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      <title>Proceedings of the National Academy of Sciences</title>
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      <title>In This Issue</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-31T07:00:00Z</dc:date>
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      <title>Toward AI foundation models for epidemics: Promise, challenges, and paths forward</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526192123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;Foundation models—large AI systems pretrained on broad, heterogeneous data—are transforming scientific discovery. These models (e.g., GPT, GenCast, AlphaFold) excel at learning generalizable representations and adapting to new tasks with limited data. Yet,...</description>
      <dc:title>Toward AI foundation models for epidemics: Promise, challenges, and paths forward</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526192123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-13T07:00:00Z</dc:date>
      <dc:creator>Max S. Y. LauC. Jessica E. MetcalfZewen LiuBryan T. GrenfellWei JinaDepartment of Biostatistics and Bioinformatics, Emory University, Atlanta, GA 30322bDepartment of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08544cDepartment of Computer Science, Emory University, Atlanta, GA 30322</dc:creator>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;Cuban-born Pedro A. Sanchez (1940-2026) became the face of tropical soil science at Cornell University and the North Carolina State University. His combination of process-based understanding of soils, emphasis on farmer choices and conducive policy ...</description>
      <dc:title>Pedro A. Sanchez (1940–2026), a social soil scientist</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604417123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-20T07:00:00Z</dc:date>
      <dc:creator>Meine van NoordwijkGenerose NziguhebaThomas P. TomichMary ScholesFahmuddin AgusLeigh WinowieckiJoyce KasyokiPeter A. MinangaCentre for International Forestry Research and World Agroforestry, Nairobi 00100, KenyabFlemish Institute for Biotechnology, Gent 9000, BelgiumcDepartment of Environmental Science and Policy, University of California Davis, Davis, CA 95616dSchool of Animal, Plant and Environmental Sciences, University of the Witwatersrand, Johannesburg-Braamfontein 2050, South AfricaePusat Riset Tanaman Hortikultura dan Perkebunan, National Research and Innovation Agency, Cibinong-Jakarta 10340, Indonesia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
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      <title>Using wavelet decomposition to determine the dimension of structures from projected images</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534122123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceTurbulence is a fundamental process in a wide range of natural and laboratory systems. Experiments and observations often measure projected images of tracers in turbulent flows. Because the underlying structures are fractal, such observations ...</description>
      <dc:title>Using wavelet decomposition to determine the dimension of structures from projected images</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534122123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Svitlana MayborodaDavid N. SpergelaDepartment of Mathematics, ETH Zurich, Zürich 8092, SwitzerlandbFlatiron Institute, New York, NY 10011</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
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      <title>How to revive science in America</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;</description>
      <dc:title>How to revive science in America</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537854123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Harvey V. Fineberga
                    Harvard University, Cambridge, MA
                    02138
                b
                    Gordon and Betty Moore Foundation, Palo Alto, CA
                    94304
                c
                    Science Philanthropy Alliance, New York, NY
                    10010
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      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
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      <title>Invertebrate miRNA pva-small RNA-11881/pva-miR-11881 as a potential RNA-based therapeutic against white spot syndrome virus in infected shrimp</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSmall RNAs and microRNAs are key regulators of shrimp antiviral defense through modulating viral and host gene expression. The genomic origin of a promising small/microRNA, pva-miR-11881, from the Pacific white shrimp was identified, and its ...</description>
      <dc:title>Invertebrate miRNA pva-small RNA-11881/pva-miR-11881 as a potential RNA-based therapeutic against white spot syndrome virus in infected shrimp</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525793123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-16T07:00:00Z</dc:date>
      <dc:creator>Pun SangchaiPeter SarnowKunlaya SomboonwiwataCenter of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, ThailandbDepartment of Microbiology and Immunology, School of Medicine, Stanford University, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525793123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516062123?af=R">
      <title>The archaeal roots of eukaryotic life</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516062123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;Resolving the biological and geological events that led to the origin of eukaryotes is an ongoing challenge in biology. A major step in the evolution of complex cellular life was the merger between an ancestral host cell and a bacterium (that became the ...</description>
      <dc:title>The archaeal roots of eukaryotic life</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516062123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-13T07:00:00Z</dc:date>
      <dc:creator>Valerie De AndaKathryn E. ApplerEmily Aguilar-PineGeorgina L. AitoloGalen P. HalversonBrett J. BakeraDepartment of Integrative Biology, University of Texas at Austin, Austin, TX 78747bDepartment of Marine Science, Marine Science Institute, University of Texas at Austin, Port Aransas, TX 78373cDepartment of Earth and Planetary Sciences/Geotop, McGill University, Montréal, QC H3A0E8, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516062123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516062123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2512673123?af=R">
      <title>Future strategies for phosphorus sustainability amid worsening global cycle imbalances</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2512673123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePhosphorus (P) is intricately and inseparably associated with both food security and environmental sustainability. The comprehensive processes of the global anthropogenic P cycle, along with scientific objectives and implementation strategies ...</description>
      <dc:title>Future strategies for phosphorus sustainability amid worsening global cycle imbalances</dc:title>
      <dc:identifier>doi:10.1073/pnas.2512673123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-16T07:00:00Z</dc:date>
      <dc:creator>Wei LiuHaijun WangZhiwen LiTian QinMingyang LiWuhu GuoYuejin ChenYanqi LiuEvgeny AbakumovWenjuan WangWending HuangXiaowen JiYingming ZhouXuejun LiuHuoqing XiaoZugen LiuHannan Ahmad AnjumXianchuan XieaKey Laboratory of Poyang Lake Environment and Resource Utilization, Engineering Research Center of Watershed Carbon Neutralization, Ministry of Education, Key Laboratory of Ecological Hydrological Monitoring and Research in Poyang Lake Basin of Jiangxi Province, School of Resource and Environment, Nanchang University, Nanchang 330031, ChinabDepartment of Applied Ecology, Saint Petersburg State University, Saint Petersburg 199178, Russian FederationcYunnan Key Laboratory of Ecological Protection and Resource Utilization of River-lake Networks, International Joint Laboratory for Yunnan River and Lake Ecosystem Restoration Green Technology, Institute for Ecological Research and Pollution Control of Plateau Lakes, School of Ecology and Environmental Science, Yunnan University, Kunming 650500, ChinadEnvironmental Chemistry Laboratory, Department of Toxic Substances Control, California Environmental Protection Agency, Berkeley, CA 94710eJiangxi Provincial Key Laboratory of Environmental Pollution Control, Jiangxi Academy of Eco-environmental Sciences and Planning, Nanchang, Jiangxi 330039, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2512673123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2512673123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520565123?af=R">
      <title>Archaeogenetic insights into the demographic history of Late Neanderthals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520565123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceKnowledge of the population history of Neanderthals remains incomplete, including the evolutionary processes that preceded their extinction. This study provides evidence for a widespread genetic replacement in the demographic history of ...</description>
      <dc:title>Archaeogenetic insights into the demographic history of Late Neanderthals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520565123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Charoula M. FotiadouJesper Borre PedersenHélène RougierMirjana RoksandicMaria A. SpyrouKathrin NägeleElla ReiterHervé BocherensAndrew W. KandelMiriam N. HaidleTimo P. StreicherNicholas J. ConardFlora SchiltRicardo Miguel GodinhoThorsten UthmeierLuc DoyonPatrick SemalJohannes KrauseAlvise BarbieriDušan MihailovićIsabelle CrevecoeurCosimo PosthaArchaeo- and Palaeogenetics, Institute for Archaeological Sciences, Department of Geosciences, University of Tübingen, Tübingen 72074, GermanybSenckenberg Centre for Human Evolution and Palaeoenvironment at the University of Tübingen, Tübingen 72074, GermanycResearch Center “The Role of Culture in Early Expansions of Humans (ROCEEH)” of the Heidelberg Academy of Sciences and Humanities, University of Tübingen, Tübingen 72074, GermanydDepartment of Anthropology, California State University Northridge, Northridge, CA 91330eNatural Sciences and Engineering Research Council of Canada, Canada Research Chair in Human Evolution, Department of Anthropology, University of Winnipeg, Winnipeg MB R3T 3C7, CanadafHUMAN ORIGINS—Cluster of Excellence for Integrative Human Origins Studies (EXC 3101), University of Tübingen, Tübingen 72074, GermanygDepartment of Archaeogenetics, Max Planck Institute for Evolutionary Anthropology, Leipzig 04103, GermanyhBiogeology, Department of Geosciences, University of Tübingen, Tübingen 72074, GermanyiDepartment of Early Prehistory and Quaternary Ecology, University of Tübingen, Tübingen 72070, GermanyjDepartment of Art and Culture, History and Antiquity, Vrije Universiteit Amsterdam, Amsterdam 1081 HV, The NetherlandslkInterdisciplinary Center for Archaeology and the Evolution of Human Behavior (ICArEHB), Faculdade das Ciências Humanas e Sociais, Universidade do Algarve (UAlg), Campus de Gambelas, Faro 8005-139, PortugallFriedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Department of Classical World and Asian Cultures, Institute of Prehistory and Protohistory, Erlangen 91054, GermanymDe la Préhistorie à l’Actuel: Culture, Environnement et Anthropologie, CNRS, Université de Bordeaux, Ministère de la Culture, Pessac 33615, FrancenService of Scientific Heritage, Royal Belgian Institute of Natural Sciences, Brussels 1000, BelgiumoDepartment of Archaeology, Faculty of Philosophy, University of Belgrade, Belgrade 11000, Serbia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520565123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520565123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528398123?af=R">
      <title>Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528398123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSARS-CoV-2 and other coronaviruses are significant contributors to respiratory diseases globally, and understanding the function of essential coronaviral enzymes and their regulation is an important field of study. TRIM proteins are a family ...</description>
      <dc:title>Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528398123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Kannan BalakrishnanSurajit ChakrabortyCindy ChiangCaleb M. StrattonShanti PandeyAnna A. TumanovaShaun K. OlsenMichaela U. GackaFlorida Research and Innovation Center, Cleveland Clinic, Port Saint Lucie, FL 34987bDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528398123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525676123?af=R">
      <title>Convergent evolution increases boron transport through SNPs and tandem duplications at BOR1 and BOR2 in Arabidopsis thaliana</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525676123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceBoron is an essential nutrient for plant growth, but many soils lack sufficient amounts, limiting crop production worldwide. To understand how plants adapt to boron-deficient environments, we studied wild mustard plants that naturally ...</description>
      <dc:title>Convergent evolution increases boron transport through SNPs and tandem duplications at BOR1 and BOR2 in Arabidopsis thaliana</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525676123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Emmanuel TergeminaCélia NetoMd Mamunur RashidHerculano DinisDavid E. SaltAngela M. HancockaDepartment of Plant Developmental Biology, Max Planck Institute for Plant Breeding Research, Cologne 50829, GermanybParque Natural do Fogo, Direção Nacional do Ambiente, Chã d’Areia, Praia, Santiago 115, Cabo VerdecAssociação Projecto Vitó, Xaguate, Cidade de São Filipe, Fogo 8234, Cabo VerdedSchool of Biosciences, University of Nottingham, Sutton Bonington LE12 5RD, United KingdomeDepartment of Botany and Plant Pathology, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525676123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525676123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533700123?af=R">
      <title>KLF2 overrides the resident memory CD8 T cell differentiation program, in opposition to KLF3</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533700123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMemory T cells, generated after an immune response, fall into two main groups, depending on whether they circulate between tissues and blood or are “resident” in tissues. Various phenotypic and functional properties characterize recirculating ...</description>
      <dc:title>KLF2 overrides the resident memory CD8 T cell differentiation program, in opposition to KLF3</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533700123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Taylor A. DePauwKexin GaiJian ShenNicholas J. MauriceKa Hyun RheeWilliam J. ValenteChristine H. O’ConnorWeiguo CuiChangwei PengStephen C. JamesonaCenter for Immunology, University of Minnesota Medical School, Minneapolis, MN 55455bDepartment of Pathology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611cUniversity of Minnesota Supercomputing Institute, Minneapolis, MN 55455</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533700123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533700123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2511296123?af=R">
      <title>The m5C orchestrator NSUN7 drives SPARC/HMGB1 axis–mediated inflammation to exacerbate kidney injury</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2511296123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceRNA modifications like 5-methylcytosine (m5C) are emerging as critical regulators of inflammation, but their functional role in kidney diseases remains unknown. We identify NOP2/Sun RNA methyltransferase family member 7 (NSUN7) promotes renal ...</description>
      <dc:title>The m5C orchestrator NSUN7 drives SPARC/HMGB1 axis–mediated inflammation to exacerbate kidney injury</dc:title>
      <dc:identifier>doi:10.1073/pnas.2511296123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Yu-hang DongShuai-shuai XieShuai SunYu RenQin YangJie WeiRui HouXiang-yu LiJing-wen WuWen-xian MaJu-tao YuMeng-ting HeChao LiJia-nan WangMing-lu JiZi-yi LiuZe-hui DongXiao-yu ShenXin-yu ChenXiao-guo SuoWei DongJuan JinJie WangWen-bin WangXiao-ming MengaDepartment of Toxicology, School of Public Health, Anhui Medical University, Hefei 230032, ChinabInflammation and Immune Mediated Diseases Laboratory of Anhui Province, The Key Laboratory of Anti-inflammatory of Immune Medicines, Ministry of Education, Anhui Institute of Innovative Drugs, School of Pharmacy, Anhui Medical University, Hefei 230032, ChinacDepartment of Urology, The First Affiliated Hospital of Anhui Medical University, Hefei 230022, ChinadAnhui Province Key Laboratory of Urological and Andrological Diseases Research and Medical Transformation, Institute of Urology, Anhui Medical University, Hefei 230022, ChinaeDepartment of Clinical Pharmacology, The Second Affiliated Hospital of Anhui Medical University, Hefei 230601, ChinafDepartment of Nephrology, The Second Affiliated Hospital of Anhui Medical University, Hefei 230601, ChinagSchool of Medicine, Tongji University, Shanghai 200092, ChinahDepartment of Immunology, School of Basic Medical Sciences, Anhui Medical University, Hefei 230032, ChinaiDepartment of Pharmacology, School of Basic Medical Sciences, Anhui Medical University, Hefei 230032, ChinajDepartment of Emergency Surgery, The Second Affiliated Hospital of Anhui Medical University, Hefei 230601, ChinakDepartment of General Surgery, The Second Affiliated Hospital of Anhui Medical University, Hefei 230601, ChinalDepartment of Vascular Surgery, The Second Affiliated Hospital of Anhui Medical University, Hefei 230601, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2511296123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2511296123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2504045123?af=R">
      <title>Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2504045123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceInfluenza remains a major global health threat. We introduce oseltamivir-based aziridines that unite transition-state mimicry for tight binding with aziridine-enabled covalent capture of the catalytic tyrosine. This dual function yields potent,...</description>
      <dc:title>Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents</dc:title>
      <dc:identifier>doi:10.1073/pnas.2504045123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Merijn B. L. VriendsElisha MoranMartín CalveloThomas HansenIsabelle B. PicklesXincheng XinMarieke BiezenoZachary W. B. ArmstrongMaria J. FerrazLei LiAlice LilleyRuth HarveyDmitri V. FilippovQinghua LiaoSybrin P. SchröderGijsbert A. van der MarelMarta ArtolaJohannes M. F. G. AertsJames N. BlazaJeroen D. C. CodéeCarme RoviraHerman S. OverkleeftGideon J. DaviesaDepartment of Bio-organic Synthesis, Leiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The NetherlandsbDepartment of Chemistry, University of York Heslington, York YO10 5DD, United KingdomcDepartament de Química Inorgaǹica i Orgaǹica (Seccióde Química Orgaǹica) and Institut de Química TeorÌica I Computacional, Universitat de Barcelona, Barcelona 08028, SpaindFundació Catalana de Recerca i Estudis Avancats, Barcelona 08010, SpaineDepartment of Medical Biochemistry, Leiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The NetherlandsfWorldwide Influenza Centre, The Francis Crick Institute, London NW1 1AT, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2504045123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2504045123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2515413123?af=R">
      <title>General and selective nickel-electrocatalyzed cross-electrophile C*(sp2)–C(sp2) coupling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2515413123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceC(sp2)–C(sp2) bonds are pivotal in pharmaceuticals, natural products, and functional organic/polymeric materials. Thus, developing robust, efficient methods to construct C(sp2)–C(sp2) linkages is an important objective in synthetic chemistry. ...</description>
      <dc:title>General and selective nickel-electrocatalyzed cross-electrophile C*(sp2)–C(sp2) coupling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515413123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Wenbin XieZhe SongQinqin ShiPanping ShengGu XuKaikai WenLutang ZhaoTobin J. MarksZhi-Xiang WangHui HuangaCollege of Materials Science and Opto-Electronic Technology, University of Chinese Academy of Sciences, Beijing 100049, P. R. ChinabSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 100049, P. R. ChinacBeijing Institute of Nanoenergy and Nanosystems, Chinese Academy of Sciences, Beijing 100140, P. R. ChinadDepartment of Chemistry and the Materials Research Center, Northwestern University, Evanston, IL 60208eCenter of Materials Science and Optoelectronics Engineering, University of Chinese Academy of Sciences, Beijing 100049, P. R. ChinafSchool of Chemical Engineering and Technology, State Key Laboratory of Chemical Engineering and Low-Carbon Technology, Tianjin University, Tianjin 300072, P. R. China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515413123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514681123?af=R">
      <title>Identifying a cancer therapeutic target: Cell-SELEX identifies a membrane protein for aptamer-mediated growth suppression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514681123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThis study establishes an integrated workflow from the identification of a high-affinity aptamer (CW06) to the identification of its target, SLC25A24. We further reveal a therapeutic mechanism wherein the aptamer exerts antitumor effects by ...</description>
      <dc:title>Identifying a cancer therapeutic target: Cell-SELEX identifies a membrane protein for aptamer-mediated growth suppression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514681123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Wei CuiHang XiaoXiaohong WenChen LiSuxia BaoJiahao ZengYangbing LiYan QiaoKemin WangHonghui WangJin HuangQiuping GuoaState Key Laboratory of Chemo and Biosensing, Hunan University, Changsha 410082, People’s Republic of ChinabCollege of Biology, Hunan University, Changsha 410082, People’s Republic of ChinacKey Laboratory for Bio-Nanotechnology and Molecular Engineering of Hunan Province, Hunan University, Changsha 410082, People’s Republic of ChinadCollege of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, People’s Republic of ChinaeDepartment of Pathophysiology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, People’s Republic of ChinafHunan Research Center of the Basic Discipline for Cell Signaling, Hunan University, Changsha 410082, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514681123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514681123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537053123?af=R">
      <title>Recurrent SARS-CoV-2 Omicron broadly neutralizing humanized antibodies in different single human VH1-2-rearranging mouse models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537053123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMouse models that generate antibody repertoires from human gene segments that predominantly encode single antibody lineages are useful for evaluating preclinical HIV-1 vaccine strategies. One such model was used for discovery of a humanized ...</description>
      <dc:title>Recurrent SARS-CoV-2 Omicron broadly neutralizing humanized antibodies in different single human VH1-2-rearranging mouse models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537053123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Himanshu BatraSai LuoKevin O. SaundersJaclyn S. HigginsFanchong JianJun ZhangMd Golam KibriaG. M. JonaidQingchen J. ZhouAmanda EatonKenneth CroninMichael L. MalloryMelissa MattocksRobert J. EdwardsRobert ParksEsther M. LeeAdam Yongxin YeAimee Chapdelaine WilliamsGeeyoun JungKatayoun MansouriS. Munir AlamDavid C. MontefioriMing TianRalph S. BaricYunlong CaoBarton F. HaynesBing ChenFrederick W. AltaHoward Hughes Medical Institute, Boston Children’s Hospital, Boston, MA 02115bProgram in Cellular and Molecular Medicine, Boston Children’s Hospital, Boston, MA 02115cDepartment of Genetics, Harvard Medical School, Boston, MA 02115dDuke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710eDepartment of Surgery, Duke University, Durham, NC 27710fDepartment of Integrative Immunobiology, Duke University School of Medicine, Durham, NC 27710gDepartments of Epidemiology and Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599hBiomedical Pioneering Innovation Center, Peking University, Beijing 100871, ChinaiChangping Laboratory, Beijing 102206, ChinajDivision of Molecular Medicine, Boston Children’s Hospital, Harvard Medical School, Boston, MA 02115kDepartment of Pediatrics, Harvard Medical School, Boston, MA 02115lDepartment of Medicine, Duke University School of Medicine, Durham, NC 27710mDepartment of Immunology, Duke University School of Medicine, Durham, NC 27710</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537053123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537053123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526787123?af=R">
      <title>Cross-cultural evidence that shame is a defense against reputational damage</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526787123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe question of whether a psychological system is adaptive or maladaptive, and whether it is universal or culturally variable, depends on the researcher’s frame of reference, and different frames can yield radically different answers. Yet ...</description>
      <dc:title>Cross-cultural evidence that shame is a defense against reputational damage</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526787123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Yiftach ArgamanDaniel SznycerJan CrusiusFlorian van LeeuwenYohsuke OhtsuboHitomi IshiharaJin-Ying ZhuangQi-Jun ZhouThomas CastelainFélix NetoJoana NetoAssaf KronaDepartment of Psychology, University of Greifswald, Greifswald 17489, GermanybDepartment of Psychology, Oklahoma State University, Stillwater, OK 74078cDepartment of Social Psychology, Tilburg University, Tilburg 5037 AB, The NetherlandsdDepartment of Social Psychology, Graduate School of Humanities and Sociology, The University of Tokyo, Tokyo 113-0033, JapaneSchool of Psychology and Cognitive Science, East China Normal University, Shanghai 200062, ChinafComparative Minds research group, Department of Psychology, University of Girona, Girona 17003, SpaingDepartment of Psychology, University of Porto, Porto 4200-135, PortugalhResearch on Economics, Management, and Information Technologies, Universidade Portucalense, Porto 4200-135, PortugaliDepartment of Psychology, University of Haifa, Haifa 3103301, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526787123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526787123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602460123?af=R">
      <title>CD47 stabilizes ROBO2 to regulate glioblastoma progression by preventing ITCH-mediated ubiquitination</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602460123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceCD47, a key innate immune checkpoint, limits phagocytosis by myeloid cells and enables cancer immune evasion, but anti-CD47 therapies show poor efficacy in glioblastoma (GBM). Here, we uncover a critical cell-intrinsic role for CD47 in GBM, ...</description>
      <dc:title>CD47 stabilizes ROBO2 to regulate glioblastoma progression by preventing ITCH-mediated ubiquitination</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602460123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Ruhi PolaraBriony L. GliddonRaja GanesanLorena T. DaviesJohn ToubiaSakthi LeninGhizal SiddiquiOlivia Morris-HanonMelinda N. TeaPaul A. B. MorettiDung A. NguyenChung Hoow KokChloe ShardAlexander H. StaudacherMichael P. BrownDarren J. CreekGuillermo A. GomezDaniel ThomasStuart M. PitsonNirmal RobinsonaCentre for Cancer Biology, College of Health, Adelaide University and SA Pathology, Adelaide, SA 5001, AustraliabCologne Cluster of Excellence in Cellular Stress Responses in Aging-Associated Diseases, University Clinic Cologne, Cologne 50931, GermanycData and Bioinformatics Innovation, Department of Genetics and Molecular Pathology, SA Pathology, Adelaide, SA 5000, AustraliadDrug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville Campus, Parkville, VIC 3052, AustraliaeSchool of Medicine, College of Health, Adelaide University, Adelaide, SA 5000, AustraliafCancer Clinical Trials Unit, Royal Adelaide Hospital, Adelaide, SA 5000, AustraliagPrecision Cancer Medicine Theme, South Australian Health and Medical Research Institute, Adelaide, SA 5001, AustraliahDepartment of Hematology and Bone Marrow Transplantation, Royal Adelaide Hospital, Adelaide, SA 5000, AustraliaiSchool of Biological Sciences, College of Science, Adelaide University, Adelaide, SA 5005, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602460123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602460123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530834123?af=R">
      <title>Amplifying toughness in silica-reinforced natural rubber by preserving long chains</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530834123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceNatural rubber is the most widely used bioelastomer, valued for its high crack resistance arising from long rubber chains and strain-induced crystallization (SIC). However, this advantage is not fully realized in silica-reinforced natural ...</description>
      <dc:title>Amplifying toughness in silica-reinforced natural rubber by preserving long chains</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530834123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Matthew Wei Ming TanGuodong NianZheqi ChenXianyang BaoYakov KutsovskyZhigang SuoaJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138bSchool of Materials Science and Engineering, Nanyang Technological University, Singapore 639798, SingaporecExpert-in-Residence, Office of Technology Development, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530834123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530834123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520144123?af=R">
      <title>Status of the sunken nuclear submarine Komsomolets in the Norwegian Sea</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520144123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe Komsomolets nuclear powered submarine sank with nuclear weapons onboard toward the end of the Cold War between the United States and the former Soviet Union and their respective allies. The events of the Cold War propagated societal fears ...</description>
      <dc:title>Status of the sunken nuclear submarine Komsomolets in the Norwegian Sea</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520144123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Justin P. GwynnHilde Elise HeldalHans-Christian TeienAndrey VolynkinSimon M. JeromeOle Christian LindaSection High North, Department for International Nuclear Safety and Security, and Research and Development, Norwegian Radiation and Nuclear Safety Authority, The Fram Centre, Tromsø 9007, NorwaybDepartment of Contaminants and Biohazards, Institute of Marine Research, Bergen 5005, NorwaycFaculty of Environmental Sciences and Natural Resource Management, Norwegian University of Life Sciences, Ås 1433, NorwaydNorwegian Nuclear Research Centre, Oslo 0371, NorwayeInorganic Chemistry Laboratory, Institute of Marine Research, Bergen 5005, Norway</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520144123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520144123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534576123?af=R">
      <title>A high-coverage Neandertal genome from the Altai Mountains reveals population structure among Neandertals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534576123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceWe present a high-quality genome of a ~110,000-y-old male Neandertal from Denisova Cave in the Altai Mountains. He as well as a ~120,000-y-old Neandertal from the same cave lived in smaller and more isolated groups than later Neandertals in ...</description>
      <dc:title>A high-coverage Neandertal genome from the Altai Mountains reveals population structure among Neandertals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534576123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Diyendo MassilaniStéphane PeyrégneLeonardo N. M. IasiCesare de FilippoFabrizio MafessoniAlba Bossoms MesaArev P. SümerYaniv SwielDivyaratan PopliShahar SilvermanMichael James BoyleMaxim B. KozlikinMichael V. ShunkovAnatoly P. DereviankoTom HighamKaterina DoukaMatthias MeyerHugo ZebergJanet KelsoSvante PääboaDepartment of Genetics, Yale School of Medicine, New Haven, CT 06510bDepartment of Evolutionary Genetics, Max Planck Institute for Evolutionary Anthropology, Leipzig 04103, GermanycDepartment of Life Sciences, University of Trieste, Trieste 34127, ItalydInstitute of Archaeology and Ethnography of the Siberian Branch of the Russian Academy of Sciences, Novosibirsk 630090, RussiaeDepartment of Evolutionary Anthropology, Faculty of Life Sciences, University of Vienna, Vienna 1030, AustriafHuman Evolution and Archaeological Sciences Network, University of Vienna, Vienna 1030, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534576123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534576123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514066123?af=R">
      <title>Unprecedented Amazonian rainforests damage during the 2023–2024 droughts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514066123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe Amazonian rainforests account for around a quarter of global forest carbon stocks, and they are increasingly threatened by severe droughts, particularly the record-breaking and consecutive droughts of 2023–2024. Using long-term continuous ...</description>
      <dc:title>Unprecedented Amazonian rainforests damage during the 2023–2024 droughts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514066123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Hao BaiXiangzhuo LiuHui YangJerome ChavePhilippe CiaisJean-Pierre WigneronSassan SaatchiJingfeng XiaoThuy Le ToanXiaomei HuZiyan YangLijun WangLei FanYitong YaoXiuzhi ChenYanxu LiuBaolin XueQinghua GuoZhiyao TangHongyan LiuJingyun FangShengli TaoaInstitute of Ecology, College of Urban and Environmental Sciences, and State Key Laboratory of Vegetation Structure, Function and Construction, Peking University, Beijing 100871, ChinabUMR 1391 Interaction Sol Plante Atmosphère, Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement, Villenave d’Ornon 33140, FrancecCollege of Urban and Environmental Sciences, Peking University, Beijing 100871, ChinadCentre de Recherche sur la Biodiversité et l’Environnement, UMR 5300, Centre National de la Recherche Scientifique (CNRS), Institut pour la Recherche et le Développement, Institut National Polytechnique de Toulouse, Université de Toulouse, Toulouse Cedex 9 31062, FranceeLaboratoire des Sciences du Climat et de l’Environnement, Commissariat à l’Energie Atomique et aux Energies Alternatives, Centre National de la Recherche Scientifique, Université de Versailles St Quentin en Yvelines, Université Paris-Saclay, Gif-sur-Yvette 91191, FrancefJet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91109gInstitute of the Environment and Sustainability, University of California, Los Angeles, CA 90095hEarth Systems Research Center, Institute for the Study of Earth, Oceans, and Space, University of New Hampshire, Durham, NH 03824iCentre d’Etudes Spatiales de la Biosphère, Toulouse 31400, FrancejChongqing Jinfo Mountain Karst Ecosystem National Observation and Research Station, School of Geographical Sciences, Southwest University, Chongqing 400715, ChinakDivision of Geological and Planetary Sciences, California Institute of Technology, Pasadena, CA 91125lSchool of Atmospheric Sciences, Guangdong Province Data Center of Terrestrial and Marine Ecosystems Carbon Cycle, Sun Yat-sen University, Zhuhai, Guangdong 510275, ChinamState Key Laboratory of Earth Surface Processes and Hazards Risk Governance, Faculty of Geographical Science, Beijing Normal University, Beijing 100875, ChinanAdvanced Interdisciplinary Institute of Satellite Applications, Beijing Normal University, Beijing 100875, ChinaoInstitute of Remote Sensing and Geographic Information System, School of Earth and Space Sciences, Peking University, Beijing 100871, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514066123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514066123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2427242123?af=R">
      <title>Unveiling the developmental and tumor-suppressive roles of the p53 variant p53psi</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2427242123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe TP53 gene is known to encode a powerful tumor suppressor, but alternative splicing of this gene also produces multiple isoforms whose biological functions remain poorly understood. Some of these isoforms have even been implicated in cancer ...</description>
      <dc:title>Unveiling the developmental and tumor-suppressive roles of the p53 variant p53psi</dc:title>
      <dc:identifier>doi:10.1073/pnas.2427242123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Chiara GorriniSoode JafariGordon DuncanBryan SnowLiam HendrikseLouis McLoughlinJillian HaightAndrew WakehamChantal TobinAndrew EliaParamesh RamachandranRhoda LawBevan GangTsai-Ling LuIsabel Morgado-PalacinAnnick You-TenThorsten BergerRaffaella SordellaTak W. MakaPrincess Margaret Cancer Centre, University Health Network, Toronto, ON M5G 2M9, CanadabSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, United KingdomcCold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724dCentre for Oncology and Immunology, Hong Kong Special Administrative Region of China, ChinaeDepartment of Pathology, School of Clinical Medicine, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Queen Mary Hospital, Hong Kong Special Administrative Region of China, ChinafDepartments of Immunology and Medical Biophysics, University of Toronto, Toronto, ON M5G 2C4, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2427242123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2427242123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2515805123?af=R">
      <title>Mineral-facilitated aqueous synthesis of hydrogen cyanide from prebiotically abundant amino acids for chemical evolution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2515805123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceOrigin of life strongly relies on reactive carbon and nitrogen precursors, among which hydrogen cyanide (HCN) is one of the most versatile molecules that can be used for synthesizing almost all essential biomolecules. However, recent ...</description>
      <dc:title>Mineral-facilitated aqueous synthesis of hydrogen cyanide from prebiotically abundant amino acids for chemical evolution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515805123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Zening YangYamei LiNorio KitadaiMasahiro YamamotoYuichiro UenoYanjing LuAilong LiKiyohiro AdachiAkira YamaguchiDaisuke HashizumeRyuhei NakamuraaEarth-Life Science Institute, Institute of Future Science, Institute of Science Tokyo, Meguro-ku, Tokyo 152-8550, JapanbDepartment of Chemical Science and Engineering, School of Materials and Chemical Technology, Institute of Science Tokyo, Ookayama, Meguro-ku, Tokyo 152-8552, JapancBiofunctional Catalyst Research Team, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, JapandInstitute for Extra-Cutting-Edge Science and Technology Avant-Garde Research, Japan Agency for Marine-Earth Science and Technology, Yokosuka 237-0061, JapaneDepartment of Earth and Planetary Sciences, Institute of Science Tokyo, Meguro-ku, Tokyo 152-8551, JapanfMaterials Characterization Support Team, RIKEN Center for Emergent Matter Science, Wako, Saitama 351-0198, JapangDepartment of Materials Science and Engineering, School of Materials and Chemical Technology, Institute of Science Tokyo, Ookayama, Meguro-ku, Tokyo 152-8552, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515805123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2515805123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520352123?af=R">
      <title>GFAP+ FOXF2+ ependymal cells promote blood–brain barrier repair via DLL4–NOTCH signaling after neural injury</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520352123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceEpendymal cells (EP) in the adult ventricular-subventricular zone (V-SVZ) are recognized for diverse functions beyond cerebrospinal fluid (CSF) dynamics, yet their identity, specialization, and roles in niche interactions and postinjury repair ...</description>
      <dc:title>GFAP+ FOXF2+ ependymal cells promote blood–brain barrier repair via DLL4–NOTCH signaling after neural injury</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520352123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Qi XieHui LuXiaoman WangSiya WuQian HeMengqi YuanShuang ZhangLinlin HuChangxiong GongXiaofeng ChengYiliang FangZhaoyou MengYilong WangSen LinQingwu YangaDepartment of Neurology, Second Affiliated Hospital, Army Medical University (Third Military Medical University), Chongqing 400037, ChinabChongqing Institute for Brain and Intelligence, Guangyang Bay Laboratory, Chongqing 400064, ChinacDepartment of Obstetrics and Gynecology, Southwest Hospital of the Third Military Medical University (The First Affiliated Hospital of the Army Medical University), Chongqing 400038, ChinadDepartment of Neurology, Beijing Tiantan Hospital, Capital Medical University, Beijing 100070, ChinaeChinese Institute for Brain Research, Beijing 102206, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520352123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520352123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535653123?af=R">
      <title>Phages drive the dissemination of antibiotic resistance genes by facilitating host adaptation to heavy metal stress</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535653123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAntibiotic resistance threatens global health. The role of phages in the spread of antibiotic resistance genes (ARGs) has recently attracted widespread attention. Heavy metal contamination, pervasive in agricultural soils, has emerged as a ...</description>
      <dc:title>Phages drive the dissemination of antibiotic resistance genes by facilitating host adaptation to heavy metal stress</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535653123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Luo-Qin ShenLu WangZhiyuan YaoDa LinYu-Qiu YeWan-rong ZhangMao YeMing-Ming SunShuai DuDi WuPatrick O’ConnorDong ZhuaState Key Laboratory of Regional and Urban Ecology, Ningbo Observation and Research Station, Institute of Urban Environment, Chinese Academy of Sciences, Xiamen 361021, ChinabCollege of Resources and Environment, University of Chinese Academy of Sciences, Beijing 100049, ChinacZhejiang Key Laboratory of Pollution Control for Port-Petrochemical Industry, CAS Haixi Industrial Technology Innovation Center in Beilun, Ningbo 315830, ChinadSchool of Civil &amp; Environmental Engineering and Geography Science, State Key Laboratory for Quality and Safety of Agro-products, Ningbo University, Ningbo 315211, ChinaeCollege of Environmental Science and Engineering, Ocean University of China, Qingdao 266100, ChinafYunnan Provincial Key Lab of Soil Carbon Sequestration and Pollution Control, Faculty of Environmental Science &amp; Engineering, Kunming University of Science &amp; Technology, Kunming 650500, ChinagNational Engineering Research Center for Soil Nutrient Management and Pollution Remediation, Institute of Soil Science, Chinese Academy of Sciences, Nanjing 210008, ChinahSoil Ecology Lab, Nanjing Agricultural University, Nanjing 210095, ChinaiInstitute for Global Food Security, School of Biological Sciences, Queen’ s University, Belfast BT9 5DL, United KingdomjCentre for Global Food and Resources, Faculty of Health and Medical Sciences, University of Adelaide, Adelaide 500S, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535653123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535653123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514645123?af=R">
      <title>NLRP1B is an integrated decoy that subverts Shigella flexneri E3 ligase activity to promote effector-triggered immunity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514645123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceEffector-triggered immunity is the process through which the immune system recognizes and responds to the activities of pathogen-encoded toxins and enzymes. Integrated decoy receptors mimic other host proteins to subvert the activities of ...</description>
      <dc:title>NLRP1B is an integrated decoy that subverts Shigella flexneri E3 ligase activity to promote effector-triggered immunity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514645123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Siwon ChungHannah HudsonKaitlin A. StrombergAndrew SandstromaDepartment of Immunology, University of Texas Southwestern Medical Center, Dallas, TX 75390</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514645123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514645123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529493123?af=R">
      <title>Dynamic translocation of Inside-Out proteins to the cell surface underlies cellular adaptation to cancer-induced stress</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529493123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThis study describes “Inside-Out” (I-O) proteins, a class of intracellular proteins that translocate to the cell surface under stress or disease conditions through a mechanism distinct from conventional secretion pathways. I-O proteins are ...</description>
      <dc:title>Dynamic translocation of Inside-Out proteins to the cell surface underlies cellular adaptation to cancer-induced stress</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529493123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Tomasz SlezakKelly M. O’LearyTanya Guevara AvellaNatalia MusialJinyang LiAnna AndrzejczakElizabeth F. ScottDuc Anh LeAnthony A. KossiakoffaDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637bIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdańsk 80-307, PolandcDepartment of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław 53-114, PolanddInstitute for Biophysical Dynamics, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529493123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529493123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534717123?af=R">
      <title>Self-regulated dual-mode solar energy harvesting</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534717123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHarvesting solar energy is of fundamental importance to the green economy. However, traditional technologies are single-mode, converting sunlight to either heat or electricity. We introduce dual-mode solar harvesters that leverage phase-...</description>
      <dc:title>Self-regulated dual-mode solar energy harvesting</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534717123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Raphael KayRafiq OmairJoanna AizenbergaHarvard John A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138bDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534717123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534717123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528407123?af=R">
      <title>Depth of nutrient uptake by deep-rooted plants is regulated by water availability</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528407123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePlant uptake of water and nutrients occurs mostly in soil top layers. Some plants with deep roots can also obtain water from deeper regions in the saprolite, the boundary between soil and bedrock. Deep water uptake can provide resistance to ...</description>
      <dc:title>Depth of nutrient uptake by deep-rooted plants is regulated by water availability</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528407123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Langlang LiJohn N. ChristensenMarkus BillWenming DongYuxin WuCurtis BeutlerMatthias SprengerBrian W. GulickSharon E. BoneBoris FaybishenkoJohn SandersChunwei ChouAmanda HendersonNicholas J. BouskillKenneth H. WilliamsBenjamin GilbertaDepartment of Earth and Planetary Science, University of California, Berkeley, CA 94720bEarth and Environmental Science Area, Lawrence Berkeley National Laboratory, Berkeley, CA 94720cRocky Mountain Biological Laboratory, Crested Butte, CO 81224dDepartment of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695eDepartment of Geosciences, Stony Brook University, Stony Brook, NY 11794fStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025gDepartment of Environmental Science, Policy and Management, University of California, Berkeley, CA 94720hDepartment of Biological and Ecological Engineering, Oregon State University, Corvallis, OR 97331</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528407123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528407123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602529123?af=R">
      <title>Inorganic phosphate and the rapid mobilization of metabolic energy in neurons</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602529123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceNeurons rapidly change their metabolism to meet the energy demands caused by depolarization. Understanding the mechanism of this fast response has been challenging due in part to the difficulty in measuring the small-molecule regulators of ...</description>
      <dc:title>Inorganic phosphate and the rapid mobilization of metabolic energy in neurons</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602529123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Paul C. RosenShivang SullerePanhui FuJuan R. Martínez-FrançoisDaniel J. BrooksErica KimChenghua GuGary YellenaDepartment of Neurobiology, Harvard Medical School, Boston, MA 02115bDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139cHHMI, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602529123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602529123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537571123?af=R">
      <title>Cell type diversification and phenotype convergence underlying white fin-ornamentation of cyprinid fishes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537571123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceUnderstanding how cell types arise is fundamental to explaining animal complexity. Pigment cells offer opportunities to address this question because they display striking variation. We show that white pigment cells, likely important to ...</description>
      <dc:title>Cell type diversification and phenotype convergence underlying white fin-ornamentation of cyprinid fishes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537571123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Delai HuangTiffany LiuAugust A. CarrPietro H. de MelloYipeng LiangLeah P. ShriverFrançois ChauvignéStephen L. JohnsonJoan CerdàGary J. PattiDavid M. ParichyaDepartment of Biology, University of Virginia, Charlottesville, VA 22903bDepartment of Chemistry, Washington University, St. Louis, MO 63110cCenter for Mass Spectrometry and Metabolic Tracing, Washington University, St. Louis, MO 63110dDepartment of Medicine, Washington University School of Medicine, St. Louis, MO 63110eInstitute of Marine Sciences, Spanish National Research Council, Barcelona 08003, SpainfInstitute of Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra (Cerdanyola del Vallès) 08193, SpaingDepartment of Genetics, Washington University School of Medicine, St. Louis, MO 63110hDepartment of Cell Biology, University of Virginia, Charlottesville, VA 22903</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537571123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537571123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524661123?af=R">
      <title>Convergent motifs of early olfactory processing are recapitulated by layer-wise efficient coding</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524661123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAnimals from insects to rodents rely on smell as their primary means of sensing their environment. Strikingly, animals as different as ants and humans have convergently evolved similar sensory architectures to solve the common problem of ...</description>
      <dc:title>Convergent motifs of early olfactory processing are recapitulated by layer-wise efficient coding</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524661123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Juan Carlos Fernández del CastilloFarhad PashakhanlooVenkatesh N. MurthyJacob A. Zavatone-VethaCenter for Brain Science, Harvard University, Cambridge, MA 02138bProgram in Biophysics, Harvard University, Cambridge, MA 02138cDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138dKempner Institute for the Study of Natural and Artificial Intelligence, Harvard University, Cambridge, MA 02138eSociety of Fellows, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524661123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524661123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523453123?af=R">
      <title>Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523453123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceBacterial ribosomal RNA (rRNA) methylations are important for ribosome function and antibiotic sensitivity, but little is known about how they are incorporated during ribosome biogenesis. Using single-particle cryo-EM and complementary ...</description>
      <dc:title>Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523453123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Mohamed I. BarmadaErin N. McGinitySuparno NandiDebayan DeyNatalia ZelinskayaGeorge M. HarrisLindsay R. ComstockChristine M. DunhamGraeme L. ConnaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322bGraduate Program in Biochemistry, Cell and Developmental Biology, Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322cDepartment of Chemistry, Wake Forest University, Winston-Salem, NC 27106dDepartment of Chemistry, Emory University, Atlanta, GA 30322</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523453123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523453123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526550123?af=R">
      <title>Fab–Fc and Fab–Fab interactions of variable strength and valency contribute to the high concentration viscosity of IgG1 antibodies</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526550123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSubcutaneous injection is increasingly favored over intravenous infusion for antibody therapies such as IgG for multiple reasons including faster administration and greater convenience for patients. Subcutaneous delivery commonly requires ...</description>
      <dc:title>Fab–Fc and Fab–Fab interactions of variable strength and valency contribute to the high concentration viscosity of IgG1 antibodies</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526550123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Joel HeislerJennifer L. HofmannZhenyu TanJonathan ZarzarSaeed IzadiPaul J. CarteraDepartment of Antibody Engineering, Genentech, Inc., South San Francisco, CA 94080bDepartment of AI for Drug Discovery, Genentech, Inc., South San Francisco, CA 94080cDepartment of Pharmaceutical Development, Genentech, Inc., South San Francisco, CA 94080</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526550123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526550123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528153123?af=R">
      <title>The phospholipid profile of T cells shapes ACSL4 dependency and ferroptosis sensitivity of naive, effector, and memory T cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528153123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceFerroptosis, a regulated cell death program induced by phospholipid (PL) peroxidation, has been extensively studied in cancer cells as a therapeutic strategy; however, its characterization in primary T cells remains poorly understood. Here, ...</description>
      <dc:title>The phospholipid profile of T cells shapes ACSL4 dependency and ferroptosis sensitivity of naive, effector, and memory T cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528153123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Gariné MagarditchianIvan BerestAikaterini ZiogouMai MatsushitaMichelle ReidAlaa OthmanManfred KopfaDepartment of Biology, Institute of Molecular Health Sciences, ETH Zurich, Zurich 8093, SwitzerlandbFunctional Genomics Center Zurich, Metabolomics Unit, Zurich 8057, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528153123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528153123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535665123?af=R">
      <title>The psychology of offensive and defensive intergroup violence: Preregistered insights from 58 countries</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535665123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHistorically, intergroup violence has been motivated by both offensive and defensive goals, often blending narratives of protection with ambitions of domination. In a preregistered study spanning 58 countries, we show that defensive and ...</description>
      <dc:title>The psychology of offensive and defensive intergroup violence: Preregistered insights from 58 countries</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Jonas R. KunstTomasz BestaMichał JaśkiewiczAnna Natalia GajdaMarkus SandenMina Marie FlatebøSulaiman Olanrewaju AdebayoMarios AdonisCollins Badu AgyemangRaymond Agyenim BoatengSerap Arslan AkfiratSamir Al-adawiChiara AmbrosioGulnaz AnjumJohn Jamir Benzon R. ArutaIvars AustersOumar BarryBrock BastianMaja BeckerMichael BenderNora Cornelia Glerud BenningstadIslam BorincaGöksu CelikkolJiří ČeněkTrawin ChaleeraktrakoonPhatthanakit ChobthamkitHoon-Seok ChoiSuyeong ChoiPatricia CiordasAnn-Cathrin CoenenAleksandra CuptaPiyanjali de ZoysaSandesh DhakalLauren E. DuncanTuğçenaz ElcilBarkan EskiiliEdgardo EtchezaharRenata FrancSilvia GaldiMagdalena GarvanovaPaul GillAugusto GnisciAngel GómezTalía Gómez YepesIgor GrossmannEmily A. HainesFatjona HakaBoaz HameiriImaduddin HamzahMai HelmyRoland ImhoffShanmukh KambleFiona KazarovytskaAnna KendeNarine KhachatryanSasha Y. KimelJack W. KleinAdam KomisarofDavid LackoTimo Juhani LajunenBarbara LášticováClaudio López-CalleWilson López-LópezBarbara Kalebić MaglicaRomualdas MalinauskasSona ManusyanKhatuna MartskvishviliGustave Adolphe MessangaMarta MiklikowskaJelena MinicTamara MohorićFrancesca MottolaSilvana MulaPasquale MussoDieynaba Gabrielle NdiayeFélix NetoJoana NetoLaina Ngom DiengIhuoma Faith ObiomaTosin Tunrayo OlonisakinSimon OzerPenny PanagiotopoulouBeata Pastwa-WojciechowskaVassilis PavlopoulosTomislav PavlovićInha PetrovskaAndrzej PiotrowskiXenia Daniela PoslonLotte PummererMahima RainaJano Ramos-DiazVilja RobertssonBettina RottweilerDavid L. SamRosa ScardignoMarion K. SchulmeyerAnna StefaniakAnna StudzinskaMark J. M. SullmanMarcin SzulcWilly Taffo NembouéErgyul TairNicole TauschNarendra Singh ThagunnaEmma F. ThomasJoaquín UngarettiColette Van LaarŽermēna VazneAlexandra VázquezJose Villanueva-AlvaradoAnna WlodarczykKumar YogeeswaranMilan ObaidiaDepartment of Communication and Culture, BI Norwegian Business School, Oslo 0484, NorwaybInstitute of Psychology, University of Gdańsk, Gdańsk 80-309, PolandcDepartment of Psychology, University of Oslo, Oslo 0315, NorwaydDepartment of Psychology, Ekiti State University, Ado-Ekiti 360101, NigeriaeDepartment of Social Sciences, School of Humanities and Social Sciences, University of Nicosia, Nicosia 2417, CyprusfDepartment of Psychology, University of Ghana, Accra LG 25, GhanagDivision of Social Sciences, Humanities and Design, College of Professional and Continuing Education, Hong Kong Polytechnic University, CPCE, Hong Kong, ChinahDepartment of Psychology, Dokuz Eylul University, Izmir 35390, TurkeyiDepartment of Behavioral Medicine, College of Medicine and Health Sciences, Sultan Qaboos University, Muscat 123, OmanjDepartment of Psychology, University of Campania “Luigi Vanvitelli”, Caserta 81100, ItalykDepartment of Psychology, Centre for Social Issues Research, University of Limerick, Limerick V94 T9PX, IrelandlDepartment of Psychology, De La Salle University, Manila 1004, PhilippinesmDepartment of Psychology, University of Latvia, Riga LV-1586, LatvianDepartment of Psychology, Université Cheikh Anta Diop de Dakar, Dakar 5005, SenegaloMelbourne School of Psychological Sciences, University of Melbourne, Melbourne 3010, AustraliapCognition, Langues, Langage, Ergonomie, Université de Toulouse, CNRS, Toulouse 31058, FranceqDepartment of Social Psychology, Tilburg University, Tilburg 5037 AB, NetherlandsrDepartment of Social Psychology, University of Groningen, Groningen 9712 CP, NederlandssDepartment of Social Studies, Mendel University in Brno, Brno 613 00, Czech RepublictDepartment of Psychology, Thammasat University, Pathumthani 12121, ThailanduDepartment of Psychology, Sungkyunkwan University, Seoul 03063, South KoreavDepartment of Psychology, University of Waterloo, Waterloo, ON N2L 3G1, CanadawDepartment of Social Psychology, ELTE Eötvös Loránd University, Budapest 1053, HungaryxDepartment of Psychiatry, University of Colombo, Colombo 00800, Sri LankayCentral Department of Psychology, Tribhuvan University, Kathmandu 44618, NepalzDepartment of Psychology, Smith College, Northampton, MA 01063aaDepartment of Psychology, Istanbul Gedik University, Istanbul 34876, TurkeybbDepartment of Evolutionary Psychology and Education, Autonomous University of Madrid, Madrid 28049, SpainccDepartment of Psychology, Ivo Pilar Institute of Social Sciences, Zagreb 10000, CroatiaddDepartment of Information Systems and Technologies, University of Library Studies and Information Technologies, Sofia 1784, BulgariaeeDepartment of Security and Crime Science, University College London, London WC1H 9EZ, United KingdomffDepartment of Social and Organizational Psychology, Universidad Nacional de Educación a Distancia, Madrid 28040, SpainggAfrican Centre for Epistemology and Philosophy of Science, University of Johannesburg, Johannesburg 2092, South AfricahhCollege of Education, Psychology and Social Work, Flinders University, Adelaide SA 5042, AustraliaiiFaculty of Social Sciences, University of Tirana, Tirana 1001, AlbaniajjProgram in Conflict Management and Mediation, Tel Aviv University, Tel Aviv 6997801, IsraelkkDepartment of Community Guidance, Politeknik Pengayoman Indonesia, Depok 16514, IndonesiallDepartment of Psychology, College of Education, Sultan Qaboos University, Muscat 123, OmanmmDepartment of Social and Legal Psychology, Johannes Gutenberg-Universität Mainz, Mainz 55122, GermanynnDepartment of Psychology, Karnatak University Dharwad, Dharwad 580003, IndiaooFaculty of Philosophy and Psychology, Yerevan State University, Yerevan 0025, ArmeniappDepartment of Psychology, California State University San Marcos, San Marcos, CA 92096qqHong Kong Institute of Asia-Pacific Studies, Chinese University of Hong Kong, Shatin, ChinarrFaculty of Letters, Keio University, Yokohama 223-8521, JapanssInstitute of Psychology, Czech Academy of Sciences, Brno 602 00, Czech RepublicttDepartment of Psychology, Norwegian University of Science and Technology, Trondheim 7491, NorwayuuDepartment of Psychology, University of Helsinki, Helsinki 00014, FinlandvvInstitute for Research in Social Communication, Slovak Academy of Sciences, Bratislava 841 04, SlovakiawwFaculty of Psychology, Universidad de Cuenca, Cuenca 010107, EcuadorxxFaculty of Psychology, Pontificia Universidad Javeriana, Bogotá 110231, ColombiayyFaculty of Humanities and Social Sciences, Department of Psychology, University of Rijeka, Rijeka 51000, CroatiazzDepartment of Health, Physical and Social Education, Lithuanian Sports University, Kaunas 44221, LithuaniaaaaDepartment of Psychology, Ivane Javakhisvhili Tbilisi State University, Tbilisi 0179, GeorgiabbbDepartment of Philosophy-Psychology-Sociology, University of Dschang, Dschang B.P. 94, CamerooncccInstitute for Globally Distributed Open Research and Education, Gothenburg 413 90, SwedendddDepartment of Psychology, Linnaeus University, Växjö 351 95, SwedeneeeDepartment of Psychology, University of Priština, Kosovska Mitrovica 38220, SerbiafffUniversità degli Studi di Cagliari, Cagliari 09124, ItalygggDepartment of Educational Sciences, Psychology, Communication, University of Bari Aldo Moro, Bari 70122, ItalyhhhFaculty of Psychology and Educational Sciences, University of Porto, Porto 4099-002, PortugaliiiResearch on Economics, Management and Information Technologies, Universidade Portucalense, Porto 4200-072, PortugaljjjInstitute of Psychology, Goethe University Frankfurt, Frankfurt am Main 60323, GermanykkkDepartment of Health Sciences, Hamburg University of Applied Sciences, Hamburg 20099, GermanylllLifestyle Diseases Research Entity, Faculty of Health Sciences, North-West University, Mahikeng 2735, South AfricammmDepartment of Psychology and Behavioural Sciences, Aarhus University, Aarhus 8000, DenmarknnnDepartment of Educational Sciences and Social Work, University of Patras, Patras 265 04, GreeceoooDepartment of Psychology, National and Kapodistrian University of Athens, Athens 157 72, GreecepppDepartment of Psychology, Ivan Franko National University of Lviv, Lviv 79000, UkraineqqqDepartment of Psychology, University of Bremen, Bremen 28359, GermanyrrrDepartment of Humanities and Social Sciences, Indian Institute of Technology Kharagpur, Kharagpur 721302, IndiasssFacultad de Ciencias de la Salud, Universidad Privada del Norte, Lima 15082, PerutttDepartment of Psychology, University of Gothenburg, Gothenburg 405 30, SwedenuuuNational Counterterrorism Innovation, Technology, and Education Center, University of Nebraska, Omaha, NE 68182vvvDepartment of Psychosocial Science, University of Bergen, Bergen 5020, NorwaywwwDepartment of Psychology, Universidad Privada de Santa Cruz de la Sierra, Santa Cruz de la Sierra, BoliviaxxxSchool of Psychology and Neuroscience, University of St Andrews, St Andrews KY16 9JP, United KingdomyyyDepartment of Humanities, Icam School of Engineering, Toulouse campus, Toulouse 31300, FrancezzzDepartment of Psychology, Institute for Population and Human Studies, Bulgarian Academy of Sciences, Sofia 1113, BulgariaaaaaCenter for Social and Cultural Psychology, University of Leuven (KU Leuven), Leuven 3000, BelgiumbbbbDepartment of Health Psychology and Paedagogy, Riga Stradins University, Riga LV-1007, LatviaccccDepartment of Psychology, Pontifical Catholic University of Peru, Lima 15088, PeruddddSchool of Psychology, Universidad Católica del Norte, Antofagasta 1270709, ChileeeeeDepartment of Psychology, University of Canterbury, Christchurch 8140, New ZealandffffDepartment of Psychology, University of Copenhagen, Copenhagen 1353, Denmark</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
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      <prism:doi>10.1073/pnas.2535665123</prism:doi>
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      <title>Small molecule–constrained paratope mimetic bicyclic peptides as potent inhibitors of group 1 and 2 influenza A virus hemagglutinins</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537533123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceWe report on the applicability of a CLIPS (chemical linkage of peptides onto scaffolds) chemistry–based strategy to miniaturize an anti-influenza hemagglutinin (HA) antibody into design of stable and functional bicyclic peptides by merging ...</description>
      <dc:title>Small molecule–constrained paratope mimetic bicyclic peptides as potent inhibitors of group 1 and 2 influenza A virus hemagglutinins</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537533123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Rameshwar U. KadamJarek JuraszekBoerries BrandenburgDivita GargXueyong ZhuMandy JongeneelenChan TangWim B. G. SchepensChristophe BuyckBart StoopsJan VermondRonald VogelsRobert H. E. FriesenMaria J. P. van DongenIan A. WilsonaDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037bJohnson &amp; Johnson Innovative Medicine, Leiden 2333 CN, The NetherlandscDiscovery Chemistry, Johnson &amp; Johnson Innovative Medicine, Beerse 2340, BelgiumdComputer-Aided Drug Design, Johnson &amp; Johnson Innovative Medicine, Beerse 2340, BelgiumeThe Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537533123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525327123?af=R">
      <title>Adipose Dicer-1 modulates systemic insulin signaling and longevity via a miR-8–Aop–Dilp6 axis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525327123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe adipose tissue is a central hub of metabolic and endocrine regulation with a major impact on aging. We identify the conserved miRNA-processing enzyme Dicer-1 (Dcr-1) as a crucial regulator of adipose tissue physiology and lifespan. Reduced ...</description>
      <dc:title>Adipose Dicer-1 modulates systemic insulin signaling and longevity via a miR-8–Aop–Dilp6 axis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525327123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>María C. IngaramoFrancisco RamelloSilvano J. SantanderYemina AbelendoAndrés DekantyaInstituto de Agrobiotecnología del Litoral, Consejo Nacional de Investigaciones Científicas y Técnicas, Santa Fe 3000, ArgentinabFacultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Santa Fe 3000, Argentina</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525327123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532683123?af=R">
      <title>Unique structural and ligand-binding properties of the Staphylococcus aureus serine hydrolase FphE</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532683123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceStaphylococcus aureusis a harmful bacterium that can form antibiotic-resistant biofilms, making infections harder to treat. An enzyme in this bacterium, called FphE, is unique toS. aureusand plays a crucial role in its pathogenicity, making ...</description>
      <dc:title>Unique structural and ligand-binding properties of the Staphylococcus aureus serine hydrolase FphE</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532683123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Jeyun JoTulsi UpadhyayXiangyan YouJohn M. BennettHyunbin LeeMatthew BogyoMatthias FellneraDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305bDepartment of Biochemistry, University of Otago, Dunedin 9054, New ZealandcDepartment of Chemistry, Stanford University, Stanford, CA 94305dDepartment of Biochemistry, Stanford University, Stanford, CA 94305eDepartment of Microbiology and Immunology, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532683123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528466123?af=R">
      <title>Cnpy1 is a candidate endoplasmic reticulum chaperone of vomeronasal type 2 GPCRs</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528466123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMany vertebrates detect chemical cues that drive social and reproductive behaviors through a specialized vomeronasal system. The vomeronasal organ contains two major types of sensory neurons that express V1R- or V2R-type G protein–coupled ...</description>
      <dc:title>Cnpy1 is a candidate endoplasmic reticulum chaperone of vomeronasal type 2 GPCRs</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528466123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>G. V. S. DevakinandanAbdul RishadNandana NandaSyed Dastagir HussainSishir SubediAdish DaniaTata Institute of Fundamental Research, Hyderabad 500046, IndiabGraduate Program in Bioinformatics, University of British Columbia, Vancouver, BC V6T 1Z4, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528466123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528466123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523864123?af=R">
      <title>Monoclonal antibodies from COVID-19 convalescent patients target cryptic epitopes for broad SARS-CoV-2 neutralization</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523864123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe rapid emergence of SARS-CoV-2 variants that efficiently spread and evade antibody-based treatments underscores the need for countermeasures that remain effective as the virus evolves. In this study, two human mAbs, TAU-1109 and TAU-2310, ...</description>
      <dc:title>Monoclonal antibodies from COVID-19 convalescent patients target cryptic epitopes for broad SARS-CoV-2 neutralization</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523864123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Aakanksha HaritMichael MorRon YefetLee S. Izhaki-TavorMeital Gal-TanamyNatalia T. FreundMoshe DessauaThe Lab for Structural Biology of Infectious Diseases, The Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, IsraelbDepartment of Clinical Microbiology and Immunology, Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv 6997801, IsraelcMolecular Virology Lab, The Azrieli Faculty of Medicine, Bar-Ilan University, Safed 1311502, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523864123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523864123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R">
      <title>Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacterium Anabaena sp. PCC 7120</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe light reactions of oxygenic photosynthesis are powered by Photosystem I (PSI) and Photosystem II (PSII), which consist of a core and the peripheral light-harvesting antenna complexes. In cyanobacteria, phycobilisomes (PBSs) serve as the ...</description>
      <dc:title>Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacterium Anabaena sp. PCC 7120</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530459123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Zhiyuan MaoZhenhua LiXingyue LiLiangliang ShenTingyun KuangWenda WangJian-Ren ShenGuangye HanaState Key Laboratory of Forage Breeding-by-Design and Utilization, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, ChinabUniversity of Chinese Academy of Sciences, Beijing 100049, ChinacBeijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinadChina National Botanical Garden, Beijing 100093, ChinaeAcademician Workstation of Agricultural High-Tech Industrial Area of the Yellow River Delta, National Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land, Dongying 257300, ChinafInstitute for Interdisciplinary Science, Advanced Research Field, and Graduate School of Environmental Life, Natural Science and Technology, Okayama University, Okayama 700-8530, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530459123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514928123?af=R">
      <title>HairTime: A noninvasive assay for estimating circadian phase from a single hair sample</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514928123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceCircadian timing varies widely among individuals, influencing sleep, behavior, and health. However, assessing individual circadian phase outside laboratory settings remains difficult because gold-standard methods such as dim-light melatonin ...</description>
      <dc:title>HairTime: A noninvasive assay for estimating circadian phase from a single hair sample</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514928123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Bert MaierLuísa K. PilzSelin ÖzcakirAli RahjoueiAshraf N. AbdoJan de ZeeuwDieter KunzAchim KrameraDivision of Chronobiology, Charité–Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin 10117, GermanybDepartment of Anesthesiology and Intensive Care Medicine, Campus Charité Mitte and Campus Virchow-Klinikum, Charité–Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin 10117, GermanycExperimental and Clinical Research Center, Charité–Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin 10117, GermanydInstitute of Physiology, Sleep Research and Clinical Chronobiology, Charité–Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt Universität zu Berlin, Berlin 10117, GermanyeClinic for Sleep &amp; Chronomedicine, St. Hedwig Hospital, Berlin 10115, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514928123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514928123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520119123?af=R">
      <title>Endogenous ATP–powered nanomotors directing neural stem cell differentiation for Parkinson’s disease treatment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520119123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceNanomotors capable of harvesting endogenous energy offer a transformative strategy for regenerative medicine. In this work, we present Apyrase@Au nanomotors that convert endogenous adenosine triphosphate into directional propulsion and ...</description>
      <dc:title>Endogenous ATP–powered nanomotors directing neural stem cell differentiation for Parkinson’s disease treatment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520119123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Miaomiao DingBin ChenJing XiaoJinghui RongYe FengChao GaoDailing DuYingfeng TuFei PengaSchool of Materials Science and Engineering, Sun Yat-sen University, Guangzhou 510275, ChinabNational Medical Products Administration Key Laboratory for Research and Evaluation of Drug Metabolism &amp; Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou 510515, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520119123</prism:doi>
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      <title>A modular platform for Sterically Masked Activated Cytokines (SMACks)</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2513720123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceCytokines are versatile signaling proteins crucial for immune responses, influencing cell growth, specialization, and inflammation. However, their widespread receptor expression makes it challenging to target delivery to specific cell types. ...</description>
      <dc:title>A modular platform for Sterically Masked Activated Cytokines (SMACks)</dc:title>
      <dc:identifier>doi:10.1073/pnas.2513720123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Travis J. MorgensternNaruhisa OtaZhonghua LinLaura M. LechermannHerman GillAnnie OgasawaraSimon WilliamsKevin A. MarroquinAlexis ScherlChristopher W. DaviesJames R. ByrnesDhaya SeshasayeeJames T. KoerberaDepartment of Antibody Engineering, Genentech Inc., South San Francisco, CA 94080bDepartment of Immunology, Genentech Inc., South San Francisco, CA 94080cDepartment of Translational Imaging, Genentech Inc., South San Francisco, CA 94080dDepartment of Research Pathology, Genentech Inc., South San Francisco, CA 94080</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2513720123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536554123?af=R">
      <title>Genomic epidemiology of Salmonella and Campylobacter in poultry production: Quantifying the contribution of primary breeders</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536554123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAnalyzing whole-genome sequences from over 800 processing facilities across 6 y, this analysis provides the most comprehensive system-wide quantitative assessment of contamination sources in US broiler production to date. Clustering ...</description>
      <dc:title>Genomic epidemiology of Salmonella and Campylobacter in poultry production: Quantifying the contribution of primary breeders</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536554123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>David J. LipmanaDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305bDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD 21218cDepartment of Computer Science, Center for Computational Biology, Johns Hopkins University, Baltimore, MD 21218</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536554123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536554123?af=R</prism:url>
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      <title>Tyrosine phosphoproteome profiling identifies cell-intrinsic signals limiting the efficacy of tyrosine kinase inhibitor therapies</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522090123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe last 25 y have seen a remarkable number of new anticancer therapies specifically targeting tyrosine kinases, which frequently drive tumorigenesis when hyperactive. While these therapies have brought undeniable improvements in survival time ...</description>
      <dc:title>Tyrosine phosphoproteome profiling identifies cell-intrinsic signals limiting the efficacy of tyrosine kinase inhibitor therapies</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522090123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Cameron T. FlowerForest M. WhiteaKoch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139bDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139cProgram in Computational and Systems Biology, Massachusetts Institute of Technology, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522090123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522090123?af=R</prism:url>
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      <title>Microstrain-engineered platinum nanoclathrins for fuel cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518463123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePlatinum (Pt)-based catalysts are vital yet costly for proton exchange membrane fuel cells (PEMFC). While well-defined nanostructures enhance Pt utilization and stability, their dense structures impede mass transport, limiting practical ...</description>
      <dc:title>Microstrain-engineered platinum nanoclathrins for fuel cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518463123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Zhiyong YuQing YaoChen SunLiangqun ZhaoYonggang FengRui QinFei XueXueli YanZhiwei HuWei-Hsiang HuangChih-Wen PaoLili HanNanjun ChenXiaoqing HuangaState Key Laboratory of Physical Chemistry of Solid Surfaces, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, ChinabState Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou 350002, ChinacSchool of Chemical Sciences, University of Chinese Academy of Sciences, Beijing 101408, ChinadInnovation Laboratory for Sciences and Technologies of Energy Materials of Fujian Province, Xiamen 361005, ChinaeCoKey Lab of Advanced Energy Storage and Conversion, Zhejiang Province Key Lab of Leather Engineering, College of Chemistry and Materials Engineering, Wenzhou University, Wenzhou, Zhejiang 325035, ChinafInternational Research Center for Renewable Energy, State Key Laboratory of Multiphase Flow in Power Engineering, Xi’an Jiaotong University, Xi’an 710049, ChinagMax Planck Institute for Chemical Physics of Solids, Dresden 01187, GermanyhNational Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518463123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518463123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516011123?af=R">
      <title>DIRAS2 modulates MAPK pathway–mediated ferroptosis to regulate excitation/inhibition balance and seizure susceptibility</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516011123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe role of DIRAS2 in epilepsy remains unexplored. In this study, we demonstrate that DIRAS2 alleviates epileptic seizure susceptibility and activity and regulates the excitatory/inhibitory balance. Mechanistically, DIRAS2 suppresses ...</description>
      <dc:title>DIRAS2 modulates MAPK pathway–mediated ferroptosis to regulate excitation/inhibition balance and seizure susceptibility</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516011123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Chenlu ZhangLiqin HuHui ZhangMin YangYuansong ZhangNingning ZhangYuanhang XuYuping ZhaoLingxin RenHaokun GuoWei LiXuefeng WangYong YangXin TianaThe First Clinical Medical College of Shanxi Medical University, Department of Neurology, First Hospital of Shanxi Medical University, Taiyuan, Shanxi 030000, ChinabDepartment of Geriatrics, Laboratory of Research and Translation for Geriatric Diseases, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, ChinacDepartment of Neurology, The First Affiliated Hospital of Chongqing Medical University, Chongqing Key Laboratory of Major Neurological and Mental Disorders, Chongqing 400016, ChinadDepartment of Epilepsy Center, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, ChinaeKey Laboratory of Major Brain Disease and Aging Research (Ministry of Education), Chongqing Medical University, Chongqing 400016, ChinafHunan Provincial Key Laboratory of Animal Models and Molecular Medicine, School of BioMedical Sciences, Hunan University, Changsha, Hunan 410000, ChinagDepartment of Neurology, The Second Hospital &amp; Clinical Medical School, Lanzhou University, Lanzhou 730030, ChinahDepartment of pathophysiology, Institute of Basic Medicine and Forensic Medicine, North Sichuan Medical College, Nanchong 637100, ChinaiDepartment of Neurology, The Affiliated Hospital of Qingdao University, Qingdao, Shandong 266000, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516011123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516011123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520822123?af=R">
      <title>Uncovering the embodied dimension of the wandering mind</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520822123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceNeuroimaging studies often treat the resting state as a purely cognitive baseline, overlooking the participant’s embodied experience within the scanner. Here, we show that individuals robustly vary in their degree of body-wandering, such that ...</description>
      <dc:title>Uncovering the embodied dimension of the wandering mind</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520822123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Leah BanellisNiia NikolovaMalthe BrændholdtMelina VejløIgnacio RebolloNicolas LegrandFrancesca FardoJonathan SmallwoodMicah G. AllenaDepartment of Clinical Medicine, Center of Functionally Integrative Neuroscience, Aarhus University, Aarhus 8000, DenmarkbDepartment of Decision Neuroscience and Nutrition, German Institute of Human Nutrition, Nuthetal 14558, GermanycCenter for Humanities Computing, Aarhus University, Aarhus 8000, DenmarkdDepartment of Clinical Medicine, Danish Pain Research Center, Aarhus University, Aarhus 8000, DenmarkeDepartment of Psychology, Queen’s University, Kingston, ON K7L 3N6, CanadafDepartment of Psychiatry, University of Cambridge, Cambridge CB2 0SZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520822123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520822123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525213123?af=R">
      <title>PHGDH phosphorylation mediated by WNK1 serves as a dual marker of metabolic vulnerability and responsiveness to oxaliplatin treatment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525213123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceGastric cancer remains one of the leading causes of cancer mortality, with limited tools to predict which patients will benefit from neoadjuvant chemotherapy. Our study reveals that aberrant activation of the serine metabolism enzyme PHGDH, ...</description>
      <dc:title>PHGDH phosphorylation mediated by WNK1 serves as a dual marker of metabolic vulnerability and responsiveness to oxaliplatin treatment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525213123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Shaobo FangGuoguo JinMingyang YanYanming SongSimin ZhaoChengjuan ZhangYang ShaoKexin ZhaoMeng LiuZhenwei WangXinyang JiaQinxin GuoManman GuoMeiyun WangZhiping GuoZigang DongaDepartment of Radiology, Zhengzhou University People’s Hospital &amp; Henan Provincial People’s Hospital, Zhengzhou 450003, ChinabChina-United States (Henan) Hormel Cancer Institute, Jinshui District, Zhengzhou, Henan 450003, ChinacHenan Key Laboratory of Chronic Disease Management, Fuwai Central China Cardiovascular Hospital, Zhengzhou 450000, ChinadCentral China Subcenter of National Center for Cardiovascular Diseases, Henan Cardiovascular Disease Center, Fuwai Central-China Cardiovascular Hospital, Central China Fuwai Hospital of Zhengzhou University, Zhengzhou 450046, ChinaeTianjian Laboratory of Advanced Biomedical Sciences, Institute of Advanced Biomedical Sciences, Zhengzhou University, Zhengzhou, Henan 450001, ChinafDepartment of Pathophysiology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, Henan 450001, ChinagDepartment of Pathology, Affiliated Cancer Hospital of Zhengzhou University &amp; Henan Cancer Hospital, Zhengzhou, Henan 450008, ChinahBiomedical Research Institute, Henan Academy of Sciences, Zhengzhou 450001, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525213123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525213123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R">
      <title>A conserved ethylene-triggered cell death mechanism may underlie hollow stem formation across plant species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHollow stems are a widespread trait that has independently evolved multiple times across the plant kingdom, representing a case of convergent evolution. This trait plays important roles in plant development and environmental adaptation, yet ...</description>
      <dc:title>A conserved ethylene-triggered cell death mechanism may underlie hollow stem formation across plant species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530957123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Mengxiao YanWeijuan FanYinghui MengJiamin ZhaoWei YangZiyin XuYusen GaoHaiyan ZhuangWuyu ZhouYuqin WangQingjun HuangLing YuanHongxia WangJun YangaShanghai Key Laboratory of Plant Functional Genomics and Resources, Shanghai Chenshan Botanical Garden, Shanghai 201602, ChinabDepartment of Urban Construction and Ecological Technology, Shanghai Institute of Technology, Shanghai 201418, ChinacCollege of Life Sciences, Shanghai Normal University, Shanghai 200234, ChinadCAS Center for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, ChinaeUniversity of Chinese Academy of Sciences, Beijing 101408, ChinafDepartment of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312gKentucky Tobacco Research and Development Center, University of Kentucky, Lexington, KY 40546-0236</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530957123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526916123?af=R">
      <title>The power of leadership in changing social norms in heterogeneous societies</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526916123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSocial norms, though essential for social order, often persist even when no longer beneficial. In a large-scale laboratory experiment, we investigate whether leaders can promote beneficial change in societies with different rates of preference ...</description>
      <dc:title>The power of leadership in changing social norms in heterogeneous societies</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526916123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Fabio GaleottiJona KrutajMarie Claire VillevalaCNRS, Université Lumière Lyon 2, Université Jean-Monnet Saint-Etienne, Emlyon Business School, Groupe d’Analyse et de Théorie Economique, Lyon 69007, FrancebCentre for Decision Research and Experimental Economics, University of Nottingham, Nottingham NG7 2QL, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526916123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526916123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524075123?af=R">
      <title>Neural signatures of human psychological resilience driven by acute stress</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524075123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHuman resilience to stress extends beyond basic physiological responses, engaging higher-order processes such as self-confidence and positive attitudes. This study demonstrates that neural markers of resilience emerge more than 60 min after ...</description>
      <dc:title>Neural signatures of human psychological resilience driven by acute stress</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524075123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Noriya WatanabeShinichi YoshidaRuedeerat KeerativittayayutMasaki TakedaaResearch Center for Brain Communication, Kochi University of Technology, Kami, Kochi 782-8502, JapanbDepartment of Informatics, Faculty of Informatics, Shizuoka Institute of Science and Technology, Fukuroi, Shizuoka 437-8555, JapancSchool of Informatics, Kochi University of Technology, Kami, Kochi 782-8502, JapandSchool of Radiological Technology, Faculty of Health Science Technology, Chulabhorn Royal Academy, Bangkok 10210, Thailand</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524075123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524075123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532775123?af=R">
      <title>Tau catalyzes amyloid-β aggregation and toxicity in a polymorph-dependent manner</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532775123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceInteractions between amyloidogenic proteins drive the progression of neurodegenerative diseases, yet the molecular mechanisms remain unknown. In this work, we describe the crosstalk between amyloid-β (Aβ) and tau polymorphs occurring in ...</description>
      <dc:title>Tau catalyzes amyloid-β aggregation and toxicity in a polymorph-dependent manner</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532775123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Michele MosconiChiara LeonardiZev Armour-GarbBeatrice RocuttoMarten BeegGeorg MeislLei Ortigosa-PascualLuca BrogginiMario SalmonaStefano RicagnoTuomas P. J. KnowlesLuisa DiomedeaDepartment of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri Scientific Institutes for Research, Hospitalization and Healthcare, Milano 20156, ItalybCenter for Misfolding Diseases, Yusuf Hamied Department of Chemistry, Cambridge University, Cambridge CB2 1EW, United KingdomcBiochemistry and Structural Biology, Department of Chemistry, Lund University, Lund 223 62, SwedendDepartment of Biosciences, Università degli Studi di Milano, Milano 20133, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532775123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532775123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529586123?af=R">
      <title>Receptor sequence divergence, gain, loss, duplication, and neofunctionalization drive olfactory adaptation in Drosophila suzukii</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529586123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe family Drosophilidae includes about 4,000 species, and the genusDrosophilacontains around 1,500, yet only three are true fruit pests. One of them,Drosophila suzukii, has spread worldwide and now causes major losses to the berry ...</description>
      <dc:title>Receptor sequence divergence, gain, loss, duplication, and neofunctionalization drive olfactory adaptation in Drosophila suzukii</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529586123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Qi XueHany K. M. DweckaDepartment of Entomology, The Connecticut Agricultural Experiment Station, New Haven, CT 06511</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529586123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535429123?af=R">
      <title>Ultrasound-responsive liposomes: A mechanistic framework to decode the effects of acoustic parameters</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535429123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceUltrasound can trigger the release of drugs from ultrasound-responsive liposomes at precise locations within the body, enabling on-target delivery of therapeutics while minimizing side effects. While multiple factors influence the clinical ...</description>
      <dc:title>Ultrasound-responsive liposomes: A mechanistic framework to decode the effects of acoustic parameters</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535429123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Ignasi SimonRebecca F. A. van den ElshoutGandhika K. WardhanaMasoumeh AqamolaeiIsabella S. T. de JongeRemco HartkampRiccardo AlessandriTiago L. CostaAlina Y. RweiaDepartment of Chemical Engineering, Delft University of Technology, Delft 2629 HZ, the NetherlandsbDepartment of Microelectronics, Delft University of Technology, Delft 2628 CD, the NetherlandscDepartment of Process and Energy, Delft University of Technology, Delft 2628 CB, the NetherlandsdDepartment of Chemical Engineering, KU Leuven, Leuven 3001, Belgium</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535429123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535429123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534915123?af=R">
      <title>Global stability of ecological and evolutionary dynamics via equivalence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534915123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePrice and Maynard-Smith applied game theory—the mathematical study of strategic interactions—to biology, from mating contests in animals to the spread of mutations in a population. They refined Nash Equilibria to take into account the ...</description>
      <dc:title>Global stability of ecological and evolutionary dynamics via equivalence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534915123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Stefano AllesinaaDepartment of Ecology and Evolution, University of Chicago, Chicago, IL 60637bNorthwestern Institute on Complex Systems, Northwestern University, Evanston, IL 60208</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534915123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518366123?af=R">
      <title>Polypharmacology of S-1117, an Fc-fused IgG-selective degrading enzyme, for chronic treatment of autoantibody-mediated diseases</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518366123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThis study presents S-1117, a pan-IgG protease engineered using Seismic’s IMPACT platform to address the limitations of existing therapies in IgG-mediated diseases. The superior pharmacokinetic profile and the polypharmacology of S-1117, ...</description>
      <dc:title>Polypharmacology of S-1117, an Fc-fused IgG-selective degrading enzyme, for chronic treatment of autoantibody-mediated diseases</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518366123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Liliana M. SanmarcoAlex PellerinTobias GreenAgustin PlasenciaJordan M. AndersonNam LeAndita NewtonJiyun ChenMaria Cecilia RamelloRyan PecknerJulia ManassonYi XingHeather VitalNathan Higginson-ScottJohn S. SundyKevin L. OtipobyIvan D. MascanfroniaSeismic Therapeutic, Watertown, MA 02472bIndependent Consultant, Moraga, CA 94556</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518366123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518366123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534817123?af=R">
      <title>DNA methylation site loss for plasticity-led novel trait genetic fixation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534817123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHow environmentally induced traits become genetically fixed remains a fundamental puzzle in evolutionary biology. Using wild medaka fish populations, we found that seasonal DNA methylation changes control gut-length plasticity, and loss of ...</description>
      <dc:title>DNA methylation site loss for plasticity-led novel trait genetic fixation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534817123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Takafumi KatsumuraSuguru SatoKana YamashitaShoji OdaTakashi GakuhariShodai TanakaKazuko FujitaniToshiyuki NishimakiTadashi ImaiYasutoshi YoshiuraHirohiko TakeshimaYasuyuki HashiguchiYoichi SekitaHiroshi MitaniMotoyuki OgawaHideaki TakeuchiHiroki OotaaDepartment of Anatomy, Kitasato University School of Medicine, Sagamihara 252-0374, JapanbDepartment of Biological Science, Graduate School of Natural Science and Technology, Okayama University, Okayama 700-8530, JapancDepartment of Human Life Design and Science, Faculty of Design, Kyushu University, Fukuoka 815-8540, JapandDepartment of Biological Sciences, Kitasato University School of Science, Sagamihara 252-0373, JapaneDepartment of Integrated Biosciences, The University of Tokyo, Kashiwa 277-8562, JapanfInstitute of Human and Social Sciences, Kanazawa University, Kanazawa 920-1192, JapangMolecular Biology Research Center, Kitasato University School of Medicine, Sagamihara 252-0374, JapanhProduction Engineering Division, Fisheries Technology Institute, Japan Fisheries Research and Education Agency, Onomichi 722-0061, JapaniDepartment of Advanced Aquaculture Science, Fukui Prefectural University, Fukui 917-0116, JapanjDepartment of Marine Biology, Tokai University School of Biological Sciences, Shizuoka 424-8610, JapankDepartment of Biology, Faculty of Medicine, Osaka Medical and Pharmaceutical University, Takatsuki 569-8686, JapanlDepartment of Biosciences, Kitasato University School of Science, Sagamihara 252-0373, JapanmDepartment of Integrative Life Sciences, Graduate School of Life Science, Tohoku University, Sendai 980-8577, JapannDepartment of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534817123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534817123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525390123?af=R">
      <title>Data-driven Mori–Zwanzig modeling of Lagrangian particle dynamics in turbulent flows</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525390123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceModeling the motion of small particles in turbulent flows is central to a wide range of scientific and engineering problems ranging from cloud formation and pollutant transport to manufacturing and nuclear fusion. Yet, despite a century of ...</description>
      <dc:title>Data-driven Mori–Zwanzig modeling of Lagrangian particle dynamics in turbulent flows</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525390123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Xander M. de WitAlessandro GabbanaMichael WoodwardYen Ting LinFederico ToschiDaniel LivescuaDepartment of Applied Physics and Science Education, Fluids and Flows group and J.M. Burgers Center for Fluid Mechanics, Eindhoven University of Technology, Eindhoven 5600 MB, NetherlandsbComputational Physics and Methods Group (CCS-2), Los Alamos National Laboratory, Los Alamos, NM 87545cCenter for Nonlinear Studies, Los Alamos National Laboratory, Los Alamos, NM 87545dDepartment of Physics and Earth Science, University of Ferrara, INFN Ferrara, Ferrara 44121, ItalyeInformation Science Group (CCS-3), Los Alamos National Laboratory, Los Alamos, NM 87545fInstituto per le Applicazioni del Calcolo, Consiglio Nazionale delle Ricerche, Rome I-00185, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525390123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525390123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522217123?af=R">
      <title>Chromatin accessibility regulates age-dependent nuclear mechanotransduction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522217123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAlthough cells continuously integrate diverse environmental cues, the mechanisms by which aging reprograms mechanical and biochemical signaling remain poorly understood. We demonstrate that aged fibroblasts lose the capacity to mount ...</description>
      <dc:title>Chromatin accessibility regulates age-dependent nuclear mechanotransduction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522217123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Yawen LiaoLuezhen YuanTrinadha Rao SornapudiMax LandRajshikhar GuptaG. V. ShivashankaraLaboratory of Multiscale Bioimaging, Paul Scherrer Institute, Villigen 5232, SwitzerlandbDepartment of Health Sciences and Technology, ETH Zurich, Zurich 8092, SwitzerlandcBroad Institute of Massachusetts Institute of Technology and Harvard, Cambridge, MA 02142dMassachusetts Institute of Technology, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522217123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522217123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525423123?af=R">
      <title>Fibro-adipogenic progenitor cells from murine SMA muscles are intrinsically adipogenic</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525423123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSMA is a disorder primarily known for neuronal degeneration, but patients continue to experience muscle weakness, atrophy, fibrosis, and fat infiltration even after receiving therapies. These persistent symptoms point to disease mechanisms ...</description>
      <dc:title>Fibro-adipogenic progenitor cells from murine SMA muscles are intrinsically adipogenic</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525423123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Yangyi E. LuoZoe Abe-TehTarek AlsaghirKatie D. HeidenKari B. BassoElisabeth R. BartonaDepartment of Applied Physiology and Kinesiology, University of Florida, Gainesville, FL 32611bMyology Institute, University of Florida, Gainesville, FL 32601cDepartment of Chemistry, Mass Spectrometry Research and Education Center, University of Florida, Gainesville, FL 32611</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525423123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525423123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519393123?af=R">
      <title>Maternal Krüppel-like factor 2 (KLF2)+ CD4 T cells promote fertility and fetal tolerance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519393123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePregnancy is remarkable in that mothers tolerate the developing fetus expressing immunologically foreign paternal antigens. These foreign antigens stimulate rejection in other contexts, such as organ transplantation. Investigating how fetal ...</description>
      <dc:title>Maternal Krüppel-like factor 2 (KLF2)+ CD4 T cells promote fertility and fetal tolerance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519393123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Ngan N. M. NguyenAlexander E. BradyAbigail RussiGiang PhamBo LiLucien H. TurnerMichael KotliarArtem BarskiXiaofei SunSing Sing WayaDivision of Infectious Diseases, Center for Inflammation and Tolerance, Cincinnati Children’s Hospital Medical Center, University of Cincinnati College of Medicine, Cincinnati, OH 45229bReproductive Sciences Center, Division of Developmental Biology, Cincinnati Children’s Hospital Medical Center, University of Cincinnati College of Medicine, Cincinnati, OH 45229cDivision of Allergy and Immunology, Cincinnati Children’s Hospital Medical Center, University of Cincinnati College of Medicine, Cincinnati, OH 45229</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519393123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519393123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514371123?af=R">
      <title>Large future genetic diversity losses are predicted from conservation indicators even with habitat protection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514371123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceGenetic diversity is crucial for both species adaptation and survival. Recently, it has been included as a target for protection in the United Nations’ Global Biodiversity Framework. However, we lack scalable predictive methods to quantify ...</description>
      <dc:title>Large future genetic diversity losses are predicted from conservation indicators even with habitat protection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514371123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Kristy S. MualimJeffrey P. SpenceClemens WeißOliver SelmoniMeixi LinMoises Exposito-AlonsoaDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305bDepartment of Biology, Stanford University, Stanford, CA 94305cDepartment of Integrative Biology, University of California Berkeley, Berkeley, CA 94720dDepartment of Genetics, Stanford University, Stanford, CA 94305eInstitute for Human Genetics, University of California, San Francisco, CA 94158fDepartment of Epidemiology &amp; Biostatistics, University of California, San Francisco, CA 94158gStanford Cancer Institute, Stanford University, Stanford, CA 94305hDepartment of Global Ecology, Carnegie Institution for Science, Stanford, CA 94305iHHMI, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514371123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514371123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2510265123?af=R">
      <title>Targeting the ANGPTL4/NRP1/ABL1/RAD51 axis reverses cisplatin resistance by impairing DNA damage repair in head and neck cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2510265123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHere, we identify a molecular pathway that drives cisplatin resistance in head and neck squamous cell carcinoma (HNSCC). The angiogenic factor angiopoietin-like 4 (ANGPTL4) engages Neuropilin1 to activate ABL1, which in turn phosphorylates and ...</description>
      <dc:title>Targeting the ANGPTL4/NRP1/ABL1/RAD51 axis reverses cisplatin resistance by impairing DNA damage repair in head and neck cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2510265123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Emmanuel B. AsieduAjay KumarAlexander ChoiDerek Osorio LucianoKevin LoDeepti SharmaTao MaFeyruz RassoolAkrit SodhiSilvia MontaneraDepartment of Oncology and Diagnostic Sciences, School of Dentistry, University of Maryland, Baltimore, MD 21201bThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21287cDepartment of Radiation Oncology, School of Medicine, University of Maryland, Baltimore, MD 21201dGreenebaum Comprehensive Cancer Center, University of Maryland, Baltimore, MD 21201</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2510265123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2510265123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518064123?af=R">
      <title>Controlled propagation of soliton bullets in an engineered strain field</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518064123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceUnderstanding the propagation of nonlinear excitations is a crucial challenge in multiple science and engineering domains. We use liquid crystals (LCs) as model materials in which we can easily design strain profiles and propagate highly ...</description>
      <dc:title>Controlled propagation of soliton bullets in an engineered strain field</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518064123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Alexis de la CotteXingzhou TangChuqiao ChenS. J. KoleNoe AtzinJuan J. de PabloNicholas L. AbbottaSmith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853bPritzker School of Molecular Engineering, University of Chicago, Chicago, IL 60637cCollege of Electronic and Optical Engineering and College of Flexible Electronics (Future Technology), Nanjing University of Posts and Telecommunications, Nanjing 210023, ChinadDepartment of Applied Mathematics and Theoretical Physics, Centre for Mathematical Sciences, University of Cambridge, Cambridge CB3 0WA, United KingdomeDepartment of Chemical and Biomolecular Engineering, Tandon School of Engineering, New York University, Brooklyn, NY 11201fDepartment of Computer Science, Courant Institute of Mathematical Sciences, New York University, New York, NY 10012gDepartment of Physics, New York University, New York, NY 10012hMaterials Science Division, Argonne National Laboratory, Lemont, IL 60439</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518064123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518064123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523055123?af=R">
      <title>VIBES: A multiscale modeling approach integrating within-host and between-hosts dynamics in epidemics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523055123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificancePredicting an epidemic’s course requires understanding how pathogen biology and human behavior independently shape transmission. While these scales are inextricably connected, traditional epidemiological methods often struggle to isolate ...</description>
      <dc:title>VIBES: A multiscale modeling approach integrating within-host and between-hosts dynamics in epidemics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523055123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Paulo Cesar VenturaYong Dam JeongMaria LitvinovaAllisandra G. KummerShingo IwamiHongjie YuStefano MerlerAlessandro VespignaniKeisuke EjimaMarco AjelliaLaboratory for Computational Epidemiology and Public Health, Department of Epidemiology and Biostatistics, Indiana University School of Public Health, Bloomington, IN 47405binterdisciplinary Biology Laboratory, Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, JapancDepartment of Mathematics, Pusan National University, Busan 46241, Republic of KoreadDepartment of Applied Mathematics, Pukyong National University, Busan 48513, Republic of KoreaeDepartment of Epidemiology and Biostatistics, Indiana University, School of Public Health Bloomington, IN 47405fShanghai Institute of Infectious Disease and Biosecurity, Fudan University, Shanghai 200032, ChinagSchool of Public Health, Fudan University, Key Laboratory of Public Health Safety, Ministry of Education, Shanghai 200032, ChinahDepartment of Infectious Diseases, Huashan Hospital, Fudan University, Shanghai 200040, ChinaiCenter for Health Emergencies, Bruno Kessler Foundation, Trento 38123, ItalyjLaboratory for the Modeling of Biological and Socio-Technical Systems, Northeastern University, Boston, MA 02115kLee Kong Chian School of Medicine, Nanyang Technological University, Singapore 308232, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523055123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523055123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527861123?af=R">
      <title>Probing charge-transfer processes in Pt/TiO2 photocatalysts by amperometric/potentiometric photo-SECM</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527861123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceSolar-driven photocatalysis holds promise for sustainable and cost-efficient energy and chemical production, yet its advancement is hindered by the lack of in operando technique to understand charge-carrier behavior at the nanoscale. Here, we ...</description>
      <dc:title>Probing charge-transfer processes in Pt/TiO2 photocatalysts by amperometric/potentiometric photo-SECM</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527861123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Tianyu BoHaoqing SuZiyuan WangJe Hyun BaeGaukhar AskarovaShu HuMichael V. MirkinaDepartment of Chemistry and Biochemistry, Queens College, Flushing, NY 11367bThe Graduate Center of The City University of New York, New York, NY 10016cDepartment of Chemical and Environmental Engineering, Yale University, New Haven, CT 06510dEnergy Sciences Institute, Yale West Campus, West Haven, CT 06516eAdvanced Science Research Center of The City University of New York, New York, NY 10031</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527861123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527861123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531743123?af=R">
      <title>Life-like behavior emerging in active and flexible microstructures</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531743123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAdaptive motion in microorganisms arises from a coupling between flexibility and activity—an interplay long difficult to replicate in synthetic microsystems. Harnessing this coupling could enable feedback between shape and motion and thus life-...</description>
      <dc:title>Life-like behavior emerging in active and flexible microstructures</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531743123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Mengshi WeiDaniela J. KraftaLeiden Institute of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden 2300 RA, The Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531743123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531743123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534303123?af=R">
      <title>Energy landscape statistics and thermodynamics of a machine-learned model of water</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534303123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceWater’s anomalous properties emerge from its complex hydrogen-bond networks in the liquid phase, which are difficult to model accurately. Quantum-level accuracy typically entails prohibitive computational costs, limiting large-scale ...</description>
      <dc:title>Energy landscape statistics and thermodynamics of a machine-learned model of water</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534303123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Ryan J. SzukaloAndreas NeophytouAxel GomezNicolas GiovambattistaFrancesco SciortinoPablo G. DebenedettiaDepartment of Chemistry, Princeton University, Princeton, NJ 08544bDipartimento di Fisica, Sapienza Università di Roma, Roma 00185, ItalycDepartment of Physics, Brooklyn College of the City University of New York, Brooklyn, NY 11210dPh.D. Programs in Physics and Chemistry, The Graduate Center of the City University of New York, New York, NY 10016eDepartment 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534303123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534303123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522792123?af=R">
      <title>Multigenerational and gender-symmetric transmission of migration behaviors in historical Quebec</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522792123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceLong-run family effects on migration behaviors are extremely hard to measure due to the scarcity of data that combine complete residential histories and complete kin relations. This work harnesses historical microdata from Quebec, Canada to ...</description>
      <dc:title>Multigenerational and gender-symmetric transmission of migration behaviors in historical Quebec</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522792123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Marielle Côté-GendreauaOffice of Population Research, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522792123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522792123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602991123?af=R">
      <title>VAMP8 function reveals tight linkage between endocytic recycling and endocytosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602991123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceWe demonstrate that vesicle-associated membrane protein 8 (VAMP8) depletion inhibits recycling of endocytic cargo and reroutes transferrin receptors toward lysosomal degradation, thereby impairing endocytic vesicle formation and inhibiting ...</description>
      <dc:title>VAMP8 function reveals tight linkage between endocytic recycling and endocytosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602991123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Ailing LiuYueping LiZheng HuangWen ChenPeiliu XuXiangying WeiGuosheng HuShuangquan LiuXiaoxia LiuYaohui HeDanling WangSandra L. SchmidZhiming ChenaDepartment of Clinical Laboratory of The First Affiliated Hospital, Ministry of Education Key Laboratory of Rare Pediatric Diseases, Institute of Cytology and Genetics, Hengyang Medical School, University of South China, Hengyang 421001, Hunan, ChinabNational Health Commission Key Laboratory of Birth Defect Research and Prevention, Hunan Provincial Maternal and Child Health Care Hospital, Changsha 410008, Hunan, ChinacInstitute for Future Sciences, University of South China, Changsha 410000, Hunan, ChinadFujian Key Laboratory on Conservation and Sustainable Utilization of Marine Biodiversity, Fuzhou Institute of Oceanography, College of Geography and Oceanography, Minjiang University, Fuzhou 350108, ChinaeBiomedical Research Center of South China, College of Life Sciences, Fujian Normal University, Fuzhou 350117, ChinafKey Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Department of Pathophysiology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, ChinagBiohub, San Francisco, CA 94158</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602991123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602991123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529147123?af=R">
      <title>Ultrasensitive measurement of brain penetration mechanics and blood vessel rupture with microscale probes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529147123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMicroscale neural probes are central to next-generation brain–machine interfaces, yet how they physically penetrate the living brain remains poorly quantified. Using a high-sensitivity force sensor integrated with real-time microscopy, we ...</description>
      <dc:title>Ultrasensitive measurement of brain penetration mechanics and blood vessel rupture with microscale probes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529147123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-26T07:00:00Z</dc:date>
      <dc:creator>Abdulmalik ObaidMina-Elraheb HannaSong-Wen HuangYu-Ting HuOmar JáidarWilliam NixJun B. DingNicholas A. MeloshYu-Wei WuaDepartment of Materials Science and Engineering, Stanford University, Stanford, CA 94304bInstitute of Molecular Biology, Academia Sinica, Taipei 115, TaiwancDepartment of Life Science, College of Life Science, National Taiwan University, Taipei 106, TaiwandDepartment of Neurosurgery, Stanford University, Stanford, CA 94305eDepartment of Neurology and Neurological Sciences, Stanford University, Stanford, CA 94305fTaiwan International Graduate Program in Interdisciplinary Neuroscience, Academia Sinica, Taipei 115, TaiwangMolecular and Cell Biology Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, TaiwanhGenome and Systems Biology Degree Program, College of Life Science, National Taiwan University, Taipei 106, TaiwaniGraduate Institute of Life Sciences, National Defense Medical University, Taipei 115, TaiwanjNeuroscience Program in Academia Sinica, Academia Sinica, Taipei 115, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529147123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529147123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524738123?af=R">
      <title>Dynamical modeling of individual sensory reactivity and habituation learning</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524738123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHow organisms process sensory information to generate behavior is typically studied by averaging and comparing group means. Although useful to understand general principles, such studies “average out” potentially meaningful differences between ...</description>
      <dc:title>Dynamical modeling of individual sensory reactivity and habituation learning</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524738123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Marina BoonMatthew SmartAnton V. PersikovBoyd van ReijmersdalMehrdad MaghbouliRobert A. MarmionBob CarpenterStanislav Y. ShvartsmanAnnette SchenckaDepartment of Human Genetics, Radboud University Medical Center, Nijmegen 6525 GA, the NetherlandsbDonders Institute for Brain, Cognition and Behaviour, Radboud University Medical Center, Nijmegen 6525 EN, the NetherlandscCenter for Computational Biology, Flatiron Institute, New York, NY 10010dLewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544eCenter for Computational Mathematics, Flatiron Institute, New York, NY 10010fDepartment of Molecular Biology, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524738123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524738123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525773123?af=R">
      <title>Germline-targeted baboon apolipoprotein L-1 protects mice against African trypanosomes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525773123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceApolipoprotein L-1 (APOL1) provides primates immunity to trypanosome infection. Other animals do not express the protein and are thus susceptible to trypanosomiasis, with cattle in particular routinely succumbing to infection. Fresard et al., ...</description>
      <dc:title>Germline-targeted baboon apolipoprotein L-1 protects mice against African trypanosomes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525773123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Sara FresardSarah J. PangburnKayla LeissDaphne Boodwa-KoDaniella KovacsicsChris J. SchoenherrJeremy S. RabinowitzAris N. EconomidesLi LiWeigang QiuBernardo Gonzalez-BaradatAlessandro RosaRussell ThomsonJayne RaperJoseph VerdiaBiology Program, The Graduate Center at the City University of New York, New York City, NY 10016bDepartment of Biological Sciences, Hunter College at the City University of New York, New York City, NY 10065cRegeneron Pharmaceuticals, Tarrytown, NY 10591</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525773123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525773123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517661123?af=R">
      <title>Physics-constrained neural ordinary differential equation models to discover and predict microbial community dynamics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517661123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMicrobial communities drive essential biological processes across ecosystems, yet predicting their dynamics and functions remains challenging due to context-dependent interactions. We develop a physics-constrained neural ordinary differential ...</description>
      <dc:title>Physics-constrained neural ordinary differential equation models to discover and predict microbial community dynamics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517661123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Jaron ThompsonBryce M. ConnorsVictor M. ZavalaOphelia S. VenturelliaDepartment of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI 53706bDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706cDepartment of Biological Engineering, Duke University, Durham, NC 27708dDepartment of Molecular Genetics and Microbiology, Duke University, Durham, NC 27708</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517661123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517661123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2420179123?af=R">
      <title>One test, many tongues: Surveying language proficiency across the globe</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2420179123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceMeasuring language proficiency is essential for research in many areas, including second language acquisition, psycholinguistics, and cognitive science. We propose a method to derive language proficiency tests from texts and apply it to ...</description>
      <dc:title>One test, many tongues: Surveying language proficiency across the globe</dc:title>
      <dc:identifier>doi:10.1073/pnas.2420179123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Pol van RijnYue SunHarin LeeRaja MarjiehIlia SucholutskyFrancesca LanzariniElisabeth AndréNori JacobyaMax Planck Institute for Empirical Aesthetics, Computational Auditory Perception Research Group, Frankfurt am Main 60322, GermanybDeutsche Bundesbank, Research Data and Service Centre, Frankfurt am Main 60431, GermanycCooperative Brain Imaging Center, Goethe University, Frankfurt am Main 60590, GermanydErnst Strüngmann Institute for Neuroscience, Frankfurt am Main 60528, GermanyeMax Planck Institute for Human Cognitive and Brain Sciences, Leipzig 04103, GermanyfPrinceton University, Department of Psychology, Princeton, NJ 08544gUniversity of Augsburg, Chair for Human-Centered Artificial Intelligence, Augsburg 86159, GermanyhCornell University, Department of Psychology, Ithaca, NY 14850</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2420179123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2420179123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535016123?af=R">
      <title>Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during early Legionella infection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535016123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceLegionella pneumophilaremodels host membrane trafficking to establish a replication-permissive niche, yet the molecular basis of this process is not fully understood. Here, we elucidate the structural basis by which the effector SetA couples ...</description>
      <dc:title>Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during early Legionella infection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535016123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Ha Na ImYeon LeeYunju SongHyunggu HahnHyerry JeonDonghyuk ShinSangho LeeKyung-Hee KimKyung-Tae KimSe Won SuhDong Man JangHyoun Sook KimaResearch Institute, National Cancer Center, Goyang 10408, Republic of KoreabDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of KoreacDepartment of Biomedical Sciences, Seoul National University, Seoul 03080, Republic of KoreadDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of KoreaeDepartment of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of KoreafDepartment of Applied Chemistry, School of Science and Technology, Kookmin University, Seoul 02707, Republic of KoreagDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535016123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535016123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2509778123?af=R">
      <title>CALHM5 deficiency alleviates aortic aneurysm by regulating smooth muscle calcium homeostasis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2509778123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAneurysmal diseases represent a serious risk to human health. Ion channels rank as the second most prevalent target for clinical drug development. We identified calcium homeostasis modulators 5 as an ion channel, possessing calcium ion ...</description>
      <dc:title>CALHM5 deficiency alleviates aortic aneurysm by regulating smooth muscle calcium homeostasis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2509778123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Bo YangTing XuQianqian YangLiangzhu MoJianyi HuoTaiyang MuYating ZhiYun DuHaojie WangLingchuan GuoZhen ZhuYulong FengYu RuiLi ZhuWilliam A. CoetzeeQinqin GaoHua-Qian YangaDepartment of Cardiology, The Fourth Affiliated Hospital of Soochow University, Cyrus Tang Medical Institute, Medical College of Soochow University, Suzhou 215028, ChinabInstitute for Fetology, Department of Pathology, First Affiliated Hospital of Soochow University, Suzhou 215006, ChinacDepartment of Cardiology, First Affiliated Hospital of Soochow University, Suzhou 215006, ChinadDepartment of Laboratory Medicine, Suzhou Ninth Hospital Affiliated to Soochow University, Cyrus Tang Medical Institute, Medical College of Soochow University, Suzhou 215200, ChinaeDepartments of Pathology, Neuroscience and Physiology, Biochemistry and Molecular Pharmacology, Medicine, and New York University School of Medicine, New York, NY 10016</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2509778123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2509778123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524664123?af=R">
      <title>Small-molecule CBLB inhibitor abolishes EGFR ubiquitination, reduces receptor endocytosis, and diminishes cell motility signaling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524664123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceCasitas B-lineage lymphoma (CBL) E3 ubiquitin ligases mediate ubiquitin conjugation of epidermal growth factor receptor (EGFR) but their functional contributions to EGFR endocytic trafficking and signaling remain poorly defined. Here, we ...</description>
      <dc:title>Small-molecule CBLB inhibitor abolishes EGFR ubiquitination, reduces receptor endocytosis, and diminishes cell motility signaling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524664123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Itziar Pinilla-MacuaRatul MukerjiFrederick CohenAlexander SorkinaDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261bNurix Therapeutics, Inc., Brisbane, CA 94005</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524664123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524664123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R">
      <title>Specialization of independently acquired flagellar FliC proteins in plant-associated Sphingomonas balances swimming and immunogenicity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe bacterial flagellum controls microbial motility and surface attachment. Some flagella contain a flg22 peptide epitope that is recognized by the plant immune receptor FLS2. This immune surveillance creates a trade-off between flagellar ...</description>
      <dc:title>Specialization of independently acquired flagellar FliC proteins in plant-associated Sphingomonas balances swimming and immunogenicity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535583123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Dor RussChinmay SahaKarnelia PaulZhiyu ZhengTheresa F. LawManuel Anguita-MaesoDerek S. LundbergConnor R. FitzpatrickJeffery L. DanglaDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill 27599, NCbHHMI, University of North Carolina at Chapel Hill, Chapel Hill 27599, NCcDepartment of Plant Biology, Swedish University of Agricultural Sciences, Uppsala 75007, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535583123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531552123?af=R">
      <title>Giant photorefractive and photoexpansion effects in a van der Waals semiconductor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531552123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceWe report a van der Waals semiconductor, crystalline As2S3, that exhibits an exceptionally large light-induced refractive index change (photorefraction Δnup to 0.3) together with controllable photoexpansion of up to 7%. These effects occur ...</description>
      <dc:title>Giant photorefractive and photoexpansion effects in a van der Waals semiconductor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531552123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Anton A. MinnekhanovGeorgy A. ErmolaevAlexey P. TsapenkoIlia M. FradkinGleb I. TselikovAdilet N. ToksumakovAleksandr S. SlavichArslan B. MazitovSergey A. SmirnovNikita D. OrekhovIvan A. KruglovSergei A. IvanovIlya P. RadkoAndrey A. VyshnevyyAleksey V. ArseninKostya S. NovoselovValentyn S. VolkovaEmerging Technologies Research Center, XPANCEO, Dubai 00000, United Arab EmiratesbNational Graphene Institute, University of Manchester, Manchester M13 9PL, United KingdomcDepartment of Materials Science and Engineering, National University of Singapore, Singapore 117544, SingaporedInstitute for Functional Intelligent Materials, National University of Singapore, Singapore 117544, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531552123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531552123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527522123?af=R">
      <title>Correspondence of large-scale functional brain network decline across aging mice and humans</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527522123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHuman aging is accompanied by changes in large-scale functional brain network organization, which have important consequences for cognition and brain disease. Using awake functional MRI data acquired in mice across a range of adulthood, we ...</description>
      <dc:title>Correspondence of large-scale functional brain network decline across aging mice and humans</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527522123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Ezra Winter-NelsonEyal BergmannMicaela Y. ChanGabriella VillLiang HanZiwei ZhangAlexandra KavushanskyIrit DolgopyatJad AslehJennifer D. WhitesellItamar KahnGagan S. WigaCenter for Vital Longevity, The University of Texas at Dallas, Dallas, TX 75235bDepartment of Psychology, School of Behavioral and Brain Sciences, The University of Texas at Dallas, Dallas, TX 75080cDepartment of Neuroscience, Rappaport Faculty of Medicine, Technion—Israel Institute of Technology, Haifa, Israel 3525433dZuckerman Mind Brain Behavior Institute and Department of Neuroscience, Columbia University, New York, NYeAllen Institute for Brain Science, Seattle, WA 98109fDepartment of Psychiatry, The University of Texas Southwestern Medical Center, Dallas, TX 75390</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527522123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527522123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529273123?af=R">
      <title>Versatile artificial muscles by decoupling anisotropy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529273123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceArtificial muscles promise to bring compliant, high-performance actuation into robotics but have been constrained by limited versatility (the ability to adapt to diverse applications). We introduce the helical anisotropically reinforced ...</description>
      <dc:title>Versatile artificial muscles by decoupling anisotropy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529273123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Eric WeissmanRohan KhatavkarJiefeng SunaSchool for Engineering of Matter, Transport and Energy, 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>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529273123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529273123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2513459123?af=R">
      <title>Biologically grounded on-chip model identifies selective topographic reorganization within hyperexcitable corticostriatal networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2513459123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceTopographic wiring is fundamental to brain function, yet how such spatial precision emerges during development remains unclear, especially in the striatum, which lacks clear anatomical boundaries. Using a biologically grounded brain-on-chip ...</description>
      <dc:title>Biologically grounded on-chip model identifies selective topographic reorganization within hyperexcitable corticostriatal networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2513459123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
      <dc:creator>Maxime PoinsotMarine Dos SantosBaptiste MarthyAna Borges-CorreiaEduardo GasconBenoit CharlotMaxime CazorlaaAix Marseille Université, CNRS, Institut de Neurosciences de la Timone, Marseille FR-13005, FrancebAix Marseille Université, Centrale Med, CNRS, Institut Fresnel, Marseille FR-13013, FrancecUniversité Montpellier, CNRS, Institut d’Electronique et des Systèmes, Montpellier FR-34000, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2513459123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2513459123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514753123?af=R">
      <title>Immune cell profiling reveals expanded stem cell–like memory T cells in anti-GAD65-associated neurological syndromes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514753123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceAutoimmune neurological syndromes (AINS) with antibodies targeting glutamic acid decarboxylase 65 (anti-GAD65 AINS) show limited response to currently available immunotherapies and are associated with poor clinical outcomes. A better ...</description>
      <dc:title>Immune cell profiling reveals expanded stem cell–like memory T cells in anti-GAD65-associated neurological syndromes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514753123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Sumanta BarmanSaskia RäuberKatharina EisenhutDaniela EsserMartijn van DuijnMadeleine ScharfMarisol Herrera-RiveroPaul DisseLara-Maria PreuthValeria GulyaevaIlja SchwanEliza vom SteinMarius JonasDuygu PulMichael HemingLouisa Müller-MinyManuela PaunovicChristine StrippelEbru HaholuJan BartoschElisabeth KaufmannJustina DargvainieneSabine KahlMarius RingelsteinEric BindelsHeinz WiendlNikolas H. StoeckleinJohannes FischerNorbert GoebelsLars KomorowskiMichael RodenAndrea RossiMonika StollAlbert J. BeckerMotaz HamedChristian G. BienRomana HöftbergerJan BauerSven G. MeuthMaarten J. TitulaerFrank LeypoldtGerd Meyer zu HörsteFranziska ThalerNico Melzera
                    Department of Neurology, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, Düsseldorf
                    40225, Germany
                b
                    Institute of Clinical Neuroimmunology, University Hospital, Ludwig-Maximilians-Universität München, Munich
                    81377, Germany
                c
                    Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-Universität München, Martinsried
                    82152, Germany
                d
                    Institute of Clinical Chemistry, University Hospital Schleswig-Holstein, Kiel 24105/Lübeck
                    23538, Germany
                e
                    Department of Neurology, Erasmus MC University Medical Center, Rotterdam
                    3015 GD, the Netherlands
                f
                    Institute for Experimental Immunology, affiliated to Euroimmun Medizinische Labordiagnostika Aktiengesellschaft, Lübeck
                    23560, Germany
                g
                    Institute of Epidemiology and Social Medicine, University of Münster, Münster
                    48149, Germany
                h
                    Department of Neurology, University Hospital Münster, Münster
                    48149, Germany
                i
                    Graduate School of Systemic Neurosciences, Ludwig-Maximilians-Universität München, Planegg
                    82152, Germany
                j
                    Department of Neurology, University Hospital, Ludwig-Maximilians-Universität München, Munich
                    81377, Germany
                k
                    Department of Endocrinology and Diabetology, Medical Faculty and University Hospital Düsseldorf, Heinrich-Heine-University, Düsseldorf
                    40225, Germany
                l
                    Institute for Clinical Diabetology, German Diabetes Center, Leibniz Institute for Diabetes Research at Heinrich-Heine-University, Düsseldorf
                    40225, Germany
                m
                    German Center for Diabetes Research, München-Neuherberg
                    85764, Germany
                n
                    Department of Neurology, Center for Neurology and Neuropsychiatry, Landschaftsverband Rheinland-Klinikum, Heinrich Heine University, Düsseldorf
                    40629, Germany
                o
                    Department of Hematology, Erasmus MC University Medical Center, Rotterdam
                    3015 GD, the Netherlands
                p
                    Department of General, Visceral and Pediatric Surgery, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, Düsseldorf
                    40225, Germany
                q
                    Institute for Transplantation Diagnostics and Cell Therapeutics, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, Düsseldorf
                    40225, Germany
                r
                    Genome Engineering and Model Development Lab, Institut für umweltmedizinische Forschung-Leibniz Research Institute for Environmental Medicine, Düsseldorf
                    40225, Germany
                s
                    Department of Genetic Epidemiology, Institute of Human Genetics, University of Münster, Münster
                    48149, Germany
                t
                    Institute of Cellular Neurosciences II, University Hospital Bonn, Bonn
                    53127, Germany
                u
                    Clinic for Neurosurgery, University Hospital of Bonn, Bonn
                    53127, Germany
                v
                    Department of Epileptology, Bethel Epilepsy Center, Medical School Ostwestfalen-Lippe, Bielefeld University, Bielefeld
                    33617, Germany
                w
                    Division of Neuropathology and Neurochemistry, Department of Neurology and Comprehensive Center for Clinical Neurosciences and Mental Health, Medical University of Vienna, Vienna
                    1090, Austria
                x
                    Department of Neuroimmunology, Centre for Brain Research, Medical University of Vienna, Vienna
                    1090, Austria
                y
                    Department of Neurology, University Hospital Schleswig-Holstein, Kiel
                    24105, Germany
                Juna M. de VriesMariska M. P. NagtzaamSuzanne C. FrankenYvette S. CrijnenJuliette BrennerRobin W. van SteenhovenJeroen KerstensMarienke A. A. M. de BruijnAnna E. M. BastiaansenRemco M. HoogenboezemSharon VeenbergenPeter A. E. Sillevis SmittMarwa Al-DubaiLuise AppeltshauserIlya AyzenbergCarolin Baade-BüttnerAndreas van BaalenSebastian BaatzOliver BährBettina BalintIason BartzokisSebastian BauerAnnette BaumgartnerTobias BaumgartnerAntonios BayasStefanie BeckerSonka BeneschRobert BergerBirgit BergerMartin BerghoffSarah BernsenAchim BertheleChristian BienCorinna BienJulia BierwithAndreas BinderStefan BittnerDaniel BittnerFranz BlaesAstrid BlaschekAmelie BohnMoritz BöhringerMarie BraunSergio Castro-GomezJustina DargvainieneTimo DebaJulia Maren DeckerJohanna-Maria DietmaierAndre DikJulian DominikKathrin DopplerMona DreesmannLena EdelhoffLaura EhrhardtSven EhrlichKatharina EisenhutAlexander EmmerDominique EndresMarina Entscheva-StorrDaniela EsserThorleif EtgenJürgen Hartmut FaissKim Kristin FalkTimo FaustmannWalid FazeliAlexander FinkeCarsten FinkeFelix FischbachDirk FitznerMarina Flotats-BastardasMathias FousseTobias FreilingerManuel FrieseHannah FuhrerArmin Johannes GaeblerMarco GallusMarcel GebhardChristian GeisClemens GödelAnna GorslerArmin GrauOliver GrauerBritta GreshakeCatharina roßThomas GrüterAiden HaghikiaRobert HandrekaIris HannibalNiels HansenSandra HansmannJens HarmelAntonia HarmsYetzenia Dubraska Haro AlizoAlkomiet HasanMartin HäuslerIda Sybille HaussleiterJoachim HavlaChung Ha-YeunWolfgang HeideValentin HeldKerstin HellwigMarina HerwerthPhilip HillebrandFrank HoffmannChristian HofmannUlrich Hofstadt-van OyDominica Hudasch (ehem. Ratuszny)Yannik HülsmannMartinv HümmertPeter HuppkeHagen HuttnerFatme Seval IsmailMartina JansenMareike JansenMarius JonasAleksandra JuranekDaniel KampMichael KarenfortAnnika KatherMax KaufmannChristoph KellinghausConstanze Kerin (geb. Mönig)Ruth KerkhoffRolf KernJaqueline KlausewitzMichael KlugeSusanne KnakeBenjamin KnierEllen KnierimFrank KohlertInga KonecznyFelix KonenPeter KörtvélyessyStjepana KovacAndrea KraftMarkus KrämerVerena KrausChristos KrogiasGregor KuhlenbäumerOlga KukhlenkoTania KümpfelAlbrecht KunzeHanna LappChristoph LehrichMartin LesserJan LewerenzFrank LeypoldtAndreas LinsaDaniel LüdeckeJan LünemannMarie MadlenerMichael MalterNils MargrafCarlos Martinez QuesadaMonika MeisterNico MelzerKristin Stefanie MelzerTil MengeSven MeuthGerd Meyer zu HörsteFabian MöllerMarie-Luise MonoSigrid MuesHiltrud MuhleAnna-Katharina MundorfMarc NikolausJost ObrockiFriedemann PaulLoana PennerLena Kristina PfefferThomas PfefferkornSteffen PfeufferAlexandra PhilipsenJohannes PiepgrasJulika PitschFelix von PodewilsMosche PompschJosef PrillerAnne-Katrin PröbstelHarald PrüßDuygu PulDaniel RappJohanna Maria Helena RauSaskia RäuberMarkus RauchenzaunerRobert RehmannIna ReichenGernot ReimannMomsen ReinckeRaphael ReineckeJonathan ReppleNele RetzlaffSigrid ReuterMarius RingelsteinHenrik RohnerFelix RosenowKevin RostásyTheodor RüberStephan RüeggYannic SaathoffJens SchaumbergHanna SchellhornRuth SchillingJens SchmidtMelissa SchmitzIna-Isabelle SchmützHauke SchneiderPatrick SchrammStephan SchreiberStefanie SchreiberGesa SchreyerIna SchröderSimon SchusterPhilip SchwenkenbecherGünter SeidelFrank SeifertThomas Seifert-HeldMakbule SenelKai SiebenbrodtOlga SimovaClaudia SommerJuliane SpieglerOliver StammelSlobodan StankovicAndreas SteinbrecherJohann SteinerHenning StolzeMuriel StoppeKarin Storm van’s GravesandeChristine StrippelDietrich SturmKlarissa Hanja StürnerKurt-Wolfram SühsSteffen SyrbeSimone TaubeFranziska ThalerFlorian Then BerghKatrin ThiesAnja TietzCorinna TrebstGeorge TrendelenburgRegina TrollmannThanos TsaktanisHayrettin TumaniMehtap TürediChristian UrbanekRem VaizianNiklas VogelMax VogtmannMatthias von MeringKatharina von ZedtwitzJudith WagnerJan WagnerElias WagnerBarbara WagnerKlaus-Peter WandingerMirko WegschneiderJudith WeiserRobert WeissertNjiku Melchior WellmerBrigitte WildemannJonathan WickelKarsten WittKatharina WurdackYavor YalachkovLara Zieger</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514753123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514753123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527755123?af=R">
      <title>How the 2025 NIH grant terminations varied by researchers’ demographic groups</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527755123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;In early 2025, the NIH unexpectedly terminated 2,291 active research grants, withdrawing $2.45 billion and disrupting thousands of projects. While the economic magnitude of these cuts is known, less is understood about how they differed across researchers’...</description>
      <dc:title>How the 2025 NIH grant terminations varied by researchers’ demographic groups</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527755123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
      <dc:creator>Diego F. M. OliveiraQian HuangTeresa K. WoodruffBrian UzziaSchool of Electrical Engineering and Computer Science, University of North Dakota, Grand Forks, ND 58202bEdward R. Murrow College of Communication, Washington State University, Pullman, WA 99164cDepartment of Obstetrics, Gynecology, and Reproductive Biology, Michigan State University, East Lansing, MI 48824dNorthwestern Institute on Complex Systems and Data Science, Northwestern University, Evanston, IL 60208</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527755123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527755123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523152123?af=R">
      <title>Gender gaps in reading increase during unplanned and planned school closures</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523152123?af=R</link>
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      <dc:creator>Viraj R. TorsekaraDepartment of Life Sciences, GITAM School of Science, Gandhi Institute of Technology and Management (GITAM), Visakhapatnam, Andhra Pradesh 530045, India</dc:creator>
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      <dc:creator>Herman WoloskerDaniel J. LieblaDepartment of Biochemistry, The Ruth and Bruce Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa 3525433, IsraelbThe Miami Project to Cure Paralysis, Department of Neurological Surgery, University of Miami Miller School of Medicine, Miami, FL 33136</dc:creator>
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      <dc:creator>Matthew J. ChurchKatie N. CoatesaFlathead Lake Biological Station, University of Montana, Polson, MT 59860</dc:creator>
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      <dc:title>Bird dispersal of fruit-like yam bulbils: Is this a new form of Batesian mimicry?</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-19T07:00:00Z</dc:date>
      <dc:creator>Kenji SuetsuguSteven D. JohnsonaDepartment of Biology, Graduate School of Science, Kobe University, Kobe, Hyogo 657-8501, JapanbInstitute for Advanced Research, Kobe University, Kobe, Hyogo 657-8501, JapancCentre for Functional Biodiversity, School of Life Sciences, University of KwaZulu‐Natal Pietermaritzburg, Scottsville, Pietermaritzburg 3209, South Africa</dc:creator>
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      <dc:title>Completeness as a fitness landscape for cognitive architectures</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-19T07:00:00Z</dc:date>
      <dc:creator>Pier Luigi SaccoaDepartment of Neurosciences, Imaging, and Clinical Studies, University of Chieti-Pescara, Chieti 66100, Italy</dc:creator>
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      <dc:title>Correction for Li et al., Functionally heterogeneous intratumoral CD4+CD8+ double-positive T cells can give rise to single-positive T cells</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-23T07:00:00Z</dc:date>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Sun et al., The Japanese Archipelago sheltered cave lions, not tigers, during the Late Pleistocene</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <dc:title>Correction for Ranjan et al., The E3 ubiquitin ligase RNF186 and RNF186 risk variants regulate innate receptor-induced outcomes</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <dc:title>Correction for Goyette et al., Targeting Axl favors an antitumorigenic microenvironment that enhances immunotherapy responses by decreasing Hif-1α levels</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-24T07:00:00Z</dc:date>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <dc:date>2026-03-19T07:00:00Z</dc:date>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-19T07:00:00Z</dc:date>
      <dc:creator>Guillaume ChomickiZhi ChenYing LiXingrong PengGao ChenaDepartment of Biosciences, Durham University, Durham DH1 3LE, United KingdombState Key Laboratory of Phytochemistry and Natural Medicines, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650204, ChinacYunnan Key Laboratory for Integrative Conservation of Plant Species with Extremely Small Populations, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650204, ChinadUniversity of Chinese Academy of Sciences, Beijing 100049, ChinaeYunnan Key Laboratory of Plant Diversity and Biogeography, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China</dc:creator>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606841123?af=R">
      <title>Retraction for Li et al., Primed 3D injectable microniches enabling low-dosage cell therapy for critical limb ischemia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606841123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;</description>
      <dc:title>Retraction for Li et al., Primed 3D injectable microniches enabling low-dosage cell therapy for critical limb ischemia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606841123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606841123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606841123?af=R</prism:url>
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