals that risk of human exposure is not related to the abundance of white-tailed deer or to seasonal temperature extremes. Instead, risk correlates ...</description>
      <dc:title>The ecology of Lyme disease: Long-term data, surprises, and a synthesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610907123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Richard S. OstfeldShannon L. LaDeauKelly OggenfussCharles D. CanhamMichael FargioneRaymond J. WinchcombeFelicia KeesingaCary Institute of Ecosystem Studies, Millbrook, NY 12545bhttps://ror.org/04yrgt058Bard College, Program in Biology, Annandale-on-Hudson, NY 12504</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610907123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610907123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527702123?af=R">
      <title>Chronic psychosocial stress: A primary driver of sleep apnea onset in rats and humans</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527702123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceSleep apnea (SA) is a sleep-related respiratory disorder linked to severe health risks like hypertension and obesity. While the exact causes remain unclear, stress-related neurological conditions, such as anxiety, double the risk of SA. To ...</description>
      <dc:title>Chronic psychosocial stress: A primary driver of sleep apnea onset in rats and humans</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527702123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Marianne GagnonStéphanie FournierÉmilie GobeilMarie-Pier BouchardLoralie Mei GuayFrançois MarcouillerVincent JosephNatalie J. MichaelBenoit J. ArsenaultRichard Kinkeadahttps://ror.org/03gf7z214Research Center of the Québec Heart and Lung Institute, Québec, QC G1V 4G5, Canadabhttps://ror.org/04sjchr03Faculty of Pharmacy, Université Laval, Québec, QC G1V 0A6, Canadachttps://ror.org/04sjchr03Groupe de Recherche en Santé Respiratoire, Université Laval, Québec, QC, Canadadhttps://ror.org/04sjchr03Department of Pediatrics, Faculty of Medicine, Université Laval, Québec, QC G1V 0A6, Canadaehttps://ror.org/04sjchr03Department of Medicine, Faculty of Medicine, Université Laval, Québec, QC G1V 0A6, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527702123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527702123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605305123?af=R">
      <title>An ER retention motif controls the heteromeric stoichiometry of hERG1a/1b channels</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605305123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceSubunit stoichiometry is a key determinant of ion channel function, yet how defined stoichiometries are established during biogenesis remains poorly understood. Here we demonstrate that heteromeric hERG1a/1b channels assemble with a fixed 2:2 ...</description>
      <dc:title>An ER retention motif controls the heteromeric stoichiometry of hERG1a/1b channels</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605305123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Sudharsan KannanLiliana R. ErnandezGail A. Robertsonahttps://ror.org/01y2jtd41Department of Neuroscience, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI 53705</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605305123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605305123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602410123?af=R">
      <title>Structural rearrangements underlying the activation of STIM1 by ER calcium depletion</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602410123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe endoplasmic reticulum (ER) Ca2+sensor STIM1 controls store-operated calcium entry, a Ca2+signaling pathway essential for many physiological processes. Upon sensing agonist-induced depletion of ER Ca2+, a large conformational change ...</description>
      <dc:title>Structural rearrangements underlying the activation of STIM1 by ER calcium depletion</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602410123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Ruoyi QiuRichard S. Lewisahttps://ror.org/00f54p054Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602410123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602410123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527860123?af=R">
      <title>Urbanization weakens the global latitudinal diversity gradient in birds</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527860123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceOne of Earth’s most enduring ecological patterns is the dramatic increase in diversity from the poles to equator. Yet equally striking and global is the reduction in local diversity due to urbanization. We tested whether urbanization’s local ...</description>
      <dc:title>Urbanization weakens the global latitudinal diversity gradient in birds</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527860123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Jory GriffithJennifer M. SundayAnna L. Hargreavesahttps://ror.org/01pxwe438Department of Biology, McGill University, Montreal, QC H3A 1B1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527860123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527860123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536343123?af=R">
      <title>Morphogenesis of bacterial colonies in liquid crystalline environments</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536343123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMany bacteria live in environments with the characteristics of liquid crystals—fluids whose molecules are elongated and locally align in the same direction. How this alignment affects bacterial colonies remains unknown. We show that when ...</description>
      <dc:title>Morphogenesis of bacterial colonies in liquid crystalline environments</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536343123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Sebastian Gonzalez La CorteThomas G. J. ChandlerSaverio E. SpagnolieNed S. WingreenSujit S. Dattaahttps://ror.org/00hx57361Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544bhttps://ror.org/0130frc33Department of Mathematics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3250chttps://ror.org/01y2jtd41Department of Mathematics, University of Wisconsin–Madison, Madison, WI 53706dhttps://ror.org/00hx57361Department of Molecular Biology, Princeton University, Princeton, NJ 08544ehttps://ror.org/05dxps055Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125fhttps://ror.org/00hx57361Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536343123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536343123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528342123?af=R">
      <title>Initiation of rotational collective migration in Drosophila through tissue geometry and mechanochemical feedback</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528342123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCollective cell migration shapes tissues during development, closes wounds, and drives cancer invasion. When collective migration occurs in sheets of cells, called epithelia, the individual cells within the sheet must become oriented in a ...</description>
      <dc:title>Initiation of rotational collective migration in Drosophila through tissue geometry and mechanochemical feedback</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528342123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Sierra SchwabachSreejith SanthoshAudrey Miller WilliamsMaureen CeteraMattia SerraSally Horne-Badovinacahttps://ror.org/024mw5h28Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637bhttps://ror.org/0168r3w48Department of Physics, University of California, San Diego, CA 92093chttps://ror.org/024mw5h28Committee on Development, Regeneration, and Stem Cell Biology, The University of Chicago, Chicago, IL 60637</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528342123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528342123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528506123?af=R">
      <title>Marine heatwaves and undernutrition in low- and middle-income countries</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528506123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceClimate change has increased ocean temperatures as well as the frequency and intensity of unusually warm ocean waters, known as marine heatwaves. Because fish distribution and productivity can be impacted by these events, marine heatwaves ...</description>
      <dc:title>Marine heatwaves and undernutrition in low- and middle-income countries</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528506123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Clark GraySally C. DowdNoah ShaulBrian C. ThiedeJanet A. Nyeahttps://ror.org/0130frc33Department of Geography and Environment, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599bEnvironment, Ecology and Energy Program, Institute of Marine Sciences, University of North Carolina Chapel Hill, Morehead City, NC 28557cBioinformatics and Computational Biology Program, University of North Carolina Chapel Hill, Chapel Hill, NC 27599dhttps://ror.org/04p491231Department of Agricultural Economics, Sociology, and Education, The Pennsylvania State University, University Park, PA 16802eDepartment of Earth, Marine and Environmental Sciences, Institute of Marine Sciences, University of North Carolina Chapel Hill, Morehead City, NC 28557</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528506123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528506123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600891123?af=R">
      <title>The immunophenotype and proviral landscape of HIV-infected CD4 T cells during antiretroviral therapy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600891123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe persistence of HIV in CD4+ T cells during antiretroviral therapy (ART) remains a barrier to cure. To study this reservoir, we developed an open-source DAb-seq platform that sequences proviral DNA and surface epitopes in single cells and ...</description>
      <dc:title>The immunophenotype and proviral landscape of HIV-infected CD4 T cells during antiretroviral therapy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600891123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Cyrille L. DelleySakshi ShahKevin M. JoslinYujung P. ParkBenjamin DemareeMichael P. BuschMars StoneSteven G. DeeksEli A. BoritzAdam R. AbateIain C. Clarkahttps://ror.org/043mz5j54Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158bhttps://ror.org/04n1n3n22Department of Bioengineering, University of California, Berkeley, California Institute for Quantitative Biosciences, Berkeley, CA 94720chttps://ror.org/00r2ye360Vitalant Research Institute, San Francisco, CA 94105dhttps://ror.org/043mz5j54Department of Laboratory Medicine, University of California, San Francisco, CA 94158ehttps://ror.org/043mz5j54Department of Medicine, University of California, San Francisco, CA 94158fhttps://ror.org/043z4tv69Virus Persistence and Dynamics Section, Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600891123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600891123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614472123?af=R">
      <title>Expulsion of nuclear DNA to the cytoplasm after viral entry: A mechanism for activation of the cGAS pathway</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614472123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCells mount antiviral responses when they detect infection by a virus, and viruses have evolved mechanisms to resist the host responses. In this study, we have discovered a new form of host response. Upon entry of viruses that occurs by fusion ...</description>
      <dc:title>Expulsion of nuclear DNA to the cytoplasm after viral entry: A mechanism for activation of the cGAS pathway</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614472123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Nicolás RomeroHyung Suk OhMax E. MertensMaria EricssonKyle N. StearnsAnne MosconaDavid M. KnipeaDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115bElectron Microscopy Core, Department of Cell Biology, Harvard Medical School, Boston, MA 02115cDepartment of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032dCenter for Host–Pathogen Interaction, Department of Pediatrics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032eDepartment of Physiology and Cellular Biophysics, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032fDepartment of Microbiology and Immunology, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614472123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614472123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617943123?af=R">
      <title>Select intratumoral riboflavin-auxotrophic Enterococcus species enhance cell surface MR1 expression and MAIT TCR activation in lung cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617943123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMAIT cells are innate-like T cells that survey tissues through recognition of bacterially derived riboflavin metabolites presented by MHC class Irelated protein 1 (MR1), a nonclassical antigen-presenting molecule. Bacteria inside tumors may ...</description>
      <dc:title>Select intratumoral riboflavin-auxotrophic Enterococcus species enhance cell surface MR1 expression and MAIT TCR activation in lung cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617943123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Pakhi BirlaLansaol YangWanting ShanSakura MinamisawaOmkar DhaygudeHaritha ManojAlex J. LeeJacqueline FerriYing ZhengAndrew NorthcuttHongni FanHadley BeauregardZhen ZengKellie N. SmithFyza Y. ShaikhCynthia L. SearsDrew M. PardollFranck Housseauahttps://ror.org/00za53h95Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, Baltimore, MD 21205bBloomberg ~ Kimmel Institute for Cancer Immunotherapy, Johns Hopkins School of Medicine, Baltimore, MD 21205chttps://ror.org/01692sz90Department of Pathology and Oncology, Faculty of Medicine, Juntendo University, Tokyo 113-842, Japandhttps://ror.org/00za53h95Department of Mechanical Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, MD 21218ehttps://ror.org/00za53h95Department of Medicine, Division of Infectious Disease, Johns Hopkins University, Baltimore, MD 21205</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617943123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617943123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537388123?af=R">
      <title>FEMA phase-out? Catastrophic extremes challenge decentralization of US flood insurance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537388123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceFlood damages are often understood as isolated events, but they emerge as clustered losses driven by climate-variable synoptic weather regimes. Clustered losses strain insurance systems, including the U.S. National Flood Insurance Program. As ...</description>
      <dc:title>FEMA phase-out? Catastrophic extremes challenge decentralization of US flood insurance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537388123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Adam NayakMengjie ZhangPierre GentineUpmanu Lallahttps://ror.org/00hj8s172Department of Earth and Environmental Engineering, Columbia University, New York, NY 10027bhttps://ror.org/00hj8s172Columbia Water Center, Columbia Climate School, Columbia University, New York, NY 10027chttps://ror.org/00hj8s172Learning the Earth with Artificial Intelligence and Physics, National Science Foundation Science and Technology Center, Columbia University, New York, NY 10027dhttps://ror.org/03efmqc40School of Complex Adaptive Systems, College of Global Futures, Arizona State University, Tempe, AZ 85281ehttps://ror.org/03efmqc40The Water Institute, Arizona State University, Tempe, AZ 85281</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537388123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537388123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612072123?af=R">
      <title>Myoglianin coordinates hormonal and nutrient signaling to control metamorphosis and tissue growth in the fall armyworm</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612072123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe fall armyworm is a major pest whose rapid growth and development lead to significant crop losses. Understanding the biological mechanisms that control its metamorphosis could help identify new targets for pest management. This study shows ...</description>
      <dc:title>Myoglianin coordinates hormonal and nutrient signaling to control metamorphosis and tissue growth in the fall armyworm</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612072123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Xien ChenJinmo KooHyejin ParkYuchen ZhaoSubba Reddy Palliahttps://ror.org/02k3smh20Department of Entomology, College of Agriculture, Food and Environment, University of Kentucky, Lexington, KY 40546bhttps://ror.org/05ckt8b96Key Laboratory of Plant Protection Resources and Pest Management of the Ministry of Education, Key Laboratory of Integrated Pest Management on the Loess Plateau of Ministry of Agriculture and Rural Affairs, Department of Entomology, College of Plant Protection, Northwest A&amp;F University, Yangling 712100, Shaanxi, Chinachttps://ror.org/040c17130Department of Plant Medicine, Kyungpook National University, Daegu 41566, Republic of Koreadhttps://ror.org/040c17130Institute of Plant Medicine, Kyungpook National University, Daegu 41566, Republic of Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612072123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612072123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605763123?af=R">
      <title>Proliferation as a natural strategy to suppress neoplasia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605763123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCell proliferation is a routine part of tissue maintenance, but each time cells proliferate, there is a risk they acquire a mutation that could lead to cancer. In this study, we developed a mathematical framework to assess the relationship ...</description>
      <dc:title>Proliferation as a natural strategy to suppress neoplasia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605763123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Anish A. SarmaLea GoentoroJohn Doyleahttps://ror.org/05dxps055Division of Engineering and Applied Sciences, California Institute of Technology, Pasadena, CA 91125bhttps://ror.org/05dxps055Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605763123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605763123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536998123?af=R">
      <title>NatA complex is a leaf-intrinsic brake on systemic responses induced by root endophytic fungi</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536998123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificancePlants live in lifelong partnership with beneficial soil fungi that prime systemic immunity, yet how they prevent runaway defense in distant leaves has remained unknown. Here, we show that the NatA N-terminal acetyltransferase complex acts as ...</description>
      <dc:title>NatA complex is a leaf-intrinsic brake on systemic responses induced by root endophytic fungi</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536998123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Xiao-Jie ChenGu-Zi ChenYao XuZheng-Long LiYu-Meng ZhangXin-Meng ZhuZe-Ting SongFeifei YuJiang-Yun GaoJian‐Xiang LiuJia-Jia Hanahttps://ror.org/0040axw97State Key Laboratory of Vegetation Structure, Function and Construction (VegLab), Yunnan University, Kunming 650500, ChinabYunnan Key Laboratory of Biological Adaptation, Conservation and Utilization; Ministry of Education Key Laboratory for Transboundary Ecosecurity of Southwest China; Institute of Biodiversity, School of Ecology and Environmental Science, Yunnan University, Kunming 650500, Chinachttps://ror.org/0040axw97State Key Laboratory for Conservation and Utilization of Bio‐Resources in Yunnan, Yunnan University, Kunming 650500, Chinadhttps://ror.org/04v3ywz14College of Grassland Science and Technology, China Agricultural University, Beijing 100083, ChinaeState Key Laboratory of Plant Environmental Resilience, College of Life Sciences, Zhejiang University, Hangzhou 310027, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536998123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536998123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610136123?af=R">
      <title>The genetic architecture of tomato flavor variation through crop domestication and improvement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610136123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThis work advances our fundamental understanding of the impact of tomato domestication and breeding on fruit flavor chemistry, tracing the pattern of inheritance of deleterious alleles from wild accessions through to modern commercial ...</description>
      <dc:title>The genetic architecture of tomato flavor variation through crop domestication and improvement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610136123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Xiang LiDenise M. TiemanYue HuangLuis Felipe V. FerrãoManoj SapkotaZhuoliang LangAnastasiya KuhalskayaRonglin HaoPu LiuJing ChenSaleh AlseekhMarcio F. R. ResendeEsther van der KnaapXueren YinHarry J. Kleeahttps://ror.org/0327f3359School of Horticulture, Anhui Agricultural University, Hefei 230036, People’s Republic of Chinabhttps://ror.org/0327f3359State Key Laboratory for Tea Plant Germplasm Innovation and Resource Utilization, Anhui Agricultural University, Hefei 230036, People’s Republic of Chinachttps://ror.org/02y3ad647Horticultural Sciences, University of Florida, Gainesville, FL 32611-0690dhttps://ror.org/02k3smh20Department of Horticulture, University of Kentucky, Lexington, KY 40546ehttps://ror.org/01fbde567Max Planck Institute of Molecular Plant Physiology, Potsdam-Golm 14476, Germanyfhttps://ror.org/0020pnp42Center of Plant Systems Biology and Biotechnology, Plovdiv 4000, BulgariagInstitute of Plant Breeding, Genetics &amp; Genomics, University of Georgia, Athens, GA 30602hDepartment of Horticulture, University of Georgia, Athens, GA 30602</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610136123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610136123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531697123?af=R">
      <title>Group size effects and collective misalignment in LLM multi-agent systems</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531697123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceLarge language models (LLMs) are increasingly deployed in large numbers, and their interactions make collective behavior harder to anticipate than that of a single model. While most studies compare one model with a collective of fixed size, we ...</description>
      <dc:title>Group size effects and collective misalignment in LLM multi-agent systems</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531697123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Ariel FlintLuca Maria AielloRomualdo Pastor-SatorrasAndrea Baronchelliahttps://ror.org/04cw6st05Department of Mathematics, City St George’s, University of London, London EC1V 0HB, United KingdombData Science Section, IT University of Copenhagen, Copenhagen 2300, DenmarkcNetworks and Graphs Collaboratory, Pioneer Centre for AI, Copenhagen 1350, Denmarkdhttps://ror.org/03mb6wj31Departament de Física, Universitat Politècnica de Catalunya, Barcelona 08034, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531697123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531697123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534903123?af=R">
      <title>Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534903123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceProteostasis depends on the coordinated actions of Hsp70 chaperones and their diverse J-domain protein (JDP) cochaperones, yet whether these act redundantly or carry distinct cellular functions has remained unresolved. Here, we uncover that ...</description>
      <dc:title>Human Hsp70 paralogs display selective J-domain interactions tuning proteostasis under stress</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534903123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Roni SuhlerLars J. W. van BeurdenMerav D. ShmueliOfrah FaustRina Rosenzweigahttps://ror.org/0316ej306Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot 760001, Israelbhttps://ror.org/0316ej306Department of Systems Immunology, Weizmann Institute of Science, Rehovot 760001, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534903123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534903123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610782123?af=R">
      <title>An upstream open reading frame represses translation of the neuronal potassium channel KCNQ2</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610782123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceProtein synthesis is controlled by several types of regulatory features within messenger RNA (mRNA). For example, upstream open reading frames (uORFs) within the 5’-untranslated region (5’-UTR) of mRNA transcripts can regulate protein ...</description>
      <dc:title>An upstream open reading frame represses translation of the neuronal potassium channel KCNQ2</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610782123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Dalton J. HueyEduardo GuadarramaJean-Marc DeKeyserCarlos G. VanoyeChristine Q. SimmonsQianru LiEmily K. StroupZhe JiAlfred L. GeorgeaDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610782123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610782123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603853123?af=R">
      <title>A nose-to-brain circuit underlies anxiety regulation by nasal afferent frequency in mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603853123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAnxiety disorders are the most prevalent mental disorders worldwide, underscoring an urgent need for effective noninvasive therapeutic approaches. Here, we demonstrate that nasal afferent frequency alone causally and bidirectionally regulates ...</description>
      <dc:title>A nose-to-brain circuit underlies anxiety regulation by nasal afferent frequency in mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603853123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Xinsong GuoMengyan LiuQingcheng XiongHowai NgaiMingdong HeXinying LiYingwei ZhengFuqiang XuMinghong MaRuiqi WuaShanghai Pudong Hospital, Fudan University Pudong Medical Center, State Key Laboratory of Brain Function and Disorders, Ministry of Education Frontiers Center for Brain Science, Institutes of Brain Science, Fudan University, Shanghai 200032, Chinabhttps://ror.org/03ab0at74State Key Laboratory of Digital Medical Engineering, Key Laboratory of Biomedical Engineering of Hainan Province, School of Biomedical Engineering, Hainan University, Sanya 572025, ChinacJiangsu Key Laboratory of Brain Disease and Bioinformation, School of Basic Medicine Sciences, Xuzhou Medical University, Xuzhou, Jiangsu 221004, Chinadhttps://ror.org/034t30j35Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, Guangdong 518055, Chinaehttps://ror.org/00b30xv10Department of Neuroscience, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603853123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603853123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533429123?af=R">
      <title>The KAT2/HDACⅡa–PGK–ALDO axis constitutes a dual degradation inhibition cascade links energy stress to glycolytic amplification</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533429123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCells adapt to energy stress by reprogramming glycolysis, a process governed by the precise regulation of posttranslational modifications in glycolytic enzymes. Here, we uncover a metazoan-conserved signaling axis—KAT2/HDACIIa–PGK–ALDO—that ...</description>
      <dc:title>The KAT2/HDACⅡa–PGK–ALDO axis constitutes a dual degradation inhibition cascade links energy stress to glycolytic amplification</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533429123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Chaogang WangMingyang DuYutong LiuJiafeng WangZhuxiang JiangHaigang QiWei WangRihao CongGuofan ZhangLi Liahttps://ror.org/034t30j35State Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266000, ChinabLaboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266000, Chinachttps://ror.org/034t30j35Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266000, Chinadhttps://ror.org/05qbk4x57College of Marine Sciences, University of Chinese Academy of Sciences, Qingdao 266400, Chinaehttps://ror.org/04k5rxe29Stem Cell Research and Cellular Therapy Center, Affiliated Hospital of Guangdong Medical University, Zhanjiang, Guangdong 524001, ChinafNational and Local Joint Engineering Laboratory of Ecological Mariculture, Qingdao 266000, ChinagShandong Center of Technology Innovation for Oyster Seed Industry, Qingdao 266000, ChinahLaboratory for Marine Fisheries Science and Food Production Processes, Qingdao Marine Science and Technology Center, Qingdao 266000, ChinaiOyster Industrial Technology Institute of Zhanjiang, Southern Marine Science and Engineering Guangdong Laboratory (Zhanjiang), Zhanjiang 524000, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533429123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533429123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533465123?af=R">
      <title>Characterizing the impact of incorporating spatially aggregated human mobility data into infectious disease models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533465123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceInfectious disease models serve an important role in disease forecasting and outbreak response. As data on human mobility become increasingly detailed and widely used, the question of spatial scale is paramount to effectively approximating ...</description>
      <dc:title>Characterizing the impact of incorporating spatially aggregated human mobility data into infectious disease models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533465123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Ronan CorgelKyra H. GrantzLauren GardnerDerek A. T. CummingsHarendra de SilvaThilini SomaratneDhammika SilvaLakKumar FernandoAmy WesolowskiaDepartment of Epidemiology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205bDepartment of Civil and Systems Engineering, Johns Hopkins Whiting School of Engineering, Baltimore, MD 21218cDepartment of Biomedical Engineering, Johns Hopkins Whiting School of Engineering, Baltimore, MD 21218dhttps://ror.org/02phn5242Faculty of Medicine, Department of Paediatrics, University of Colombo, Colombo 00800, Sri LankaeCentre for Clinical Management of Dengue and Dengue Hemorrhagic Fever, Negombo General Hospital, Negombo 11500, Sri Lanka</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533465123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533465123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607117123?af=R">
      <title>TaIAA25 negatively regulates wheat alkaline tolerance by inhibiting plasma membrane H+-ATPase activity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607117123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceGlobal soil salinization/alkalization severely restricts crop yields by imposing high salt and high pH stress on plants. Although auxin and plasma membrane (PM) H+-ATPase participate in alkaline tolerance, their connecting pathway remains ...</description>
      <dc:title>TaIAA25 negatively regulates wheat alkaline tolerance by inhibiting plasma membrane H+-ATPase activity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607117123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <dc:creator>Fengxiang YinMinghan CuiJianing LiuYue LiuChen ZhuLin WeiQing ZhouGuangmin XiaShuwei LiuaThe Key Laboratory of Plant Development and Environmental Adaptation Biology, Ministry of Education, Shandong Key Laboratory of Precision Molecular Crop Design and Breeding, Shandong Key Laboratory of Plant Stress Biology and Genetic Improvement, School of Life Sciences, Shandong University, Qingdao 266237, ChinabNational Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land, Dongying 257347, Chinachttps://ror.org/03x08qn04State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607117123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607117123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522958123?af=R">
      <title>A human pluripotent stem cell triculture platform to elucidate microglial regulation of retinal ganglion cells in neuroinflammation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522958123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMicroglia are critical regulators of neuroinflammation and neuronal health, yet their contributions to human retinal neurodegeneration remain poorly understood due to the lack of physiologically relevant human models. Here, we present a human ...</description>
      <dc:title>A human pluripotent stem cell triculture platform to elucidate microglial regulation of retinal ganglion cells in neuroinflammation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522958123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Jade HarkinCátia GomesReham AfifyShruti V. PatilShelby M. HetzerKaylee D. TutrowKiersten H. PeñaAaron BakerSailee S. LavekarKang-Chieh HuangJason S. Meyerahttps://ror.org/02ets8c94Department of Pharmacology and Toxicology, Indiana University School of Medicine, Indianapolis, IN 46202bhttps://ror.org/02ets8c94Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, IN 46202chttps://ror.org/02ets8c94Department of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, IN 46202dhttps://ror.org/01kg8sb98Department of Biology, Indiana University Purdue University Indianapolis, Indianapolis, IN 46202ehttps://ror.org/02ets8c94Department of Ophthalmology, Indiana University School of Medicine, Indianapolis, IN 46202</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522958123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522958123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527470123?af=R">
      <title>The dual-function enzyme PpLipO protects polar marine bacteria from phospholipid peroxidation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527470123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMembrane lipid peroxidation is a hallmark of oxidative stress that threatens cellular integrity across all domains of life. Although bacterial membranes are enriched in monounsaturated fatty acids that oxidize more slowly than eukaryotic ...</description>
      <dc:title>The dual-function enzyme PpLipO protects polar marine bacteria from phospholipid peroxidation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527470123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Yu-Zhong ZhangWen-Xin JiangXiang-Ming ZhaoJie HaoYao LuChao GaoChun-Yang LiQi-Long QinXiu-Lan ChenYin ChenPing-Yi Liahttps://ror.org/03x08qn04Marine Biotechnology Research Center, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Chinabhttps://ror.org/04rdtx186Ministry of Education Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System &amp; College of Marine Life Sciences, Ocean University of China, Qingdao 266003, Chinachttps://ror.org/041w4c980Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center &amp; Laoshan Laboratory, Qingdao 266237, Chinadhttps://ror.org/01a77tt86School of Life Sciences, University of Warwick, Coventry CV4 7AL, United Kingdomehttps://ror.org/03angcq70School of Biosciences, University of Birmingham, Birmingham B15 2TT, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527470123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527470123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612884123?af=R">
      <title>Dynamic multiphase flow triggers chaotic mixing in porous media</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612884123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceChemical and biological processes in soils, rocks, and industrial porous media are often controlled by the mixing of chemicals by fluid flow. When a single fluid phase carries dissolved chemicals through a porous medium, the mixing process is ...</description>
      <dc:title>Dynamic multiphase flow triggers chaotic mixing in porous media</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612884123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Gaute LingaKevin PierceMarcel MouraJoachim MathiesenFrançois RenardTanguy Le Borgneahttps://ror.org/01xtthb56PoreLab, The Njord Centre, Department of Physics, University of Oslo, Oslo 0316, Norwaybhttps://ror.org/05xg72x27PoreLab, Department of Physics, Norwegian University of Science and Technology, Trondheim 7491, Norwaychttps://ror.org/01xtthb56The Njord Centre, Department of Geosciences, University of Oslo, Oslo 0316, Norwaydhttps://ror.org/035b05819Niels Bohr Institute, University of Copenhagen, København N 2200, Denmarkehttps://ror.org/03x42jk29Institut des Sciences de la Terre, Université Grenoble Alpes, Université Savoie Mont Blanc, CNRS, Institut de Recherche pour le Développement, Université Gustave Eiffel, Grenoble 38000, Francefhttps://ror.org/015m7wh34Géosciences Rennes, Université de Rennes, CNRS, Unité Mixte de Recherche 6118, Rennes 35000, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612884123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612884123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2504068123?af=R">
      <title>USP14 competitively binds to FBXW7 to stabilize MTDH and promotes metastasis and drug resistance of head and neck squamous cell carcinoma</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2504068123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe metadherin (MTDH) gene encodes astrocyte elevated gene-1 (AEG-1)/lysine-rich CEACAM1 coisolated protein (LYRIC) in humans, and it is markedly upregulated in many cancer types. Our previous work has shown that MTDH contributes to head and ...</description>
      <dc:title>USP14 competitively binds to FBXW7 to stabilize MTDH and promotes metastasis and drug resistance of head and neck squamous cell carcinoma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2504068123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Xueying WangYang ZhouJiaqi TanDiekuo ZhangChao LiuJuncheng WangXin ZhangGangcai ZhuYong LiuaDepartment of Otolaryngology Head and Neck Surgery, Xiangya Hospital, Central South University, Changsha, Hunan 410008, People’s Republic of Chinabhttps://ror.org/05jb9pq57Department of Radiation Oncology, Shandong Provincial Hospital Affiliated to Shandong First Medical University, Jinan 250000, People’s Republic of ChinacOtolaryngology Major Disease Research Key Laboratory of Hunan Province, Changsha, Hunan 410008, People’s Republic of ChinadNational Clinical Research Center for Geriatric Disorders (Xiangya Hospital), Changsha, Hunan 410008, People’s Republic of ChinaeClinical Research Center for Laryngopharyngeal and Voice Disorders in Hunan Province, Changsha, Hunan 410008, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2504068123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2504068123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535939123?af=R">
      <title>Heme-binding protein CYB5D1 couples intraflagellar redox to calcium signaling for coordinated flagellar beating</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535939123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceIn this study, we focused on CYB5D1, an evolutionarily conserved, heme-binding axonemal protein that functions as a redox-sensitive switch. This protein converts redox dynamics into Ca2+-mediated mechanical dominance switching, representing a ...</description>
      <dc:title>Heme-binding protein CYB5D1 couples intraflagellar redox to calcium signaling for coordinated flagellar beating</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535939123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Yiwen LinLijuan ZhaoGai LiuXuan DengStephen M. KingKaiyao Huangahttps://ror.org/034t30j35Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, Chinabhttps://ror.org/05qbk4x57College of Life Sciences, University of Chinese Academy of Sciences, Beijing 100039, Chinachttps://ror.org/04ypx8c21School of Life Sciences, Zhengzhou University, Zhengzhou 450001, Chinadhttps://ror.org/02kzs4y22Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535939123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535939123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607072123?af=R">
      <title>Atomistic twinning process with ultra-high shear in hexagonal close-packed crystals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607072123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceOur results demonstrate that extreme stress states accessible in nanocrystals, together with favorable energetic conditions, can activate deformation modes that are inaccessible in bulk materials and absent from existing twinning theories. ...</description>
      <dc:title>Atomistic twinning process with ultra-high shear in hexagonal close-packed crystals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607072123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Yang HeDengke ChenChongmin WangTing ZhuYuyang WangBin LiScott X. Maoahttps://ror.org/01an3r305Department of Mechanical Engineering and Materials Science, University of Pittsburgh, Pittsburgh, PA 15261bhttps://ror.org/01zkghx44Woodruff School of Mechanical Engineering, Georgia Institute of Technology, Atlanta, GA 30332chttps://ror.org/05h992307Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, WA 99352dhttps://ror.org/04rswrd78Department of Manufacturing Engineering, Iowa State University, Ames, IA 50011ehttps://ror.org/02dqehb95School of Materials 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607072123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607072123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611013123?af=R">
      <title>Soft matter, hard rules: Emulsions follow the laws of granular suspension rheology</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611013123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceMany everyday materials—from mayonnaise and foams to living tissues—are made of densely packed soft particles. Predicting how these materials flow has remained a longstanding challenge because pressure changes the shape of the particles and ...</description>
      <dc:title>Soft matter, hard rules: Emulsions follow the laws of granular suspension rheology</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611013123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Wenjun ChenEric De GiuliMatthieu WyartYoël ForterreJasna BrujićBloen Metzgerahttps://ror.org/0190ak572Department of Physics, Center for Soft Matter Research, New York University, New York, NY 10003bhttps://ror.org/04bgbbh33Aix Marseille Université, CNRS, Institut Universitaire des Systémes Thermiques Industriels, Marseille 13453, Francechttps://ror.org/05g13zd79Department of Physics, Toronto Metropolitan University, Toronto, M5B 2K3, Canadadhttps://ror.org/00za53h95Department of Physics and Astronomy, Johns Hopkins University, Baltimore, MD 21218ehttps://ror.org/02s376052Institute of Physics, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne CH-1015, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611013123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611013123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607561123?af=R">
      <title>Identification of potent inhibitors of JUN N-terminal kinases for treatment of endometriosis and associated pain</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607561123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceEndometriosis is a painful and debilitating gynecological disease impacting &amp;gt;190 million women worldwide. Patients with endometriosis have few therapeutic options and often undergo repeated surgical interventions. Using DNA-encoded chemistry ...</description>
      <dc:title>Identification of potent inhibitors of JUN N-terminal kinases for treatment of endometriosis and associated pain</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607561123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Chandrashekhar MadasuTirupataiah SirupangiGenesis J. HerreraKurt M. BohrenKiran L. SharmaZhi TanHai Minh TaFei YuanMurugesan PalaniappanCaterina ClementiSuni TangAnna Catherine UnserJennifer WilkinsonMatthew B. RobersXiaoming GuanFeng LiChoel KimBanumathi SankaranRamakrishna KommaganiSrinivas ChamakuriDamian W. YoungPiraye Y. BiemMartin M. MatzukStephen S. PalmerDiana Monsivaisahttps://ror.org/02pttbw34Department of Pathology and Immunology, Baylor College of Medicine, Houston, TX 77030bhttps://ror.org/02pttbw34Center for Drug Discovery, Baylor College of Medicine, Houston, TX 77030chttps://ror.org/02pttbw34Verna and Marrs McLean, Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030dCelmatix Therapeutics, New York, NY 10006ePromega Corporation, Madison, WI 53711fhttps://ror.org/02pttbw34Department of Obstetrics and Gynecology, Baylor College of Medicine, Houston, TX 77030ghttps://ror.org/02jbv0t02Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607561123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607561123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614314123?af=R">
      <title>Regulatory logic of neuronal differentiation in the Drosophila visual system</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614314123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThis study addresses a significant gap in our understanding of how different types of neurons are genetically specified. Unique combinations of transcription factors (gene regulatory proteins) in each cell type mediate this process during ...</description>
      <dc:title>Regulatory logic of neuronal differentiation in the Drosophila visual system</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614314123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>McKenzie TreeseYen-Chung ChenAbigail TyreeRose CoyneCathleen LakeOjong Besong TabiRaghuvanshi RajeshYu-Chieh David ChenHuzaifa HassanHua LiClaude DesplanMehmet Neset Özelahttps://ror.org/04bgfm609Stowers Institute for Medical Research, Kansas City, MO 64110bhttps://ror.org/0190ak572Department of Biology, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614314123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614314123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622262123?af=R">
      <title>Neuronal overexpression of Kcnn1 in A53T α-synuclein mice suppresses phospho-serine 129 α-synuclein formation and doubles survival time</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622262123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceParkinson’s Disease and several other neurodegenerative diseases are driven by misfolding and aggregation of the neuronal protein α-synuclein. We studied a transgenic mouse model expressing the Parkinson’s-associated A53T mutant human α-...</description>
      <dc:title>Neuronal overexpression of Kcnn1 in A53T α-synuclein mice suppresses phospho-serine 129 α-synuclein formation and doubles survival time</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622262123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Maria NagyWayne A. FentonArthur L. HorwichaDepartment of Genetics, Yale School of Medicine, New Haven, CT 06510</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622262123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622262123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606216123?af=R">
      <title>Repression of ferroptotic cell death mediated antitumor immunity by mitochondrial calcium signaling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606216123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceFerroptosis is a unique type of programmed cell death caused by excessive lipid peroxidation and represents a vulnerability in certain types of cancer. However, the signaling mechanisms that modulate ferroptosis and its functional consequence ...</description>
      <dc:title>Repression of ferroptotic cell death mediated antitumor immunity by mitochondrial calcium signaling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606216123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Jianwen ChenBao ZhaoHong DongZhiwei LiaoShen WangAnjun MaYajun SunXiang ChengShengyin LinXinghui LiGang XinKai HeBei LiuYu L. LeiQin MaKymberly M. GowdyRuili XieXiaolin ChengZihai LiHaitao Wenahttps://ror.org/00rs6vg23Department of Microbial Infection and Immunity, Infectious Disease Institute, The Ohio State University, Columbus, OH 43210bhttps://ror.org/00rs6vg23Pelotonia Institute for Immuno-Oncology, The Ohio State University Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210chttps://ror.org/00rs6vg23Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, The Ohio State University, Columbus, OH 43210dhttps://ror.org/00rs6vg23Department of Biomedical Informatics, The Ohio State University, Columbus, OH 43210ehttps://ror.org/00rs6vg23Department of Otolaryngology-Head and Neck Surgery, The Ohio State University, Columbus, OH 43210fhttps://ror.org/00rs6vg23Department of Neuroscience, The Ohio State University, Columbus, OH 43210ghttps://ror.org/00rs6vg23Department of Internal Medicine, Division of Medical Oncology, The Ohio State University, Columbus, OH 43210hhttps://ror.org/00rs6vg23Division of Hematology, Department of Internal Medicine, The Ohio State University, Columbus, OH 43210ihttps://ror.org/04twxam07Department of Head and Neck Surgery, The University of Texas MD Anderson Cancer Center, Houston, TX 77030jhttps://ror.org/00rs6vg23Division of Pulmonary, Critical Care, and Sleep Medicine, Department of Internal Medicine, The Ohio State University, Columbus, OH 43210khttps://ror.org/00rs6vg23Translational Data Analytics Institute, The Ohio State University, Columbus, OH 43210</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606216123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606216123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606983123?af=R">
      <title>Neutrophil-intrinsic Vgll4 constrains tumorigenesis by preventing a STAT3/STAT5-driven immunosuppressive switch</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606983123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceNeutrophils exhibit remarkable functional plasticity in tumors, yet how their antitumor functions are preserved within the tumor microenvironment (TME) remains poorly understood. Here, we identify Vgll4 as a safeguard of neutrophil identity of ...</description>
      <dc:title>Neutrophil-intrinsic Vgll4 constrains tumorigenesis by preventing a STAT3/STAT5-driven immunosuppressive switch</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606983123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Lin ShaoJingwu YueShilong WangRuixian YuShuting ChengPingping NieXiaoya JiangYi HanWenjia WangYan MengMoubin LinMiao HeJianfeng ChenZhaocai ZhouShi JiaoaState Key Laboratory of Genetics and Development of Complex Phenotypes, School of Life Sciences, Zhongshan Hospital, Fudan University, Shanghai 200438, Chinabhttps://ror.org/013q1eq08Department of General Surgery, QingPu Branch of Zhongshan Hospital Affiliated to Fudan University, Shanghai 201700, Chinachttps://ror.org/03rc6as71Department of Stomatology, Shanghai Tenth People’s Hospital, Tongji University Cancer Center, School of Medicine, Tongji University, Shanghai 200072, Chinadhttps://ror.org/0220qvk04Department of Gastroenterology, Shanghai Ninth People’s Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200023, Chinaehttps://ror.org/03rc6as71Department of General Surgery, Yangpu Hospital, Tongji University School of Medicine, Shanghai 200090, ChinafState Key Laboratory of Brain Function and Disorders and Ministry of Education Frontiers Center for Brain Science, Department of Neurobiology, Zhongshan Hospital, Institutes of Brain Science, Fudan University, Shanghai 200032, Chinaghttps://ror.org/013q1eq08Department of Immunology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, ChinahTianfu Jincheng Laboratory, Chengdu 610093, Chinaihttps://ror.org/059gcgy73Collaborative Innovation Center for Cancer Personalized Medicine, School of Public Health, Nanjing Medical University, Nanjing 211166, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606983123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606983123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604642123?af=R">
      <title>A spinoreticular pathway mediates nocifensive responses to noxious mechanical stimuli</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604642123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceUnderstanding the spinal circuits that mediate mechanical pain is critical for elucidating the neural basis of nociception and neuropathic pain. Here, we identify a projection-definedSncg+spinoreticular pathway targeting the lateral ...</description>
      <dc:title>A spinoreticular pathway mediates nocifensive responses to noxious mechanical stimuli</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604642123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Yuan LiuQing LiJun-Kai LinYifei HanXiaoyu YangZining XuWanqiu ZhouYan-Gang SunYan-Nong Douahttps://ror.org/034t30j35Institute of Neuroscience, Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Shanghai 200031, Chinabhttps://ror.org/030bhh786Department of Biology, School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, ChinacLingang Laboratory, Shanghai 200031, ChinadState Key Laboratory of Brain Cognition and Brain-Inspired Intelligence Technology, Shanghai 200031, Chinaehttps://ror.org/05qbk4x57University of Chinese Academy of Sciences, Beijing 100049, Chinafhttps://ror.org/013q1eq08Department of Anesthesiology, Huashan Hospital, Fudan University, Shanghai 200040, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604642123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604642123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533109123?af=R">
      <title>High-resolution mapping of osteoblast metabolism and bone matrix turnover in vivo</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533109123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceBone formation depends on how osteoblasts use nutrients to build and remodel extracellular matrix, but this process has been difficult to measure directly inside intact bone. We developed a correlative electron microscopy–NanoSIMS platform ...</description>
      <dc:title>High-resolution mapping of osteoblast metabolism and bone matrix turnover in vivo</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533109123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Kai ChenJinyu GuoXiaojun ChenBuran ChenHeng QiuHui YangPaul GuagliardoSitao HuChau BuiKavishadhi ChandrasekaranQiongxiang LinBo HeQi ChenJiake XuStephen G. YoungMatthew B. GreenblattK. Swaminathan IyerNathan J. PavlosHaibo Jiangahttps://ror.org/047272k79School of Biomedical Sciences, The University of Western Australia, Perth, WA 6009, Australiabhttps://ror.org/047272k79School of Molecular Sciences, The University of Western Australia, Perth, WA 6009, Australiachttps://ror.org/02zhqgq86Department of Chemistry, The University of Hong Kong, Hong Kong, Chinadhttps://ror.org/047272k79Centre for Microscopy, Characterisation and Analysis, The University of Western Australia, Perth, WA 6009, Australiaehttps://ror.org/047272k79Harry Perkins Institute of Medical Research, The University of Western Australia, Perth, WA 6009, AustraliafNingbo Regen Biotech Co., Ningbo, Zhejiang 315157, Chinaghttps://ror.org/034t30j35Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, Chinahhttps://ror.org/046rm7j60Departments of Medicine and Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095ihttps://ror.org/02r109517Department of Pathology and Laboratory Medicine, Weill Cornell Medicine, New York, NY 10065jhttps://ror.org/04vf9tr09Laboratory for Synthetic Chemistry and Chemical Biology Limited, Health@InnoHK, Innovation and Technology Commission, Hong Kong, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533109123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533109123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619778123?af=R">
      <title>A cloaked glutamate decarboxylase sustains the GABA shunt in Mycobacterium tuberculosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619778123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceEnzymes annotated within well-characterized superfamilies are often assumed to have conserved functions, yet this assumption can obscure novel biochemical activities with important biological implications. In this study, we reveal that...</description>
      <dc:title>A cloaked glutamate decarboxylase sustains the GABA shunt in Mycobacterium tuberculosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619778123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>H. Minh ThaiDebbie M. HuntYugen MiyaharaManisha PriyaHtin L. AungRémi ZallotLuiz Pedro S. de Carvalhoahttps://ror.org/02y3ad647Department of Chemistry, The Herbert Wertheim University of Florida (UF) Scripps Institute for Biomedical Innovation and Technology, Jupiter, FL 33458bhttps://ror.org/02dxx6824The Skaggs Graduate School, The Scripps Research Institute, La Jolla, CA 92037chttps://ror.org/04tnbqb63Mycobacterial Metabolism and Antibiotic Research Laboratory, The Francis Crick Institute, London NW1 1AT, United Kingdomdhttps://ror.org/01jmxt844Division of Health Sciences, Department of Microbiology and Immunology, Faculty of Biomedical Sciences, University of Otago, Dunedin 9016, New Zealandehttps://ror.org/02hstj355Department of Life Sciences, Manchester Metropolitan University, Manchester M1 5GD, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619778123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619778123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610398123?af=R">
      <title>Perceptual and neural constraints on photometric measures of heterochromatic brightness</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610398123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceLuminance, defined by the candela, is the international standard for quantifying the visual impact of light and underpins lighting, imaging, and display technologies. Yet it is mainly based on flicker measurements that do not reflect how we ...</description>
      <dc:title>Perceptual and neural constraints on photometric measures of heterochromatic brightness</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610398123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Shuchen GuanJing ChenRobert EnnisMatteo ToscaniMatteo ValsecchiAndrea van DoornJan KoenderinkKarl R. Gegenfurtnerahttps://ror.org/033eqas34Department of Psychology and Center for Mind, Brain and Behavior, Justus-Liebig-Universität Giessen, Giessen 35394, Germanybhttps://ror.org/0056pyw12School of Psychology, Shanghai University of Sport, Shanghai 200438, Chinachttps://ror.org/05wwcw481Department of Psychology, Faculty of Science and Technology, Bournemouth University, Poole BH12 5BB, United Kingdomdhttps://ror.org/01111rn36Department of Psychology, University of Bologna, Bologna 40127, Italyehttps://ror.org/04pp8hn57Department of Experimental Psychology, Utrecht University, Utrecht 3584 CS, the Netherlandsfhttps://ror.org/05f950310Laboratory for Experimental Psychology, Catholic University of Leuven, Leuven 3000, Belgium</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610398123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610398123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612355123?af=R">
      <title>Numerical investigation of the equilibrium Kauzmann transition in a two-dimensional atomistic glass</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612355123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceUnderstanding whether liquids undergo a thermodynamic transition into an “ideal glass” is a central open question in condensed matter physics. After decades of study, first-principle theoretical calculations in finite dimensions remain ...</description>
      <dc:title>Numerical investigation of the equilibrium Kauzmann transition in a two-dimensional atomistic glass</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612355123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Gerhard JungMisaki OzawaGiulio BiroliLudovic Berthierahttps://ror.org/02rx3b187Laboratoire Interdisciplinaire de Physique, Université Grenoble Alpes, Saint-Martin-d’Hères 38402, Francebhttps://ror.org/054pv6659Institut für Theoretische Physik, Universität Innsbruck, Innsbruck 6020, Austriachttps://ror.org/05f82e368Laboratoire de Physique de l’Ecole Normale Supérieure, Université Paris Sciences et Lettres, CNRS, Sorbonne Université, Université de Paris, Paris 75005, Francedhttps://ror.org/03zx86w41Gulliver, CNRS UMR 7083, École supérieure de physique et de chimie industrielles de la ville de Paris, Paris Sciences et Lettres Research University, Paris 75005, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612355123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612355123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601204123?af=R">
      <title>An insoluble de novo protein enables survival of Escherichia coli by sequestering a gene repressor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601204123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceDiscovering proteins that were not sampled by evolution, but nonetheless provide life-sustaining functions, can offer insights about the origin and evolution of life. Here, we reportResc4, an insoluble protein isolated from a library of de ...</description>
      <dc:title>An insoluble de novo protein enables survival of Escherichia coli by sequestering a gene repressor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601204123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Guanyu LiaoSha TaoJessica L. DessauYejin BannMichael H. Hechtahttps://ror.org/00hx57361Department of Chemistry, Princeton University, Princeton, NJ 08544</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601204123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601204123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523784123?af=R">
      <title>Regulatory divergence of homoeologs underlies network optimization for fiber improvement in domesticated cotton</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523784123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAllotetraploid species contain duplicated genes derived from two ancestral genomes. These duplicated genes, known as homoeologs, often diverge in expression during development and evolution. How selection shapes thecis-regulatory landscape of ...</description>
      <dc:title>Regulatory divergence of homoeologs underlies network optimization for fiber improvement in domesticated cotton</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523784123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Zhengyang QiJinglei YangYanchao XuXuehan TianZhiwei ChenYawen WangBoyang ChenYang MengWei ZhangZeyu ZhangXinhui NieLili TuXianlong ZhangJonathan F. WendelFang LiuMaojun Wangahttps://ror.org/023b72294National Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan 430070, Chinabhttps://ror.org/0313jb750State Key Laboratory of Cotton Biology, Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang 455000, Chinachttps://ror.org/04x0kvm78Key Laboratory of Oasis Ecology Agricultural of Xinjiang Production and Construction Corps, Agricultural College, Shihezi University, Shihezi 832003, Chinadhttps://ror.org/04rswrd78Department of Ecology, Evolution, and Organismal Biology, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523784123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523784123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537018123?af=R">
      <title>Stochastic theory for pattern formation and front propagation in transitional pipe turbulence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537018123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe precise route to turbulence in a pipe remains poorly understood. The fraction of turbulence grows continuously when the flow speed exceeds a critical threshold, following a nonequilibrium phase transition called directed percolation. Above ...</description>
      <dc:title>Stochastic theory for pattern formation and front propagation in transitional pipe turbulence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537018123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Xueying WangHong-Yan ShihNigel Goldenfeldahttps://ror.org/047426m28Department of Physics, University of Illinois at Urbana-Champaign, Loomis Laboratory of Physics, Urbana, IL 61801-3080bNational Institute for Theory and Mathematics in Biology, Chicago, IL 60611chttps://ror.org/01tpvdq80Institute of Physics, Academia Sinica, Taipei 115201, Taiwandhttps://ror.org/02mh1d616Physics Division, National Center for Theoretical Sciences, Taipei 106319, Taiwanehttps://ror.org/0168r3w48Department of Physics, University of California San Diego, La Jolla, CA 92093</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537018123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537018123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608091123?af=R">
      <title>What controls the superconducting dome of electron-doped FeSe?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608091123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceSuperconducting “domes,” where the transition temperature rises and falls as a material is tuned, are ubiquitous across high-temperature superconductors, the class most relevant for technologies such as lossless power transmission and high-...</description>
      <dc:title>What controls the superconducting dome of electron-doped FeSe?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608091123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Paul T. MalinowskiChad J. MowersYaoju TarnDarrell G. SchlomBrendan D. FaethKyle M. Shenahttps://ror.org/05bnh6r87Department of Physics, Laboratory of Atomic and Solid State Physics, Cornell University, Ithaca, NY 14853bhttps://ror.org/05bnh6r87Department of Materials Science and Engineering, Cornell University, Ithaca, NY 14853chttps://ror.org/05bnh6r87Kavli Institute at Cornell for Nanoscale Science, Cornell University, Ithaca, NY 14853dhttps://ror.org/037p86664Leibniz-Institut für Kristallzüchtung, Berlin 12489, Germanyehttps://ror.org/05bnh6r87Platform for the Accelerated Realization, Analysis, and Discovery of Interface Materials, Cornell University, Ithaca, NY 14853</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608091123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608091123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616934123?af=R">
      <title>Primary amine–functionalized radially amphiphilic polypeptides target bacterial phospholipids in polyanionic matrices for biofilm therapy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616934123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceBiofilm-associated infections are exceptionally difficult to eradicate because the polyanionic biofilm matrix sequesters many antimicrobial agents before they reach bacterial membranes. We show that primary amine–functionalized radially ...</description>
      <dc:title>Primary amine–functionalized radially amphiphilic polypeptides target bacterial phospholipids in polyanionic matrices for biofilm therapy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616934123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Yuhao ZhangYu HuangYeqing HeXinshuang ZhangQianyu MaJiawen ChenChanjuan SuHuosheng ZhouSongyin HuangHoubing ZhangDong LuoYan BaoYuqin ShenShiyan XiaoMenghua Xiongahttps://ror.org/0530pts50School of Biomedical Sciences and Engineering, South China University of Technology, Guangzhou International Campus, Guangzhou 511442, People’s Republic of Chinabhttps://ror.org/0530pts50National Engineering Research Centre for Tissue Restoration and Reconstruction, South China University of Technology, Guangzhou 510006, People’s Republic of Chinachttps://ror.org/04c4dkn09State Key Laboratory of Precision and Intelligent Chemistry, Department of Polymer Science and Engineering, Hefei National Laboratory for Physical Sciences at Microscale, University of Science and Technology of China, Hefei 230026, Anhui, People’s Republic of Chinadhttps://ror.org/00zat6v61Department of Periodontology, School and Hospital of Stomatology, Guangdong Engineering Research Center of Oral Restoration and Reconstruction, Guangzhou Medical University, Guangzhou 510182, Guangdong, People’s Republic of Chinaehttps://ror.org/0064kty71Guangdong Provincial Key Laboratory of Malignant Tumor Epigenetics and Gene Regulation, Joint Laboratory for RNA Medicine, Medical Research Center, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou 510120, People’s Republic of Chinafhttps://ror.org/0064kty71Center for Biotherapy, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou 510120, People’s Republic of Chinaghttps://ror.org/0530pts50Key Laboratory of Biomedical Engineering of Guangdong Province, and Innovation Centre for Tissue Restoration and Reconstruction South China University of Technology, Guangzhou 510006, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616934123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616934123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608998123?af=R">
      <title>Structural basis of ligand recognition and gating in a heteromeric Deg-3/Des-2 nicotinic acetylcholine receptor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608998123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAnimals rely on cell-surface receptors to detect chemical and physical signals from their surroundings and within their bodies. Nicotinic acetylcholine receptors (nAChRs) mediate signaling in the central nervous system and at neuromuscular ...</description>
      <dc:title>Structural basis of ligand recognition and gating in a heteromeric Deg-3/Des-2 nicotinic acetylcholine receptor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608998123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Yingjie NingQiqi JiangZizhuo LuJie YuJingpeng Geahttps://ror.org/030bhh786School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, ChinabLingang Laboratory, Shanghai 200031, ChinacShanghai Clinical Research and Trial Center, Shanghai 201210, Chinadhttps://ror.org/034t30j35Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, ChinaeShanghai Key Laboratory of Aging Studies, Shanghai 201210, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608998123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608998123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612340123?af=R">
      <title>The TaLYK5–TaDSK2a module serves as a molecular switch between plant growth and immunity during fungal attack</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612340123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificancePlants face challenge from pathogenic microbes, yet the immunity–growth trade-off remains underexplored. Here, we identify a TaLYK5–TaDSK2a module regulating this trade-off in response to the stripe rust pathogenPuccinia striiformisf. sp....</description>
      <dc:title>The TaLYK5–TaDSK2a module serves as a molecular switch between plant growth and immunity during fungal attack</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612340123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Yu WuDan YangHaibin ZhaoQin WuYue LiXinyuan LiJian MaQiantao JiangYazhou ZhangYunfeng JiangPengfei QiXiaojie WangYuming WeiQiang Xuahttps://ror.org/0388c3403State Key Laboratory of Crop Gene Exploration and Utilization in Southwest China, Triticeae Research Institute, Sichuan Agricultural University, Chengdu, Sichuan 611130, Chinabhttps://ror.org/01dyr7034Shaanxi Key Laboratory of Research and Utilization of Resource Plants on the Loess Plateau, Yan’an University, Yan’an, Shaanxi 716000, ChinacState Key Laboratory for Crop Stress Resistance and High-Efficiency Production, College of Plant Protection, Northwest Agriculture and Forestry University, Yangling, Shaanxi 712100, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612340123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612340123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530122123?af=R">
      <title>Tmem117, an oligodendrocyte-enriched regulator of NCX activity, links myelin homeostasis to counterregulation and metabolic health</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530122123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThis study uncovers a surprising connection between myelin integrity and whole-body metabolism through the transmembrane protein Tmem117, whose molecular mechanism of action was previously unknown. We show that Tmem117 is crucial for ...</description>
      <dc:title>Tmem117, an oligodendrocyte-enriched regulator of NCX activity, links myelin homeostasis to counterregulation and metabolic health</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530122123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Melvin AlappatMarta Anna MazurkiewiczIris ZambounisAlice MastrangeloVicente Mario Algaba MartínezThomas GramppFrancesco PriscoAnja KiparAlexandre PicardMusadiq A. BhatDietmar BenkeHanns Ulrich ZeilhoferBernard ThorensSevasti Gaspariahttps://ror.org/02crff812Institute of Pharmacology and Toxicology, University of Zurich, Zurich CH-8057, Switzerlandbhttps://ror.org/02crff812Neuroscience Center Zurich, University of Zurich and Swiss Federal Institute of Technology (ETH) Zurich, Zurich CH-8057, SwitzerlandcDepartment of Health Sciences and Technology, ETH Zurich, Zurich CH-8092, Switzerlanddhttps://ror.org/02crff812Laboratory for Animal Model Pathology, Institute of Veterinary Pathology, Vetsuisse Faculty, University of Zurich, Zurich CH-8057, Switzerlandehttps://ror.org/019whta54Center for Integrative Genomics, University of Lausanne, Lausanne CH-1015, Switzerlandfhttps://ror.org/04n35qp23Institute of Pharmaceutical Sciences, Swiss Federal Institute of Technology (ETH) Zurich, Zurich CH-8093, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530122123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530122123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617376123?af=R">
      <title>A hypersensitive neuromorphic airflow sensor inspired by vision-compensatory scorpion mechanoreceptors for respiratory pattern analysis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617376123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceCommercial airflow sensors typically rely on time-sampling of indirect physical quantities to measure flow velocity, whereas vision-degenerated scorpions utilize the sophisticated evolutionary structure of trichobothria and event-driven neural ...</description>
      <dc:title>A hypersensitive neuromorphic airflow sensor inspired by vision-compensatory scorpion mechanoreceptors for respiratory pattern analysis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617376123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-20T07:00:00Z</dc:date>
      <dc:creator>Pinkun WangYuechun DingBo LiChangchao ZhangXiancun MengGuangjun ChenYou ChenRuijuan DuQingsong FanJunqiu ZhangShichao NiuZhiwu HanLuquan Renahttps://ror.org/00js3aw79Key Laboratory of Bionic Engineering, Ministry of Education, Jilin University, Changchun 130022, Chinabhttps://ror.org/024mw5h28Pritzker School of Molecular Engineering, University of Chicago, Chicago, IL 60637chttps://ror.org/00js3aw79The National Key Laboratory of Automotive Chassis Integration and Bionics, Jilin University, Changchun 130022, Chinadhttps://ror.org/0394yh759Institute of Structured and Architected Materials, Liaoning Academy of Materials, Shenyang 110167, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617376123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617376123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606669123?af=R">
      <title>Urban tree canopy fragmentation and child mortality in low- and middle-income countries</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606669123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceAlthough international health agendas increasingly promote nature-based solutions, little is known about whether the spatial configuration of urban trees associates with child survival. Using longitudinal data from more than 420,000 children ...</description>
      <dc:title>Urban tree canopy fragmentation and child mortality in low- and middle-income countries</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606669123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-21T07:00:00Z</dc:date>
      <dc:creator>Dengkai ChiDaniel RichardsGabriele ManoliJun YangJohn S. JiYe ZhangBrenda LinAmy HahsCongqiang LiuYue ZhuYeshan QiuJing WangPaolo BurlandoSimone FatichiPuay Yok Tanahttps://ror.org/012tb2g32School of Earth System Science, Institute of Surface-Earth System Science, Tianjin University, Tianjin 300072, Chinabhttps://ror.org/01x6n3581Singapore–ETH Centre, Future Cities Laboratory Global, Singapore 138602, Singaporechttps://ror.org/03j13xx78Bioeconomy Science Institute, Lincoln 7608, New Zealanddhttps://ror.org/02s376052Laboratory of Urban and Environmental Systems, École Polytechnique Fédérale de Lausanne, Lausanne 1015, Switzerlandehttps://ror.org/03cve4549Department of Earth System Science, Institute for Global Change Studies, Ministry of Education Ecological Field Station for East Asian Migratory Birds, Tsinghua University, Beijing 100084, Chinafhttps://ror.org/03cve4549Vanke School of Public Health, Tsinghua University, Beijing 100084, Chinaghttps://ror.org/03cve4549School of Architecture, Tsinghua University, Beijing 100084, Chinahhttps://ror.org/03qn8fb07Commonwealth Scientific and Industrial Research Organisation Environment, Dutton Park, QLD 4102, Australiaihttps://ror.org/01ej9dk98School of Agriculture, Food and Ecosystem Sciences, Burnley Campus, The University of Melbourne, Melbourne, VIC 3121, Australiajhttps://ror.org/01r4q9n85State Key Laboratory of Internet of Things for Smart City, Department of Arts and Design, University of Macau, Macao Special Administrative Region 999078, ChinakDepartment of Architecture, College of Design and Engineering, Singapore 117566, Singaporelhttps://ror.org/05a28rw58Institute of Environmental Engineering, Eidgenössische Technische Hochschule Zurich, Zurich 8093, SwitzerlandmDepartment of Civil and Environmental Engineering, College of Design and Engineering, Singapore 117576, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606669123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606669123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602779123?af=R">
      <title>ALKBH3 inhibition normalizes neovessels by reprogramming endothelial fate in diabetic microvasculopathy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602779123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceDiabetic microvasculopathy drives organ damage worldwide, with diabetic retinopathy (DR) as a leading cause of blindness. Current anti-vascular endothelial growth factor (VEGF) therapies only suppress abnormal vessel growth but fail to ...</description>
      <dc:title>ALKBH3 inhibition normalizes neovessels by reprogramming endothelial fate in diabetic microvasculopathy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602779123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-21T07:00:00Z</dc:date>
      <dc:creator>Yi-Chen ZhangZi-Qin DingShi-Yao XuJi-Yu ChenMing-Hui ChenBing-Qing LuoYing WangYan-Yi WuXin-Yao LvXing-Zhu LiuChen ZhaoQing-Huai LiuXue Chenahttps://ror.org/04py1g812Department of Ophthalmology, The First Affiliated Hospital of Nanjing Medical University, Nanjing Medical University, Nanjing 210029, Chinabhttps://ror.org/034t30j35Key Laboratory for Nano-Bio Interface, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou 215123, Chinachttps://ror.org/013q1eq08Eye Institute and Department of Ophthalmology, Eye, Ear, Nose, and Throat Hospital, Fudan University, Shanghai 200031, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602779123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602779123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607359123?af=R">
      <title>Tox regulates hair cell stereocilia development and Cdh23 expression in mice and zebrafish</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607359123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceIn this study, we identify an immune-independent role for the transcription factor Tox in the development of hair cells (HCs) across zebrafish and mice. Tox is highly expressed in HCs in both species, with its expression dynamically increasing ...</description>
      <dc:title>Tox regulates hair cell stereocilia development and Cdh23 expression in mice and zebrafish</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607359123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-21T07:00:00Z</dc:date>
      <dc:creator>Jing ZhangJie GongJing ZhouGuiyi ZhangShengda CaoSiwei GuoYu XiaoXiaoxu ZhaoWen LiYuhan WangRuifeng QiaoMin WangZiyi LiuGuodong HongYunhao WuXiuli BiHailong TuShuyuan ShenJiangang GaoDong LiuXiaolong Fuahttps://ror.org/0207yh398Department of Development Biology, School of Life Science, Shandong University, Qingdao 266237, Shandong, Chinabhttps://ror.org/05jb9pq57Department of Otolaryngology, Shandong Provincial Hospital, School of Clinical and Basic Medical Sciences, Medical Science and Technology Innovation Center, Shandong First Medical University &amp; Shandong Academy of Medical Sciences, Jinan 250117, Shandong, Chinachttps://ror.org/02afcvw97Department of Biotechnology, School of Life Sciences, Nantong Laboratory of Development and Diseases, Co-innovation Center of Neuroregeneration, Nantong University, Nantong 226001, Chinadhttps://ror.org/056ef9489Department of Otorhinolaryngology, Qilu Hospital of Shandong University, National Health Commission Key Laboratory of Otorhinolaryngology (Shandong University), Jinan 250012, Shandong, ChinaeDepartment of Otolaryngology Head and Neck Surgery, Shengjing Hospital of China Medical University, Shenyang 110004, People’s Republic of Chinafhttps://ror.org/01skt4w74Department of Neurology, School of Life Science, Beijing Institute of Technology, Beijing 100081, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607359123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607359123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611441123?af=R">
      <title>Macrophages diverge into profibrotic SAMs and proresolving ReM2 cells to regulate liver fibrosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611441123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceLiver fibrosis, a scarring process that underlies chronic liver disease, remains untreatable. Macrophages are immune cells that either promote scarring or help the liver heal, but how they decide between these roles is unclear. Using a mouse ...</description>
      <dc:title>Macrophages diverge into profibrotic SAMs and proresolving ReM2 cells to regulate liver fibrosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611441123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-21T07:00:00Z</dc:date>
      <dc:creator>Dezhen ZhangXinjie LiuDong MaLingling LiaoFugang DuanYiming WangTongzhen ZhangJiang LiuWei DongJunfei JinZhenhua LuoHaining Zhouahttps://ror.org/034t30j35State Key Laboratory of Epigenetic Regulation and Intervention, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, Chinabhttps://ror.org/05qbk4x57University of Chinese Academy of Sciences, Beijing 100101, Chinachttps://ror.org/037p24858Institute of Precision Medicine, The First Affiliated Hospital, Sun Yat-Sen University, Guangzhou 510080, Guangdong, Chinadhttps://ror.org/000prga03Guangxi Key Laboratory of Molecular Medicine in Liver Injury and Repair, The First Affiliated Hospital of Guilin Medical University, Guilin, Guangxi 541001, Chinaehttps://ror.org/000prga03Guangxi Health Commission Key Laboratory of Basic Research in Sphingolipid Metabolism Related Diseases, The First Affiliated Hospital of Guilin Medical University, Guilin 541001, Guangxi, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611441123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611441123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520063123?af=R">
      <title>Loss of Sox10 prevents tumor initiation in vivo and induces luminal-to-basal reprogramming in Neu+ tumor cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520063123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceThe Sox10 transcription factor is critical for mammary stem cell function and plasticity. Animal studies showed that different subtypes of breast cancers arise from luminal epithelial cells and suggested the implication of luminal stem cells ...</description>
      <dc:title>Loss of Sox10 prevents tumor initiation in vivo and induces luminal-to-basal reprogramming in Neu+ tumor cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520063123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-21T07:00:00Z</dc:date>
      <dc:creator>Brennan GarlandSamuel DelisleJohn Abou-HamadChristiano de SouzaRiana ZuccariniDavid P. CookRebecca C. AuerLuc A. Sabourinahttps://ror.org/03c4mmv16Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON K1H8M5, Canadabhttps://ror.org/05jtef216Department of Cancer Therapeutics, The Ottawa Hospital Research Institute, Ottawa, ON K1H 8L6, Canadachttps://ror.org/03c4mmv16Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON K1H8M5, Canadadhttps://ror.org/03c4mmv16Department of Surgery, University of Ottawa, Ottawa, ON K1H 8M5, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520063123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520063123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601643123?af=R">
      <title>A transient global warming event during Earth’s penultimate icehouse</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601643123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;SignificanceDeep-time hyperthermal events are critical for parameterization of climate sensitivity and tipping-point thresholds and for understanding the impacts of modern climate warming on marine ecosystems. To date, known hyperthermal events have been ...</description>
      <dc:title>A transient global warming event during Earth’s penultimate icehouse</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601643123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-10T07:00:00Z</dc:date>
      <dc:creator>Le YaoThomas J. AlgeoQiulai WangWang ZhengQiang WeiYu-ping QiGuzel M. SungatullinaGenming LuoGanqing JiangGuoqiang TangJian ZhangHui WangYaqiu ZhaoXing HuangQiu-Li LiXiang-dong WangShucheng XieXian-Hua Liahttps://ror.org/034t30j35State Key Laboratory of Palaeobiology and Stratigraphy, Nanjing Institute of Geology and Palaeontology, Chinese Academy of Sciences, Nanjing 210008, Chinabhttps://ror.org/05qbk4x57University of Chinese Academy of Sciences, Beijing 100049, Chinachttps://ror.org/04gcegc37State Key Laboratory of Geomicrobiology and Environmental Changes, China University of Geosciences, Wuhan 430074, Chinadhttps://ror.org/01e3m7079Department of Geosciences, University of Cincinnati, Cincinnati, OH 45221ehttps://ror.org/05pejbw21State Key Laboratory of Oil and Gas Reservoir Geology and Exploitation, Chengdu University of Technology, Chengdu 610059, Chinafhttps://ror.org/012tb2g32School of Earth System Science, Institute of Surface-Earth System Science, Tianjin University, Tianjin 300072, Chinaghttps://ror.org/034t30j35State Key Laboratory of Tibetan Plateau Earth System, Environment and Resources, Institute of Tibetan Plateau Research, Chinese Academy of Sciences, Beijing 100101, Chinahhttps://ror.org/05256ym39Department of Paleontology and Stratigraphy, Kazan Federal University, Kazan 420008, Russiaihttps://ror.org/0406gha72Department of Geoscience, University of Nevada, Las Vegas, NV 89154-4010jState Key Laboratory of Lithospheric Evolution, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, Chinakhttps://ror.org/01rxvg760State Key Laboratory for Mineral Deposits Research, School of Earth Sciences and Engineering and Frontiers Science Center for Critical Earth Material Cycling, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601643123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601643123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617990123?af=R">
      <title>Probabilistically defining environmentally relevant concentrations in ecotoxicology</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617990123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;A long-standing issue in ecotoxicology is the arbitrarily chosen and ambiguous definition of “environmentally relevant” concentrations, which undermines research comparability and hampers risk characterization. Here, we propose a probabilistic framework ...</description>
      <dc:title>Probabilistically defining environmentally relevant concentrations in ecotoxicology</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617990123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Tao SunHuifeng WuLennart WeltjeEvgenios AgathokleousEdward J. CalabreseJohn P. Sumpterahttps://ror.org/034t30j35Shandong Key Laboratory of Coastal Zone Environmental Processes and Ecological Security, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences, Yantai 264003, People’s Republic of ChinabLaboratory for Marine Fisheries Science and Food Production Processes, Qingdao Marine Science and Technology Center, Qingdao 266237, People’s Republic of ChinacBASF Agricultural Solutions Deutschland GmbH, Ecotoxicology, Limburgerhof 67117, GermanydDivision of Plant Pathology and Plant Protection, Georg-August-University Göttingen, Göttingen 37077, Germanyehttps://ror.org/02y0rxk19Key Laboratory of Ecosystem Carbon Source and Sink, China Meteorological Administration (ECSS-CMA), School of Ecology and Applied Meteorology, Nanjing University of Information Science and Technology, Nanjing 210044, People’s Republic of Chinafhttps://ror.org/01q8k8p90Climate and Atmosphere Research Center, The Cyprus Institute, Nicosia 2121, Cyprusghttps://ror.org/0072zz521Department of Environmental Health Sciences, University of Massachusetts, Amherst, MA 01003hhttps://ror.org/00dn4t376Department of Life Sciences, Brunel University London, Uxbridge UB8 3PH, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617990123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617990123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610388123?af=R">
      <title>Value misalignment in X’s feed algorithm is a reflection of value tensions in engagement</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610388123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;Social media feed algorithms rank content that is purported to be preferred by users, but the engagement behaviors that drive these algorithms are (at best) indirect proxies for users’ explicitly self-stated values. Are the resulting feeds value aligned, ...</description>
      <dc:title>Value misalignment in X’s feed algorithm is a reflection of value tensions in engagement</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610388123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Ziv EpsteinFarnaz JahanbakhshTiziano PiccardiAxel PeytavinIsabel GallegosShardul SapkotaDora ZhaoJohan UganderMichael S. Bernsteinahttps://ror.org/042nb2s44Schwarzman College of Computing, Massachusetts Institute of Technology, Cambridge, MA 02143bhttps://ror.org/00jmfr291Electrical Engineering and Computer Science, University of Michigan, Ann Arbor, MI 48109chttps://ror.org/00za53h95Computer Science Department Johns Hopkins University, Baltimore, MD 21218dhttps://ror.org/00f54p054Computer Science Department Stanford University, Stanford, CA 94305ehttps://ror.org/03v76x132Department of Statistics &amp; Data Science Yale University, New Haven, CT 06511</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610388123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610388123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621879123?af=R">
      <title>The transgenerational toll of maternal spaceflight</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621879123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>The transgenerational toll of maternal spaceflight</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621879123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Mahsa GifaniGregory W. Burnsahttps://ror.org/05hs6h993Department of Obstetrics, Gynecology and Reproductive Biology, Michigan State University, Grand Rapids, MI 49503</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621879123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621879123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622914123?af=R">
      <title>The free-rider detection problem: How groups balance fairness and cooperation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622914123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>The free-rider detection problem: How groups balance fairness and cooperation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622914123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Jörg Grossahttps://ror.org/02crff812Social and Economic Psychology Section, Institute of Psychology, University of Zurich, 8050 Zurich, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622914123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622914123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620768123?af=R">
      <title>Random repeats open a route into folded protein space</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620768123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Random repeats open a route into folded protein space</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620768123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>James W. Murrayahttps://ror.org/041kmwe10Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620768123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620768123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612932123?af=R">
      <title>Does a chloroplast membrane protein bind DNA in the nucleus?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612932123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Does a chloroplast membrane protein bind DNA in the nucleus?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612932123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Preetom RegonDana Charuviahttps://ror.org/05hbrxp80Institute of Plant Sciences, 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>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612932123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612932123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627119123?af=R">
      <title>Correction for Chioino et al., Mitofusin-2 in ventral striatal D1 neurons regulates effort-based motivation through sex-specific mitochondrial–synaptic reprogramming</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627119123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Chioino et al., Mitofusin-2 in ventral striatal D1 neurons regulates effort-based motivation through sex-specific mitochondrial–synaptic reprogramming</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627119123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2627119123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2627119123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625637123?af=R">
      <title>Correction for Brown et al., Deuterated water and the formation of the satellites of Uranus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625637123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Brown et al., Deuterated water and the formation of the satellites of Uranus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625637123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2625637123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2625637123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2626818123?af=R">
      <title>Correction for Wang et al., A ligandable PNT domain establishes ERG as a directly targetable oncogenic driver in prostate cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626818123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Wang et al., A ligandable PNT domain establishes ERG as a directly targetable oncogenic driver in prostate cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626818123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626818123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626818123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627895123?af=R">
      <title>Correction for Dervishi et al., Sterol divergence across eukaryotic kingdoms determines membrane susceptibility to saponins, a class of plant defense compounds</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627895123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Dervishi et al., Sterol divergence across eukaryotic kingdoms determines membrane susceptibility to saponins, a class of plant defense compounds</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627895123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2627895123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2627895123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2626420123?af=R">
      <title>Correction for Yang et al., Superenhancer drives a tumor-specific splicing variant of MARCO to promote triple-negative breast cancer progression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626420123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Yang et al., Superenhancer drives a tumor-specific splicing variant of MARCO to promote triple-negative breast cancer progression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626420123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626420123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626420123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2626815123?af=R">
      <title>Correction for Herpe et al., When alternative becomes essential: The role of mitochondrial glycerol-3-phosphate dehydrogenase</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626815123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Herpe et al., When alternative becomes essential: The role of mitochondrial glycerol-3-phosphate dehydrogenase</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626815123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626815123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626815123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627297123?af=R">
      <title>Correction for Zhou et al., Warming substantially amplifies Antarctic coastal polynyas as key carbon sinks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627297123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Zhou et al., Warming substantially amplifies Antarctic coastal polynyas as key carbon sinks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627297123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2627297123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2627297123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617958123?af=R">
      <title>Reply to Regon and Charuvi: Evidence supporting a nuclear chromatin-associated role of BpELIP1 in BpFLC regulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617958123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Regon and Charuvi: Evidence supporting a nuclear chromatin-associated role of BpELIP1 in BpFLC regulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617958123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-17T07:00:00Z</dc:date>
      <dc:creator>Yi LiuSui WangTangchun ZhengHuiying SuoDi XiaoDong ZengXiangling YouHeike W. SederoffVincent L. ChiangXiyang ZhaoRonald R. SederoffGuanzheng Quahttps://ror.org/02yxnh564State Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, Chinabhttps://ror.org/05dmhhd41Jilin Provincial Key Laboratory of Tree and Grass Genetics and Breeding, College of Forestry and Grassland Science, Jilin Agricultural University, Changchun 130118, Chinachttps://ror.org/0515nd386National Key Laboratory of Smart Farm Technologies and Systems, Northeast Agricultural University, Harbin 150030, Chinadhttps://ror.org/0515nd386Key Laboratory of Soybean Biology of Chinese Education Ministry, Northeast Agricultural University, Harbin 150030, Chinaehttps://ror.org/04xv2pc41National Engineering Research Center for Floriculture, School of Landscape Architecture, Beijing Forestry University, Beijing 100083, Chinafhttps://ror.org/02yxnh564College of Life Science, Northeast Forestry University, Harbin 150040, Chinaghttps://ror.org/023cbka75Key Laboratory of Horticulture Crop Genomics and Genetic Improvement in Xinjiang, Institute of Fruits and Vegetables, Xinjiang Academy of Agricultural Sciences, Urumqi 830091, Chinahhttps://ror.org/04tj63d06Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695ihttps://ror.org/04tj63d06Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617958123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617958123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2626100123?af=R">
      <title>QnAs with Richard Ostfeld</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626100123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>QnAs with Richard Ostfeld</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626100123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-19T07:00:00Z</dc:date>
      <dc:creator>Sandeep Ravindran</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626100123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626100123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627721123?af=R">
      <title>Retraction for Knyazeva et al., A chemical inhibitor of IST1-CHMP1B interaction impairs endosomal recycling and induces noncanonical LC3 lipidation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627721123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 34, August 2026. &lt;br/&gt;</description>
      <dc:title>Retraction for Knyazeva et al., A chemical inhibitor of IST1-CHMP1B interaction impairs endosomal recycling and induces noncanonical LC3 lipidation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627721123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-18T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>34</prism:number>
      <prism:coverDate>2026-08-25T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-25T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2627721123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2627721123?af=R</prism:url>
      <prism:copyright/>
   </item>
</rdf:RDF>