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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;Segregation is a multidimensional phenomenon deeply entwined with historical, social, and ecological contexts. The ecology of segregation framework explores how social norms institutionalize racism, classism, and power dynamics to drive inequitable ...</description>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Kyle J. SilvaBrandon J. Schmeichelahttps://ror.org/01f5ytq51Department of Psychological and Brain Sciences, Texas A&amp;M University, College Station, TX 77845-4235</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610948123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610948123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617210123?af=R">
      <title>Earthquake-triggered cascading hazards under Arctic amplification</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617210123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceArctic warming is rapidly changing the permafrost and glacierized places, yet its influence on earthquake-related hazards remains poorly understood. We investigate a major 2025 Arctic earthquake that triggered a large rock avalanche and ...</description>
      <dc:title>Earthquake-triggered cascading hazards under Arctic amplification</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617210123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Guilherme W. S. de MeloReginald L. HermannsJacob M. BendleIngo GrevemeyerSylvain FiolleauSimone CescaAderson F. do NascimentoLars OttemöllerGökhan AslanQuentin BrissaudVolker OyeHeidrun Koppahttps://ror.org/02h2x0161Division of Dynamics of the Seafloor-Marine Geodynamics, Division of Dynamics of the Seafloor-Marine Geodynamics, GEOMAR Helmholtz Centre for Ocean Research Kiel, Kiel 24148, Germanybhttps://ror.org/036dwbr90Geological Survey of Norway, Trondheim 7040, NorwaycHelmholtz Centre for Geosciences Potsdam, Potsdam 14467, Germanydhttps://ror.org/04wn09761Departamento de Geofisica, Federal University of Rio Grande do Norte, Natal 59078-900, Brazilehttps://ror.org/03zga2b32Department of Earth Science, University of Bergen, Bergen 5020, Norwayfhttps://ror.org/02vw8cm83Norwegian Seismic Array, Kjeller 2027, Norwayghttps://ror.org/04v76ef78Faculty of Mathematics and Natural Sciences, Institute of Geoscience, Kiel University, Kiel 24118, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617210123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617210123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611733123?af=R">
      <title>At least a fivefold gap in effective global marine protection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611733123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceGlobal efforts to protect 30% of the ocean may substantially overestimate conservation success if outcomes are assumed rather than measured. Current assessments emphasize protected area coverage and stated protection levels instead of whether ...</description>
      <dc:title>At least a fivefold gap in effective global marine protection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611733123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Ella ClausiusGraham J. EdgarCamille MellinGenevieve A. C. PhillipsAmanda E. BatesLisandro Benedetti-CecchiChristopher J. BrownJoshua E. CinnerMark John CostelloJosé A. Sanabria-FernándezDavid A. GillCyril HautecoeurFreddie J. HeatherNatali LazzariJonathan S. LefcheckEva MaireDavid MouillotJasmin M. SchusterJoanna K. SchmidRick D. Stuart-Smithahttps://ror.org/01nfmeh72Institute for Marine and Antarctic Studies, University of Tasmania, Hobart, TAS 7004, Australiabhttps://ror.org/028g18b61The Environment Institute and School of Biological Sciences, Adelaide University, Adelaide, SA 5000, Australiachttps://ror.org/01nfmeh72Centre for Marine Socioecology, University of Tasmania, Hobart, TAS 7004, Australiadhttps://ror.org/04s5mat29Department of Biology, University of Victoria, Victoria, BC V8P 5C2, Canadaehttps://ror.org/03ad39j10Department of Biology, University of Pisa, Pisa 56126, Italyfhttps://ror.org/00t74vp97Consorzio Nazionale Interuniversitario per le Scienze del Mare (Consorzio Nazionale Interuniversitario per le Scienze del Mare (CoNISMa, Rome 00196, Italyghttps://ror.org/0384j8v12Thriving Oceans Research Hub, School of Geosciences, University of Sydney, Camperdown, NSW 2050, AustraliahFaculty of Biosciences and Aquaculture, Nord Universitet, Bodo 8049, Norwayihttps://ror.org/006gw6z14Department of Ecology and Evolution, Doñana Biological Station, Sevilla 41092, Spainjhttps://ror.org/04gsp2c11College of Science and Engineering, James Cook University, Townsville, QLD 4811, Australiakhttps://ror.org/00py81415Duke Marine Laboratory, Nicholas School of the Environment, Duke University, Beaufort, NC 28516lMARine Biodiversity, Exploitation and Conservation (MARBEC), Université de Montpellier, CNRS, Ifremer, Institut de recherche pour le développement, Montpellier 34090, Francemhttps://ror.org/030eybx10EqualSea Lab-Cross-disciplinary Research Center in Environmental Technologies (CRETUS), University of Santiago de Compostela, A Coruña 15782, SpainnBest Environmental Applied Research, Dunkirk, MD 20754ohttps://ror.org/04f2nsd36Lancaster Environment Centre, Lancaster University, Lancaster LA1 4YQ, United Kingdomphttps://ror.org/039cthy03Kelp Rescue Initiative, Bamfield Marine Sciences Center, Bamfield, BC V0R 1B0, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611733123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611733123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534165123?af=R">
      <title>Naegleria amoebae seek confinement and crawl persistently through narrow spaces</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534165123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe “brain-eating amoeba”Naegleria fowlericauses a devastating brain infection with a ~95% fatality rate, yet how these normally harmless pond-dwellers invade the human brain remains mysterious. Using the model speciesN. gruberi, we show ...</description>
      <dc:title>Naegleria amoebae seek confinement and crawl persistently through narrow spaces</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534165123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-10T07:00:00Z</dc:date>
      <dc:creator>Katrina B. VelleMeera RamaswamyBabak Vajdi HokmabadTania Martín-PérezTeodoro Tapia CarrascoWilliam S. CallahanHarrison S. KimEmily M. LarkinAbdurrahman H. ElZafaranySamantha M. JacquesSujit S. DattaMarc EdwardsLillian K. Fritz-Laylinahttps://ror.org/00fzmm222Department of Biology, University of Massachusetts Dartmouth, North Dartmouth, MA 02747bhttps://ror.org/017zqws13Department of Mechanical Engineering, University of Minnesota, Minneapolis, MN 55455chttps://ror.org/00hx57361Princeton Center for Complex Materials, Princeton University, Princeton, NJ 08544dhttps://ror.org/00hx57361Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544ehttps://ror.org/04pmn0e78Faculty of Pharmacy, Department of Biomedicine and Biotechnology, University of Alcalá, Alcalá de Henares 28805, Spainfhttps://ror.org/028vqfs63Department of Biology, Amherst College, Amherst, MA 01002ghttps://ror.org/0072zz521HHMI, University of Massachusetts Amherst, Amherst, MA 01003hhttps://ror.org/0072zz521Department of Biology, University of Massachusetts Amherst, Amherst, MA 01003ihttps://ror.org/05dxps055Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534165123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534165123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526924123?af=R">
      <title>Corporate ESG assessments fail to capture actual deforestation exposure</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526924123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceDeforestation is a cross-cutting issue that can impact all three pillars of Environmental, Social, and Governance (ESG). To serve as effective tools for investors and financial institutions to mitigate deforestation, ESG assessments should ...</description>
      <dc:title>Corporate ESG assessments fail to capture actual deforestation exposure</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526924123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Yingtong ZhuJohan SulaemanLuis Roman Carrascoahttps://ror.org/01tgyzw49Department of Biological Sciences, National University of Singapore, Singapore 117543, Republic of Singaporebhttps://ror.org/01tgyzw49Sustainable and Green Finance Institute, National University of Singapore, Singapore 117602, Republic of Singaporechttps://ror.org/01tgyzw49Department of Finance, Business School, National University of Singapore, Singapore 119245, Republic of Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526924123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526924123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600775123?af=R">
      <title>Spatially refined satellite gravimetry captures human signatures in global terrestrial water storage trends</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600775123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceIt is well known that human activities directly impact the water cycle and the distribution of water resources, but quantifying such effects from space is challenging. By directly estimating mass change rates from raw satellite range ...</description>
      <dc:title>Spatially refined satellite gravimetry captures human signatures in global terrestrial water storage trends</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600775123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Mary Michael O’NeillMatthew RodellBryant D. Loomisahttps://ror.org/027ka1x80Hydrological Sciences Laboratory, Earth Sciences Division, National Aeronautics and Space Administration, Goddard Space Flight Center, Greenbelt, MD 20771bhttps://ror.org/047s2c258Earth System Science Interdisciplinary Center, University of Maryland, College Park, MD 20742chttps://ror.org/027ka1x80Earth Sciences Division, National Aeronautics and Space Administration, Goddard Space Flight Center, Greenbelt, MD 20771dhttps://ror.org/027ka1x80Geodesy and Geophysics Laboratory, Earth Sciences Division, National Aeronautics and Space Administration, Goddard Space Flight Center, Greenbelt, MD 20771</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600775123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600775123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532733123?af=R">
      <title>Patagonian Ice Sheet discharge enhanced by AMOC slowdown through thermal bipolar seesaw</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532733123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe Atlantic Meridional Overturning Circulation (AMOC), a major regulator of global climate, is weakening under ongoing warming, yet its far-field impacts remain uncertain. Past AMOC slowdown events during the last glacial period provide ...</description>
      <dc:title>Patagonian Ice Sheet discharge enhanced by AMOC slowdown through thermal bipolar seesaw</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532733123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Takuto KasuyaYuta KuniyoshiKana NagashimaHitoshi HasegawaAyako Abe-OuchiJulia R. HagemannHelge W. ArzCarina B. LangeFrank LamyShinya IwasakiWing-Le ChanNaomi HaradaMasafumi MurayamaFuyuki SaitoYusuke Okazakiahttps://ror.org/00p4k0j84Department of Earth and Planetary Sciences, Graduate School of Science, Kyushu University, Fukuoka 819-0395, Japanbhttps://ror.org/059qg2m13Research Institute for Global Change, Earth Surface System Research Center, Japan Agency for Marine-Earth Science and Technology, Yokosuka 237-0061, Kanagawa, Japanchttps://ror.org/057zh3y96Atmosphere and Ocean Research Institute, The University of Tokyo, Kashiwa 277-8564, Chiba, Japandhttps://ror.org/01xxp6985Department of Global Environment and Disaster Prevention, Faculty of Science and Technology, Kochi University, Kochi 780-8520, Japanehttps://ror.org/01xxp6985Marine Core Research Institute, Kochi University, Nankoku 783-8502, Kochi, Japanfhttps://ror.org/05vt9qd57Department of Marine and Coastal Science, Rutgers University, New Brunswick, NJ 08901-8520gDivision of Geoscience, Marine Geology Section, Alfred Wegener Institute Helmholtz Centre for Polar and Marine Research, Bremerhaven 27570, Germanyhhttps://ror.org/03xh9nq73Department of Marine Geosciences, Paleoceanography and Sedimentology Group, Leibniz Institute for Baltic Sea Research Warnemünde, Rostock 18119, Germanyihttps://ror.org/0460jpj73Departamento de Oceanografía &amp; Centro de Investigación Oceanográfica en el Pacífico Suroriental (COPAS-Coastal), Universidad de Concepción, Concepción 4030000, Chilejhttps://ror.org/029ycp228Centro de Investigación Dinámica de Ecosistemas Marinos de Altas Latitudes, Universidad Austral de Chile, Valdivia 5110566, Chilekhttps://ror.org/0168r3w48Geosciences Research Division, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92037lhttps://ror.org/02e16g702Division of Earth System Science, Faculty of Environmental Earth Science, Hokkaido University, Sapporo 060-0810, Hokkaido, Japanmhttps://ror.org/01xxp6985Faculty of Agriculture and Marine Science, Kochi University, Nankoku 783-8502, Kochi, Japannhttps://ror.org/02c3vg160Department of Dinosaur Paleontology and Geology, Faculty of Dinosaur Paleontology, Fukui Prefectural University, Katsuyama 911-0025, Fukui, Japanohttps://ror.org/059qg2m13Research Institute for Global Change, Research Center for Environmental Modeling and Application, Japan Agency for Marine-Earth Science and Technology, Yokohama 236-0001, Kanagawa, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532733123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532733123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622980123?af=R">
      <title>Maintaining transcriptome solubility constrains mRNA sequence composition</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622980123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceRNA base-pairing enables folding and regulation, but it also creates pervasive opportunities for unintended RNA–RNA interactions in the crowded intracellular environment. We identify this as a transcriptome-scale physical problem. Simulations ...</description>
      <dc:title>Maintaining transcriptome solubility constrains mRNA sequence composition</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622980123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Marco TodiscoChristalyn AuslerAnkur Jainahttps://ror.org/04vqm6w82Whitehead Institute for Biomedical Research, Cambridge, MA 02142bhttps://ror.org/042nb2s44Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622980123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622980123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608431123?af=R">
      <title>Bioinspired fabric architecture harnessing anisotropy for omnidirectional mechanical protection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608431123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificancePowder bed fusion-printed fiber-reinforced composites exhibit high specific strength and energy absorption, making them attractive for mechanical protection applications. However, fiber alignment induced by powder recoating imposes pronounced ...</description>
      <dc:title>Bioinspired fabric architecture harnessing anisotropy for omnidirectional mechanical protection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608431123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Yuanyuan TianHanzhi ChiWei Shian TeyZuoqi ZhangJingbo FanZheng Han LimAdrian OngJerry QiKun Zhouahttps://ror.org/02e7b5302Singapore Centre for 3D Printing, School of Mechanical and Aerospace Engineering, Nanyang Technological University, Singapore 639798, Singaporebhttps://ror.org/01zkghx44The George W. Woodruff School of Mechanical 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608431123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608431123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2422760122?af=R">
      <title>Beyond redlining: Gentrification, displacement, disadvantages, and exclusivity predict urban environmental and health inequities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2422760122?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceHistorical injustices and racial devaluation have concentrated inequities and privileges in certain urban neighborhoods. Yet, these neighborhoods are not static but dynamic and have changed over time. A nuanced understanding of the changes is ...</description>
      <dc:title>Beyond redlining: Gentrification, displacement, disadvantages, and exclusivity predict urban environmental and health inequities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2422760122</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Idowu AjibadeKevan B. MoffettJason MaxfieldKate GregoryAxcelle BellJackson VoelkelTodd RosenstielAaron R. Ramirezahttps://ror.org/03czfpz43Department of Environmental Sciences, Emory University, Atlanta, GA 30322bSchool of the Environment, Washington State University, Vancouver, WA 98686chttps://ror.org/00yn2fy02Department of Geography, Portland State University, Portland, OR 97201dhttps://ror.org/03qt6ba18Department of Biology, Georgia State University, Atlanta, GA 30302ehttps://ror.org/00a6ram87Department of Biology and Environmental Studies, Reed College, Portland, OR 97202</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2422760122</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2422760122?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2416889122?af=R">
      <title>Historic residential segregation impacts biodiversity data availability disparately across the tree of life</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2416889122?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceHistoric race-based zoning policies like redlining in the United States are associated with present day health, income, and environmental inequities. We quantify how redlining across 195 cities is related to key biodiversity metrics across all ...</description>
      <dc:title>Historic residential segregation impacts biodiversity data availability disparately across the tree of life</dc:title>
      <dc:identifier>doi:10.1073/pnas.2416889122</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Diego Ellis-SotoMelissa Chapmanahttps://ror.org/01an7q238Department of Environmental Science Policy and Management, University of California, Berkeley, CA 94720bhttps://ror.org/03v76x132Department of Ecology and Evolutionary Biology, Yale University, New Haven, CT 06511chttps://ror.org/05a28rw58Department of Environmental Systems Science, ETH Zurich, Zurich 8001, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2416889122</prism:doi>
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      <title>From past, persisting, and consolidating ecologies of segregation to ecologies of repair</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2422767122?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;Across the United States and Europe, urban and periurban spaces have historically been shaped by land dispossession and enclosure that systematically exclude marginalized, non-White communities from the benefits of society, including access to nature. ...</description>
      <dc:title>From past, persisting, and consolidating ecologies of segregation to ecologies of repair</dc:title>
      <dc:identifier>doi:10.1073/pnas.2422767122</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Isabelle AnguelovskiJames J. T. ConnollyEsteve CorberaDavid N. PellowFushcia-Ann HooverJacqueline L. ScottMarccus D. HendricksChristopher J. Schellahttps://ror.org/052g8jq94Institució Catalana de Recerca i Estudis Avançats, Universitat Autònoma de Barcelona, Barcelona 08010, Spainbhttps://ror.org/052g8jq94Institute of Environmental Science and Technology and Department of Geography, Universitat Autònoma de Barcelona, Barcelona 08193, Spainchttps://ror.org/03rmrcq20School of Regional and Community Planning, University of British Columbia, Vancouver, BC V6T 1Z2, CanadadEnvironmental Studies Program, University of Santa Barbara, Santa Barbara, CA 93106eDepartment of Earth, Environmental and Geographical Sciences, University of North Carolina, Charlotte, NC 27599fhttps://ror.org/03dbr7087Department of Social Justice Education, University of Toronto, Toronto, ON M5S 1V6, Canadaghttps://ror.org/047s2c258Stormwater Infrastructure Resilience and Justice Lab, School of Architecture, Planning, and Preservation, University of Maryland, College Park, MD 20742hhttps://ror.org/01an7q238Department of Environmental Policy, Science, and Management, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2422767122</prism:doi>
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      <title>Housing tenure, climate resilience, and ecological segregation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2422764123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThis study demonstrates how climate adaptation strategies, even when legally compliant and technically sound, can reproduce social inequality within welfare-state systems. In Copenhagen, city-wide mandates such as the separation of stormwater ...</description>
      <dc:title>Housing tenure, climate resilience, and ecological segregation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2422764123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Natalie M. GulsrudOriol Garcia-AntúnezAnton S. OlafssonMarina Bergen Jensenahttps://ror.org/035b05819Department of Geosciences and Natural Resource Management, Faculty of Science, University of Copenhagen, Frederiksberg 1958, DenmarkbDepartment of Economics and Management, Faculty of Agriculture and Forestry, University of Helsinki, Helsinki 00014, Finlandchttps://ror.org/040af2s02Faculty of Biological and Environmental Sciences, Helsinki Institute of Sustainability Science, University of Helsinki, Helsinki 00100, Finland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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      <title>Expanding frameworks: Integrating vulnerability, exposure, and critical infrastructure to assess pluvial flood risks in New York City</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520315122?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceExtreme rainfall is increasing in frequency and intensity, exposing urban systems to growing flood risks. Most flood risk assessments narrowly focus on the direct impacts of flooding, overlooking the broader, compounding consequences that may ...</description>
      <dc:title>Expanding frameworks: Integrating vulnerability, exposure, and critical infrastructure to assess pluvial flood risks in New York City</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520315122</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Pablo Herreros-CantisTimon McPhearsonBernice R. RosenzweigMalgosia MadajewiczElizabeth M. CookVeronica OlivottoEvan DennisFranco A. MontaltoJennifer CherrieraUrban Systems Lab, New York University, New York, NY 10003bhttps://ror.org/00eqwze33Basque Centre for Climate Change (BC3), Leioa 48940, Spainchttps://ror.org/052g8jq94Institute of Environmental Science and Technology (ICTA), Universitat Autònoma de Barcelona, Edifici Z, Cerdanyola del Vallès 08193, SpaindCary Institute of Ecosystem Studies, Millbrook, NY 12545ehttps://ror.org/05f0yaq80Stockholm Resilience Centre, Stockholm University, Stockholm SE-106 91, Swedenfhttps://ror.org/00j62qv07Beijer Institute of Ecological Economics, The Royal Swedish Academy of Sciences, Stockholm 104 05, Swedenghttps://ror.org/04sxj4848Department of Environment Science, Sarah Lawrence College, Bronxville, NY 10708hhttps://ror.org/00hj8s172Center for Climate Systems Research, Columbia Climate School, Columbia University, New York City, NY 10964ihttps://ror.org/04rt94r53Environmental Science Department, Barnard College, New York, NY 10027jhttps://ror.org/00453a208City College of New York, The City University of New York, NY 10031khttps://ror.org/04bdffz58Department of Civil, Architectural and Environmental Engineering, Drexel University, Philadelphia, PA 19104lhttps://ror.org/00453a208Department of Earth and Environmental Sciences, Brooklyn College-The City University of New York, Brooklyn, NY 11210mhttps://ror.org/00453a208Earth and Environmental Sciences, Graduate Center-The City University of New York, New York, NY 10016</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520315122</prism:doi>
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      <title>Uncovering minimal control of cell fate by natural dynamics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604777123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceHow can biological systems be reprogrammed without disrupting their regulatory programs? Traditional control of biological networks permanently alters regulatory interactions, for instance by indefinitely overexpressing a gene that would ...</description>
      <dc:title>Uncovering minimal control of cell fate by natural dynamics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604777123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Ferio BrahmanaCorbin HopperWoojeong LeeKwang-Hyun Choahttps://ror.org/05apxxy63Department of Bio and Brain Engineering, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2604777123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531269123?af=R">
      <title>Local delivery of interferon restores antigen presentation and sensitizes medulloblastoma to T cell killing</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531269123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceMedulloblastoma is the most common malignant brain tumor in children, associated with substantial long-term treatment toxicity and relapse. Immunotherapies remain largely ineffective in pediatric brain tumors, highlighting the need to overcome ...</description>
      <dc:title>Local delivery of interferon restores antigen presentation and sensitizes medulloblastoma to T cell killing</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531269123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Tanja EisemannKendall R. ChambersMeher Beigi MasihiTheophilos TzaridisSajina GCVeronika PisterIsaac YoumAditi DuttaAlexander T. WenzelKoei ChinZhenhua XuYanxin PeiScott L. PomeroyJill P. MesirovErnest FraenkelAnindya BagchiLukas ChavezRobert J. Wechsler-Reyaahttps://ror.org/03m1g2s55Cancer Genome and Epigenetics Program, National Cancer Institute-Designated Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037bhttps://ror.org/01esghr10Department of Neurology and Herbert Irving Comprehensive Cancer Center, Columbia University Medical Center, New York, NY 10032chttps://ror.org/042nb2s44Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139dhttps://ror.org/009avj582Department of Biomedical Engineering, Oregon Health and Science University, Portland, OR 97239ehttps://ror.org/0168r3w48Department of Computer Science and Engineering, University of California San Diego, La Jolla, CA 92093fhttps://ror.org/0168r3w48Department of Medicine, University of California San Diego, La Jolla, CA 92093ghttps://ror.org/0168r3w48Moores Cancer Center, University of California San Diego, La Jolla, CA 92093hhttps://ror.org/03wa2q724Brain Tumor Institute, Center for Cancer and Immunology, Children’s National Hospital, Washington, DC 20010ihttps://ror.org/00y4zzh67Department of Pediatrics, School of Medicine and Health Sciences, George Washington University, Washington, DC 20012jhttps://ror.org/00dvg7y05Department of Neurology, Boston Children’s Hospital, Harvard Medical School, Boston, MA 20037khttps://ror.org/042nb2s44Broad Institute of Massachusetts Institute of Technology and Harvard, Cambridge, MA 02142</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531269123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617361123?af=R">
      <title>SelO functions as a tumor suppressor through AMPylating Cdk5rap3</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617361123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThis study establishes an AMPylation-mediated signaling pathway in mammalian cells, mechanistically revealing how AMPylation intricately coordinates with other protein modifications, such as ubiquitination and SUMOylation. It demonstrates how ...</description>
      <dc:title>SelO functions as a tumor suppressor through AMPylating Cdk5rap3</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617361123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Li WuJie WuWenqiang XieXue LuChunda ChenTeng ZhangJie ShenYixiao ZhaoLu ChenYeyi LiQiujing YuYuan FuTing Wangahttps://ror.org/02mh8wx89Department of Pharmacology, Tianjin Key Laboratory of Inflammatory Biology, The province and ministry co-sponsored collaborative innovation center for medical epigenetics, State Key Laboratory of Experimental Hematology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, Chinabhttps://ror.org/04qr3zq92The Sichuan Provincial Key Laboratory for Genetic Diseases and Institute for Laboratory Medicine, Sichuan Provincial People’s Hospital, School of Medicine, University of Electronic Science and Technology of China, Chengdu 610072, Chinachttps://ror.org/02n96ep67Shanghai Key Laboratory of Regulatory Biology, School of Life Sciences, East China Normal University, Shanghai 200241, Chinadhttps://ror.org/034t30j35Systems Biology Center, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin Airport Economic Area, Tianjin 300308, Chinaehttps://ror.org/0152hn881Department of Hepatobiliary Cancer, Tianjin Medical University Cancer Institute &amp; Hospital, Tianjin 300060, Chinafhttps://ror.org/04qr3zq92Department of Health Management Centre &amp; Institute of Health Management, Sichuan Provincial People’s Hospital, School of Medicine, University of Electronic Science and Technology of China, Chengdu 610072, Chinaghttps://ror.org/02mh8wx89Department of Pharmacology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 300070, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617361123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525317123?af=R">
      <title>Intestinal plasmacytoid dendritic cells preferentially produce interferon lambda, contributing to localized innate immune responses</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525317123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThis study demonstrates that plasmacytoid dendritic cells (pDC) are a substantial source of homeostatic interferon lambda (IFN-λ) in the intestine. We have found that gut-intrinsic signaling reprograms pDC to produce increased levels of IFN-λ ...</description>
      <dc:title>Intestinal plasmacytoid dendritic cells preferentially produce interferon lambda, contributing to localized innate immune responses</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525317123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>David A. ConstantJacob A. Van WinklePhilip A. NorwoodGargi MishraKimberly A. MeyerMargaret E. LaneyShelby R. MaddenAlec GriffithPatrick Fernandes RodriguesRam SavanTimothy J. Niceahttps://ror.org/009avj582Department of Molecular Microbiology and Immunology, Oregon Health &amp; Science University, Portland, OR 97239bhttps://ror.org/00cvxb145Department of Immunology, University of Washington, Seattle, WA 98195cDepartment of Pathology and Immunology, Department of Pathology and Immunology, Washington University, St. Louis, MO 63110</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525317123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606537123?af=R">
      <title>Structural underpinnings of human Slo1 inhibition by scorpion and fungal toxins</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606537123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceIndole diterpene (ID) class of fungal alkaloids and specific scorpion toxins inhibit mammalian Slo1 with high affinity and specificity, but the precise chemistry of protein–ligand interactions that sculpt their inhibitory effects is not ...</description>
      <dc:title>Structural underpinnings of human Slo1 inhibition by scorpion and fungal toxins</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606537123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Gopal S. KallureKamalendu PalGabriel W. PratherSandipan Chowdhuryahttps://ror.org/036jqmy94Department of Molecular Physiology and Biophysics, The University of Iowa, Carver College of Medicine, Iowa City, IA 52242</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606537123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600684123?af=R">
      <title>Human preferences are susceptible to covertly misaligned AI advice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600684123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceMany people are turning to AI for advice that shapes their decisions. Yet, they cannot see the incentives behind such advice and typically assume it aligns with their interests. But what happens when an advisor has hidden objectives that push ...</description>
      <dc:title>Human preferences are susceptible to covertly misaligned AI advice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600684123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Sahand SabourJune M. LiuSiyang LiuChris Z. YaoShiyao CuiWen ZhangXuanming ZhangYaru CaoAdvait BhatJian GuanWei WuRada MihalceaHongning WangTim AlthoffTatia M. C. LeeMinlie Huangahttps://ror.org/03cve4549The Conversational AI Group, Department of Computer Science and Technology, Institute for Artificial Intelligence, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/02zhqgq86The State Key Laboratory of Brain and Cognitive Sciences, Department of Psychology, The University of Hong Kong, Hong Kong Special Administrative Region 999077, Chinachttps://ror.org/02zhqgq86Laboratory of Neuropsychology and Human Neuroscience, Department of Psychology, The University of Hong Kong, Hong Kong Special Administrative Region 999077, Chinadhttps://ror.org/00jmfr291The Language and Information Technologies Group, Department of Computer Science and Engineering, University of Michigan, Ann Arbor, MI 48109ehttps://ror.org/04r72en83Department of Psychology, University of International Relations, Haidian District, Beijing 100091, Chinafhttps://ror.org/034t30j35Neural Engineering Center, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, Chinaghttps://ror.org/00cvxb145The Behavioral Data Science Group, Paul G. Allen School of Computer Science and Engineering, University of Washington, Seattle, WA 98195hhttps://ror.org/00g5w7n47Ant Research Natural Language Processing, Ant Group, Beijing 100081, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600684123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600684123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621491123?af=R">
      <title>Geometry-driven jets underlie dispersal of plants and fungi by raindrops</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621491123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceRain-driven dispersal is a key mechanism by which many plants and fungi spread their offspring, yet the physical processes governing this phenomenon remain understudied. This work explains the mechanism of jet formation during drop impacts on ...</description>
      <dc:title>Geometry-driven jets underlie dispersal of plants and fungi by raindrops</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621491123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Ana-Maria BratuValentin LaplaudAntoine GarciaChristophe JosserandStéphanie DrevensekCamille DupratArezki Boudaoudahttps://ror.org/042tfbd02Laboratoire d‘Hydrodynamique, CNRS, Ecole polytechnique, Institut Polytechnique de Paris, Palaiseau Cedex 91128, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621491123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622424123?af=R">
      <title>Structure and function of TM6SF1 reveals role in mTORC1 signaling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622424123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceWe determine the cryo-electron microscopy structure of transmembrane 6 superfamily 1 (TM6SF1) and show that it is a lysosomal membrane protein that associates with LAMTOR1, a component of Ragulator complex, in a cholesterol-dependent manner. ...</description>
      <dc:title>Structure and function of TM6SF1 reveals role in mTORC1 signaling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622424123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Sen HongLiangjie JiaRong WangNadia Elghobashi-MeinhardtHelen H. HobbsXiaochun Liahttps://ror.org/05byvp690The Eugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center, Dallas, TX 75390bhttps://ror.org/05byvp690HHMI, University of Texas Southwestern Medical Center, Dallas, TX 75390chttps://ror.org/05byvp690Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390dhttps://ror.org/05m7pjf47School of Chemistry, University College Dublin, South Belfield, Dublin D04 V1W8, Ireland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622424123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622424123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615377123?af=R">
      <title>Visible light leaves evaporation and interfacial structure of neat water unchanged at the air–water interface</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615377123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceVisible light has been proposed to drive a new form of “photomolecular” evaporation at water surfaces, but the actual sensitivity of neat interfacial water to visible photons remains unknown. Here, we directly quantify how visible illumination ...</description>
      <dc:title>Visible light leaves evaporation and interfacial structure of neat water unchanged at the air–water interface</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615377123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Yucong ChenJoseph C. ShirleyZi Xuan NgYongkang WangYuki NagataArsh S. HazrahMischa Bonnahttps://ror.org/00sb7hc59Department of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Mainz 55128, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615377123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615377123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601714123?af=R">
      <title>Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601714123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceNeurons communicate via synapses that can dynamically adjust their strength and are hence “plastic.” We investigated synaptotagmin 7 (syt7), a key regulator of synaptic plasticity. We found that alternative splicing functions as a master ...</description>
      <dc:title>Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601714123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Nikunj MehtaDevin T. LarsonMitch WozneyShweta MishraSmrithika SubramaniSimi KaurAvani JainEdwin R. Chapmanahttps://ror.org/01y2jtd41Department of Neuroscience, University of Wisconsin-Madison, Madison, WI 53705bhttps://ror.org/01y2jtd41HHMI, University of Wisconsin-Madison, Madison, WI 53705chttps://ror.org/01y2jtd41Analytics Division, Wisconsin School of Business, University of Wisconsin-Madison, Madison, WI 53705</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601714123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601714123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531341123?af=R">
      <title>Temperate phages limit their own propagation under spatial constraint in biofilms on chitin</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531341123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceBacteria often produce and live within biofilm communities in natural environments, where they also encounter many threats including bacteriophages. Here, we show how temperate phages can confer a competitive advantage to their hosts via lytic ...</description>
      <dc:title>Temperate phages limit their own propagation under spatial constraint in biofilms on chitin</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531341123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Yixuan PengJacob D. HoltTriana N. DaliaDaniel SchultzAnkur B. DaliaCarey D. NadellaDepartment of Biological Sciences, Dartmouth, Hanover, NH 03755bDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755cDepartment of Biology, Indiana University, Bloomington, IN 47405</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531341123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531341123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2600693123?af=R">
      <title>Regulation of immune signal integration and memory by inflammation-induced chromosome conformation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2600693123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceInnate immune cells integrate inflammatory cues and retain transcriptional memory, a phenomenon previously attributed mainly to one-dimensional epigenetic mechanisms. We show that inflammatory cytokine exposure remodels the three-dimensional (...</description>
      <dc:title>Regulation of immune signal integration and memory by inflammation-induced chromosome conformation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2600693123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Bence DanielAndy Y. ChenKatalin SandorWenxi ZhangZhuang MiaoKathryn E. YostCaleb A. LareauHoward Y. ChangAnsuman T. Satpathya4D Nucleome Consortium, National Institutes of Health, Bethesda, MD 20892bhttps://ror.org/00f54p054Department of Pathology, Stanford University, Stanford, CA 94305chttps://ror.org/00f54p054Center for Personal Dynamic Regulomes, Stanford University, Stanford, CA 94305dhttps://ror.org/00f54p054Department of Bioengineering, Stanford University, Stanford, CA 94305ehttps://ror.org/00f54p054HHMI, Stanford University, Stanford, CA 94305fhttps://ror.org/0184qbg02Parker Institute for Cancer Immunotherapy, San Francisco, CA 94129</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2600693123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2600693123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534924123?af=R">
      <title>Identification and structural characterization of stereochemical promiscuity in a taste receptor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534924123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceTaste receptor type 1 (TAS1R) proteins, including sweet and umami receptors in humans, recognize nutrients such as sugars and amino acids. To detect diverse chemicals using a limited repertoire of receptors, many TAS1Rs exhibit broad substrate ...</description>
      <dc:title>Identification and structural characterization of stereochemical promiscuity in a taste receptor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534924123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Rakuto MizoguchiYasuka TodaMana NagaeTakashi YoshidaHiroaki MatsuuraKunio HirataVi Toan LamDuy Phuoc TranAkio KitaoYohei MiyanoiriMaiko HosotaniYuji AshikawaChiaki ItoNaotaka TsutsumiNorihisa YasuiYoshiro IshimaruAtsuko Yamashitaahttps://ror.org/02pc6pc55Division of Pharmaceutical Sciences, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japanbhttps://ror.org/02rqvrp93Department of Agricultural Chemistry, School of Agriculture, Meiji University, Kawasaki 214-8571, Japanchttps://ror.org/05dqf9946School of Life Science and Technology, Institute of Science Tokyo, Yokohama 226-8501, Japandhttps://ror.org/035t8zc32Division of Integrative Protein Science, Institute for Protein Research, The University of Osaka, Suita 565-0871, JapaneRIKEN SPring-8 Center, Sayo 679-5148, Japanfhttps://ror.org/05dqf9946School of Life Science and Technology, Institute of Science Tokyo, Meguro, Tokyo 152-8550, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534924123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534924123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606002123?af=R">
      <title>Nonperturbative nonlinear magnonics in a strongly driven antiferromagnet</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606002123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceNonlinear behavior is a defining feature of systems driven far from equilibrium, yet collective excitations in solids are typically studied only in weak, perturbative regimes. In particular, how spin waves (magnons) evolve under intense ...</description>
      <dc:title>Nonperturbative nonlinear magnonics in a strongly driven antiferromagnet</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606002123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>David RohrbachZhuquan ZhangTakayuki KuriharaKeith A. Nelsonahttps://ror.org/042nb2s44Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/057zh3y96Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606002123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606002123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607481123?af=R">
      <title>Dynamic Polycomb–CBC crosstalk orchestrates mRNA production at transcriptionally active loci in plants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607481123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe repressive Polycomb protein complex mediates gene silencing, yet its involvement in regulating transcriptionally active genes remains elusive. We identified that plant chromodomain H3K27me3 reader LIKE HETEROCHROMATIN PROTEIN1 (LHP1) binds ...</description>
      <dc:title>Dynamic Polycomb–CBC crosstalk orchestrates mRNA production at transcriptionally active loci in plants</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607481123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Yuanyuan XieLifeng DuZhijuan ChenXiaoyi LiDanhua JiangFangqing ZhaoZicong Liahttps://ror.org/03x08qn04State Key Laboratory of Microbial Technology, the Key Laboratory of Plant Development and Environmental Adaptation Biology, Ministry of Education, Shandong Key Laboratory of Precision Molecular Crop Design and Breeding, School of Life Sciences, Shandong University, Qingdao 266237, Chinabhttps://ror.org/034t30j35State Key Laboratory of Animal Biodiversity Conservation and Integrated Pest Management, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, Chinachttps://ror.org/03zd3ta61School of Life Science, Shanxi Normal University, Taiyuan, Shanxi 030031, Chinadhttps://ror.org/01tgyzw49Temasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607481123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607481123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616693123?af=R">
      <title>A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616693123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceCues driving the subcellular localization of integral membrane proteins in bacteria are often poorly understood. Using bacterial sporulation as a model for complex membrane reorganization, we demonstrate that theBacillus subtilisprotein ShfA ...</description>
      <dc:title>A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616693123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Vani PandeTaylor B. UpdegroveVivek AnantharamanAshley BaeJiji ChenL. AravindKumaran S. RamamurthiaLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892bComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894cAdvanced Imaging and Microscopy Resource, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616693123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616693123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611995123?af=R">
      <title>The CTNNB1–TRIM28 complex governs hormone-induced RNA polymerase II dynamics in kidney epithelial cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611995123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;Significanceβ-catenin (CTNNB1) is a multifunctional protein essential for development, yet its transcriptional role in terminally differentiated epithelial cells remains poorly understood. Here, we demonstrate that CTNNB1 forms a specialized ...</description>
      <dc:title>The CTNNB1–TRIM28 complex governs hormone-induced RNA polymerase II dynamics in kidney epithelial cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611995123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Hyo-Ju JangEuijung ParkHyun Jun JungTae-Hwan Kwonahttps://ror.org/040c17130Department of Biochemistry and Cell Biology, School of Medicine, Kyungpook National University, Daegu 41944, Koreabhttps://ror.org/040c17130Brain Korea 21 FOUR Kyungpook National University Convergence Educational Program, Department of Biomedical Science, Kyungpook National University, Daegu 41944, Koreachttps://ror.org/040c17130Department of Medicine, School of Medicine, Kyungpook National University, Daegu 41944, Koreadhttps://ror.org/04qn0xg47Bioinformatics Core, Biomedical Research Institute, Kyungpook National University Hospital, Daegu 41944, Koreaehttps://ror.org/00za53h95Division of Nephrology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611995123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611995123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527033123?af=R">
      <title>Uncovering heterogeneous effects via localized feature selection</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527033123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceOne main theme in multi-omics studies is to identify features that represent molecular mechanisms of diseases, referred to as feature selection. Here, we highlight the importance of accounting for heterogeneity across diverse populations in ...</description>
      <dc:title>Uncovering heterogeneous effects via localized feature selection</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527033123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Xiaoxia LiuJiaqi GuZhaomeng ChenBenjamin ChuLinxi LiuTim MorrisonRobert R. ButlerJacob EdelsonJinzhou LiFrank M. LongoHua TangIuliana Ionita-LazaChiara SabattiEmmanuel CandèsZihuai HeaDepartment of Biomedical Informatics, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, NY 14203bhttps://ror.org/032db5x82Department of Mathematics and Statistics, University of South Florida, Tampa, FL 33620chttps://ror.org/00f54p054Department of Statistics, Stanford University, Stanford, CA 94305dhttps://ror.org/00f54p054Department of Biomedical Data Science, Stanford University, Stanford, CA 94305ehttps://ror.org/01an3r305Department of Statistics, University of Pittsburgh, Pittsburgh, PA 15260fhttps://ror.org/00f54p054Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA 94305ghttps://ror.org/01tgyzw49Department of Statistics and Data Science, National University of Singapore, 117546, Singaporehhttps://ror.org/00f54p054Department of Genetics, Stanford University, Stanford, CA 94305ihttps://ror.org/00hj8s172Department of Biostatistics, Columbia University Mailman School of Public Health, New York, NY 10032jhttps://ror.org/00f54p054Department of Mathematics, Stanford University, Stanford, CA 94305khttps://ror.org/00f54p054Quantitative Sciences Unit, Department of Medicine, Stanford University, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527033123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527033123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615469123?af=R">
      <title>Origin flexibility governs robust ssDNA engagement by the DnaA initiator</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615469123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceChromosome replication must initiate reliably even though origin DNA sequences vary widely across species. We show that the conserved bacterial initiator protein DnaA achieves this robustness by flexibly engaging single-stranded DNA. Rather ...</description>
      <dc:title>Origin flexibility governs robust ssDNA engagement by the DnaA initiator</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615469123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Nanato KiyoharaYasutaka WakasugiKohei IharaAyaka KubaruSena MarukiNaho KojimaSachiko YoshitomiTsutomu KatayamaShogo Ozakiahttps://ror.org/00p4k0j84Department of Molecular Biology, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615469123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615469123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608171123?af=R">
      <title>ACTA2-directed actin filaments license STING trafficking and activation for antiviral immunity and autoimmune pathogenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608171123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe endoplasmic reticulum-to-Golgi trafficking of stimulator of interferon genes (STING) is essential for innate immunity, yet the machinery driving this process has remained a mystery. Here, we identify a dedicated actin filament network, not ...</description>
      <dc:title>ACTA2-directed actin filaments license STING trafficking and activation for antiviral immunity and autoimmune pathogenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608171123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Xianteng HouQing WuYangting DuChangwan WangJunyan ZhuYingbo JiangShe ChenLisha ZhouXiaoyu WuHongyan WangHui YangFajian Houahttps://ror.org/05qbk4x57State Key Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences; University of Chinese Academy of Sciences, Shanghai 200031, Chinabhttps://ror.org/00wksha49National Institute of Biological Sciences, Beijing 102206, Chinachttps://ror.org/04fzhyx73Taizhou Central Hospital (Taizhou University Hospital), Taizhou University, Taizhou, Zhejiang 318000, Chinadhttps://ror.org/013q1eq08Department of Neurosurgery, Huashan Hospital, Institute for Translational Brain Research, Shanghai Medical College, Fudan University, Shanghai 200032, ChinaeState Key Laboratory of Medical Neurobiology and Ministry of Education Frontier Science Center for Brain Science, Shanghai Medical College, Fudan University, Shanghai 200032, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608171123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608171123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616547123?af=R">
      <title>NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616547123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceUnderstanding enzyme mechanisms requires precise knowledge of active-site protonation states—features largely inaccessible to conventional structural biology. Here, we introduce an accelerated NMR crystallography workflow that makes practical ...</description>
      <dc:title>NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616547123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Christopher G. WilliamsSonglin WangVeronica CartaPatricia S. LanganAlexander F. ThomeSebastian A. RamosJacob B. HolmesRittik K. GhoshKevin L. WeissGregory J. O. BeranJoshua D. HartmanLeighton CoatesChad M. RienstraLeonard J. MuelleraDepartment of Chemistry, University of California-Riverside, Riverside, CA 92521bhttps://ror.org/01y2jtd41Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706chttps://ror.org/01y2jtd41National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, Madison, WI 53706dhttps://ror.org/01qz5mb56Oak Ridge National Laboratory, Neutron Scattering Science Division, Oak Ridge, TN 37831</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616547123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616547123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608168123?af=R">
      <title>Detection and sequencing of Ap2N-capped RNAs in human cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608168123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceApart from the canonical eukaryotic mRNA cap, an increasing number of noncanonical caps (nicotinamide adenine dinucleotide, dinucleotide polyphosphates) have been discovered on other RNA types in both prokaryotes and eukaryotes. Here, using ...</description>
      <dc:title>Detection and sequencing of Ap2N-capped RNAs in human cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608168123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Pavel VopalenskyOndřej NešutaMaria-Bianca MititeluAnton ŠkríbaAmbra SpampinatoKlára ViktorinováZuzana BuchováJana BřezinováPaul E. Reyes-GutierrezOndřej LukšanHana Cahovaahttps://ror.org/04nfjn472Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Prague 6 16000, Czechiabhttps://ror.org/024d6js02Department of Cell Biology, Faculty of Science, Charles University, Prague 2 12800, Czechia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608168123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608168123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612550123?af=R">
      <title>An eco-evolutionary theory of host-associated microbiomes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612550123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceSymbiotic microbiomes are central to the function, survival, and environmental adaptation of macro-organismal hosts. Yet the mechanisms by which microbiomes become host-specific and heritable through evolutionary processes remain unclear. ...</description>
      <dc:title>An eco-evolutionary theory of host-associated microbiomes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612550123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Gui AraujoTorsten ThomasNicole S. WebsterJosé M. MontoyaMiguel Lurgiahttps://ror.org/053fq8t95Department of Biosciences, Swansea University, Swansea SA2 8PP, United Kingdombhttps://ror.org/05d6wfd23Theoretical and Experimental Ecology Station, CNRS, Moulis 09200, Francechttps://ror.org/03r8z3t63Centre for Marine Science and Innovation, School of Biological, Earth and Environmental Sciences, University of New South Wales, New South Wales, Sydney 2052, Australiadhttps://ror.org/01nfmeh72Research Division, University of Tasmania, Tasmania, Hobart 7001, Australiaehttps://ror.org/02qg15b79Theoretical Sciences Visiting Program, Okinawa Institute of Science and Technology Graduate University, Onna 904-0495, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612550123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612550123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619869123?af=R">
      <title>Stimuli-induced reversible transformation between isomers of copper(I) clusters sharing an identical core</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619869123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceDue to its importance in the field of chemistry, structural isomerization has been one of the most studied fields. Compared to the organic small molecules, the precise synthesis of isomeric metal clusters remains a great challenge. Herein, by ...</description>
      <dc:title>Stimuli-induced reversible transformation between isomers of copper(I) clusters sharing an identical core</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619869123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Yao WangFang-Xue XiaoZiyong ChenEric Ka-Ho WongJun YiLiang-Liang YanVivian Wing-Wah Yamahttps://ror.org/02j89k719State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fujian College, University of the Chinese Academy of Sciences, Fuzhou 350002, Fujian, People’s Republic of Chinabhttps://ror.org/02zhqgq86Institute of Molecular Functional Materials, State Key Laboratory of Synthetic Chemistry, and Department of Chemistry, The University of Hong Kong, Hong Kong 999077, People’s Republic of Chinachttps://ror.org/020azk594College of Chemistry and Materials Science, Fujian Normal University, Fuzhou 350108, Fujian, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619869123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619869123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616336123?af=R">
      <title>Porous medium heterogeneity favors chemotaxis to nutrient hotspots in flow</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616336123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceChemotactic bacteria, capable of sensing and navigating chemical gradients, play an important role in subsurface biogeochemical processes, nutrient cycling, and degradation. However, how chemotaxis is modulated by flow in subsurface ...</description>
      <dc:title>Porous medium heterogeneity favors chemotaxis to nutrient hotspots in flow</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616336123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Maximilian F. StollMarco DentzRoman StockerJoaquin Jimenez-MartinezaDepartment of Water Resources and Drinking Water, Eawag, Dübendorf 8600, Switzerlandbhttps://ror.org/05a28rw58Institute of Environmental Engineering, Department of Civil, Environmental, and Geomatic Engineering, ETH Zurich, Zurich 8093, Switzerlandchttps://ror.org/02gfc7t72Institute of Environmental Assessment and Water Research—Spanish National Research Council, Barcelona E-08034, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616336123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616336123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620060123?af=R">
      <title>Structure-controlled quantum magnetotransport in Ba–Cu–As pnictide single crystals</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620060123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceComplex pnictide metals contain diverse local coordination environments, but direct links between particular structural motifs and electronic reconstruction remain difficult to establish. Here, we develop a single-crystal Ba–Cu–As platform in ...</description>
      <dc:title>Structure-controlled quantum magnetotransport in Ba–Cu–As pnictide single crystals</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620060123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Souvik SasmalHengdi ZhaoShima ShahabfarVikas SainiAdam BalvanzYihao WangJagannath JenaJohn PearsonAnand BhattacharyaChristopher WolvertonDuck Young ChungMercouri G. Kanatzidisahttps://ror.org/05gvnxz63Materials Science Division, Argonne National Laboratory, Lemont, IL 60439bDepartment of Materials Science and Engineering, Northwestern University, Evanston, IL 60208chttps://ror.org/03s53g630National High Magnetic Field Laboratory, Los Alamos National Laboratory, Los Alamos, NM 87545dDepartment of Chemistry, Northwestern University, Evanston, IL 60208ehttps://ror.org/05gvnxz63Center for Nanoscale Materials, Argonne National Laboratory, Lemont, IL 60439</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620060123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620060123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607727123?af=R">
      <title>Gene expression programs underlying spinal commissural neuron differentiation and axon growth across the midline</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607727123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceSpinal commissural neurons project their axons across the midline and have long served as a prime model system for axon pathfinding. However, lack of genetic access to these neurons has prevented a comprehensive analysis of their development, ...</description>
      <dc:title>Gene expression programs underlying spinal commissural neuron differentiation and axon growth across the midline</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607727123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Jane R. AbolafiaHanna HameedyLakshmi PrakashZiqi WangElze AmileviciuteSrikar DudipalaAlexander Jaworskiahttps://ror.org/05gq02987Department of Neuroscience, Brown University, Providence, RI 02912bRobert J. and Nancy D. Carney Institute for Brain Science, Providence, RI 02912</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607727123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607727123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531822123?af=R">
      <title>FAP53 facilitates formation of microtubule doublets</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531822123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe function of cilia depends on the unique scaffold built from microtubule doublets (MTDs). Here, we identify FAP53 as a factor that facilitates MTD assembly. We show that FAP53 alone is sufficient to promote MTD-like assembly in vitro, and ...</description>
      <dc:title>FAP53 facilitates formation of microtubule doublets</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531822123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Ming LiGuanghan ChenZhe ChenZhengyang GuoZi WangYongping ChaiWei LiGuangshuo Ouahttps://ror.org/03cve4549State Key Laboratory for Membrane Biology, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/03cve4549Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, Chinachttps://ror.org/03cve4549Beijing Frontier Research Center for Biological Structure, Tsinghua University, Beijing 100084, Chinadhttps://ror.org/03cve4549McGovern Institute for Brain Research, Tsinghua University, Beijing 100084, Chinaehttps://ror.org/03cve4549Ministry of Education Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, Chinafhttps://ror.org/03cve4549School of Life Sciences, Tsinghua University, Beijing 100084, Chinaghttps://ror.org/03cve4549School of Basic Medical Sciences, Tsinghua University, Beijing 100084, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531822123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531822123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536118123?af=R">
      <title>Decoupling food insecurity from shocks: A global analysis of food system resilience</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536118123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceOur study provides a global assessment of food system resilience, based on panel data from high-, middle-, and low-income countries and using a resilience-as-capacity framework. By integrating multicountry indicators of shocks, governance, ...</description>
      <dc:title>Decoupling food insecurity from shocks: A global analysis of food system resilience</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536118123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Christophe BénéAlessandro SassoAbdul-Rahim AbdulaiJane BattersbyAndrea CattaneoGreg CollinsBrice EvenTimothy FrankerbergerJessica FanzoAlejandro GuarinJessica A. GephartChristopher D. GoldenSheryl HendriksMario HerreroTim LangPreetmoninder LidderElodie Maitre d’HotelTrang NguyenCuong M. NguyenAndreea C. NowakRichard A. NyiawungBart de Steenhuijsen PitersMichaela SaisanaU. Rashid SumailaJose-Luis Vivero-PolLal RattanPatrick WebbJing ZhangaInternational Center for Tropical Agriculture, Cali 763537, ColombiabEuropean Commission, Joint Research Centre, Ispra 21027, ItalycFood Environment and Consumer Behaviour, International Center for Tropical Agriculture, Cali 763537, Colombiadhttps://ror.org/03p74gp79Environmental and Geographical Science, University of Cape Town, Cape Town 7701, South Africaehttps://ror.org/00pe0tf51Agrifood Economics and Policy Division, Food and Agriculture Organization of the United Nations, Rome 00153, ItalyfTechnical Assistance to Non-Governmental Organizations International, Tucson, AZ 85701gFood Environment and Consumer Behaviour, International Center for Tropical Agriculture, Hanoi 11900, Vietnamhhttps://ror.org/04qw24q55Global Nutrition Group, Wageningen University and Research, Wageningen 6700 AA, The NetherlandsiThe School of Advanced International Studies Europe, Johns Hopkins University, Bologna 40126, ItalyjFood Systems Transformation Lead at the World Benchmarking Alliance, London WC1V 6LJ, United Kingdomkhttps://ror.org/00cvxb145School of Aquatic and Fishery Sciences, University of Washington, Seattle, WA 98195-5020lDepartment of Nutrition, Harvard TH Chan School of Public Health, Boston, MA 02115mhttps://ror.org/00bmj0a71Department of Agricultural Economics, Natural Resources Institute, University of Greenwich, London ME4 4TB, United Kingdomnhttps://ror.org/00g0p6g84Department of Agricultural Economics, Extension and Rural Development, University of Pretoria, Pretoria 0028, South Africaohttps://ror.org/05bnh6r87Department of Global Development, College of Agriculture and Life Sciences, and Cornell Atkinson Center for Sustainability, Cornell University, Ithaca 14853, NYphttps://ror.org/04cw6st05School of Health &amp; Medical Sciences, Centre for Food Policy, City St George’s University of London, London EC1R 1UW, United Kingdomqhttps://ror.org/00pe0tf51Food and Agriculture Organization of the United Nations, Rome 00153, Italyrhttps://ror.org/05kpkpg04French Agricultural Research Centre for International Development, Montpellier 34398 Montpellier Cedex 5, Franceshttps://ror.org/04qw24q55Food System Transformation, Wageningen Social &amp; Economic Research, Wageningen University &amp; Research, Wageningen 6708 PB, the NetherlandstClimate Action, Bioversity International, Rome 00153, Italyuhttps://ror.org/04qw24q55Plant Production Systems Group, Wageningen University and Research, Wageningen 6700 AK, The Netherlandsvhttps://ror.org/01aff2v68School of Environment, Enterprise and Development, University of Waterloo, Waterloo, ON N2L 3G1, Canadawhttps://ror.org/04qw24q55Food System Transformation, Wageningen Social and Economic Research, Wageningen University and Research, Wageningen 6708 PB, The Netherlandsxhttps://ror.org/03rmrcq20Institute for the Oceans and Fisheries and the School of Public Policy and Global Affairs, University of British Columbia, Vancouver, BC V6T 1Z2, CanadayCameroon Country Office, World Food Programme, Yaounde P.O. Box 7308, Cameroonzhttps://ror.org/00rs6vg23College of Food, Agricultural, and Environmental Sciences Rattan Lal Center for Carbon Management and Sequestration, The Ohio State University, Columbus, OH 43210aahttps://ror.org/05bnh6r87Ashley School of Global Development and Environment, Cornell University, Ithaca, NY 14853bbhttps://ror.org/052gg0110Environmental Change Institute, University of Oxford, Oxford OX1 3QY, United Kingdomcchttps://ror.org/052gg0110Agricultural Resilience Impact and Innovation Hub, Department of Biology, University of Oxford, Oxford OX1 3EL, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536118123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536118123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612044123?af=R">
      <title>Martensitic-like transition between liquid crystalline and crystalline phases of a prototypical discotic organic semiconductor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612044123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceMartensitic transformations are ultrafast and reversible phase transitions that are leveraged across material science, from making steel harder to enabling shape memory alloys. Here, we demonstrate that an aligned columnar liquid crystal can ...</description>
      <dc:title>Martensitic-like transition between liquid crystalline and crystalline phases of a prototypical discotic organic semiconductor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612044123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Nurjahan KhatunJoe F. KhouryAgnes C. NkeleLingyu WangTieqiong ZhangPartha P. PaulPaul Chibuike OkoliNabila ShamimMatteo PasqualiKushal Bagchiahttps://ror.org/008zs3103Department of Chemistry, Rice University, Houston, TX 77005bhttps://ror.org/008zs3103Department of Chemical and Biomolecular Engineering, Rice University, Houston, TX 77005chttps://ror.org/008zs3103Applied Physics Program-Smalley-Curl Institute, Rice University, Houston, TX 77005dhttps://ror.org/05gzmn429Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025ehttps://ror.org/0449kf092Department of Chemical Engineering, Prairie View A&amp;M University, Prairie View, TX 77446fhttps://ror.org/008zs3103The Smalley-Curl Institute, Rice University, Houston, TX 77005</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612044123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620741123?af=R">
      <title>Domestication as gene–culture coevolution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620741123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceHuman cultural practices have shaped the evolution of domesticated plants and animals, yet few mathematical models describe how culturally transmitted preferences in one species interact dynamically with genetic evolution in another. We ...</description>
      <dc:title>Domestication as gene–culture coevolution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620741123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-15T07:00:00Z</dc:date>
      <dc:creator>Chase Van AmburgDrew BabelMarcus W. Feldmanahttps://ror.org/00f54p054Department of Biology, Stanford University, Stanford, CA 94305</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620741123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620741123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614319123?af=R">
      <title>Estimating protein isoform abundances with [math]</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614319123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceTranscripts of genes are translated into protein isoforms, which play crucial roles in biological processes; dysregulation of translation can generate disease. In large-scale studies, however, accurately estimating isoform abundances is ...</description>
      <dc:title>Estimating protein isoform abundances with [math]</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614319123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Lorenzo TestaLambertus KleiAlesia RengleAnastasia K. YocumDavid A. LewisBernie DevlinKathryn RoederMatthew L. MacDonaldahttps://ror.org/05x2bcf33Department of Statistics and Data Science, Carnegie Mellon University, Pittsburgh, PA 15213bhttps://ror.org/025602r80L’EMbeDS Department, Sant’Anna School of Advanced Studies, Pisa 56127, Italychttps://ror.org/01an3r305Department of Psychiatry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213dhttps://ror.org/01an3r305Department of Statistics, University of Pittsburgh, Pittsburgh, PA 15260eA2IDEA, LLC., Ann Arbor, MI 48103fhttps://ror.org/01an3r305Center for Neuroscience, University of Pittsburgh, Pittsburgh, PA 15213ghttps://ror.org/05x2bcf33Department of Computational Biology, Carnegie Mellon University, Pittsburgh, PA 15213hhttps://ror.org/01an3r305Biomedical Mass Spectrometry Center, University of Pittsburgh, Pittsburgh, PA 15260</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614319123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614319123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612191123?af=R">
      <title>Integrating NMR and contact-response analysis reveals the allosteric network driving domain closure in Enzyme I</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612191123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceAllosteric regulation enables proteins to transmit signals over long distances, but the mechanisms linking local ligand binding to global conformational changes remain difficult to resolve. Here, we combine NMR-based chemical shift covariance ...</description>
      <dc:title>Integrating NMR and contact-response analysis reveals the allosteric network driving domain closure in Enzyme I</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612191123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Aayushi SinghDaniel BurnsSergey L. SedinkinSayan DasDavit A. PotoyanVincenzo Vendittiahttps://ror.org/04rswrd78Department of Chemistry, Iowa State University, Ames, IA 50011bhttps://ror.org/04rswrd78Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612191123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612191123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532289123?af=R">
      <title>TRPM2 is a direct pain transducer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532289123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceTRPM2 channels are expressed in immune inflammatory cells participating in immune inflammation and pain. In this research, we demonstrated that TRPM2 channels in sensory neurons are essential to directly transduce chronic arthritis pain and ...</description>
      <dc:title>TRPM2 is a direct pain transducer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532289123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Linda VargheseMujahid AlizadaJinquan YangYe FengXiaoqiu YuanMitali MalhotraXuming Zhangahttps://ror.org/01a77tt86School of Life Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532289123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2532289123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613102123?af=R">
      <title>Bacterial stress responses lower mRNA–protein level correlations</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613102123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceWe employed an integrative transcriptomics and proteomics approach to investigate mRNA–protein correlations in three clinically relevant pathogens under 10 infection-relevant stress conditions. We identified genes whose mRNA–protein ...</description>
      <dc:title>Bacterial stress responses lower mRNA–protein level correlations</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613102123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Sena G. SüerJérôme ArnouxYi Y. LimGaneshwari DhurveRabia ŞenCemal ErdemAndré MateusKemal Avicanahttps://ror.org/05kb8h459Department of Molecular Biology, Umeå University, Umeå 90187, Swedenbhttps://ror.org/05kb8h459Integrated Science Lab (IceLab), Umeå University, Umeå 90187, Swedenchttps://ror.org/05kb8h459Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå 90187, Swedendhttps://ror.org/05kb8h459Science for Life Laboratory (SciLifeLab), Umeå University, Umeå 90187, Swedenehttps://ror.org/05kb8h459Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, Umeå 90187, Swedenfhttps://ror.org/05kb8h459Department of Medical Biosciences, Umeå University, Umeå 90187, Swedenghttps://ror.org/05kb8h459Department of Chemistry, Umeå University, Umeå 90187, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613102123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613102123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625812123?af=R">
      <title>Adenylate cyclase Mac1 functions as a cutin monomer receptor to drive appressorium development and infection in Magnaporthe oryzae</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625812123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificancePlants are protected by a waxy cuticle, which fungal pathogens such asMagnaporthe oryzae, the cause of rice blast disease, must breach to infect. This study identifies the fungal protein Mac1 not only as an enzyme that makes the signaling ...</description>
      <dc:title>Adenylate cyclase Mac1 functions as a cutin monomer receptor to drive appressorium development and infection in Magnaporthe oryzae</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625812123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Hui LiYan LiJing WangQing WangXiaohong LiuMinghua WuChunyue AnYingying CaiPengyun HuangXueming ZhuJiongyi YanXuetao ShiJiaoyu WangFu-Cheng LinJianping Luahttps://ror.org/00a2xv884College of Life Sciences, Zhejiang University, Hangzhou 310058, ChinabXianghu Laboratory, Hangzhou 311231, Chinachttps://ror.org/02qbc3192State Key Laboratory for Quality and Safety of Agro-Products, Key Laboratory of Agricultural Microbiome of Zhejiang Province, Key Laboratory of Biotechnology in Plant Protection of Ministry of Agriculture and Rural Affairs, Institute of Plant Protection and Microbiology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, ChinadState Key Laboratory for Rice Biology, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, Chinaehttps://ror.org/01knv0402School of Medicine, Linyi University, Linyi 276000, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2625812123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2625812123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605004123?af=R">
      <title>Multimodal integration supports neural processing of grammatical negation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605004123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceContrary to classical unimodal linguistic theories, there is growing consensus supporting the view of language as a multimodal system. The present study provides neurocognitive evidence for this view by examining negation, a core aspect of ...</description>
      <dc:title>Multimodal integration supports neural processing of grammatical negation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605004123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Hatice ZoraPeter HagoortAslı Özyürekahttps://ror.org/00671me87Max Planck Institute for Psycholinguistics, Nijmegen 6525 XD, The Netherlandsbhttps://ror.org/016xsfp80Donders Institute for Brain, Cognition and Behaviour, Radboud University, Nijmegen 6525 HT, The Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605004123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605004123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2624510123?af=R">
      <title>Atypical RanGAP drives nucleocytoplasmic transport in a parasitic Alveolate</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624510123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe transport of macromolecules between the nucleus and cytoplasm is a hallmark of eukaryotic cells. As such, the proteins that regulate this process are thought to have been encoded in the last eukaryotic common ancestor, and are generally ...</description>
      <dc:title>Atypical RanGAP drives nucleocytoplasmic transport in a parasitic Alveolate</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624510123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Pravin S. DewanganMichael L. Reeseahttps://ror.org/05byvp690Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas, TX 75390bhttps://ror.org/05byvp690Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, TX 75390</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2624510123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2624510123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621019123?af=R">
      <title>Unraveling the epidemiological and dispersal dynamics of the 2024–2025 chikungunya virus epidemic on Réunion Island</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621019123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceLeveraging &amp;gt;3,000 geo-referenced viral genomes sequenced during the 2024–2025 chikungunya virus epidemic on Réunion Island, we reconstruct the virus dispersal history and show that its spread is structured by human population density, ...</description>
      <dc:title>Unraveling the epidemiological and dispersal dynamics of the 2024–2025 chikungunya virus epidemic on Réunion Island</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621019123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Etienne FrumenceRaphaëlle KlittingKyla SerresYucai ShaoFilippo MontiMuriel VincentMandev S. GillMarc A. SuchardPhilippe LemeyXavier de LamballerieMarie-Christine Jaffar-BandjeeSimon DellicouraLaboratoire de Virologie, Centre Hospitalier Universitaire Félix Guyon, Saint-Denis, La Réunion 97400, FrancebCentre National de Référence Associé des Arbovirus, Saint-Denis, La Réunion 97490, Francechttps://ror.org/02vjkv261Centre National de Référence des Arbovirus, Institut National de la Santé et de la Recherche Médicale, Institut de Recherche Biomédicale des Armées, Marseille 13005, Francedhttps://ror.org/02vjkv261Unité des Virus Émergents (Aix-Marseille Univ, Università di Corsica, IRD 190, Institut National de la Santé et de la Recherche Médicale 1207, Institut de Recherche Biomédicale des Armées), Marseille 13005, Franceehttps://ror.org/01r9htc13Spatial Epidemiology Lab, Université Libre de Bruxelles, Brussels 1050, Belgiumfhttps://ror.org/006e5kg04Interuniversity Institute of Bioinformatics in Brussels, Université Libre de Bruxelles, Vrije Universiteit Brussel, Brussels 1050, Belgiumghttps://ror.org/046rm7j60Department of Biostatistics, Fielding School of Public Health, University of California, Los Angeles, CA 90095hhttps://ror.org/00dfw9p58Santé publique France – La Réunion, Saint-Denis, La Réunion 97743, FranceiDepartment of Statistics, University of Georgia, Athens, GA 30602jInstitute of Bioinformatics, University of Georgia, Athens, GA 30602khttps://ror.org/046rm7j60Department of Biomathematics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095lhttps://ror.org/046rm7j60Department of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, CA 90095mhttps://ror.org/05f950310Department of Microbiology, Immunology and Transplantation, Rega Institute, University of Leuven – KU Leuven, Leuven 3000, BelgiumnLaboratoire Infections Virales Aiguës et Tropicales, Assistance Publique – Hôpitaux de Marseille, Marseille 13005, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621019123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621019123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603334123?af=R">
      <title>TRPV4 mediates low-humidity responses in epidermal keratinocytes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603334123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceLow humidity is a common environmental stress that affects organismal physiology and homeostasis, yet how tissues sense and respond to atmospheric dryness remains poorly defined. Here, we identify the calcium-permeable cation channel transient ...</description>
      <dc:title>TRPV4 mediates low-humidity responses in epidermal keratinocytes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603334123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Manami TanakaShunsuke ChikumaMariko Hara-Chikumaahttps://ror.org/02kn6nx58Department of Pharmacology, School of Medicine, Keio University, Tokyo 160-8582, Japanbhttps://ror.org/00zdnkx70Institute of Biotechnology, College of Life Sciences and Medicine, National Tsing-Hua University, Hsinchu 300044, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603334123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603334123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609841123?af=R">
      <title>Glycans influence IgE and IgG recognition by rodent IgG-Fc receptors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609841123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceRodent models are widely used to study antibody-mediated immunity, yet important immune mechanisms can differ across species. We identify one such difference in how Fc receptors (FcRs) recognize antibodies in mice and rats. In rats, FcγRIV ...</description>
      <dc:title>Glycans influence IgE and IgG recognition by rodent IgG-Fc receptors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609841123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Shirui XuShuo DuMeijie DengGuanbo WangJunyu Xiaoahttps://ror.org/02v51f717State Key Laboratory of Gene Function and Modulation Research, School of Life Sciences, Peking University, Beijing 100871, People’s Republic of Chinabhttps://ror.org/04v3ywz14State Key Laboratory of Veterinary Public Health Safety, College of Veterinary Medicine, China Agricultural University, Beijing 100193, People’s Republic of Chinachttps://ror.org/02v51f717Biomedical Pioneering Innovation Center, Peking University, Beijing 100871, People’s Republic of Chinadhttps://ror.org/02v51f717Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, People’s Republic of ChinaeBeijing Key Laboratory of Clinical Evaluation of Cardiovascular-Kidney-Metabolic and Immuno-Inflammatory Innovative Drugs and Medical Devices, Beijing 100191, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609841123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609841123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606205123?af=R">
      <title>Catechol-O-methyltransferase connects dopamine homeostasis to redox signaling, metal homeostasis, and protein folding in schizophrenia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606205123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceDysregulated dopamine (DA) signaling and impaired redox homeostasis are central to the pathophysiology of schizophrenia (SCZ) and Parkinson’s disease (PD). Here, Tripathi and Chakraborty et al. demonstrate that loss of membrane-bound catechol-...</description>
      <dc:title>Catechol-O-methyltransferase connects dopamine homeostasis to redox signaling, metal homeostasis, and protein folding in schizophrenia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606205123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Sunil Jamuna TripathiSuwarna ChakrabortyNeil B. WoodDillon HoopesSarah BarkerEdwin Vázquez-RosaJiu AnChunxuan MaYuan HouSudarshana M. SharmaFeixiong ChengBobby ThomasBenjamin C. OrsburnStephen D. FriedSolomon H. SnyderAndrew A. PieperBindu D. Paulahttps://ror.org/00za53h95Department of Physiology, Pharmacology and Therapeutics, Johns Hopkins University School of Medicine, Baltimore, MD 21205bhttps://ror.org/00za53h95Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218chttps://ror.org/051fd9666Department of Psychiatry, Case Western Reserve University, Cleveland, OH 44106dhttps://ror.org/01gc0wp38Brain Health Medicines Center, Harrington Discovery Institute, University Hospitals Cleveland Medical Center, Cleveland, OH 44106ehttps://ror.org/051fd9666Department of Pathology, Case Western Reserve University, School of Medicine, Cleveland, OH 44106fhttps://ror.org/051fd9666Institute for Transformative Molecular Medicine, School of Medicine Case Western Reserve University, Cleveland, OH 44106ghttps://ror.org/051fd9666Department of Neurosciences, Case Western Reserve University, School of Medicine, Cleveland, OH 44106hhttps://ror.org/00za53h95Department of Neuroscience, Johns Hopkins University, Baltimore, MD 21218ihttps://ror.org/03xjacd83Genomic Medicine Institute Lerner Research Institute Cleveland Clinic, Cleveland, OH 44106jhttps://ror.org/012jban78Department of Biochemistry and Molecular Biology, Hollings Cancer Center, Medical University of South Carolina, Charleston, SC 29425khttps://ror.org/051fd9666Department of Molecular Medicine Cleveland Clinic Lerner College of Medicine, Case Western Reserve University, Cleveland, OH 44106lhttps://ror.org/051fd9666Case Comprehensive Cancer Center, Case Western Reserve University, School of Medicine, Cleveland, OH 44106mhttps://ror.org/012jban78Darby Children’s Research Institute, Medical University of South Carolina, Charleston, SC 29425nhttps://ror.org/012jban78Department of Pediatrics, Medical University of South Carolina, Charleston, SC 29425ohttps://ror.org/012jban78Department of Neuroscience, Medical University of South Carolina, Charleston, SC 29425phttps://ror.org/012jban78Department of Drug Discovery, Medical University of South Carolina, Charleston, SC 29425qhttps://ror.org/00za53h95Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218rhttps://ror.org/00za53h95The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205shttps://ror.org/00za53h95Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205thttps://ror.org/01nh3sx96Geriatric Psychiatry, Geriatric Research Education and Clinical Center, Louis Stokes Veterans Affairs Medical Center, Cleveland, OH 44106uCleveland Alzheimer’s Disease Research Center, Cleveland, OH 44106</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606205123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606205123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615158123?af=R">
      <title>Isolation and in vitro characterization of BchE, the cobalamin-dependent anaerobic magnesium protoporphyrin IX monomethylester cyclase</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615158123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceBacteriochlorophyll biosynthesis enzyme BchE is a cobalamin-dependent radicalS-adenosylmethionineenzyme that catalyzes a six-electron oxidation of Mg-protoporphyrin IX monomethylester in the absence of molecular oxygen. This reaction entails ...</description>
      <dc:title>Isolation and in vitro characterization of BchE, the cobalamin-dependent anaerobic magnesium protoporphyrin IX monomethylester cyclase</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615158123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Nicholas J. YorkXuekai ZhangSquire J. Bookerahttps://ror.org/04p491231Department of Chemistry, The Pennsylvania State University, University Park, PA 16802bhttps://ror.org/00b30xv10Department of Chemistry, School of Arts and Sciences, University of Pennsylvania, Philadelphia, PA 19401chttps://ror.org/04p491231Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802dhttps://ror.org/00b30xv10Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104eHHMI, Chevy Chase, MD 20815</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615158123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615158123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608395123?af=R">
      <title>Magnetic vortex state of natural lunar γ-Fe</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608395123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceMetallic iron is one of the most widespread magnetic carriers on the lunar surface. Previous studies have primarily identified metallic iron in the α phase, whereas γ-Fe, an allotrope generally stable only at high temperatures, has not been ...</description>
      <dc:title>Magnetic vortex state of natural lunar γ-Fe</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608395123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Pengfei LiuZiliang JinZheng GongLong LiKang WangXiandi ZengJing LiuDongsheng SongHaifeng DuKelei ZhuChuanxin YanJinhua LiKeke ZhangWyn WilliamsAnn M. HirtaMacau Institute of Space Technology and Application, Macau University of Science and Technology, Macau 999078, ChinabState Key Laboratory of Lunar and Planetary Sciences, Macau University of Science and Technology, Macau 999078, Chinachttps://ror.org/01rxvg760State Key Laboratory for Critical Earth Material Cycling and Mineral Deposits, School of Earth Sciences and Engineering, Nanjing University, Nanjing 210023, Chinadhttps://ror.org/034t30j35Anhui Province Key Laboratory of Condensed Matter Physics at Extreme Conditions, High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, Anhui, Chinaehttps://ror.org/05th6yx34Information Materials and Intelligent Sensing Laboratory of Anhui Province, Institutes of Physical Science and Information Technology, Anhui University, Hefei 230601, Chinafhttps://ror.org/034t30j35Key Laboratory of Deep Petroleum Intelligent Exploration and Development, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, Chinaghttps://ror.org/05qbk4x57College of Earth and Planetary Sciences, University of Chinese Academy of Sciences, Beijing 100049, Chinahhttps://ror.org/01nrxwf90School of GeoSciences, University of Edinburgh, Edinburgh EH9 3FE, United Kingdomihttps://ror.org/05a28rw58Institute of Geophysics, Department of Earth and Planetary Sciences, ETH Zürich, Zürich CH-8092, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608395123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2608395123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610818123?af=R">
      <title>Soft photonic hydrogel interfaces for autonomous and dynamic thermoregulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610818123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceAdaptive passive cooling materials can reduce energy consumption by regulating temperature in response to changing environments without external power input. However, existing systems often rely on heterogeneous multilayer architectures that ...</description>
      <dc:title>Soft photonic hydrogel interfaces for autonomous and dynamic thermoregulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610818123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Qin YeYimou HuangShuai GuoJiepin WangKaiqi LiangChan Jae ShinZhen YuXingkui GuoMang ZhaoHaojie LuYaoxin ZhangQing LiZhuo ChenHongjie YanZhong-Zhen YuMeijie ChenWubin BaiSwee Ching Tanahttps://ror.org/00f1zfq44School of Energy Science and Engineering, Central South University, Changsha 430001, Chinabhttps://ror.org/01tgyzw49Department of Materials Science and Engineering, National University of Singapore, Singapore 117575, Singaporechttps://ror.org/0130frc33Department of Applied Physical Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514dhttps://ror.org/00df5yc52Center for Nanomaterials and Nanocomposites, College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, Chinaehttps://ror.org/0220qvk04China-UK Low Carbon College, Shanghai Jiao Tong University, Shanghai 201306, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610818123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610818123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526862123?af=R">
      <title>Color–concept associations reveal a new conceptual space</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526862123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceHuman minds can infer complex meanings from quite simple percepts; for instance, colors in data visualizations may signify political allegiances, intensity of continuous variables, or categories of discrete data. Such inferences support our ...</description>
      <dc:title>Color–concept associations reveal a new conceptual space</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526862123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Kushin MukherjeeLaurent LessardMichael GleicherTimothy T. RogersKaren B. Schlossahttps://ror.org/00f54p054Department of Psychology, Stanford University, Stanford, CA 94305bDepartment of Mechanical and Industrial Engineering, Northeastern University, Boston, MA 02115chttps://ror.org/01y2jtd41Department of Computer Sciences, University of Wisconsin–Madison, Madison, WI 53706dhttps://ror.org/01y2jtd41Department of Psychology, University of Wisconsin–Madison, Madison, WI 53706ehttps://ror.org/01y2jtd41Wisconsin Institute for Discovery, University of Wisconsin–Madison, Madison, WI 53715fhttps://ror.org/02jx3x895Institute of Cognitive Neuroscience, University College London, London WC1N 3AZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526862123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526862123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606441123?af=R">
      <title>Reallocating fossil subsidies via social assistance reduces poverty and preserves emissions cuts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606441123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceGlobal efforts to phase out fossil fuel subsidies often stall because the immediate socioeconomic costs, particularly heightened poverty and inequality, outweigh the perceived environmental gains. While the necessity of compensatory measures ...</description>
      <dc:title>Reallocating fossil subsidies via social assistance reduces poverty and preserves emissions cuts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606441123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Xiangjie ChenKuishuang FengLaixiang SunDaniele MalerbaPeipei TianNathan Hultmanahttps://ror.org/047s2c258Department of Geographical Sciences, University of Maryland, College Park, MD 20742bhttps://ror.org/02zhqgq86Department of Geography, The University of Hong Kong, Hong Kong, Chinachttps://ror.org/02zhqgq86Institute for Climate and Carbon Neutrality, The University of Hong Kong, Hong Kong, Chinadhttps://ror.org/01t3zke88German Institute of Development and Sustainability, Department “Transformation of Economic and Social Systems”, Bonn D-53113, Germanyehttps://ror.org/0207yh398Institute of Blue and Green Development, Shandong University, Weihai 264209, Chinafhttps://ror.org/047s2c258Center for Global Sustainability, School of Public Policy, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606441123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606441123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613741123?af=R">
      <title>FoldaVirus, a knowledge-based icosahedral capsid prediction tool using AlphaFold</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613741123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceCurrently, there exists a huge gap between the number of available viral coat protein (CP) sequences and the experimentally determined capsid structures. Moreover, there are no resources available that provide full capsid models. By leveraging ...</description>
      <dc:title>FoldaVirus, a knowledge-based icosahedral capsid prediction tool using AlphaFold</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613741123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Oscar Rojas LabraDavid S. Montoya-MunozNelly Santoyo-RiveraJeffrey McDonaldDaniel Montiel-GarciaDavid A. CaseVijay S. Reddyahttps://ror.org/017zqws13The Hormel Institute, University of Minnesota, Austin, MN 55912bhttps://ror.org/01da06998Department of Computer Systems and Information Technologies, Tecnologico Nacional de Mexico and Instituto Tecnológico Superior de Irapuato, Irapuato, Guanajuato C.P. 36821, Mexicochttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037dhttps://ror.org/05vt9qd57Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613741123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613741123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603322123?af=R">
      <title>Dynamic fracture and catastrophic crack branching in highly entangled hydrogels</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603322123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceThe resistance of soft materials to fracture is often interpreted in terms of how uniformly loaded polymer chains break. Here, we show that in highly entangled gels, fracture under fast deformation is instead governed by localized viscous ...</description>
      <dc:title>Dynamic fracture and catastrophic crack branching in highly entangled hydrogels</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603322123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Hang YangShuming KangYujing DuDavid A. WeitzJoost J. Vlassakahttps://ror.org/03vek6s52John A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138bhttps://ror.org/03vek6s52Department of Physics, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603322123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603322123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616684123?af=R">
      <title>Lipids regulate export of lysosomal enzymes from the endoplasmic reticulum</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616684123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceProper intracellular protein trafficking is essential for cellular homeostasis, yet how cellular metabolism regulates this process remains poorly understood. In this study, we show that inhibition of fatty acid synthesis disrupts lysosomal ...</description>
      <dc:title>Lipids regulate export of lysosomal enzymes from the endoplasmic reticulum</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616684123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Baolong XiaMyeonghoon HanIsaac ParkNorbert PerrimonaDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, MA 02115bHHMI, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616684123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616684123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613575123?af=R">
      <title>3D patterns on fractured surfaces of soft stretchable materials</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613575123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceSpontaneous pattern formation on fracture surfaces provides a unique window into the microstructural and mechanical identity of materials. This study uncovers the three-dimensional (3D) evolutionary mechanisms of “step-like” fracture patterns ...</description>
      <dc:title>3D patterns on fractured surfaces of soft stretchable materials</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613575123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Tenghao YinEtienne BarthelChung-Yuen HuiCostantino CretonMatteo Ciccottiahttps://ror.org/03zx86w41Laboratoire Sciences et Ingénierie de la Matière Molle, École supérieure de physique et de chimie industrielles de la Ville de Paris Paris, Paris Sciences et Lettres Université, Sorbonne Université, CNRS, Paris F-75005, Francebhttps://ror.org/05bnh6r87Sibley School of Mechanical and Aerospace Engineering, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613575123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613575123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2626942123?af=R">
      <title>Tobramycin enhances Mycobacterium abscessus fitness through whiB7 induction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626942123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificancePulmonary infections caused byMycobacterium abscessus(Mabsc) are increasing in prevalence, especially in people with cystic fibrosis (pwCF) and bronchiectasis, and are recalcitrant to treatment. This study demonstrates that tobramycin, an ...</description>
      <dc:title>Tobramycin enhances Mycobacterium abscessus fitness through whiB7 induction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626942123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Jodi M. CorleyJack H. CongelKelsey C. HaistAlma E. OchoaKenneth C. MalcolmWilliam J. JanssenJerry A. NickKatherine B. Hisertahttps://ror.org/016z2bp30Department of Medicine, National Jewish Health, Denver, CO 80206</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626942123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626942123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604325123?af=R">
      <title>NAD+ depletion by catalytic TIR domains triggers a distinct form of regulated necrosis in mammalian cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604325123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceSARM1 is reported to play a dual role as a negative regulator of Toll-like receptor (TLR) signaling and as executioner of Wallerian degeneration, a form of neuronal cell death. The latter function depends on the NADase activity of its Toll/...</description>
      <dc:title>NAD+ depletion by catalytic TIR domains triggers a distinct form of regulated necrosis in mammalian cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604325123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Nino A. EspinasLouise LacanteElla HartenianVanessa MackZhen-Xian NiouHui-Chen LuPetr Brozahttps://ror.org/019whta54Department of Immunobiology, University of Lausanne, Epalinges 1066, SwitzerlandbGill Institute for Neuroscience, Indiana University, Bloomington, IN 47405</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604325123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604325123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617534123?af=R">
      <title>A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617534123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceMutations in the microtubule-associated serine/threonine (MAST) kinases are increasingly being associated with neurodevelopment disorders, yet little is known about their structure, substrate specificity, or role in neurodevelopment. We reveal ...</description>
      <dc:title>A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617534123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Sumire AntonioliPatrick HeisterkampWeiqiang ChenDorothea AnratherMarkus HartlMaria Fernanda Martinez-RezaRatna TripathyMichael SchutzbierKarl MechtlerDavid A. KeaysThomas A. Leonardahttps://ror.org/05n3x4p02Max Perutz Labs, Medical University of Vienna, Vienna 1030, Austriabhttps://ror.org/05n3x4p02Vienna BioCenter PhD Program, A Doctoral School of the University of Vienna and the Medical University of Vienna, Vienna A-1030, AustriacDivision of Neurobiology, Department of Biology, Ludwig-Maximilians-University Munich, Planegg-Martinsried 82152, Germanydhttps://ror.org/05cz70a34Max Perutz Labs, Mass Spectrometry Facility, Vienna 1030, Austriaehttps://ror.org/03prydq77Department of Biochemistry and Cell Biology, Center for Molecular Biology, University of Vienna, Vienna 1030, AustriafDivision of Physiological Genomics, Biomedical Center, Ludwig-Maximilians-University Munich, Planegg-Martinsried 82152, GermanygInstitute of Molecular Pathology, Vienna 1030, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617534123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617534123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607664123?af=R">
      <title>Cross-feeding enables robust coexistence between four bacterial species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607664123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceUnderstanding the drivers of microbial diversity is essential for managing natural ecosystems and designing synthetic microbiomes. This study tests the relative importance of resource supply vs. species attributes, demonstrating that a four-...</description>
      <dc:title>Cross-feeding enables robust coexistence between four bacterial species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607664123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Snorre SulheimMiguel TeixeiraEric UlrichAlisson GillonSamuele E. A. TestaPrajwal PadmanabhaDaniel MachadoSara Mitriahttps://ror.org/019whta54Department of Fundamental Microbiology, University of Lausanne, Lausanne 1015, Switzerlandbhttps://ror.org/05xg72x27Department of Biotechnology and Food Science, Norwegian University of Science and Technology, Trondheim 7491, Norway</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607664123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607664123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2538126123?af=R">
      <title>Assessing the impacts of sufficient and reliable electricity in low-resource healthcare facilities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2538126123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceReliable electricity is essential for safe, effective healthcare, yet over one billion people worldwide rely on facilities with no access to electricity, or access to unreliable power. Using survey data, power-sensor data, and monthly health ...</description>
      <dc:title>Assessing the impacts of sufficient and reliable electricity in low-resource healthcare facilities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2538126123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-17T07:00:00Z</dc:date>
      <dc:creator>Ryan McCordSamuel B. MilesJackson M. MughumaDaniel M. KammenLaura H. Kwongahttps://ror.org/00py81415Sanford School of Public Policy, Duke University, Durham, NC 27708bhttps://ror.org/00py81415Nicholas Institute for Energy, Environment &amp; Sustainability, Duke University, Durham, NC 27708chttps://ror.org/00za53h95Ralph O’Conner Sustainable Energy Institute, Johns Hopkins University, Baltimore, MD 21218dhttps://ror.org/02wt5sv47Department of Civil and Systems Engineering, School of Advanced International Studies, Baltimore, MD 21218eResearch Centre for Humanitarian Aid, North Kivu, Democratic Republic of Congofhttps://ror.org/01an7q238Division of Environmental Health Sciences, School of Public Health, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2538126123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2538126123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603412123?af=R">
      <title>Deconstruction of lysergic acid diethylamide</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603412123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceLysergic acid diethylamide (LSD) is perhaps the best-known psychedelic and is currently being explored as a treatment for neuropsychiatric diseases. Despite being discovered over 8 decades ago, we have an incomplete understanding of how its ...</description>
      <dc:title>Deconstruction of lysergic acid diethylamide</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603412123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-08T07:00:00Z</dc:date>
      <dc:creator>Andrian G. BasarginAndras DomokosJoseph J. HennesseyIsak K. AarrestadRohini SambyalYara A. KhatibJohanna KrügerLee E. DunlapSamuel J. CarterIsabella A. RebekJohn L. McKeeSerena S. SchalkMin LiuJames C. FettingerMonica A. GonzalezAbhay PotluriDean J. TantilloOliver FiehnJohn D. McCorvyDavid E. Olsonahttps://ror.org/05rrcem69Institute for Psychedelics and Neurotherapeutics, University of California, Davis, CA 95616bhttps://ror.org/05rrcem69Chemistry and Chemical Biology Graduate Program, University of California, Davis, CA 95616chttps://ror.org/00qqv6244Department of Cell Biology, Neurobiology, and Anatomy, Medical College of Wisconsin, Milwaukee, WI 53226dhttps://ror.org/05rrcem69Neuroscience Graduate Program, University of California, Davis, CA 95618ehttps://ror.org/05rrcem69Department of Chemistry, University of California, Davis, CA 95616fhttps://ror.org/05rrcem69Pharmacology and Toxicology Graduate Program, University of California, Davis, CA 95616ghttps://ror.org/05rrcem69West Coast Metabolomics Center, University of California, Davis, CA 95616hhttps://ror.org/00qqv6244Department of Pharmacology and Toxicology, Neuroscience Research Center, Cancer Center, Medical College of Wisconsin, Milwaukee, WI 53226iDepartment of Biochemistry and Molecular Medicine, School of Medicine, University of California, Sacramento, CA 95817jhttps://ror.org/05rrcem69Center for Neuroscience, University of California, Davis, CA 95618</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603412123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603412123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613876123?af=R">
      <title>Time-boundary scattering and topological resonant transmissions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613876123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceJust as waves scatter at a spatial interface, they also scatter at a “time boundary” when a medium’s properties change suddenly in time. By developing a time-domain scattering theory, we uncover resonant transmissions—special wave modes that ...</description>
      <dc:title>Time-boundary scattering and topological resonant transmissions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613876123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Haiping Huahttps://ror.org/034t30j35Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, Chinabhttps://ror.org/05qbk4x57School of Physical Sciences, University of Chinese Academy of Sciences, Beijing 100049, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613876123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613876123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618341123?af=R">
      <title>The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618341123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceGlycyl radical enzymes (GREs) are a superfamily of enzymes that catalyze challenging chemical reactions in anaerobic environments. One such enzyme, indoleacetate decarboxylase (IAD), performs a C–C bond cleavage and decarboxylation reaction on ...</description>
      <dc:title>The structural basis of malodorant skatole formation by the glycyl radical enzyme indoleacetate decarboxylase</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618341123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Christa N. ImrichLindsey R. F. BackmanAbigail P. AllworthMary C. AndorferJared C. ParisNina M. GreeleyBeverly FuEmily P. BalskusCatherine L. Drennanahttps://ror.org/042nb2s44Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/042nb2s44MIT Summer Research Program in Biology, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/042nb2s44Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139dhttps://ror.org/03vek6s52Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138ehttps://ror.org/05a0ya142Broad Institute, Cambridge, MA 02139fHHMI, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618341123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618341123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621033123?af=R">
      <title>Faster relaxation of nonphotochemical quenching in C4 than in C3 species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621033123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceAcceleration of nonphotochemical quenching has been proposed as a means to enhance crop photosynthetic efficiency in C3 species, but whether this strategy has potential in C4 species, which include several major crops, remains unclear. Here, ...</description>
      <dc:title>Faster relaxation of nonphotochemical quenching in C4 than in C3 species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621033123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Lucía Arce CubasAsuka NakamuraLauana Pereira de OliveiraRichard L. VathR. Shawn AbrahamsJulia WalterCristina Rodrigues Gabriel SalesEmmanuel L. BernardoYuri Nakajima MunekageStephen P. LongJohannes Kromdijkahttps://ror.org/013meh722Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdombhttps://ror.org/047426m28Photosynthesis and Food Security, Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801chttps://ror.org/02qf2tx24Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japandhttps://ror.org/047426m28Department of Plant Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801ehttps://ror.org/030s54078Crop Physiology Division, Institute of Crop Science, College of Agriculture and Food Science, University of the Philippines Los Baños, Laguna 4031, Philippines</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621033123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621033123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611776123?af=R">
      <title>Unidirectional flow from continuous broken symmetries</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611776123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceControlling matter and energy transport is a fundamental challenge in physical systems, from electron transport in solids to fluid transport in vascular networks. Fluidic systems have mostly focused on local mechanisms, such as individual ...</description>
      <dc:title>Unidirectional flow from continuous broken symmetries</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611776123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Aaron WinnJustine ParmentierEleni KatiforiMartin Brandenbourgerahttps://ror.org/00b30xv10Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104bhttps://ror.org/03zq0xc17Aix-Marseille Université, CNRS, Centrale Méditerranée, Institut de Recherche sur les Phénoménes Hors Équilibre, UMR 7342, Marseille 13384, Francechttps://ror.org/00sekdz59Center for Computational Biology, Flatiron Institute, New York, NY 10010</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611776123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611776123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622259123?af=R">
      <title>Large complete and isotropic phononic band gaps in ultradense stealthy hyperuniform composites</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622259123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceWe present a technique for designing disordered two-phase media with complete phononic band gaps that block the transmission of elastic waves equally well in every direction and over a wide range of frequencies. A related feat has been ...</description>
      <dc:title>Large complete and isotropic phononic band gaps in ultradense stealthy hyperuniform composites</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622259123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Murray SkolnickPaul J. SteinhardtSalvatore Torquatoahttps://ror.org/00hx57361Princeton Materials Institute, Princeton University, Princeton, NJ 08544bhttps://ror.org/00hx57361Department of Physics, Princeton University, Princeton, NJ 08544chttps://ror.org/00hx57361Department of Chemistry, Princeton University, Princeton, NJ 08544dhttps://ror.org/00hx57361Program in Applied and Computational Mathematics, Princeton University, Princeton, NJ 08544</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622259123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622259123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616574123?af=R">
      <title>Zinc isotopic evidence for an Archean initiation of deep carbon cycling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616574123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceUnderstanding when Earth’s deep carbon cycle began is critical for reconstructing planetary evolution and habitability. We add to this debate by integrating new zinc (Zn) isotopic data for Phanerozoic and Precambrian carbonatites plus ...</description>
      <dc:title>Zinc isotopic evidence for an Archean initiation of deep carbon cycling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616574123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <dc:creator>Yun-Feng DuZhuang MaShui-Jiong WangJian SunRoger H. MitchellSebastian Tappeahttps://ror.org/04q6c7p66State Key Laboratory of Geological Processes and Mineral Resources, China University of Geosciences (Beijing), Beijing 100083, Chinabhttps://ror.org/04q6c7p66Frontiers Science Center for Deep-Time Digital Earth, China University of Geosciences (Beijing), Beijing 100083, Chinachttps://ror.org/02gp4e279State Key Laboratory of Deep Earth and Mineral Exploration, Key Laboratory of Isotope Geology of the Ministry of Natural Resources, Institute of Geology, Chinese Academy of Geological Sciences, Beijing 100037, Chinadhttps://ror.org/023p7mg82Department of Geology, Lakehead University, Thunder Bay, ON P7B 5E1, CanadaeDivision of Economic Geology &amp; Petrology, Technical University Bergakademie Freiberg, Freiberg D-09599, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616574123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616574123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535342123?af=R">
      <title>RHAMM drives formation of polyploid cancer cells and confers resistance to ER-targeted therapy in breast cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535342123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;SignificanceEndocrine resistance in estrogen receptor-positive breast cancer remains a major clinical challenge. This study identifies a role for RHAMM in driving therapy failure through the induction of polyploidization—a process long associated with ...</description>
      <dc:title>RHAMM drives formation of polyploid cancer cells and confers resistance to ER-targeted therapy in breast cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535342123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Shiyi WuSi ChenBohan LiuYuting LiuSiyue YangJiajie HuYiqing HeQinqing LiuYiwen LiuYan DuGuoliang ZhangQian GuoFeng GaoFen TangYongming XuCuixia Yangahttps://ror.org/0220qvk04Department of Clinical Laboratory, Shanghai Sixth People’s Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200233, Chinabhttps://ror.org/0220qvk04Department of Molecular Biology, Shanghai Sixth People’s Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200233, Chinachttps://ror.org/0220qvk04Faculty of Medical Laboratory Science, College of Health Science and Technology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, Chinadhttps://ror.org/0220qvk04Department of Breast Surgery, Shanghai Sixth People’s Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200233, Chinaehttps://ror.org/0220qvk04Department of Pain Management, Shanghai Sixth People’s Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200233, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535342123</prism:doi>
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      <title>The ecology of urban segregation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537180123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>The ecology of urban segregation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537180123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Steward T. A. PickettTimon McPhearsonaCary Institute of Ecosystem Studies, Millbrook, NY 12545bhttps://ror.org/0190ak572Department of Environmental Studies, Urban Systems Lab, New York University, New York, NY 10012chttps://ror.org/05f0yaq80Stockholm Resilience Centre, Beijer Institute of Ecological Economics, The Royal Swedish Academy of Sciences, Stockholm University, Stockholm SE-106 91, Sweden</dc:creator>
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      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
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      <title>Diffusion of neuromodulators for temporal credit assignment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608831123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;Biological learning achieves temporal credit assignment despite sparse and imprecise feedback, often relying on neuromodulatory signals acting over space and time. Here, we introduce a learning mechanism in which error information diffuses locally through ...</description>
      <dc:title>Diffusion of neuromodulators for temporal credit assignment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608831123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>João Barretto-BittarAnna LevinaEmmanouil GiannakakisRoxana Zeraatiahttps://ror.org/03a1kwz48Department of Computer Sciences, University of Tübingen, Tübingen 72076, Germanybhttps://ror.org/02jz4aj89Department of Data Analytics and Digitalisation, Maastricht University, Maastricht 6200 MD, Netherlandschttps://ror.org/026nmvv73Department of Computational Neuroscience, Max Planck Institute for Biological Cybernetics, Tübingen 72076dhttps://ror.org/041kmwe10Department of Bioengineering, Imperial College London, London SW7 2BP, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2608831123</prism:doi>
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      <title>Feed the microbiome, repair the gut</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2626807123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Feed the microbiome, repair the gut</dc:title>
      <dc:identifier>doi:10.1073/pnas.2626807123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Jibraan A. FawadSean R. Mooreahttps://ror.org/01z7r7q48Division of Gastroenterology, Hepatology, and Nutrition, The Children’s Hospital of Philadelphia, Philadelphia, PA 19104bCincinnati Children’s Hospital Medical Center, Cincinnati, OH 45229-3026</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2626807123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2626807123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625643123?af=R">
      <title>Developmental plasticity has important implications for plant domestication research</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625643123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Developmental plasticity has important implications for plant domestication research</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625643123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Kristen J. Gremillionahttps://ror.org/00rs6vg23Department of Anthropology, The Ohio State University, Columbus, OH 43210</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2625643123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625646123?af=R">
      <title>Turning up the heat on asymmetries in lake ice phenology</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625646123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Turning up the heat on asymmetries in lake ice phenology</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625646123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Eric Postahttps://ror.org/05rrcem69Department of Wildlife, Fish, and Conservation Biology, 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>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2625646123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2623360123?af=R">
      <title>A further modification of the elastic field of an edge dislocation is incorrect</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2623360123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>A further modification of the elastic field of an edge dislocation is incorrect</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623360123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>Dallas R. Trinkleahttps://ror.org/047426m28Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-09-22T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2623360123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2623360123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627836123?af=R">
      <title>Coding choices and short-sequence artifacts undermine claims of a conventional Paleolithic sign system</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627836123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Coding choices and short-sequence artifacts undermine claims of a conventional Paleolithic sign system</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627836123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-11T07:00:00Z</dc:date>
      <dc:creator>Alexander Koplenigahttps://ror.org/00hvwkt50Department of Lexical Studies, Leibniz Institute for the German Language, Mannheim 68161, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2630757123?af=R">
      <title>Correction for Wang et al., The diversity of soil parasitic protists shapes ecosystem stability worldwide</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2630757123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Wang et al., The diversity of soil parasitic protists shapes ecosystem stability worldwide</dc:title>
      <dc:identifier>doi:10.1073/pnas.2630757123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-18T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625156123?af=R">
      <title>Reply to Trinkle: The elastic field of an edge dislocation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625156123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Trinkle: The elastic field of an edge dislocation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625156123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-14T07:00:00Z</dc:date>
      <dc:creator>John P. HirthJian Wangahttps://ror.org/00rs6vg23Materials Science and Engineering Department, Ohio State University, Columbus, OH 43210bhttps://ror.org/043mer456Mechanical and Materials Engineering Department, University of Nebraska-Lincoln, Lincoln, NE 68588</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2631363123?af=R">
      <title>QnAs with Gregg Alan Howe</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2631363123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. &lt;br/&gt;</description>
      <dc:title>QnAs with Gregg Alan Howe</dc:title>
      <dc:identifier>doi:10.1073/pnas.2631363123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-16T07:00:00Z</dc:date>
      <dc:creator>Sandeep Ravindran</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>38</prism:number>
      <prism:coverDate>2026-09-22T07:00:00Z</prism:coverDate>
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