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      <title>Proceedings of the National Academy of Sciences</title>
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      <title>In This Issue</title>
      <link>https://www.pnas.org/doi/abs/10.1073/iti3226123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
      <dc:identifier>doi:10.1073/iti3226123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-11T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/iti3226123</prism:doi>
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      <title>Graded oxidation state calcium phosphate graphene oxide modulates the mechanical and biological behavior of bone matrices</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537761123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceBone defects demonstrate a wide range of mechanical and biological requirements. However, most synthetic grafts provide limited tunability of those properties. The present study demonstrates that the oxidation state of calcium phosphate ...</description>
      <dc:title>Graded oxidation state calcium phosphate graphene oxide modulates the mechanical and biological behavior of bone matrices</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537761123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Fatemeh S. HosseiniHo-Man KanTaraje WhitfieldChrysoula ArgyrouDilshan SilvaChenyun DengJason D. OrlandoLakshmi NairStefanie A. SydlikPeter F. MayeKevin W.-H. LoCato T. Laurencinahttps://ror.org/02der9h97The Cato T. Laurencin Institute for Regenerative Engineering, University of Connecticut, Farmington, CT 06030bhttps://ror.org/02kzs4y22Center for Regenerative Medicine and Skeletal Development, UConn School of Dental Medicine, UConn Health, Farmington, CT 06030chttps://ror.org/02der9h97Department of Chemistry, University of Connecticut, Storrs, CT 06269dhttps://ror.org/05x2bcf33Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213ehttps://ror.org/05x2bcf33Department of Biomedical Engineering, Carnegie Mellon University, Pittsburgh, PA 15213fhttps://ror.org/02der9h97Department of Biomedical Engineering, University of Connecticut, Storrs, CT 06269ghttps://ror.org/02kzs4y22Department of Orthopedic Surgery, University of Connecticut Health, Farmington, CT 06030hhttps://ror.org/02der9h97Department of Materials Science and Engineering, University of Connecticut, Storrs, CT 06269ihttps://ror.org/02der9h97Department of Chemical and Bimolecular Engineering, University of Connecticut, Storrs, CT 06269jhttps://ror.org/02kzs4y22Department of Medicine, Division of Endocrinology, School of Medicine, University of Connecticut Health Center, Farmington, CT 06030</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537761123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537761123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625473123?af=R">
      <title>Why did menopause evolve?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625473123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Why did menopause evolve?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625473123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Amy McDermott</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
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      <title>A unifying framework for the evolution of metazoa and social insects, two major evolutionary transitions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530125123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;The evolution of life is characterized by major transitions, i.e., the evolution of new targets of selection (e.g., prokaryotes, eukaryotes, multicellular organisms, social insect colonies). They arose when preexisting lower-level units cooperated and ...</description>
      <dc:title>A unifying framework for the evolution of metazoa and social insects, two major evolutionary transitions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530125123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Stephan LohmarJulius RombachLouis Allan OkwaroWei ZhouVolker NehringJudith Korbahttps://ror.org/0245cg223Evolutionary Biology and Ecology, University of Freiburg, Freiburg D-79104, Germanybhttps://ror.org/02crff812National Centre for Vector Entomology, Institute of Parasitology, Vetsuisse and Medical Faculty, University of Zürich, Zürich CH-8057, Switzerlandchttps://ror.org/048zcaj52Research Institute for the Environment and Livelihoods, Charles Darwin University, Darwin Northern Territory 0909, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2530125123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605431123?af=R">
      <title>Energy prioritization and neurometabolic scaling in a social insect brain</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605431123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceIt has been hypothesized that brain physiology has evolved to prioritize energy allocation during nutritional stress, but brain and whole-body metabolism have not been measured in combination. We examined the effect of nutritional stress on ...</description>
      <dc:title>Energy prioritization and neurometabolic scaling in a social insect brain</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605431123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Zach N. CotoDajia YeSara ArgandaJon F. HarrisonJames F. A. Tranielloahttps://ror.org/05qwgg493Department of Biology, Boston University, Boston, MA 02215bhttps://ror.org/00f54p054Department of Biology, Stanford University, Stanford, CA 94305chttps://ror.org/01v5cv687Departamento de Biología, Universidad Rey Juan Carlos, Móstoles 28933, Spaindhttps://ror.org/01v5cv687Instituto de Investigación en Cambio Global, Universidad Rey Juan Carlos, Móstoles 28933, Spainehttps://ror.org/03efmqc40School of Life Sciences, Arizona State University, Tempe, AZ 85287-4501</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605431123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605431123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605226123?af=R">
      <title>Digestion-resistant proteins support the healthy metabolite profiles associated with plant-based diets</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605226123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificancePlant-based diets are consistently associated with improved gut health, yet the mechanisms responsible remain incompletely understood. Here, we explore two aspects of plant-based foods: digestion-resistant carbohydrate (fiber) and digestion-...</description>
      <dc:title>Digestion-resistant proteins support the healthy metabolite profiles associated with plant-based diets</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605226123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Jenna E. AbuSalimMichael M. MacArthurMeera GuptaAsael RoichmanCraig J. HunterFelix C. KeberSeema ChatterjeeMahta MoussaviJavad BaroueiMartin WührDinanath SulakheChristopher J. LehmannMohamed S. DoniaJoshua D. Rabinowitzahttps://ror.org/00hx57361Department of Molecular Biology, Princeton University, Princeton, NJ 08544bhttps://ror.org/00hx57361Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08544chttps://ror.org/00hx57361Ludwig Institute for Cancer Research, Princeton University, Princeton, NJ 08544dhttps://ror.org/00hx57361Department of Chemistry, Princeton University, Princeton, NJ 08544ehttps://ror.org/03kgsv495The Mina &amp; Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israelfhttps://ror.org/0449kf092Food Security Research Center, Prairie View A&amp;M University, Prairie View, TX 77446ghttps://ror.org/0449kf092Human Nutrition and Food, Prairie View A&amp;M University, Prairie View, TX 77446hhttps://ror.org/024mw5h28Center for Research Informatics, Biological Sciences Division, University of Chicago, Chicago, IL 60637ihttps://ror.org/024mw5h28Department of Medicine, Section of Infectious Disease and Global Health, University of Chicago Medicine, Chicago, IL 60637jhttps://ror.org/024mw5h28Department of Pediatrics, Section of Pediatric Infectious Diseases, University of Chicago Medicine, Chicago, IL 60637</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605226123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605226123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609969123?af=R">
      <title>Accelerating Campylobacter zoonosis in the Anthropocene</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609969123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHuman-driven environmental change in the Anthropocene is reshaping how pathogens emerge, evolve, and spread. This study shows that the global expansion of intensive poultry farming has created a ecological system that fundamentally alters ...</description>
      <dc:title>Accelerating Campylobacter zoonosis in the Anthropocene</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609969123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Oakem J. KyneBridget S. PenmanDavid J. KellySamuel K. Sheppardahttps://ror.org/052gg0110Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford OX1 3EL, United Kingdombhttps://ror.org/052gg0110Department of Biology, Life and Mind Building, University of Oxford, Oxford OX1 3EL, United Kingdomchttps://ror.org/05krs5044School of Biosciences, The University of Sheffield, Sheffield S10 2TN, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609969123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609969123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534106123?af=R">
      <title>Global threat exposure of islands in a changing world</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534106123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceGlobal change severely threatens island ecosystems, exposing them to sea-level rise, non-native species, and land-use conversions. Because islands are small-scale systems, they are often overlooked in global threat assessments, despite holding ...</description>
      <dc:title>Global threat exposure of islands in a changing world</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534106123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Clara MarinoMartin Philippe-LesaffreFilipa Coutinho SoaresGabriel Henrique de Oliveira CaetanoAdrienne EtardNathalie ButtPol CapdevilaSeverin D. H. IrlCamille LeclercJonathan LenoirJairo PatiñoFrançois RigalAna Benítez-LópezCéline Bellardahttps://ror.org/05x5km989Fondation pour la Recherche sur la Biodiversité-Cesab, Montpellier 34000, Francebhttps://ror.org/03xjwb503Université Paris-Saclay, CNRS, AgroParisTech, Ecologie Société et Evolution, Gif-sur-Yvette 91190, Francechttps://ror.org/02gfc7t72Department of Biogeography and Global Change, Museo Nacional de Ciencias Naturales- Consejo Superior de Investigaciones Científicas (MNCN-CSIC), Madrid 28006, Spaindhttps://ror.org/043pwc612Centro de Investigação em Biodiversidade e Recursos Genéticos (CIBIO), InBIO Laboratório Associado, Campus de Vairão, Universidade do Porto, 4485-661 Vairão, Portugalehttps://ror.org/01c27hj86Centro de Investigação em Biodiversidade e Recursos Genéticos (CIBIO), InBIO Laboratório Associado, Instituto Superior de Agronomia, Universidade de Lisboa, Tapada da Ajuda, 1349-017 Lisboa, PortugalfBIOPOLIS Program in Genomics, Biodiversity and Land Planning, CIBIO, Campus de Vairão, 4485-661, Vairão, Portugalghttps://ror.org/02xfp8v59Departamento de Zoologia, Universidade de Brasília, Brasília 70910-900, Brazilhhttps://ror.org/02wfhk785Biodiversity and Natural Resources Program, International Institute for Applied Systems Analysis, Laxenburg A-2361, AustriaiThe Nature Conservancy, South Brisbane, QLD 4101, Australiajhttps://ror.org/00rqy9422School of the Environment, The University of Queensland, St. Lucia, QLD 4072, Australiakhttps://ror.org/021018s57Departament de Biologia Evolutiva, Ecologia i Ciències Ambientals, Universitat de Barcelona, Avda. Diagonal 643, Barcelona 08028, Spainlhttps://ror.org/021018s57Institut de Recerca de la Biodiversitat (IRBio), Universitat de Barcelona, Barcelona 08028, Spainmhttps://ror.org/04cvxnb49Biogeography and Biodiversity Lab, Institute of Physical Geography, Goethe-University Frankfurt, Frankfurt am Main 60438, Germanynhttps://ror.org/01amp2a31Senckenberg Biodiversity and Climate Research Centre, Frankfurt am Main 60325, Germanyohttps://ror.org/003vg9w96National Research Institute for Agriculture, Food and Environment (INRAE), Research Unit on Hydrosystem Functioning (RIVERLY), Villeurbanne Cedex 69625, Francephttps://ror.org/01gyxrk03UMR CNRS 7058 Ecologie et Dynamique des Systèmes Anthropisés, Université de Picardie Jules Verne, Amiens 80000, Franceqhttps://ror.org/02gfc7t72Island Ecology and Evolution Research Group, Instituto de Productos Naturales y Agrobiología- Consejo Superior de Investigaciones Científicas (IPNA-CSIC), La Laguna, Tenerife 38206, Spainrhttps://ror.org/00222yk13Université de Pau et des Pays de l’Adour, CNRS, Institut des Sciences Analytiques et de Physico-Chimie pour l’Environnement et les Matériaux (IPREM), Pau 64000, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534106123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534106123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610752123?af=R">
      <title>Rapid acceleration of ice-cover loss from Northern Hemisphere lakes above critical air temperature thresholds</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610752123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceIce cover is a fundamental regulator of northern lake ecosystems, yet the specific thermal thresholds that trigger abrupt phenological changes have remained elusive. We demonstrate that lake-ice sensitivity to atmospheric warming is not only ...</description>
      <dc:title>Rapid acceleration of ice-cover loss from Northern Hemisphere lakes above critical air temperature thresholds</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610752123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Jian ZhouWeijia WangYaru MaLinwang YuanChangchun HuangKun ShiPeter R. Leavittahttps://ror.org/036trcv74State Key Laboratory of Climate System Prediction and Risk Management, Nanjing Normal University, Nanjing 210023, Chinabhttps://ror.org/036trcv74School of Geography, Nanjing Normal University, Nanjing 210023, Chinachttps://ror.org/006jb1a24School of Ocean Sciences, Bangor University, Menai Bridge LL59 5AB, United Kingdomdhttps://ror.org/034t30j35Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, Nanjing 210008, Chinaehttps://ror.org/03dzc0485Limnology Laboratory, University of Regina, Regina, SK S4S 0A2, Canadafhttps://ror.org/03dzc0485Institute for Environmental Change and Society, University of Regina, Regina, SK S4S 0A2, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610752123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610752123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610453123?af=R">
      <title>A wearable patch for continuous levodopa monitoring in sweat: Towards exertion and power-free pharmacodynamic assessment in Parkinson’s disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610453123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceEffective management of Parkinson’s disease (PD) requires dynamic adjustment of levodopa dosing. Current approaches rely on subjective symptom reporting and infrequent blood sampling. We introduce here a soft, fingertip-mounted wearable ...</description>
      <dc:title>A wearable patch for continuous levodopa monitoring in sweat: Towards exertion and power-free pharmacodynamic assessment in Parkinson’s disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610453123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-27T07:00:00Z</dc:date>
      <dc:creator>Tamoghna SahaMuhammad Inam KhanKatherine LongardnerBarak SabbaghKaiwen ZhengHugo de MendozaGaoyuan JiBumsik ChoiZongnan WangRosie PhamMichael SkipworthEshita ShahMaria ReynosoChochanon MoonlaAbdulhameed AbdalDebika DattaSamar Singh SandhuPonnusamy NandhakumarArtur JedrzakShichao DingLu YinIrene LitvanJoseph Wangahttps://ror.org/0168r3w48Aiiso Yufeng Li Family Department of Chemical and Nanoengineering, University of California, San Diego, La Jolla, CA 92093bhttps://ror.org/0168r3w48Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093chttps://ror.org/0168r3w48Department of Electrical and Computer Engineering, University of California, San Diego, La Jolla, CA 92161dhttps://ror.org/0168r3w48Department of Mechanical Engineering, University of California, San Diego, La Jolla, CA 92161</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610453123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610453123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612168123?af=R">
      <title>Nature’s antivenom: Combinations of conserved rattlesnake serum metalloproteinase inhibitors block the lethal action of viper venoms</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612168123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSnakebite remains an undertreated tropical disease that affects over one million people annually, and new therapeutic approaches are needed. Here, we develop an approach to viper antivenoms inspired by the observations that these snakes are ...</description>
      <dc:title>Nature’s antivenom: Combinations of conserved rattlesnake serum metalloproteinase inhibitors block the lethal action of viper venoms</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612168123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-07-29T07:00:00Z</dc:date>
      <dc:creator>Sean B. CarrollFiona P. UkkenYetunde A. AyinuolaLuis EscalonaMontamas SuntravatElda E. SanchezaHHMI, University of Maryland-College Park, College Park, MD 20742bDepartment of Biology, University of Maryland-College Park, College Park, MD 20742cDepartment of Chemistry, Texas Agricultural and Mechanical University-Kingsville, Kingsville, TX 78363dNational Natural Toxins Research Center, Texas Agricultural and Mechanical University-Kingsville, Kingsville, TX 78363eDepartment of Biological and Health Sciences, Texas Agricultural and Mechanical University-Kingsville, Kingsville, TX 78363</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612168123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612168123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2426400123?af=R">
      <title>Landscape context constrains climate regulation recovery in Amazonian secondary forests</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2426400123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceForest regeneration is widely promoted as a strategy to restore ecosystem services in the Amazon, yet whether regenerating forests recover climate-regulating functions comparable to primary forests (PF) remains uncertain. We show that climatic ...</description>
      <dc:title>Landscape context constrains climate regulation recovery in Amazonian secondary forests</dc:title>
      <dc:identifier>doi:10.1073/pnas.2426400123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Lais Rosa-OliveiraGabrielle Ferreira PiresRicardo Gomes TomázAline Pontes-LopesLivia Maria BrumattiMarcos Heil CostaHumberto Paiva FonsecaLuiz Eduardo Oliveira e Cruz de Aragãoahttps://ror.org/0409dgb37Department of Agricultural Engineering, Federal University of Viçosa, Viçosa 36570-900, Minas Gerais, Brazilbhttps://ror.org/0409dgb37Department of Plant Pathology, Federal University of Viçosa, Viçosa 36570-900, Minas Gerais, Brazilchttps://ror.org/04xbn6x09Tropical Ecosystems and Environmental Sciences, National Institute for Space Research, São José dos Campos 12227-010, São Paulo, Brazildhttps://ror.org/03yghzc09School of Geography, Faculty of Environment, Science and Economy, University of Exeter, Exeter EX4 4QJ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2426400123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2426400123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532702123?af=R">
      <title>Contrastive learning unites sequence and structure in a global representation of protein space</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532702123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHow can the relationships between all known proteins be represented? Recent advances in AI describe proteins as vectors, where the distance between vectors relates to the similarity between proteins. These vector representations are largely ...</description>
      <dc:title>Contrastive learning unites sequence and structure in a global representation of protein space</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532702123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Guy YanaiGabriel AxelLiam M. LongoNir Ben-TalRachel Kolodnyahttps://ror.org/02f009v59Department of Computer Science, University of Haifa, Haifa 3303221, Israelbhttps://ror.org/04mhzgx49Department of Biochemistry and Molecular Biology, School of Neurobiology, Biochemistry and Biophysics, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 6997801, Israelchttps://ror.org/05dqf9946Earth-Life Science Institute, Institute of Science Tokyo, Tokyo 152-8550, Japandhttps://ror.org/04yhya597Blue Marble Space Institute of Science, Seattle, WA 98104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532702123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532702123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600701123?af=R">
      <title>Mapping the exposome–microbiota–host axis for prenatal origins of infant health</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600701123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceIn one of the largest prospective pregnancy cohorts with exposome phenotyping, we establish a prenatal exposure–microbiota–infant health axis. We demonstrate that maternal anthropometrics and clinical indicators are among the strongest ...</description>
      <dc:title>Mapping the exposome–microbiota–host axis for prenatal origins of infant health</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600701123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Minjian ChenJiawei DuanYusheng GuanYuntian XuYingtong JiangZiyi LiRui HuangJingjing ZhouAdrian CovaciHeidi AaseXinru WangYankai Xiaahttps://ror.org/059gcgy73State Key Laboratory of Reproductive Medicine and Offspring Health, Center for Global Health, School of Public Health, Nanjing Medical University, Nanjing, Jiangsu 211166, Chinabhttps://ror.org/059gcgy73Key Laboratory of Modern Toxicology of Ministry of Education, School of Public Health, Nanjing Medical University, Nanjing, Jiangsu 211166, ChinacDepartment of Occupational Medicine and Environmental Health, School of Public Health, Key Laboratory of Public Health Safety and Emergency Prevention and Control Technology of Higher Education Institutions in Jiangsu Province, Nanjing Medical University, Nanjing, Jiangsu 211166, Chinadhttps://ror.org/008x57b05Toxicological Centre, Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk 2610, Belgiumehttps://ror.org/046nvst19Department of Child Health and Development, Norwegian Institute of Public Health, Oslo 0213, Norway</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600701123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600701123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608894123?af=R">
      <title>Controls on glacial erosion rates revealed by cosmogenic nuclide measurements in southeastern Alaska</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608894123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceGlacial erosion rates vary over many orders of magnitude, but there are numerous hypotheses predicting the variables that control glacial erosion rates. Here, we determine bedrock erosion rates using cosmogenic nuclides in southeastern Alaska. ...</description>
      <dc:title>Controls on glacial erosion rates revealed by cosmogenic nuclide measurements in southeastern Alaska</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608894123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Jeremy P. BrooksAndrew G. JonesShaun A. MarcottLucas K. ZoetNathaniel A. LiftonChristian HelanowMarc W. Caffeeahttps://ror.org/01y2jtd41Department of Geoscience, University of Wisconsin-Madison, Madison, WI 53706bhttps://ror.org/02dqehb95Department of Earth, Atmospheric, and Planetary Science, Purdue University, West Lafayette, IN 47907chttps://ror.org/05f0yaq80Department of Mathematics, Stockholm University, Stockholm SE-106 91, Swedendhttps://ror.org/02dqehb95Department of Physics and Astronomy, 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>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608894123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608894123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532233123?af=R">
      <title>Deep learning maps local brain aging in relation to cognition across human adulthood</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532233123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceAlthough human brain aging is not uniform across cortical regions, most imaging-derived measures of brain age quantify this phenomenon using a single summary quantity. Building on prior voxel-level brain age approaches, we use deep learning ...</description>
      <dc:title>Deep learning maps local brain aging in relation to cognition across human adulthood</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532233123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Nikhil N. ChaudhariOwen M. Vega HuertaSamayan BhattacharyaNahian F. ChowdhuryAndrei Irimiaahttps://ror.org/03taz7m60Alfred E. Mann Department of Biomedical Engineering, Corwin D. Denney Research Center, Viterbi School of Engineering, University of Southern California, Los Angeles, CA 90089bhttps://ror.org/03taz7m60Ethel Percy Andrus Gerontology Center, Leonard Davis School of Gerontology, University of Southern California, Los Angeles, CA 90089chttps://ror.org/03taz7m60Neuroscience Graduate Program, University of Southern California, Los Angeles, CA 90089dhttps://ror.org/03taz7m60Department of Quantitative and Computational Biology, Dana &amp; David Dornsife College of Arts &amp; Sciences, University of Southern California, Los Angeles, CA 90089ehttps://ror.org/0220mzb33Centre for Healthy Brain Aging, Institute of Psychiatry, Psychology &amp; Neuroscience, King’s College London, London WC2R 2LS, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532233123</prism:doi>
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      <title>Reticulated adaptive radiation and phylogenomic diversity loss in the Hawaiian honeycreepers</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536533123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe Hawaiian honeycreeper clade is a pre-eminent example of both adaptive radiation and human-mediated rapid extinction. We present an exhaustive phylogeny of nearly all extant and historically known Hawaiian honeycreeper taxa. We identify a ...</description>
      <dc:title>Reticulated adaptive radiation and phylogenomic diversity loss in the Hawaiian honeycreepers</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536533123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Michael G. CampanaMadhvi X. VenkatramanMirian T. N. TsuchiyaAnna M. KearnsNichelle M. VanTasselAmberleigh E. HenschenNatalia A. S. PrzelomskaNancy Rotzel McInerneyMargad-Erdene OchirbatHeather R. L. LernerTaylor E. CallicrateMolly HagemannEben H. PaxtonLoren Cassin-SackettHelen F. JamesRobert C. Fleischerahttps://ror.org/01pp8nd67Center for Conservation Genomics, National Zoo and Conservation Biology Institute, Smithsonian Institution, Washington, DC 20008bhttps://ror.org/03qn8fb07Australian National Wildlife Collection, Commonwealth Scientific and Industrial Research Organisation National Research Collections Australia, Canberra 2601, ACT, Australiachttps://ror.org/043cdzb63South Carolina Department of Natural Resources Marine Resources Research Institute, Hollings Marine Laboratory, Charleston, SC 29412dhttps://ror.org/035z2ew45Department of Biological Sciences, Eastern Illinois University, Charleston, IL 61920ehttps://ror.org/03ykbk197School of the Environment and Life Sciences, Institute of the Earth and Environment, Centre of Excellence for Heritage Innovation, University of Portsmouth, Portsmouth PO1 2DY, Hampshire, United Kingdomfhttps://ror.org/01pp8nd67Department of Anthropology, National Museum of Natural History, Smithsonian Institution, Washington, DC 20560ghttps://ror.org/00ynnr806Royal Botanic Gardens, Kew TW9 3AE, Richmond, United Kingdomhhttps://ror.org/0566sj483Joseph Moore Museum, Earlham College, Richmond, IN 47374ihttps://ror.org/04m60en37Vertebrate Zoology, Bernice Pauahi Bishop Museum-State of Hawai’i Museum of Natural and Cultural History, Honolulu, HI 96817jhttps://ror.org/03eg83y24U.S. Geological Survey Pacific Island Ecosystems Research Center, Hawai‘i Volcanoes National Park, HI 96785khttps://ror.org/01x8rc503Department of Biology, University of Louisiana at Lafayette, Lafayette, LA 70503lDepartment of Vertebrate Zoology, National Museum of Natural History, Washington, DC 20560</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536533123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605142123?af=R">
      <title>Evolution on degenerate fitness landscapes is not random: Curvature drives directional drift</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605142123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceEvolutionary dynamics selects more fit phenotypes over others. But fitness landscapes are complex and high dimensional, with continuous manifolds of practically identical high fitness. Intuitively, one may imagine that evolution then proceeds ...</description>
      <dc:title>Evolution on degenerate fitness landscapes is not random: Curvature drives directional drift</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605142123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Razi FachareldeenNaama BrenneraTechnion Israel Institute of Technology, Interdisciplinary program in Applied Mathematics, Haifa 3200003, IsraelbTechnion Israel Institute of Technology, Network Biology Research Lab, Haifa 3200003, IsraelcTechnion Israel Institute of Technology, Faculty of Chemical Engineering, Haifa 3200003, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605142123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605142123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527395123?af=R">
      <title>Optimizing infectious disease mitigation under dynamic conditions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527395123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceManaging a pandemic requires balancing competing costs: interventions such as mask mandates and lockdowns reduce infections but disrupt economies and social life, while uncontrolled spread imposes treatment costs and loss of productivity and ...</description>
      <dc:title>Optimizing infectious disease mitigation under dynamic conditions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527395123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Laura MüllerFabio SartoriJonas DehningMaximilian F. EgglViola Priesemannahttps://ror.org/0087djs12Max-Planck-Institute for Dynamics and Self-Organization, Göttingen 37077, Germanybhttps://ror.org/01y9bpm73Institute for the Dynamics of Complex Systems, University of Göttingen, Göttingen 37077, Germanychttps://ror.org/04t3en479Chair of Sociology and Computational Social Science, Karlsruhe Institute, Karlsruhe Institute of Technology, Karlsruhe 76131, Germanydhttps://ror.org/02gfc7t72Institute of Neuroscience, Consejo Superior de Investigaciones Científicas - Universidad de Miguel Hernandez, Alicante 03550, Spainehttps://ror.org/041nas322Institute of Experimental Epileptology and Cognition Research, University of Bonn Medical Center, Bonn 53127, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527395123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527395123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603602123?af=R">
      <title>Adapting the MasSpec Pen for noninvasive detection of oral cavity squamous cell carcinoma</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603602123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceOral cavity squamous cell carcinoma (OCSCC) is a deadly form of head and neck cancer that disproportionately afflicts low-middle income communities. Given the poor prognosis of late-stage patients, detection of OCSCC remains crucial for ...</description>
      <dc:title>Adapting the MasSpec Pen for noninvasive detection of oral cavity squamous cell carcinoma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603602123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Charles A. WolfeTassia V. MendesFaith JackobsSarah BenchEmily X. MaBrian J. ArmijoAshley E. MontgomeryRenan V. de BritoCarlos T. ChoneMarcos N. EberlinCaroline P. CarvalhoJunaid IbrahimAndrew T. HuangNelson E. LiouErich M. SturgisRobert TibshiraniLivia S. Eberlinahttps://ror.org/02pttbw34Department of Surgery, Baylor College of Medicine, Houston, TX 77030bhttps://ror.org/04wffgt70Department of Otolaryngology, University of Campinas, Campinas 13085-566, Brazilchttps://ror.org/006nc8n95School of Engineering, Mackgraphe Department, Mackenzie Presbyterian University, São Paulo 01302-907, Brazildhttps://ror.org/02pttbw34Department of Pathology and Immunology, Baylor College of Medicine, Houston, TX 77030ehttps://ror.org/02pttbw34Department of Otolaryngology-Head and Neck Surgery, Baylor College of Medicine, Houston, TX 77030fhttps://ror.org/00f54p054Departments of Biomedical Data Sciences and Statistics, Stanford University, Palo Alto, CA 94304</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603602123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603602123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606103123?af=R">
      <title>Highly flexible vertical electrolyte-gated metal oxide transistors for neuromorphic electronics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606103123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceMetal oxide transistors are important building blocks for large-area, high-resolution displays due to their high carrier mobilities in the amorphous state. However, their use in aqueous environments for wearable biosensors and neuromorphic ...</description>
      <dc:title>Highly flexible vertical electrolyte-gated metal oxide transistors for neuromorphic electronics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606103123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Qing MaXuyang FengHaoyang WangShisheng ChenDi XueXianyu WangChen LiYao YaoLimei LiuEnbo XueGiacomo FortiWei HuangLizhen HuangLitao SunJae-Hyeok ChoLifeng ChiTobin J. MarksAntonio FacchettiBinghao WangaSchool of Electronic Science &amp; Engineering, Southeast University, Jiangning, Nanjing, Jiangsu 211189, People’s Republic of ChinabDepartment of Chemistry and Materials Research Center, Northwestern University, Evanston, IL 60208cInstitute of Functional Nano &amp; Soft Materials, Soochow University, Suzhou 215123, People’s Republic of ChinadSchool of Integrated Circuits, Southeast University, Jiangning, Nanjing, Jiangsu 211189, People’s Republic of Chinaehttps://ror.org/03tqb8s11College of Mechanical Engineering, Yangzhou University, Hanjiang, Yangzhou, Jiangsu 225127, People’s Republic of Chinafhttps://ror.org/01zkghx44School of Materials Science and Engineering, Georgia Institute of Technology, Atlanta, GA 30332</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606103123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606103123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535921123?af=R">
      <title>Co-phase separation of KRI1 and NPM1 sustains nucleolar integrity and ribosome biogenesis to fuel liver cancer progression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535921123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe treatment of hepatocellular carcinoma (HCC) remains challenging, highlighting an urgent need for novel therapeutic targets. This study elucidates a crucial mechanism in HCC progression, uncovering that the nucleolar protein KRI1 sustains ...</description>
      <dc:title>Co-phase separation of KRI1 and NPM1 sustains nucleolar integrity and ribosome biogenesis to fuel liver cancer progression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535921123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Yu LuLunbiao GanWenxiu RuYujing GuoQian HuangSha YinFengze NieSijia DiSiyu YaoHuanhuan WanFa YangWeijun QinWeihong Wenahttps://ror.org/01y0j0j86School of Life Sciences and Technology, Northwestern Polytechnical University, Xi’an 710129, Chinabhttps://ror.org/00ms48f15Department of Urology, Xijing Hospital, Fourth Military Medical University, Xi’an 710032, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535921123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535921123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602136123?af=R">
      <title>Palmitoylation of TK1 exacerbates osteoarthritis by promoting JNK-mediated metabolic reprogramming</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602136123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceOsteoarthritis (OA) is a major cause of pain and disability, yet no approved disease-modifying therapy can halt its progression. We identify thymidine kinase 1 (TK1) as a pathogenic factor linking inflammatory stress to JNK activation, ...</description>
      <dc:title>Palmitoylation of TK1 exacerbates osteoarthritis by promoting JNK-mediated metabolic reprogramming</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602136123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Zhao ZhangChaoyi ZhangYucan JuYaojia ZhouWeihua GuoJinwei XieZeyu Huangahttps://ror.org/011ashp19Department of Orthopaedic Surgery, Orthopaedic Research Institute, West China Hospital, West China Medical School, Sichuan University, Chengdu 610041, Sichuan Province, People’s Republic of ChinabAnimal Experimental Center of West China Hospital, Chengdu 610041, Sichuan Province, People’s Republic of Chinachttps://ror.org/00p991c53Department of Clinical Laboratory, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430022, 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>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602136123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602136123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613431123?af=R">
      <title>The dynamic and heterogeneous structure of the non-canonical inflammasome</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613431123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceAnimals respond to injury, infection, or toxic materials via a process called inflammation. At the molecular level, inflammation involves formation of large machines—inflammasomes—that are instrumental in triggering cascades that lead to an ...</description>
      <dc:title>The dynamic and heterogeneous structure of the non-canonical inflammasome</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613431123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Alexander I. M. SeverJames M. AraminiJeffrey P. BoninHuaying ZhaoHanlin WangJohn L. RubinsteinPeter SchuckLewis E. Kayahttps://ror.org/03dbr7087Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, CanadabProgram in Molecular Medicine, The Hospital for Sick Children Research Institute, Toronto, ON M5G 0A4, Canadachttps://ror.org/03dbr7087Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canadadhttps://ror.org/03dbr7087Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canadaehttps://ror.org/00372qc85National Institute of Biomedical Imaging and Bioengineering, NIH, Bethesda, MD 20892fhttps://ror.org/03dbr7087Department of Medical Biophysics, University of Toronto, Toronto, ON M5G 1L7, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613431123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613431123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520879123?af=R">
      <title>SIX1 is required for adult cochlear sensory epithelium homeostasis and auditory function</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520879123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceIt remains unclear whether developmental transcription factors sustain adult cochlear function. We show that SIX1, known for embryonic hair-cell specification, remains active in the adult cochlea and is essential for hearing. AdultSix1loss ...</description>
      <dc:title>SIX1 is required for adult cochlear sensory epithelium homeostasis and auditory function</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520879123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Xiaohui MaIan AsamiyaElizabeth LouieYing ChenAiqun LiPin-Xian Xuahttps://ror.org/04a9tmd77Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029bhttps://ror.org/04a9tmd77Department of Cell, Developmental and Regenerative Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520879123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520879123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527880123?af=R">
      <title>A TCR-mimic bispecific antibody reduces HIV-1 provirus and delays viral rebound in HLA-matched humanized mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527880123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceAn HIV-1 cure strategy will require novel therapeutics to facilitate immune-mediated elimination of infected cells and reduction of blood and tissue reservoirs. Here, we demonstrate that an TCR-mimic bispecific antibody that recognizes a ...</description>
      <dc:title>A TCR-mimic bispecific antibody reduces HIV-1 provirus and delays viral rebound in HLA-matched humanized mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527880123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Zhe YuanNathan L. BoardMiaoyun ZhaoGuorui ZuSrona SenguptaQingsheng LiJanet D. SilicianoRobert F. SilicianoLuis J. Montanerahttps://ror.org/04wncat98The Wistar Institute, Philadelphia, PA 19104bhttps://ror.org/00za53h95Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, MD 21205cHHMI, Baltimore, MD 21205</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527880123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527880123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608455123?af=R">
      <title>The EV-A71 RNA-binding protein Matrin 3 facilitates viral replication by stabilizing viral RNA via ZDHHC20-mediated palmitoylation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608455123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSevere hand, foot, and mouth disease caused by Enterovirus 71 (EV-A71) threatens global pediatric health, yet its infection mechanisms remain poorly understood, hindering antiviral development. Using ChIRP-MS and functional genomics, we map ...</description>
      <dc:title>The EV-A71 RNA-binding protein Matrin 3 facilitates viral replication by stabilizing viral RNA via ZDHHC20-mediated palmitoylation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608455123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Xiaoyan ZuoYongjun ChenXia XiaoZichun XiangLili RenXiaobo LeiJianwei Wangahttps://ror.org/02drdmm93National Health Commission Key Laboratory of System Biology of Pathogens and Christophe Merieux Laboratory, National Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 102600, People’s Republic of Chinabhttps://ror.org/02drdmm93State Key Laboratory of Respiratory Health and Multimorbidity, Key Laboratory of Pathogen Infection Prevention and Control (Ministry of Education), National Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 102600, 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>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608455123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608455123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517883123?af=R">
      <title>Cell surface ADGRG1 and CD86 expression identifies antitumor CD4+ T cells in human cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517883123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceStudies have demonstrated that adoptive cell transfer with antitumor CD4+T cells can be effective in treating advanced stage cancer patients. Improving methods to identify antitumor CD4+T cells through cell surface protein expression remains ...</description>
      <dc:title>Cell surface ADGRG1 and CD86 expression identifies antitumor CD4+ T cells in human cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517883123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Kyle J. HitscherichAaron J. DinermanAbraham A. HakimVictoria DulembaSivasish SindiriBillel GasmiAlakesh BeraJared J. GartnerTodd D. PrickettZhiya YuYong F. LiNivedita M. RatnamAlexandra M. GustafsonAarushi BhasinMaria R. ParkhurstNicholas D. KlemenMei Li M. KwongJames C. YangPaul F. RobbinsStephanie L. GoffSteven A. RosenbergSri KrishnaFrank J. LoweryaSurgery Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517883123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517883123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602636123?af=R">
      <title>Identification of novel functional sites in the Cav1.3 calcium channel α1-subunit using evolutionary modeling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602636123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceVoltage-gated calcium channels regulate critical physiological processes, and some genetic variants inCACNA1Dcan cause neurodevelopmental and cardiac disorders. We demonstrate that evolutionary modeling based on sequence covariation can ...</description>
      <dc:title>Identification of novel functional sites in the Cav1.3 calcium channel α1-subunit using evolutionary modeling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602636123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Xuechen TangHoria C. HermeneanAlesia YakimchykPetronel TulucNadine J. OrtnerKlaus R. Liedlahttps://ror.org/054pv6659Department of Theoretical Chemistry, University of Innsbruck, Innsbruck 6020, Austriabhttps://ror.org/054pv6659Department of Pharmacology and Toxicology, University of Innsbruck, 6020 Innsbruck, Austriachttps://ror.org/02n0bts35Gottfried Schatz Research Center, Division of Medical Physics and Biophysics, Medical University of Graz, 8010 Graz, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602636123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602636123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604124123?af=R">
      <title>Bladder mucosal afferents detect UTI and aid pathogen clearance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604124123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe bladder is innervated by complex sensory networks, yet the specific role of stretch-insensitive mucosal nerves has remained unknown for nearly two decades. Utilizing a model of selective mucosal afferent denervation we demonstrate that ...</description>
      <dc:title>Bladder mucosal afferents detect UTI and aid pathogen clearance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604124123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Cindy TayHarman SharmaStewart RamsayGeorgia BourlotosSarah K. ManningNatalie E. StevensSophie J. MillerGeraint B. RogersDavid J. LynnFeargal J. RyanAndrea M. HarringtonVladimir ZagorodnyukSteven L. TaylorLuke Grundyahttps://ror.org/01kpzv902College of Medicine and Public Health, Flinders Health and Medical Research Institute, Flinders University, Bedford Park, SA 5042, Australiabhttps://ror.org/03e3kts03Lifelong Health, South Australian Health and Medical Research Institute, Adelaide, SA 5000, AustraliacAdelaide Medical School, The University of Adelaide, Adelaide, SA 5000, Australiadhttps://ror.org/03e3kts03Microbiome and Host Health Programme, South Australian Health and Medical Research Institute, Adelaide, SA 5000, Australiaehttps://ror.org/03e3kts03Precision Cancer Medicine Theme, South Australian Health and Medical Research Institute, Adelaide, SA 5000, Australiafhttps://ror.org/03e3kts03Visceral Pain Research Group, Hopwood Centre for Neurobiology, Lifelong Health Theme, South Australian Health and Medical Research Institute, Adelaide, SA 5000, AustraliagSchool of Biomedicine, Faculty of Health and Medical Sciences, University of Adelaide, Adelaide, SA 5005, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604124123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604124123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600248123?af=R">
      <title>CIP2A–TOPBP1 complex and PP2A dynamically regulate Polθ recruitment and phosphorylation at mitotic DNA double-strand breaks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600248123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceFaithful repair of DNA double-strand breaks (DSBs) during mitosis is critical for genome stability, yet the underlying regulatory mechanisms remain poorly defined. We identify the CIP2A–TOPBP1 complex as a key regulator of mitotic DSB repair ...</description>
      <dc:title>CIP2A–TOPBP1 complex and PP2A dynamically regulate Polθ recruitment and phosphorylation at mitotic DNA double-strand breaks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600248123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Xipeng ZhaoBin ChenFeng XuJie ZhangZhicheng YaoRuru WangJie ZhangShenglan ZhouYao HouShangkun XuAn XuLijun WuGuoping Zhaoahttps://ror.org/034t30j35High Magnetic Field Laboratory, Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Chinese Academy of Sciences, Hefei, Anhui 230031, Chinabhttps://ror.org/04c4dkn09University of Science and Technology of China, Hefei, Anhui 230026, Chinachttps://ror.org/034t30j35Anhui Province Key Laboratory of Environmental Toxicology and Pollution Control Technology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei, Anhui 230031, Chinadhttps://ror.org/02qp3tb03Department of Oncology, Mayo Clinic, Rochester, MN 55905ehttps://ror.org/05th6yx34Information Materials and Intelligent Sensing Laboratory of Anhui Province, Institutes of Physical Science and Information Technology, Anhui University, Hefei, Anhui 230601, Chinafhttps://ror.org/03xb04968Anhui Medical University, Hefei, Anhui 230032, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600248123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600248123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607733123?af=R">
      <title>Ca2+ regulation of PMCA2 calcium pump expression in hair cells of Tmc1 deafness mutants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607733123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceCochlear hair cell transduction arises by activation of mechanotransducer (MET) channels containing transmembrane channel-like protein 1 (TMC1). Mutations inTmc1cause hair cell death and deafness in mice by postnatal day (P)21. However, at ...</description>
      <dc:title>Ca2+ regulation of PMCA2 calcium pump expression in hair cells of Tmc1 deafness mutants</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607733123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Amanda Bryn RolsethMaryline BeurgDakota Elle KonradBenjamin K. AugustRobert FettiplaceaDepartment of Neuroscience, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607733123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607733123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608068123?af=R">
      <title>Maternal nutrition determines the variable expressivity of STRA6-associated eye malformations</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608068123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceVitamin A is essential for eye development. Mutations in STRA6, the receptor for retinol-binding protein, cause Matthew-Wood syndrome, a congenital disorder with highly variable clinical severity. The basis of this variability has remained ...</description>
      <dc:title>Maternal nutrition determines the variable expressivity of STRA6-associated eye malformations</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608068123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Aicha SaadaneJohannes von Lintigahttps://ror.org/051fd9666Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608068123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608068123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535274123?af=R">
      <title>Developmental plasticity under human management shaped cereal evolution prior to domestication in the Early Holocene southern Levant</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535274123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceCereals were among the earliest crops domesticated in southwest Asia and remain central to global agriculture. We can track cereal domestication archaeologically using a suite of morphological traits that distinguish domestic species from ...</description>
      <dc:title>Developmental plasticity under human management shaped cereal evolution prior to domestication in the Early Holocene southern Levant</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535274123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Jade WhitlamPascal FlohrAmy BogaardMichael CharlesBill FinlaysonCheryl A. Makarewiczahttps://ror.org/052gg0110School of Archaeology, University of Oxford, Oxford OX1 3TG, United Kingdombhttps://ror.org/052gg0110Department for Continuing Education, University of Oxford, Oxford OX1 2JA, United KingdomcInstitute for Prehistoric and Protohistoric Archaeology, University of Kiel, Kiel D-24118, GermanydSante Fe Institute, Sante Fe, NM 87501eArchaeology Stable Isotope Laboratory, University of Kiel, Kiel D-24118, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535274123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535274123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610808123?af=R">
      <title>An interdependent Cbf1–CCAN interaction stabilizes the budding yeast kinetochore</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610808123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe kinetochore is a multisubunit complex that links chromosomes to microtubules, ensuring accurate genome segregation during cell division, yet the functions of many components remain unclear. Here, we identify an interdependent interaction ...</description>
      <dc:title>An interdependent Cbf1–CCAN interaction stabilizes the budding yeast kinetochore</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610808123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Sabrine HedouinChangkun HuSue Bigginsahttps://ror.org/007ps6h72Basic Sciences Division, Fred Hutchinson Cancer Center, Seattle, WA 98109bHHMI, Seattle, WA 98109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610808123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610808123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608703123?af=R">
      <title>Claims of sex-dependent effects in the behavioral and brain sciences are infrequently supported by valid statistical comparisons</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608703123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSex-inclusive research policies and interest in precision medicine have increased efforts to identify sex-dependent responses to treatments and interventions. Here, we show that claims of sex-dependent effects are disproportionately featured ...</description>
      <dc:title>Claims of sex-dependent effects in the behavioral and brain sciences are infrequently supported by valid statistical comparisons</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608703123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Madeline T. OlivierAndrew W. BrownSimon ChungColby J. VorlandDonna L. Maneyahttps://ror.org/03czfpz43Department of Psychology, Emory University, Atlanta, GA 30322bhttps://ror.org/00xcryt71Department of Biostatistics, University of Arkansas for Medical Sciences, Little Rock, AR 72205chttps://ror.org/05609b125Arkansas Children’s Research Institute, Little Rock, AR 72202dhttps://ror.org/01kg8sb98Department of Epidemiology and Biostatistics, Indiana University School of Public Health-Bloomington, Bloomington, IN 47403</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608703123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608703123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605383123?af=R">
      <title>Successful oocyte transport through the oviduct does not depend on the longitudinal alignment of oviduct epithelial folds</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605383123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceLongitudinal folds of the oviduct epithelium are conserved across vertebrates and are thought to promote cilia-driven oocyte transport, yet their functional requirement is untested. Here, we found that oocytes reach the uterus inVangl1mutant ...</description>
      <dc:title>Successful oocyte transport through the oviduct does not depend on the longitudinal alignment of oviduct epithelial folds</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605383123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Fumiko Matsukawa UsamiMasaki ArataKagayaki KatoDongbo ShiSanae OkaYingzi YangToshihiko Fujimoriahttps://ror.org/05q8wtt20Division of Embryology, National Institute for Basic Biology, Okazaki, Aichi 444-8787, Japanbhttps://ror.org/0516ah480Department of Basic Biology, The Graduate University for Advanced Studies, SOKENDAI, Okazaki, Aichi 444-8787, Japanchttps://ror.org/05q8wtt20Optics and Imaging Facility, Trans-Scale Biology Center, National Institute for Basic Biology, Okazaki, Aichi 444-8585, Japandhttps://ror.org/010rf2m76Cambial Stem Cell System RIKEN Early Career Leaders Program Research Unit, RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa 230-0045, Japanehttps://ror.org/04kj1hn59Department of Developmental Biology, Harvard School of Dental Medicine, Harvard Stem Cell Institute, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605383123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605383123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604094123?af=R">
      <title>High-throughput deformability-based microfluidic sorting reveals metastatic cancer subpopulations</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604094123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceDifferences in deformability among tumor cells are emerging as important factors in tumor progression and metastasis, but isolating and studying these subpopulations at scale has been difficult. We introduce a microfluidic platform that sorts ...</description>
      <dc:title>High-throughput deformability-based microfluidic sorting reveals metastatic cancer subpopulations</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604094123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Xiaoyan LiuYuanchao LiuJunwei LiZhibei WangMui Hoon Brenda NaiQian ChenHaodong LiXingyu JiangShaofei ShenChwee Teck Limahttps://ror.org/01tgyzw49Institute for Health Innovation and Technology, National University of Singapore, Singapore 117599, Singaporebhttps://ror.org/01tgyzw49Department of Biomedical Engineering, National University of Singapore, Singapore 117583, Singaporechttps://ror.org/02e7b5302School of Mechanical and Aerospace Engineering, Nanyang Technological University, Singapore 639798, Singaporedhttps://ror.org/05e9f5362College of Life Science, Shanxi Agricultural University, Taigu 030801, Shanxi, Chinaehttps://ror.org/049tv2d57Department of Biomedical Engineering, Southern University of Science and Technology, Shenzhen 518055, Guangdong, Chinafhttps://ror.org/01tgyzw49Mechanobiology Institute, National University of Singapore, Singapore 117411, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604094123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604094123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618523123?af=R">
      <title>Guiding covalent catalysis enables a carbon-inserting rearrangement in molybdenum cofactor biosynthesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618523123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHow enzymes orchestrate complex atomic rearrangements remains a central question in biology and chemistry. Biosynthesis of the molybdenum cofactor, essential across all domains of life, requires one of Nature’s most intricate rearrangement ...</description>
      <dc:title>Guiding covalent catalysis enables a carbon-inserting rearrangement in molybdenum cofactor biosynthesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618523123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Di LiMaria A. SchumacherKenichi Yokoyamaahttps://ror.org/00py81415Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710bhttps://ror.org/00py81415Department of Chemistry, Duke University, Durham, NC 27710</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2618523123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610287123?af=R">
      <title>Early-life sugar restriction causally reduces adult cancer incidence and slows biological aging</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610287123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceRecent quasi-experimental studies show that early-life sugar restriction reduces cardiometabolic disease risk, but whether this protection extends to cancer, and through what mechanism, has remained unknown. Exploiting the abrupt end of UK ...</description>
      <dc:title>Early-life sugar restriction causally reduces adult cancer incidence and slows biological aging</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610287123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Chen ZhuWeilong Zhangahttps://ror.org/04v3ywz14College of Economics and Management, China Agricultural University, Beijing, China, 100083bhttps://ror.org/04v3ywz14Beijing Food Safety Policy and Strategy Research Base, China Agricultural University, Beijing, China, 100083chttps://ror.org/04v3ywz14Academy of Global Food Economics and Policy (AGFEP), China Agricultural University, Beijing, China, 100083dhttps://ror.org/013meh722Faculty of Economics, University of Cambridge, Cambridge CB3 9DD, United Kingdomehttps://ror.org/013meh722Selwyn College, University of Cambridge, Cambridge CB3 9DQ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610287123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533430123?af=R">
      <title>Evolution after whole-genome duplication (WGD) drives phenotypic and transcriptomic divergence more than WGD in an autopolyploid herb</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533430123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceWhole-genome duplication (WGD) is a key driver of plant evolution, often proposed to enhance adaptation to novel or stressful environments. Comparisons among diploids, newly synthesized autotetraploids, and natural autotetraploids disentangle ...</description>
      <dc:title>Evolution after whole-genome duplication (WGD) drives phenotypic and transcriptomic divergence more than WGD in an autopolyploid herb</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533430123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Sandra GrünigRimjhim Roy ChoudhuryChristian Parisodahttps://ror.org/022fs9h90Department of Biology, University of Fribourg, 1700 Fribourg, Switzerlandbhttps://ror.org/02k7v4d05Institute of Plant Sciences, University of Bern, 3013 Bern, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533430123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608267123?af=R">
      <title>eFormate-mediated CO2 bioconversion: A modular electrochemical–microbial cascade compared across a diverse set of microorganisms</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608267123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceDecarbonizing chemical manufacturing requires efficient methods to upgrade CO2into functional carbon feedstock. Integrating CO2electroreduction with microbial upgrading generates liquid intermediates such as formate, enabling diverse ...</description>
      <dc:title>eFormate-mediated CO2 bioconversion: A modular electrochemical–microbial cascade compared across a diverse set of microorganisms</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608267123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Jihoon ChoiNicolas GrandelDeepika AwasthiGeonhui LeeAbhishant NigamYu ShanNathan E. SolandMaria Fonseca GuzmanHye-jin JoDiep N. PhamPeidong YangBlake A. Simmonsahttps://ror.org/01an7q238Department of Materials Science and Engineering, University of California, Berkeley, CA 94720bhttps://ror.org/02jbv0t02Materials Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720chttps://ror.org/02jbv0t02Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720dhttps://ror.org/03ww55028Deconstruction Division, Joint BioEnergy Institute, Emeryville, CA 94608ehttps://ror.org/01an7q238Department of Chemistry, University of California, Berkeley, CA 94720fhttps://ror.org/02jbv0t02Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720ghttps://ror.org/01an7q238Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608267123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602724123?af=R">
      <title>Cytoplasmic fluidity couples nutrient availability and enterocyte fate in vivo</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602724123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceWe demonstrate that fly gut cells possess a system to detect the quantity rather than the quality of molecules in food through changes in cytoplasmic fluidity and alter their cell fate accordingly. This provides an additional mechanistic layer ...</description>
      <dc:title>Cytoplasmic fluidity couples nutrient availability and enterocyte fate in vivo</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602724123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Yukana NakamuraMotohiro MorikawaTomomi TakanoSa Kan Yooahttps://ror.org/02qf2tx24Graduate School of Science and Technology, Kwansei Gakuin University, Sanda 669-1330, Japanbhttps://ror.org/023rffy11Laboratory for Homeodynamics, RIKEN Center for Biosystems Dynamics Research, Kobe 650-0047, Japanchttps://ror.org/03tgsfw79Division of Developmental Biology and Regenerative Medicine, Kobe University, Kobe 650-0047, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602724123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614476123?af=R">
      <title>AgRP neurons are required for the weight-lowering effects of GLP-1 receptor agonists in female mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614476123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceGlucagon-like peptide-1 receptor agonists (GLP-1RAs), including semaglutide, are highly effective antiobesity drugs, yet how the brain sustains their weight-lowering effects remains unclear. Agouti-related peptide (AgRP) neurons are viewed as ...</description>
      <dc:title>AgRP neurons are required for the weight-lowering effects of GLP-1 receptor agonists in female mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614476123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Mateus d’ÁvilaJoão Cavalcanti-de-AlbuquerqueRoberto Collado-PérezZhong-Wu LiuJenna HunterAnne WhiteJoseph SchlessingerGiuseppe D’AgostinoTamas L. Horvathahttps://ror.org/03v76x132Interdepartmental Neuroscience Program, Department of Neuroscience, Yale Graduate School of Arts and Sciences, Yale University, New Haven, CT 06510bhttps://ror.org/03v76x132Department of Comparative Medicine, Yale School of Medicine, Yale University, New Haven, CT 06510chttps://ror.org/027m9bs27Division of Integrative Physiology, School of Medical Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, United KingdomdDepartment of Pharmacology, Yale School of Medicine, New Haven, CT 06510</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614476123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614476123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602538123?af=R">
      <title>Activation of the angiotensin II type I receptor by a nonpeptide agonist</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602538123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe angiotensin II type I receptor (AT1R) is a key regulator of cardiovascular function and is traditionally activated by peptide agonists and targeted by small-molecule antagonists for the treatment of high blood pressure. Here, we explore ...</description>
      <dc:title>Activation of the angiotensin II type I receptor by a nonpeptide agonist</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602538123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Meredith A. SkibaJinghan LiuPengxiang ShenJihee KimElizabeth WrenMorgan S. A. GilmanDean StausConor McMahonJeffrey S. SmithRobert J. LefkowitzDaniel KahneLaura M. WinglerAndrew C. KruseaDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115bhttps://ror.org/03vek6s52Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138chttps://ror.org/03njmea73Department of Medicine, Duke University Medical Center, Durham, NC 27710dhttps://ror.org/03njmea73HHMI, Duke University Medical Center, Durham, NC 27710ehttps://ror.org/04b6nzv94Department of Dermatology, Brigham and Women’s Hospital, Boston, MA 02115fhttps://ror.org/00py81415Department of Pharmacology and Cancer Biology, 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>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602538123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610891123?af=R">
      <title>Economic preferences predict higher-education choices</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610891123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceWhy do people choose different paths through higher education? We study whether part of the answer lies in differences in patience and willingness to take risks. These traits are hard to study because they must be measured before education ...</description>
      <dc:title>Economic preferences predict higher-education choices</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610891123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Thomas F. EpperErnst FehrKristoffer B. HvidbergClaus T. KreinerSøren Leth-PetersenBasit ZafaraCenter for Economic Behavior and Inequality, Copenhagen K 1353, Denmarkbhttps://ror.org/05bz47575CNRS, IESEG School of Management, Univ. Lille, UMR 9221 - LEM - Lille Economie Management, F-59000 Lille, Francechttps://ror.org/02crff812Department of Economics, University of Zürich, Zürich, 8006, Switzerlanddhttps://ror.org/01aj84f44Department of Economics and Business Economics, Aarhus University, Aarhus 8000, Denmarkehttps://ror.org/035b05819Department of Economics, University of Copenhagen, Copenhagen K 1353, Denmarkfhttps://ror.org/00jmfr291Department of Economics, University of Michigan, Ann Arbor, MI 48109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610891123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532196123?af=R">
      <title>A lettuce receptor-like kinase recognizes the highly conserved heptapeptide motif within microbial Nep1-like proteins</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532196123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceUnderstanding pathogen recognition in crops is key to improving disease resistance. Our study identified a cell surface immune receptor in cultivated lettuce that mediates the recognition of the nlp24 pattern derived from secreted proteins (...</description>
      <dc:title>A lettuce receptor-like kinase recognizes the highly conserved heptapeptide motif within microbial Nep1-like proteins</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532196123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Iñigo BañalesSarah L. MehremSamara Almeida LandmanMarrit AlderkampMax PijfersStan BaijensAlix von BredowPeter SchutteSander PrevooGijs van AsseltSagayamary SagayaradjBasten SnoekRichard MichelmoreDmitry LapinGuido Van den Ackervekenahttps://ror.org/04pp8hn57Translational Plant Biology, Department of Biology, Science Faculty, Institute of Environmental Biology, Utrecht University, Utrecht 3584CH, The Netherlandsbhttps://ror.org/04pp8hn57Theoretical Biology and Bioinformatics, Department of Biology, Science Faculty, Institute of Biodynamics and Biocomplexity, Utrecht University, Utrecht 3584CH, The Netherlandschttps://ror.org/05rrcem69Genome Center, University of California, Davis, CA 95616dhttps://ror.org/05rrcem69Department of Plant Sciences, University of California, Davis, CA 95616</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532196123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602976123?af=R">
      <title>Highly localized droplet clustering in shallow cumulus clouds</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602976123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceRain initiation in clouds containing only liquid droplets, known as warm clouds, remains poorly understood. Using a fast airborne 3D imaging instrument deployed within such clouds, we identified highly localized regions (about one meter) in ...</description>
      <dc:title>Highly localized droplet clustering in shallow cumulus clouds</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602976123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Birte ThiedeMichael L. LarsenFreja NordsiekOliver SchlenczekYewon KimEberhard BodenschatzGholamhossein Bagheriahttps://ror.org/0087djs12Laboratory for Fluid Physics, Pattern Formation and Biocomplexity, Max Planck Institute for Dynamics and Self-Organization, Göttingen 37077, Germanybhttps://ror.org/01y9bpm73Department of Physics, University of Göttingen, Göttingen 37077, Germanychttps://ror.org/00390t168Department of Physics and Astronomy, College of Charleston, Charleston, SC 29424dhttps://ror.org/0036rpn28Department of Physics, Michigan Technological University Houghton, MI 49931ehttps://ror.org/05bnh6r87Department of Physics, Cornell University, Ithaca, NY 14853</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602976123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619078123?af=R">
      <title>Hyperedge approximation for stochastic processes on higher-order networks</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619078123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHow cooperation evolves in a population, and how new opinions take hold, depend on the structure of who interacts with whom. Most theories treat those interactions as pairwise—but many are not: Scientific collaborations, public goods ...</description>
      <dc:title>Hyperedge approximation for stochastic processes on higher-order networks</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619078123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Anzhi ShengAlex McAvoyYe TianSilun ZhangAngela FontanJoshua B. Plotkinahttps://ror.org/026vcq606Department of Decision and Control Systems, KTH Royal Institute of Technology, Stockholm 10044, Swedenbhttps://ror.org/026vcq606Department of Mathematics, KTH Royal Institute of Technology, Stockholm 10044, Swedenchttps://ror.org/00b30xv10Department of Biology, University of Pennsylvania, Philadelphia, PA 19104dhttps://ror.org/0130frc33School of Data Science and Society, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599ehttps://ror.org/0130frc33Department of Mathematics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599fhttps://ror.org/00b30xv10Center for Mathematical Biology, University of Pennsylvania, Philadelphia, PA 19014ghttps://ror.org/02rqvrp93Meiji Institute for Advanced Study of Mathematical Sciences, Meiji University, Nakano, Tokyo 164-8525, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619078123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526200123?af=R">
      <title>3D epigenomic landscape of the human retinal pigment epithelium</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526200123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceRetinal pigment epithelium (RPE) dysfunction causes irreversible vision loss. Although iPSC-derived RPE (iPSC-RPE) represents a promising cell source for transplantation, its functional equivalence to RPE remains incompletely defined, ...</description>
      <dc:title>3D epigenomic landscape of the human retinal pigment epithelium</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526200123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Xiyuan LiuDongmei TangJing ZhangTong LiJiaxiang HuangJia QuYijun RuanHaoxi ChaiZai-Long Chiahttps://ror.org/00rd5t069State Key Laboratory of Eye Health, Eye Hospital, Wenzhou Medical University, Wenzhou 325027, Chinabhttps://ror.org/00a2xv884Life Sciences Institute and The Second Affiliated Hospital, Zhejiang University, Hangzhou 310058, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526200123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526200123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602941123?af=R">
      <title>TPC1-dependent control of endosomal pH and transferrin uptake determines cellular iron status</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602941123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceWe elucidate here a role of the endolysosomal two-pore cation channel TPC1 in iron metabolism by analyzing both a novel TPC1 gain-of-function knock-in and a TPC1 knockout mouse model which show opposing effects on iron uptake and release from ...</description>
      <dc:title>TPC1-dependent control of endosomal pH and transferrin uptake determines cellular iron status</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602941123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Rebecca DeutschSimone JörsYvonne KlinglVeronika KudrinaDanusa MenegazDawid JaślanZala SerianzAndreas VogelCarla AbrahamianSayari BhuniaTinatini Tavhelidse-SuckChristin RichterAngela WirthNicole UrbanBernd NorthoffWolfgang WilfertNorbert KlugbauerFranz BracherMarco KellerFabian GeislerMichael SchaeferDaniel TeupserLesca HoldtSerkan BelkayaMarc FreichelChristian Grimmahttps://ror.org/02wbcav28Walther Straub Institute of Pharmacology and Toxicology, Faculty of Medicine, Ludwig-Maximilians-University, Munich 80336, Germanybhttps://ror.org/05591te55Technical University of Munich School of Medicine and Health, Department of Clinical Medicine—Clinical Department for Internal Medicine II, University Medical Center, Technical University of Munich, Munich 81675, Germanychttps://ror.org/01s1h3j07Immunology, Infection and Pandemic Research IIP, Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Munich/Frankfurt 80799, Germanydhttps://ror.org/02kkvpp62Department of Cardiology, German Heart Centre Munich, Technical University of Munich, Munich 80636, GermanyeInstitute of Pharmacology, Heidelberg University, Heidelberg 69120, Germanyfhttps://ror.org/031t5w623German Centre for Cardiovascular Research, Partner Site Heidelberg/Mannheim, Heidelberg 69115, Germanyghttps://ror.org/03s7gtk40Rudolf-Boehm-Institute for Pharmacology and Toxicology, Universität Leipzig, Leipzig 04107, Germanyhhttps://ror.org/05g1y0660Institute of Laboratory Medicine, University Hospital Munich, Munich 81377, GermanyiInstitute for Experimental and Clinical Pharmacology and Toxicology, Medical Faculty, Albert-Ludwigs-University Freiburg, Freiburg 79104, GermanyjDepartment of Pharmacy, Ludwig-Maximilians-University, Munich 81377, Germanykhttps://ror.org/02vh8a032Department of Molecular Biology and Genetics, Bilkent University, Ankara 06800, Türkiyelhttps://ror.org/052gg0110Department of Pharmacology, Faculty of Medicine, University of Oxford, Oxford OX1 3QT, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602941123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602941123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535385123?af=R">
      <title>A structural and mechanistic atlas of NTD antibody neutralization and immune escape across SARS-CoV-2 prototype and its (sub-)variants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535385123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceUnderstanding the antigenic organization of the SARS-CoV-2 spike N-terminal domain (NTD), antibody neutralization, and viral escape has been limited by fragmented epitope classification schemes and incomplete mechanistic insight. We establish ...</description>
      <dc:title>A structural and mechanistic atlas of NTD antibody neutralization and immune escape across SARS-CoV-2 prototype and its (sub-)variants</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535385123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Jianjie ZhouWenyu LiXiaoyun WangJunqing SunShuxin GuoXiaoyu RongZhou TongLianpan DaiWilliam Jun LiuJianxun QiGeorge Fu GaoQihui WangaChinese Academy of Sciences Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, Chinabhttps://ror.org/04c4dkn09School of Life Science, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, Anhui, Chinachttps://ror.org/034t30j35University of the Chinese Academy of Sciences, Beijing 100049, Chinadhttps://ror.org/05qbk4x57Medical School, University of Chinese Academy of Sciences, Beijing 101408, ChinaeFaculty of Health Sciences, University of Macau, Macau Special Administrative Region of China 999078, Chinafhttps://ror.org/03ybmxt82Guangzhou National Laboratory, Guangzhou 510005, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535385123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535385123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607754123?af=R">
      <title>The dynamics of introgression and parallel adaptation across North American Vitis species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607754123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHybridization is a major force shaping genome evolution, but its role in shaping plant diversification and taxonomic relationships across an adaptive radiation remains unclear. Here we examine hybridization, introgression, and adaptation ...</description>
      <dc:title>The dynamics of introgression and parallel adaptation across North American Vitis species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607754123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Tianpeng WangChristopher J. FiscusJacob B. LandisNoé CochetelAbraham Morales-CruzDario CantuJonás A. Aguirre-LiguoriBrandon S. Gautahttps://ror.org/04gyf1771Department of Ecology and Evolutionary Biology, University of California, Irvine, CA 92697bhttps://ror.org/05bnh6r87School of Integrative Plant Science, Section of Plant Biology, Cornell University, Cornell, NY 14853chttps://ror.org/05rrcem69Department of Viticulture and Enology, University of California, Davis, CA 95616dhttps://ror.org/02jbv0t02U.S. Department of Energy, Joint Genome Institute, Lawrence Berkeley National Laboratory, Berkeley, CA 94720ehttps://ror.org/05rrcem69Genome Center, University of California, Davis, CA 95616fhttps://ror.org/032p1n739Departamento de Ecología Tropical, Campus de Ciencias Biológicas y Agropecuarias, Universidad Autónoma de Yucatán, Merida, Mexico 97100</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607754123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607754123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535250123?af=R">
      <title>Population genomics reveals ginseng domestication and ginsenoside biosynthesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535250123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceGinseng is a globally important medicinal plant valued for its health-promoting ginsenosides, but the genetic basis underlying its domestication and metabolite divergence remains unclear. By resequencing 287 accessions, we identified five ...</description>
      <dc:title>Population genomics reveals ginseng domestication and ginsenoside biosynthesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535250123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Yating ZhangKui WangZheng LiXikai YuFengjiao WangSiwei QiaoShiquan XuJiantao ZhaoBao LiuXingtan ZhangHao ZhangWei Liahttps://ror.org/0313jb750Institute of Special Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun 130112, Chinabhttps://ror.org/0313jb750Shenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Key Laboratory of Synthetic Biology, Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen 518120, Chinachttps://ror.org/034t30j35Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, Chinadhttps://ror.org/04gh4er46State Key Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, Chinaehttps://ror.org/05bnh6r87Boyce Thompson Institute, Cornell University, Ithaca, NY 14853fhttps://ror.org/02rkvz144Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University, Changchun 130024, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535250123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535250123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603453123?af=R">
      <title>Mechanistic insights into mutations that cause diseases of phosphate dysregulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603453123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificancePhosphate is an essential mineral in the human body and phosphate dysregulation can cause severe disease. Here, we identify the functional consequences of disease-causing mutations in the phosphate-regulating hormone FGF23 and the ...</description>
      <dc:title>Mechanistic insights into mutations that cause diseases of phosphate dysregulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603453123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Liping ZhangAlisa E. LeeE TianMichael T. CollinsKelly L. RoszkoNadine L. SamaraKelly G. Ten Hagenahttps://ror.org/004a2wv92Developmental Glycobiology Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892bDepartment of Developmental Biology, Harvard School of Dental Medicine, Boston, MA 02115chttps://ror.org/004a2wv92Skeletal Disorders and Mineral Homeostasis Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892dhttps://ror.org/004a2wv92Mineral Homeostasis Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892ehttps://ror.org/004a2wv92Structural Biochemistry Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603453123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603453123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536207123?af=R">
      <title>Direct visualization of carrier density modulation effect around individual charged impurities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536207123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceUnderstanding the quantum transport of electrons around single impurity in crystalline materials is essential for modern electronics as the size of electronic devices approaches the atomic limit. The electrochemical potential fluctuation ...</description>
      <dc:title>Direct visualization of carrier density modulation effect around individual charged impurities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536207123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Yaowu LiuZichun ZhangSidan ChenShengnan XuLichen JiWei ChenXinyu ZhouXiaopeng HuWenhui DuanXi ChenQi-Kun XueShuai-Hua Jiahttps://ror.org/016g9tg59State Key Laboratory of Low-Dimensional Quantum Physics, Department of physics, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/00y0zf565Center for Quantum Nanoscience (QNS), Institute for Basic Science (IBS), Seoul 03760, Republic of Koreachttps://ror.org/053fp5c05Ewha Womans University, Seoul 03760, Republic of Koreadhttps://ror.org/03w7b4p86Frontier Science Center for Quantum Information, Beijing 100084, Chinaehttps://ror.org/04nqf9k60Beijing Academy of Quantum Information Sciences, Beijing 100193, Chinafhttps://ror.org/049tv2d57Department of Physics, Southern University of Science and Technology, Shenzhen 518055, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536207123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536207123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604207123?af=R">
      <title>Attention to heterogeneous information sources affects epidemic outcomes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604207123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe integration of human behavior into infectious disease models has been investigated a lot, and it is well recognized that human behavior drastically affects the epidemic outcome. However, less has been done to learn how different ...</description>
      <dc:title>Attention to heterogeneous information sources affects epidemic outcomes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604207123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Jiayu LiMatthew CheungMarcela Ordorica ArangoNaomi Ehrich LeonardSimon A. Levinahttps://ror.org/00hx57361Program in Applied &amp; Computati-onal Mathematics, Princeton University, Princeton, NJ 08540bhttps://ror.org/00hx57361High Meadows Environmental Institute, Princeton University, Princeton, NJ 08540chttps://ror.org/00hx57361Department of Mechanical and Aerospace Engineering, Princeton University, Princeton, NJ 08540dhttps://ror.org/00hx57361Department of Ecology and Evolutionary Biology, Princeton University, Princeton, NJ 08540</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604207123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604207123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608784123?af=R">
      <title>The evolution of the Earth’s surface iron cycle</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608784123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceIron oxide minerals produced on land by chemical weathering are transported to the ocean and buried in marine sediments, where they can form pyrite or bind to organic matter, processes that release oxygen and influence atmospheric oxygenation ...</description>
      <dc:title>The evolution of the Earth’s surface iron cycle</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608784123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Florian ScholzSebastian DoetterlDalton S. Hardistyahttps://ror.org/00g30e956Department of Earth System Sciences, University of Hamburg, Hamburg 20146, Germanybhttps://ror.org/05a28rw58Department of Environmental Systems Science, ETH Zürich, Zürich 8092, Switzerlandchttps://ror.org/05hs6h993Department of Earth and Environmental Sciences, Michigan State University, East Lansing, MI 48824</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608784123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608784123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618203123?af=R">
      <title>Unveiling previously undescribed circadian clock regulators and action mechanisms via TurboID-based profiling of the LWD1 interactome in Arabidopsis thaliana</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618203123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceElucidating the mechanisms that sustain circadian precision is crucial for understanding how plants align their internal rhythms with external environmental cycles. This study provides mechanistic insights into the action roles of LWD1 by ...</description>
      <dc:title>Unveiling previously undescribed circadian clock regulators and action mechanisms via TurboID-based profiling of the LWD1 interactome in Arabidopsis thaliana</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618203123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Chun-Kai HuangChuan-Chih HsuHuang-Lung TsaiWen-Dar LinJing-Fen WuShu-Hsing Wuahttps://ror.org/00jj3h083Institute of Plant and Microbial Biology, Academia Sinica, Taipei 115201, Taiwanbhttps://ror.org/05bqach95Institute of Molecular and Cellular Biology, National Taiwan University, Taipei 10617, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618203123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618203123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617449123?af=R">
      <title>An N-acetylated daropeptide modulates nematode development</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617449123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSymbiotic bacteria shape animal development through chemical signals, yet ribosomally synthesized peptides involved in such interactions remain poorly understood. We identify aphotorhaptin A, a structurally distinct daropeptide produced by...</description>
      <dc:title>An N-acetylated daropeptide modulates nematode development</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617449123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Suze MaRu LiXiangyang GaoEric GemmellSijia GuoHeng ChenXuedong HuangMichael CapperZhijun LiuZixin DengWei DingJesko KöhnkeXiaohui WangQi Zhangahttps://ror.org/05nkgk822National Engineering Research Center for Carbohydrate Synthesis, College of Chemistry and Materials, Jiangxi Normal University, Nanchang 330022, Chinabhttps://ror.org/013q1eq08Department of Chemistry, Fudan University, Shanghai 200433, Chinachttps://ror.org/034t30j35Laboratory of Chemical Biology, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, Chinadhttps://ror.org/04c4dkn09School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei 230026, ChinaeCollege of Animal Science and Technology, Xinjiang Agricultural Vocational and Technical University, Changji 831100, Chinafhttps://ror.org/00vtgdb53School of Chemistry, University of Glasgow, Glasgow G12 8QQ, United Kingdomghttps://ror.org/0220qvk04State Key Laboratory of Microbial Metabolism, School of Life Sciences &amp; Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, Chinahhttps://ror.org/02br7py06National Facility for Protein Science in Shanghai, Zhangjiang Lab, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai 201210, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617449123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617449123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604171123?af=R">
      <title>Checkpoint-insulated triple-signal artificial antigen-presenting cells drive antigen relay and systemic antitumor immunity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604171123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceEffective cancer vaccines must combine broad tumor antigen coverage with immune activation, yet existing platforms rarely achieved both. Here, we developed OncoAPC, a tumor-derived artificial antigen-presenting cell that integrated triple-...</description>
      <dc:title>Checkpoint-insulated triple-signal artificial antigen-presenting cells drive antigen relay and systemic antitumor immunity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604171123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Siyu ZhaoTianzi ShiTianyi TianFangming ZhangZitong ZhangHongbo XuYixuan ZhouZhilang LiZhaojing QinPengwen XuConglian YangZhiping Zhangahttps://ror.org/00p991c53Tongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan 430030, Chinabhttps://ror.org/0064kty71National-Local Joint Engineering Laboratory of Druggability and New Drug Evaluation, National Engineering Research Center for New Drug and Druggability (Cultivation), Guangdong Province Key Laboratory of New Drug Design and Evaluation, School of Pharmaceutical Sciences, Sun Yat-Sen University, Guangzhou 510006, Chinachttps://ror.org/00p991c53Department of Pharmacy, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430022, ChinadHubei Engineering Research Center for Novel Drug Delivery System, Wuhan 430030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604171123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604171123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614989123?af=R">
      <title>Hydrodynamic phase entrainment drives synchronization of sperm flagella</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614989123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceHow neighboring sperm flagella coordinate their beating has been debated for decades: hydrodynamic theory predicts that fluid coupling alone suffices, yet experiments on freely swimming sperm implicate direct mechanical contact. Using a ...</description>
      <dc:title>Hydrodynamic phase entrainment drives synchronization of sperm flagella</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614989123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Kaiyu WangRongjing ZhangJunhua Yuanahttps://ror.org/04c4dkn09Hefei National Research Center for Physical Sciences at the Microscale and Department of Physics, University of Science and Technology of China, Hefei, Anhui 230026, Chinabhttps://ror.org/02wmsc916College of Physics, Guizhou University, Guiyang 550025, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614989123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614989123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617665123?af=R">
      <title>A transposon-derived transcription factor senses ionic stress through phase separation to govern plant autophagy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617665123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSalt stress imposes cellular challenges through osmotic dehydration and ionic toxicity, yet mechanisms for ionic stress perception in plants remain unknown. We identified MUSTANG4 (MUG4) as both an ionic sensor and master autophagy regulator ...</description>
      <dc:title>A transposon-derived transcription factor senses ionic stress through phase separation to govern plant autophagy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-05T07:00:00Z</dc:date>
      <dc:creator>Yang ShaoSongyang WangLi LiangBiao GongAurore JoharyBenhui ShiLinyang ZhangYanqun XuZoé Joly-LopezZisheng LuoThomas E. BureauJiaqi SunaThe Key Laboratory of Plant Development and Environmental Adaptation Biology, Ministry of Education, Shandong Key Laboratory of Precision Molecular Crop Design and Breeding, Shandong Provincial Key Laboratory of Plant Stress Biology and Genetic Improvement, School of Life Sciences, Shandong University, Qingdao 266237, Chinabhttps://ror.org/01pxwe438Department of Biology, McGill University, Montreal, QC H3B 1A1, Canadachttps://ror.org/02ke8fw32College of Horticulture Science and Engineering, Shandong Agricultural University, Taian 271018, Chinadhttps://ror.org/002rjbv21Département de Chimie, Université du Québec à Montréal, Montréal, QC H2X 3P2, Canadaehttps://ror.org/0220qvk04Department of Food Science and Technology, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, ChinafCollege of Biosystems Engineering and Food Science, Key Laboratory of Agro-Products Postharvest Handling Ministry of Agriculture, Zhejiang Key Laboratory of Agri-Food Resources and High-Value Utilization, Zhejiang University, Hangzhou 310058, Chinaghttps://ror.org/0207yh398Shenzhen Research Institute of Shandong University, Shenzhen 518000, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617665123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617665123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615786123?af=R">
      <title>Aggregation kinetics define the temporal window of IAPP proteotoxicity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615786123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceProtein aggregation into amyloid is a hallmark of many diseases, including type 2 diabetes, yet the protein species responsible for cellular toxicity remain unclear. We show that toxicity from islet amyloid polypeptide arises from transient ...</description>
      <dc:title>Aggregation kinetics define the temporal window of IAPP proteotoxicity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615786123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Annette PlesnerPing CaoDaniel P. RaleighAndisheh AbediniaDepartment of Clinical Immunology, University Hospital–Rigshospitalet, Copenhagen 2200, Denmarkbhttps://ror.org/05qghxh33Department of Chemistry, Stony Brook University, Stony Brook, NY 11794-3400chttps://ror.org/05qghxh33Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615786123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615786123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535979123?af=R">
      <title>AI-driven PROTAC design overcomes oncogenic resilience by eliminating the CLIP1–LTK fusion protein</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535979123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe CLIP1–Leukocyte tyrosine kinase (LTK) fusion oncoprotein drives tumorigenesis through both its kinase activity and its CLIP1-mediated scaffolding function, which facilitates pathogenic multimerization. This dual mechanism limits the ...</description>
      <dc:title>AI-driven PROTAC design overcomes oncogenic resilience by eliminating the CLIP1–LTK fusion protein</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535979123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Shicheng ChenHaiting DuanSheng ZhongJingxuan GeHuifeng ZhaoYuanyi YeHuiyong SunDan LiYu KangXiaowu DongJinxin CheTingjun HouPeichen Panahttps://ror.org/00a2xv884College of Pharmaceutical Sciences, Zhejiang University, Hangzhou, Zhejiang 310058, Chinabhttps://ror.org/0400g8r85Department of Neurosurgery, State Key Laboratory of Oncology in South China, Guangdong Provincial Clinical Research Center for Cancer, Sun Yat-sen University Cancer Center, Guangzhou, Guangdong 510000, Chinachttps://ror.org/01sfm2718Department of Medicinal Chemistry, China Pharmaceutical University, Nanjing, Jiangsu 210009, Chinadhttps://ror.org/00a2xv884Zhejiang Key Laboratory of Intelligent Drug Discovery and Development, Jinhua Institute of Zhejiang University, Jinhua, Zhejiang 321299, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535979123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535979123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608715123?af=R">
      <title>Host inflammation–derived citrate enhances Salmonella Typhimurium pathogenesis by fueling growth and activating virulence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608715123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSalmonellaTyphimurium (STm) is a leading cause of foodborne gastroenteritis worldwide, contributing substantially to morbidity and mortality. Intestinal inflammation typically serves as a host defense mechanism against invading pathogens. ...</description>
      <dc:title>Host inflammation–derived citrate enhances Salmonella Typhimurium pathogenesis by fueling growth and activating virulence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608715123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Hongmin SunShuai MaChenbo KangMengjie ZhaoJingnan ChenHouliang GuoYiming WangLuoqing FengLingyan JiangBin Yangahttps://ror.org/01y1kjr75National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, Tianjin 300457, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608715123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608715123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526551123?af=R">
      <title>Polymerase ι promotes C&gt;T substitutions in smoking models and in the platinum chemotherapy–induced SBS31 mutation signature</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526551123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceDNA lesions arising from exposure to exogenous DNA damaging agents lead to genomic mutations, which can contribute to tumorigenesis in healthy cells or heterogeneity in tumors. Single base substitution (SBS) signatures describing such ...</description>
      <dc:title>Polymerase ι promotes C&gt;T substitutions in smoking models and in the platinum chemotherapy–induced SBS31 mutation signature</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526551123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Botond EngelBernadett SzikrisztZsolt GyüreJulian E. SaleDávid SzütsEszter Némethahttps://ror.org/03zwxja46Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest 1117, Hungarybhttps://ror.org/01g9ty582Molecular Medicine Division, Doctoral College of Semmelweis University, Semmelweis University, Budapest 1085, Hungarychttps://ror.org/03x94j517Division of Protein and Nucleic Acid Chemistry, Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526551123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526551123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620143123?af=R">
      <title>A bacterial fatty acid enzyme hijacks nucleic acid–sensing Toll-like receptor signaling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620143123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThis study reveals an unexpected immune defense mechanism that protects cells fromStaphylococcus aureus, a major cause of difficult-to-treat infections. We show that a pathway long believed to function only in antiviral immunity can rapidly ...</description>
      <dc:title>A bacterial fatty acid enzyme hijacks nucleic acid–sensing Toll-like receptor signaling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620143123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>William A. LathramPriscilla C. LagesChristopher D. Radkaahttps://ror.org/02k3smh20Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY 40536</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620143123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620143123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602655123?af=R">
      <title>Oxytocin increases trust in men low in dispositional trust</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602655123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceFor two decades, claims that oxytocin (OT) increases trust have been clouded by underpowered studies and inconsistent results. In what is the highest-powered trust experiment to date (95% power to detect a positive effect), we provide robust ...</description>
      <dc:title>Oxytocin increases trust in men low in dispositional trust</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602655123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Bodo VogtPaul BengartCarolyn DeclerckErnst Fehrahttps://ror.org/00ggpsq73Chair in Empirical Economics and Health Economics, Faculty of Economics and Management, Otto von Guericke University Magdeburg, Magdeburg 39106, Germanybhttps://ror.org/00ggpsq73Institute of Social Medicine and Health Systems Research, Otto von Guericke University Magdeburg, Magdeburg 39106, Germanychttps://ror.org/008x57b05Faculty of Business and Economics, University of Antwerp, Antwerp 2000, Belgiumdhttps://ror.org/02crff812Zurich Center for Neuroeconomics, Department of Economics, University of Zurich CH-8001, Zurich, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602655123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602655123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610882123?af=R">
      <title>Multifunctional miniature robots: Harnessing the photothermal effect of magnetic microparticles for light and magnetic control</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610882123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceNavigating complex physiological solid–liquid interfaces is a major challenge for miniature robots. Here, we propose a miniature robot driven by synergistic light and magnetic fields enabled by photothermal effects of the embedded magnetic ...</description>
      <dc:title>Multifunctional miniature robots: Harnessing the photothermal effect of magnetic microparticles for light and magnetic control</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610882123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Xiang XiaoXianbing ZengJing ZhouTianyi PangTianfeng ZhouJuncai SongLei LiBaiqian XuYujing LiGuanghao WuYubing Guoahttps://ror.org/01skt4w74School of Medical Science and Engineering, Beijing Institute of Technology, Beijing 100081, Chinabhttps://ror.org/01skt4w74State Key Laboratory of Chips and Systems for Advanced Light Field Display, School of Mechanical Engineering, Beijing Institute of Technology, Beijing 100081, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610882123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610882123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605755123?af=R">
      <title>Juvenile hormone receptor relies on conserved domain interfaces for dimerization-dependent activity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605755123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceJuvenile hormone (JH) sustains development and reproduction of insects, the largest of animal taxa that bears tremendous impact on ecosystems, agriculture, and transmission of infectious diseases. JH action depends on receptor proteins that, ...</description>
      <dc:title>Juvenile hormone receptor relies on conserved domain interfaces for dimerization-dependent activity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605755123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Lenka BittovaSarka TumovaMykola YatsenkoRaveendra Babu MokhamatamRoman TumaMarek JindraaDepartment of Molecular Physiology and Genetics, Institute of Entomology, Biology Center of the Czech Academy of Sciences, Ceske Budejovice 37005, Czech RepublicbDepartment of Chemistry, Faculty of Science, University of South Bohemia, Ceske Budejovice 37005, Czech RepubliccPreagon Biotech Limited, Zahornice 28903, Czech Republic</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605755123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605755123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2514189123?af=R">
      <title>Implicit biases change more slowly in larger cities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2514189123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceImplicit biases remain a contributor to discrimination despite widespread endorsement of equality. Cities are associated with lower implicit bias levels, but how do these biases change over time? Here, I develop a mathematical theory for how ...</description>
      <dc:title>Implicit biases change more slowly in larger cities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2514189123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-06T07:00:00Z</dc:date>
      <dc:creator>Andrew J. Stierahttps://ror.org/01arysc35The Santa Fe Institute, Santa Fe, NM 87501</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2514189123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2514189123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530214123?af=R">
      <title>Proof of the density threshold conjecture for pinwheel scheduling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530214123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceThe Pinwheel Scheduling Problem asks whether a set of periodic tasks, each with a maximum allowed gap between executions, can be arranged into a repeating schedule. A central open question, posed over three decades ago, asked: if the overall ...</description>
      <dc:title>Proof of the density threshold conjecture for pinwheel scheduling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530214123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Akitoshi Kawamuraahttps://ror.org/02kpeqv85Research Institute for Mathematical Sciences, Kyoto University, Kyoto 606-8502, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530214123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530214123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528246123?af=R">
      <title>Protecting episodic memory after sleep loss: Similar benefits of exercise and naps via distinct neural contributions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528246123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceSleep is essential for learning and remembering but one-third of the population worldwide sleeps insufficiently. Sleep loss is a public health problem that costs nations billions of dollars annually. Following sleep hygiene strategies may not ...</description>
      <dc:title>Protecting episodic memory after sleep loss: Similar benefits of exercise and naps via distinct neural contributions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528246123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Madhura S. LotlikarBeatrice AyotteAmy ChoiFreddie SeoEdwin M. RobertsonFabien Dal MasoMarc Roigahttps://ror.org/01pxwe438Department of Neurology and Neurosurgery, McGill University, Montreal, QC H3A 0G4, Canadabhttps://ror.org/047eze012Memory and Motor Rehabilitation Laboratory, Jewish Rehabilitation Hospital, Laval, QC H7V 1R2, CanadacFeil and Oberfeld Research Centre, Jewish Rehabilitation Hospital, Center for Interdisciplinary Research in Rehabilitation, Laval, QC H7V 1R2, Canadadhttps://ror.org/00vtgdb53Department of Brain and Cognitive Sciences, Institute of Neuroscience and Psychology, University of Glasgow, Glasgow G12 8QQ, United Kingdomehttps://ror.org/016bgq349Center for Information and Neural Networks, National Institute of Information and Communications Technology, Suita City, Osaka 565-0871, Japanfhttps://ror.org/0161xgx34École de Kinésiologie et des Sciences de l’Activité Physique, Faculté de Médecine, Université de Montréal, Montreal, QC H7N 0A5, CanadagCentre Interdisciplinaire de Recherche sur le Cerveau et l’Apprentissage, Montréal, QC H3T 1P1, CanadahDepartment of School of Physical and Occupational Therapy, Faculty of Medicine and Health Sciences, McGill University, Montreal, QC H3A 0G4, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528246123</prism:doi>
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      <title>T cell–intrinsic AIM2 exacerbates lung inflammation in OVA-LPS- and HDM-induced asthma models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520215123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceAllergic asthma is a heterogeneous disease characterized by airway inflammation and hyperresponsiveness. AIM2 (Absent in Melanoma 2), a DNA-activated inflammasome, has emerged as a critical regulator of inflammatory diseases. In humans, AIM2 ...</description>
      <dc:title>T cell–intrinsic AIM2 exacerbates lung inflammation in OVA-LPS- and HDM-induced asthma models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520215123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Wei-Chun ChouMartin HsuJohn A. WrobelElizabeth Holley-GuthrieCorey M. JaniaKaixin LiangShuangshuang YangRani S. SellerXiaoqing HuStephen A. SchworerAlessandra Livraghi-ButricoStephen L. TilleyYisong Y. WanJenny P.-Y. Tingahttps://ror.org/043ehm030Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599bDepartment of Genetics, University of North Carolina, Chapel Hill, NC 27599cDepartment of Microbiology-Immunology, University of North Carolina, Chapel Hill, NC 27599dDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599eDivision of Pulmonary and Critical Care Medicine, Department of Medicine, University of North Carolina, Chapel Hill, NC 27599fOral and Craniofacial Biomedicine Program, School of Dentistry, University of North Carolina, Chapel Hill, NC 27599gDepartment of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, NC 27599hhttps://ror.org/016978714Marsico Lung Institute and Cystic Fibrosis Research Center, University of North Carolina, Chapel Hill, NC 27599iDivision of Rheumatology, Allergy and Immunology, University of North Carolina, Chapel Hill, NC 27599</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520215123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532230123?af=R">
      <title>Eye movements reveal a dissociation between prediction and structural processing difficulty in language comprehension</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532230123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceWhen we read sentences, our eyes move back and forth in complex ways. One factor that explains this pattern is prediction: Our experience allows us to anticipate upcoming words, making it is easier to recognize predictable ones. What are the ...</description>
      <dc:title>Eye movements reveal a dissociation between prediction and structural processing difficulty in language comprehension</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532230123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>William TimkeyKuan-Jung HuangByung-Doh OhGrusha PrasadSuhas ArehalliTal LinzenBrian Dillonahttps://ror.org/0190ak572Department of Linguistics, New York University, New York, NY 10003bhttps://ror.org/042nb2s44Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/02e7b5302Division of Linguistics and Multilingual Studies, Nanyang Technological University, Singapore 639818, Singaporedhttps://ror.org/05d23ve83Department of Computer Science, Colgate University, Hamilton, NY 13346ehttps://ror.org/04fceqm38Department of Computer Science, Macalester College, St. Paul, MN 55105fhttps://ror.org/0190ak572Center for Data Science, New York University, New York, NY 10012ghttps://ror.org/0072zz521Department of Linguistics, University of Massachusetts Amherst, Amherst, MA 01003</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532230123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536213123?af=R">
      <title>Large-FOV, dual-region, two-photon fluorescence lifetime imaging microscopy (LD-2P-FLIM) for multiparameter and quantitative brain function imaging</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536213123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceTwo-photon microscopy (TPM) is ideally suited for in vivo brain function imaging because of its high resolution and deep tissue penetration. However, conventional TPM is limited by a restricted field-of-view (FOV), an inherent trade-off ...</description>
      <dc:title>Large-FOV, dual-region, two-photon fluorescence lifetime imaging microscopy (LD-2P-FLIM) for multiparameter and quantitative brain function imaging</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536213123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Shiwei YeYufeng GaoMengying DengYaozhang ShengXingyun XuXueming CaoLianjian LiuNa XiaoJunjie ZouMinghan XieLong ZengHuachuang XiangJia YuTing WuYuezhi HeJing YaoHui LiYanwu GuoJun ChuHairong ZhengChengbo LiuWei Zhengahttps://ror.org/04gh4er46Research Center for Biomedical Optics and Molecular Imaging, Shenzhen Key Laboratory for Molecular Imaging, Guangdong Provincial Key Laboratory of Biomedical Optical Imaging Technology, Key Laboratory of Biomedical Imaging Science and System, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, Chinabhttps://ror.org/034t30j35Research Center for Primate Neuromodulation and Neuroimaging, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, ChinacThe National Key Clinic Specialty, The Engineering Technology Research Center of Education Ministry of China, Guangdong Provincial Key Laboratory on Brain Function Repair and Regeneration, Department of Neurosurgery, Zhujiang Hospital, Southern Medical University, Guangzhou 510282, Chinadhttps://ror.org/034t30j35Lauterbur Research Center for Biomedical Imaging, Key Laboratory of Biomedical Imaging Science and System, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536213123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536213123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601801123?af=R">
      <title>Experience-dependent modulation of extracellular matrix integrity supports perceptual skill learning and memory</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601801123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceLearning sharpens our sensory abilities, allowing us to see fine details, distinguish similar sounds, and detect subtle differences in taste and smell, but typically requires extensive practice. To improve learning rates and outcomes, we need ...</description>
      <dc:title>Experience-dependent modulation of extracellular matrix integrity supports perceptual skill learning and memory</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601801123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
      <dc:creator>Jéssica WinneRebecca SchraderMakayla AnfusonMelissa L. Carasahttps://ror.org/047s2c258Department of Biology, University of Maryland, College Park, MD 20742bhttps://ror.org/047s2c258Brain and Behavior Institute, University of Maryland, College Park, MD 20742</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601801123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601801123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611057123?af=R">
      <title>A semantic-based community model for high-fidelity tuning of olfactory mixture distances</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611057123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;SignificanceOlfaction lacks a general quantitative framework comparable to those long established for vision and hearing, especially for complex mixtures that dominate real-world smells. Here, a community effort shows that perceptual distances between ...</description>
      <dc:title>A semantic-based community model for high-fidelity tuning of olfactory mixture distances</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611057123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Vahid SatarifardLaura SissonYikun HanPedro IlídioMatej HladišMaxence LalisXuebo SongTiffany YangWenjie YinAharon RaviaCiCi Xingyu ZhengGaia AndreolettiJake AlbrechtRobert PellegrinoZehua WangStephen YangRobbe D’hondtAchilleas GhinisJasper de BoerFelipe Kenji NakanoAlireza GharahighehiJose M. G. VilarLeonor SaizDREAM Olfactory Mixtures Prediction Consortium Benjamin Sanchez-LengelingAndreas KellerLeslie B. VosshallSébastien FiorucciAmbuj TewariJérémie TopinCeline VensMårten BjörkmanDanica KragicNoam SobelNicholas A. ChristakisJoel D. MainlandPablo Meyerahttps://ror.org/03v76x132Human Nature Lab, Yale University, New Haven, CT 06511bhttps://ror.org/05qwgg493Department of Computer Science, Boston University, Boston, MA 02215chttps://ror.org/00jmfr291Department of Statistics, University of Michigan, Ann Arbor, MI 48109dhttps://ror.org/05f950310Department of Public Health and Primary Care, Katholieke Universiteit Leuven, Kortrijk 8500, Belgiumehttps://ror.org/05f950310Itec, imec Research Group at Katholieke Universiteit Leuven, Kortrijk 8500, Belgiumfhttps://ror.org/019tgvf94Institut de Chimie de Nice, Université Côte d’Azur, CNRS, Nice 06108, Franceghttps://ror.org/052gg0110Department of Computer Science, University of Oxford, Oxford OX1 3QD, United Kingdomhhttps://ror.org/01mdfdm06Monell Chemical Senses Center, Philadelphia, PA 19104ihttps://ror.org/026vcq606School of Electrical Engineering and Computer Science, Kungliga Tekniska högskolan Royal Institute of Technology, Stockholm 10044, Swedenjhttps://ror.org/05bnh6r87Runway Startup, Cornell Tech, Cornell University, New York, NY 10044khttps://ror.org/02qz8b764Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724lhttps://ror.org/049ncjx51Sage Bionetworks, Seattle, WA 98109mhttps://ror.org/01f5ytq51Department of Animal Science, Texas A&amp;M University, College Station, TX 77843nComputer Science Department, State University of Londrina, Paraná, 86057-970, Brazilohttps://ror.org/02gfc7t72Biofisika Institutua, Consejo Superior de Investigaciones Científicas, Euskal Herriko Unibertsitatea, University of the Basque Country, Bilbao 48080, Spainphttps://ror.org/01cc3fy72IKERBASQUE, Basque Foundation for Science, Bilbao 48009, Spainqhttps://ror.org/05rrcem69Department of Biomedical Engineering, University of California, Davis, CA 95616rhttps://ror.org/03dbr7087Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, ON M5S3E5, Canadashttps://ror.org/0420db125Laboratory of Neurogenetics and Behavior, The Rockefeller University, New York, NY 10065thttps://ror.org/0420db125HHMI, The Rockefeller University, New York, NY 10065uhttps://ror.org/0316ej306Department of Neurobiology, Weizmann Institute of Science, Rehovot, 7610001, Israelvhttps://ror.org/00b30xv10Department of Neuroscience, University of Pennsylvania, Philadelphia, PA 19104wHealth Care and Life Sciences, International Business Machines Research, Yorktown Heights, NY 10598Ruhallah AmandiNicola AmorosoLoredana BellantuonoMichele DibattistaAlfonso MonacoEster PantaleoSabina TangaroGary TomElla RajaonsonCher-Tian SerSean ParkStanley LoBrian K LeeGautam AhujaSiddhant PoudyalBableen KaurDouluri Pushkala DeviRintu KutumGrant McConachieSoroush ArabshahiSaeed KarimimehrJeremy KotlyarFaraz YazdaniRéka BöröczBence SzalaiAdomas MalaiskaVictor TarcaConnor FongHugo TalibartDimitri GilisChih-Han HuangTsai-Min ChenHsuan-Kai WangJhih-Yu ChenEdward S.C. ShihChih-Hsun WuWei-Quan FangSz-Hau ChenKuei-Lin HuangSrijeet BhattacharjeeMalay BhattacharyyaSergey ShuvaevCyrille MascartKhue TranAlexei Koulakov</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611057123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614173123?af=R">
      <title>A reference protein atlas of the adult mouse brain vasculature</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614173123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;Current methods for assessing low-abundance proteins in individual cells are limited. As a result, cell functions are often inferred from single-cell RNA sequencing (scRNA-seq) data, which can be misleading due to the poor cross-gene correlation (...</description>
      <dc:title>A reference protein atlas of the adult mouse brain vasculature</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614173123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Liqun HeHenrik J. JohanssonElisa Vazquez-LiebanasJianping LiuLars MuhlKhayrun NaharMichael VanlandewijckJanne LehtiöChrister BetsholtzMaarja Andaloussi Mäeahttps://ror.org/048a87296Department of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, Uppsala SE-751 85, Swedenbhttps://ror.org/04ev03g22Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, Solna SE-171 21, Swedenchttps://ror.org/056d84691Department of Medicine-Huddinge, Karolinska Institutet, Huddinge SE-141 57, Swedendhttps://ror.org/042v6xz23Jiangxi Provincial Key Laboratory of Digestive Diseases, Department of Gastroenterology, Digestive Disease Hospital, The First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang, Jiangxi 330006, Chinaehttps://ror.org/03zga2b32Centre for Cancer Biomarkers, Department of Clinical Medicine, University of Bergen, Bergen 5020, Norway</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614173123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536909123?af=R">
      <title>DENV-4 infection suppresses transcription of DNA repair genes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536909123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;The molecular mechanisms behind Dengue virus-dependent host pathogenesis, especially genome instability, remain largely unclear. This RNA virus causes a debilitating disease during active infection and presents future risks of postdengue syndromes, ...</description>
      <dc:title>DENV-4 infection suppresses transcription of DNA repair genes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536909123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-04T07:00:00Z</dc:date>
      <dc:creator>Erica N. LamkinJessica ReichJosh A. VictorMadison GuyetteNaveen KothandaramanVihit GuptaAlfred T. HardingTristan X. JordanLee GehrkePei ZhouBenjamin tenOeverNimrat Chatterjeeahttps://ror.org/0155zta11Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405bhttps://ror.org/042nb2s44Institute for Medical Engineering and Science, Massachusetts Institute of Technology, Cambridge, MA 02138chttps://ror.org/00cvxb145Department of Microbiology, University of Washington, Seattle, WA 98109dhttps://ror.org/00cvxb145Department of Laboratory Medicine and Pathology, University of Washington, Seattle, WA 98109eDepartment of Microbiology, Harvard Medical School, Boston, MA 021383fhttps://ror.org/00py81415Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710ghttps://ror.org/0190ak572Department of Microbiology, New York University Grossman School of Medicine, New York City, NY 10016hhttps://ror.org/0155zta11University of Vermont Cancer Center, University of Vermont, Burlington, VT 05405</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536909123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536909123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619789123?af=R">
      <title>An unseen partner steers alkaloid flux toward vinblastine in Catharanthus roseus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619789123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>An unseen partner steers alkaloid flux toward vinblastine in Catharanthus roseus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619789123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Adam Jozwiakahttps://ror.org/03nawhv43Department of Botany and Plant Sciences, University of California Riverside, Riverside, CA 92521bhttps://ror.org/03nawhv43Institute for Integrative Genome Biology, University of California Riverside, Riverside, CA 92521</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619789123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619791123?af=R">
      <title>Nuclear garbage disposal: An unexpected role for amyloid precursor protein in Alzheimer’s disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619791123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Nuclear garbage disposal: An unexpected role for amyloid precursor protein in Alzheimer’s disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619791123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Mohankumar ThangavelArjun V. Masurkarahttps://ror.org/0190ak572Center for Cognitive Neurology, Department of Neurology, New York University Grossman School of Medicine, New York, NY 10016bhttps://ror.org/0190ak572Department of Neuroscience, New York University Grossman 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>32</prism:number>
      <prism:coverDate>2026-08-11T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-08-11T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619791123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619791123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619024123?af=R">
      <title>How small can a cell be?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619024123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>How small can a cell be?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619024123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <dc:creator>Nicolas Klugerahttps://ror.org/01y7b2q33Aava Medical Center, Kerava 04200, Finlandbhttps://ror.org/02hvt5f17Department of Dermatology, Tampere University Hospital, Tampere 33520, Finlandchttps://ror.org/03fdnmv92Tattoo Consultation, Department of Dermatology, Hopital Bichat-Claude Bernard, Paris 75018, France</dc:creator>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Antibiotic tolerance coupled with limited benefit from drainage: Clinical challenges in Klebsiella pneumoniae liver abscess</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Zibo GongYawen GuoXiwen LiuZhe WangGuofei LiZhihui ChangaDepartment of Radiology, Shengjing Hospital of China Medical University, Shenyang 110004, ChinabDepartment of Pathology, Shengjing Hospital of China Medical University, Shenyang 110004, ChinacDepartment of Pharmacy, Shengjing Hospital of China Medical University, Shenyang 110004, China</dc:creator>
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      <dc:title>Correction for Gardner et al., Competing models of hominin body size evolution</dc:title>
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      <dc:title>Correction for You et al., p53-dependent inhibition of FKHRL1 in response to DNA damage through protein kinase SGK1</dc:title>
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      <dc:date>2026-08-03T07:00:00Z</dc:date>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Mileo et al., Multistep electron tunneling through tryptophans in the KatG bifunctional peroxidase monitored by a nonperturbing spin probe</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Pranger et al., Five decades of seasonal phytoplankton succession examined with principal traits—An approach linking composition to function</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-07T07:00:00Z</dc:date>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Correction to Supporting Information for Huang et al., Stochastic game dynamics under demographic fluctuations</dc:title>
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      <dc:title>Correction for Singh et al., Controlled generation of 3D vortices in driven atomic Josephson junctions</dc:title>
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      <dc:title>Reply to Kluger: Tattoo-induced inflammation and immune responses: Mechanistic insights and considerations</dc:title>
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      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615420123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 32, August 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Gong et al.: Antibiotic tolerance coupled with limited benefit from drainage: Clinical challenges in Klebsiella pneumoniae liver abscess</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-08-03T07:00:00Z</dc:date>
      <dc:creator>Sarah E. RoweaDepartment of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599</dc:creator>
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