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      <title>In This Issue</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceProgression from viral hepatitis/cirrhosis to hepatocellular carcinoma (HCC) is accompanied by major changes in the tumor microenvironment. Hepatitis B- and C-positive associated liver disease demonstrated abundant cytotoxic T cells ...</description>
      <dc:title>MicroRNA-driven regulation of immunosuppressive microenvironment in hepatocellular carcinoma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618249123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Gerard J. NuovoThomas C. HeinemanEsmerina TiliCarlo M. CroceaGNOME Diagnostics, Powell, OH 43081bOncolytics Biotech Inc., San Diego, CA 92121chttps://ror.org/028t46f04Department of Cancer Biology and Genetics, The Ohio State University Comprehensive Cancer Center and The Ohio State University College of Medicine, Wexner Medical Center, Columbus, OH 43210dhttps://ror.org/00rs6vg23Department of Anesthesiology, Wexner Medical Center, The Ohio State University College of Medicine, Columbus, OH 43210</dc:creator>
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      <prism:volume>123</prism:volume>
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      <title>Taxing the talent that builds American science</title>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Taxing the talent that builds American science</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Deepak Hegdeahttps://ror.org/0190ak572New York University Stern School of Business, New York, NY 10012bhttps://ror.org/04grmx538National Bureau of Economic Research, Cambridge, MA 02138</dc:creator>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;Sea-surface temperatures are rising except in the one place models predict they should rise the most: the tropical eastern Pacific Ocean. Elected to the National Academy of Sciences in 2026, Shang-Ping Xie reconciles climate models and observations in his ...</description>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceType 1 and 2 carbonaceous chondrites are primitive, organic-rich meteorites that may have delivered a significant amount of the carbon and nitrogen available for life’s emergence on Earth. Despite extensive chemical, structural, and isotopic ...</description>
      <dc:title>Meteoritic organic matter records primitive oxygen reservoirs of the solar system</dc:title>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-21T07:00:00Z</dc:date>
      <dc:creator>Daniel R. CrockerConel M. O‘D. AlexanderMark H. ThiemensDavid T. Johnstonahttps://ror.org/03vek6s52Department of Earth and Planetary Science, Harvard University, Cambridge, MA 02138bhttps://ror.org/04jr01610Earth and Planets Laboratory, Carnegie Institution for Science, Washington, DC 20015chttps://ror.org/0168r3w48Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093</dc:creator>
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      <prism:volume>123</prism:volume>
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      <title>Compound drought–heat wave hazards are concentrated in US regions with multiple social vulnerabilities and agricultural dependence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607273123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCompound drought and heat wave (CDHW) events intensify risks to health, agriculture, energy systems, and local economies, often producing more severe impacts than isolated extremes. Their growing relevance was evident during the 2023 southern ...</description>
      <dc:title>Compound drought–heat wave hazards are concentrated in US regions with multiple social vulnerabilities and agricultural dependence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607273123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-21T07:00:00Z</dc:date>
      <dc:creator>Amitesh SabutAshok MishraDavid Zilbermanahttps://ror.org/01f5ytq51Zachry Department of Civil Engineering, Texas A&amp;M University, College Station, TX 77843bhttps://ror.org/01an7q238Department of Agricultural and Resource Economics, University of California, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
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      <title>Cassiterite U–Pb geochronology: A framework for tin provenance in the Bronze Age world</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625071123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceTin was as strategic to Bronze Age societies as crude oil is today—rare, geologically concentrated, and essential for industrial-scale bronze production. For China’s Shang dynasty, the world’s most prolific Bronze Age metal producer, ...</description>
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      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-21T07:00:00Z</dc:date>
      <dc:creator>Zhenfei SunXiaolin HeChenyuan LiYanxiang LiLixin WangBotao CaiJianli ChenWei ChenRichen ZhongSiran Liuahttps://ror.org/02egmk993Institute for Cultural Heritage and History of Science and Technology, Key Laboratory of Archaeomaterials and Conservation, University of Science and Technology Beijing, Beijing 100083, Chinabhttps://ror.org/02v51f717School of Archaeology and Museology, Peking University, Beijing 100871, Chinachttps://ror.org/033vjfk17School of History, Wuhan University, Wuhan 430072, ChinadSchool of Cultural Heritage, Northwest University, Xi’an 710127, ChinaeAnhui Provincial Institute of Archaeology, Hefei 230601, Chinafhttps://ror.org/04gcegc37State Key Laboratory of Geological Processes and Mineral Resources, China University of Geosciences, Wuhan 430078, ChinagSchool of Resources and Safety Engineering, University of Science and Technology, Beijing 100083, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2625071123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618845123?af=R">
      <title>An RNA thermogenic therapy to preserve lean mass and enhance metabolic health during GLP-1 weight loss</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618845123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCurrent antiobesity therapies reduce body weight but often induce loss of lean mass and fail to achieve durable metabolic improvements after treatment ends. We show that an adipose-targeted RNA therapeutic targeting ZFP423, a transcriptional ...</description>
      <dc:title>An RNA thermogenic therapy to preserve lean mass and enhance metabolic health during GLP-1 weight loss</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618845123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-25T07:00:00Z</dc:date>
      <dc:creator>Anneke K. ThorneNathan J. WaldeckJesse P. RoseMarisa J. StachowskiHannah GuakAlexander R. KeebleBritta KuusikElla SimonBiliana MarchevaJoseph V. MastroniPei ZhuLing Wa ChongYumiko KobayashiNicholas J. ConleyAndrew B. CohenYasuhiro OmuraChiaki OmuraWeimin SongMichael WellemsKathryn M. RamseyGrant D. BarishLisa R. BeutlerRana K. GuptaClara B. PeekElizabeth M. McNallyChelsea HeplerMark PerelisJoseph BassaDepartment of Medicine, Division of Endocrinology, Metabolism, and Molecular Medicine, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611bCenter for Genetic Medicine, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611cDepartment of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611dIonis Pharmaceuticals, Carlsbad, CA 92010ePhenome Technologies Inc., Lincolnshire, IL 60091fhttps://ror.org/00py81415Division of Endocrinology, Department of Medicine, Duke Molecular Physiology Institute, Duke University, Durham, NC 27701ghttps://ror.org/00jmfr291Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618845123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2516128123?af=R">
      <title>Large-scale semidefinite programming with graphics processing units</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2516128123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMany scientific and engineering fields, including optimization, machine learning, and quantum computing, use semidefinite programming (SDP) to tackle complex problems. Unfortunately, as these problems grow, they rapidly exceed the capabilities ...</description>
      <dc:title>Large-scale semidefinite programming with graphics processing units</dc:title>
      <dc:identifier>doi:10.1073/pnas.2516128123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Qiushi HanZhenwei LinHanwen LiuCaihua ChenQi DengDongdong GeYinyu Yeahttps://ror.org/047426m28Department of Computer Science, University of Illinois at Urbana-Champaign, Urbana, IL 61801bhttps://ror.org/00wtvfq62School of Information Management and Engineering, Shanghai University of Finance and Economics, Shanghai 200433, Chinachttps://ror.org/047426m28Department of Electrical &amp; Computer Engineering, University of Illinois at Urbana-Champaign, Urbana, IL 61801dhttps://ror.org/01rxvg760School of Management and Engineering, Nanjing University, Nanjing, Jiangsu 210008, Chinaehttps://ror.org/0220qvk04Antai College of Economics and Management, Shanghai Jiao Tong University, Shanghai 200030, Chinafhttps://ror.org/00f54p054Department of Management Science and Engineering, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2516128123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2516128123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610455123?af=R">
      <title>Projected effects of removing school-entry vaccination requirements on measles transmission in Florida</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610455123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceFlorida’s proposal to remove school vaccine mandates arrives at a moment when measles vaccination coverage in the state has fallen below the level needed to prevent sustained outbreaks. Using a mathematical model, we show that repealing the ...</description>
      <dc:title>Projected effects of removing school-entry vaccination requirements on measles transmission in Florida</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610455123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Alice OvesonAbba B. Gumelahttps://ror.org/047s2c258Department of Mathematics, University of Maryland, College Park, MD 20742bInstitute for Health Computing, University of Maryland, North Bethesda, MD 20852chttps://ror.org/00g0p6g84Department of Mathematics and Applied Mathematics, University of Pretoria, Pretoria 0002, South Africa</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610455123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610455123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613208123?af=R">
      <title>Climate-amplified wildland–urban interface disasters create persistent internal metal mixtures associated with pulmonary impairment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613208123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceWildland–urban interface (WUI) disasters create a different exposure problem than wildfires dominated primarily by biomass burning. These disasters also burn built infrastructure and mobilize legacy contaminants, generating exposure profiles ...</description>
      <dc:title>Climate-amplified wildland–urban interface disasters create persistent internal metal mixtures associated with pulmonary impairment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613208123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Alika K. MaunakeaBinh LeRafael E. de la HozAlison G. LeeZitong ZhangMartina KamakaMarsha LoweryLesley UmedaBrennan YamamotoKathrin SchillingRuben JuarezaDepartment of Anatomy, Biochemistry and Physiology, John A. Burns School of Medicine, Honolulu, HI 96813bhttps://ror.org/01wspgy28University of Hawaii Economic Research Organization, University of Hawaii at Manoa, Honolulu, HI 96822chttps://ror.org/01wspgy28Department of Economics, University of Hawaii at Manoa, Honolulu, HI 96822dhttps://ror.org/04a9tmd77Department of Environmental Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029ehttps://ror.org/04a9tmd77Department of Medicine, Icahn School of Medicine at Mount Sinai, New York, NY 10029fDepartment of Native Hawaiian Health, John A. Burns School of Medicine, Honolulu, HI 96813ghttps://ror.org/03tzaeb71Maui Wildfire Exposure Study, University of Hawaii, Honolulu, HI 96822hhttps://ror.org/00hj8s172Department of Environmental Health Sciences, Columbia University, New York, NY 10032</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613208123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613208123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611716123?af=R">
      <title>A role for heavy chain-modification in protecting hyaluronan from free radical fragmentation during inflammation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611716123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThe glycosaminoglycan hyaluronan (HA) is a major component of the extracellular matrix with roles ranging from tissue structure maintenance to cell signaling. In inflammatory conditions, HA is frequently found to be decorated with so-called ...</description>
      <dc:title>A role for heavy chain-modification in protecting hyaluronan from free radical fragmentation during inflammation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611716123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Suruchi PoddarDorothea A. ErxlebenRebecca J. DoddHeidi L. ReesinkDixy E. GreenPaul L. DeAngelisAnthony J. DayAdam R. Hallahttps://ror.org/0207ad724Virginia Tech-Wake Forest University School of Biomedical Engineering and Sciences, Wake Forest University School of Medicine, Winston-Salem, NC 27101bhttps://ror.org/027m9bs27Manchester Cell-Matrix Centre and Lydia Becker Institute of Immunology and Inflammation, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester M13 9PT, United KingdomcDepartment of Surgical and Radiological Sciences, School of Veterinary Medicine, University of California-Davis, Davis, CA 95616dhttps://ror.org/05bnh6r87Department of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853ehttps://ror.org/02aqsxs83Department of Biochemistry and Physiology, University of Oklahoma Health Campus, Oklahoma City, OK 73104fhttps://ror.org/0207ad724Atrium Health Wake Forest Comprehensive Cancer Center, Wake Forest University School of Medicine, Winston-Salem, NC 27157</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611716123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611716123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2624733123?af=R">
      <title>Three decades of urban densification reduced winter direct sunlight access across China’s old urban cores</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624733123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceUrban densification supports compact and sustainable growth, but its hidden sunlight-access consequences in existing neighborhoods remain poorly understood. This study provides a comparable cross-city assessment of densification-driven winter ...</description>
      <dc:title>Three decades of urban densification reduced winter direct sunlight access across China’s old urban cores</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624733123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Kechao WangXiangyuan WuLiutao ChenTzu-Hsin Karen ChenWu XiaoaDepartment of Land Management, Department of Land Management, School of Public Affairs, Zhejiang University, Hangzhou 310058, Chinabhttps://ror.org/00cvxb145Department of Urban Design and Planning, University of Washington, Seattle, WA 98195chttps://ror.org/00cvxb145Department of Environmental and Occupational Health Sciences, University of Washington, Seattle, WA 98195dhttps://ror.org/00a2xv884Inclusive and Smart Urban-Rural Governance Lab, Zhejiang University, Hangzhou 310058, Chinaehttps://ror.org/00a2xv884Zhejiang Key Laboratory of Agricultural Remote Sensing and Information Technology, Zhejiang University, Hangzhou 310058, Chinafhttps://ror.org/00a2xv884Land Academy for National Development, Zhejiang University, Hangzhou 310058, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2624733123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2624733123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607106123?af=R">
      <title>Cnidarian mechanosensory cells as ancestors of vertebrate hair cells: Molecular targeting of an ancient mechanotransduction complex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607106123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceTransmembrane channel-like (TMC) proteins are a family of ion channels and scramblases that serve as sensors for mechanical forces in vertebrate hair cells. They play a key role as mechanosensors in hearing and balance, with TMC1 and TMC2 ...</description>
      <dc:title>Cnidarian mechanosensory cells as ancestors of vertebrate hair cells: Molecular targeting of an ancient mechanotransduction complex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607106123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Zeeshan Z. BandayAmelia M. RandichRaymond E. HulseZhen TongJamie A. HavrilakTomas Osorno-FerroEmily WattoEvgeniya A. DemchenkoZachary FournierNicolas GrilletMarcos SotomayorMichael J. LaydenJocelyn MalamyEduardo Perozoahttps://ror.org/024mw5h28Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637bhttps://ror.org/024mw5h28Center for Mechanical Excitability, The University of Chicago, Chicago, IL 60637chttps://ror.org/046dg4z72Marine Biological Laboratory, Woods Hole, MA 02543dhttps://ror.org/012afjb06Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015ehttps://ror.org/024mw5h28Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637fhttps://ror.org/02k3smh20Department of Otolaryngology Head and Neck Surgery, Department of Physiology, University of Kentucky College of Medicine, Lexington, KY 40536</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607106123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607106123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613077123?af=R">
      <title>Longitudinal adaptations in neural and behavioral systems following hearing restoration using cochlear implants</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613077123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSuccessful cochlear implant (CI) use requires more than hearing sounds; it also requires learning to follow speech in busy everyday settings. However, much of what we know about brain adaptation after implantation comes from studies using ...</description>
      <dc:title>Longitudinal adaptations in neural and behavioral systems following hearing restoration using cochlear implants</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613077123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Shimin MoClaude AlainAndrew Dimitrijevicahttps://ror.org/03dbr7087Institute of Medical Science, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, Canadabhttps://ror.org/05n0tzs53Evaluative Clinical Sciences Platform, Sunnybrook Research Institute, Toronto, ON M4N 3M5, Canadachttps://ror.org/001fxzj49Rotman Research Institute, Baycrest Academy for Research and Education, Toronto, ON M6A 2E1, Canadadhttps://ror.org/03dbr7087Department of Psychology, University of Toronto, Toronto, ON M5S 3G3, Canadaehttps://ror.org/03dbr7087Music and Health Research Collaboratory, Faculty of Music, University of Toronto, Toronto, ON M5S 2C5, Canadafhttps://ror.org/03dbr7087Department of Otolaryngology-Head and Neck Surgery, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A1, CanadagCommunication Sciences and Disorders, College of Liberal Arts and Sciences, Wayne State Universsity, Detroit, MI 428201hhttps://ror.org/01070mq45Biological Sciences, College of Liberal Arts and Sciences, Wayne State University, Detroit, MI 428201</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613077123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613077123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611986123?af=R">
      <title>Phototropic and skototropic growth in inorganic films</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611986123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificancePhototropism, i.e., growth toward light, is a hallmark behavior of living organisms. Certain living photosynthetic organisms, such as forest vines, exhibit the uncommon emergent behavior of skototropism, in which growth proceeds toward ...</description>
      <dc:title>Phototropic and skototropic growth in inorganic films</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611986123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Madeline C. MeierWen-Hui Sophia ChengMatthias H. RichterJonathan R. ThompsonAriel A. StruzykNicolas A. BataraSisir YalamanchiliHarry A. AtwaterNathan S. LewisAzhar I. Carimahttps://ror.org/05dxps055Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125bhttps://ror.org/01b8kcc49Department of Materials Science and Engineering, National Cheng Kung University, Tainan 701, Taiwanchttps://ror.org/05dxps055Division of Engineering and Applied Sciences, California Institute of Technology, Pasadena, CA 91125dhttps://ror.org/05dxps055Beckman Institute, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611986123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611986123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617804123?af=R">
      <title>The economic returns to citizenship: Evidence from a meta-analysis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617804123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCitizenship is widely viewed as a policy lever for immigrant economic mobility, and policy and scholarly summaries often describe naturalization as improving wages and access to better jobs. Our synthesis shows why that summary needs a design ...</description>
      <dc:title>The economic returns to citizenship: Evidence from a meta-analysis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617804123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Jens HainmuellerDavid D. Laitinahttps://ror.org/00f54p054Department of Political Science, Stanford University, Stanford, CA 94305bhttps://ror.org/00f54p054Immigration Policy Lab, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617804123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617804123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608087123?af=R">
      <title>Zinc mediates the allosteric activation of Shiftless to suppress programmed −1 ribosomal frameshifting</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608087123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMany pathogenic viruses, such as HIV–1 and SARS-CoV-2, rely on programmed –1 ribosomal frameshifting (–1 PRF) to produce certain proteins essential for their replication, making this process an attractive target for broad-spectrum antivirals. ...</description>
      <dc:title>Zinc mediates the allosteric activation of Shiftless to suppress programmed −1 ribosomal frameshifting</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608087123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Shi-Ting HeYongfeng ZhengRuhong YingXu XuQiman FangXiujuan LiRunxi LuoXinqi ZhuYumin HuangYuzheng ZhouXiaonan Dongahttps://ror.org/03ybmxt82Guangzhou National Laboratory, Guangzhou, Guangdong 510005, Chinabhttps://ror.org/0064kty71Zhongshan School of Medicine, Sun Yat-Sen University, Guangzhou, Guangdong 510080, Chinachttps://ror.org/0064kty71School of Life Sciences, Sun Yat-Sen University, Guangzhou, Guangdong 510275, Chinadhttps://ror.org/00z0j0d77State Key Laboratory of Respiratory Disease, The First Affiliated Hospital of Guangzhou Medical University, Guangzhou, Guangdong 510120, Chinaehttps://ror.org/00zat6v61School of Basic Medical Sciences, Guangzhou Medical University, Guangzhou, Guangdong 511436, Chinafhttps://ror.org/049tv2d57Institute for Hepatology, National Clinical Research Center for Infectious Disease Shenzhen Third People’s Hospital, and Department of Biochemistry, The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, Shenzhen 518112, Chinaghttps://ror.org/013q1eq08Institute of Infection and Health, Fudan University, Shanghai 200438, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608087123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525555123?af=R">
      <title>The Mader model of muscle energy metabolism simulates key metabolic exercise phenomena</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525555123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceAlois Mader’s mechanistic model of human muscle energy metabolism was developed more than 40 years ago yet has remained inaccessible to most researchers. Here, we present MetaboliSim, an open-source implementation of Mader’s model that lets ...</description>
      <dc:title>The Mader model of muscle energy metabolism simulates key metabolic exercise phenomena</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525555123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Jeffrey A. RothschildAnna Katharina DunstJessie AxsomHenning WackerhageHermann Heckahttps://ror.org/01zvqw119Sports Performance Research Institute New Zealand, Auckland University of Technology, Auckland 0632, New ZealandbHigh Performance Sport New Zealand, Auckland 0632, New ZealandcInstitute for Applied Training Science, Leipzig 04109, Germanydhttps://ror.org/01z7r7q48Department of Pathology and Laboratory Medicine, Children’s Hospital of Philadelphia, Philadelphia, PA 19104ehttps://ror.org/00b30xv10Department of Neurology, University of Pennsylvania, Philadelphia, PA 19104fhttps://ror.org/02kkvpp62School of Medicine and Health, Technical University of Munich, Munich 80333, Germanyghttps://ror.org/04tsk2644Professor Emeritus, Faculty of Sports Science, Ruhr University Bochum, Bochum 44801, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525555123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615021123?af=R">
      <title>Fragmentation outweighs forest cover in shaping land surface temperature across half of global forests</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615021123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceReducing deforestation and promoting forest restoration are central to international climate mitigation efforts. Yet these policies and agendas primarily target changes in forest area, leaving the thermal influences of fragmentation ...</description>
      <dc:title>Fragmentation outweighs forest cover in shaping land surface temperature across half of global forests</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615021123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Jiawei LiJiaxin WuJun MaaState Key Laboratory of Wetland Conservation and Restoration, National Observations and Research Station for Wetland Ecosystems of the Yangtze Estuary, Ministry of Education Key Laboratory for Biodiversity Science and Ecological Engineering, School of Life Sciences, Fudan University, Shanghai 200438, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615021123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615021123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2625638123?af=R">
      <title>Human antibody heavy chain variable region exon interacts with the 3′ regulatory region to form a stable somatic hypermutation center</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2625638123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceUpon encountering pathogens, B cells enter specialized lymphoid structures known as germinal centers (GCs). GC B cells express activation-induced cytidine deaminase (AID) that initiates somatic hypermutation (SHM) of the portion of antibody ...</description>
      <dc:title>Human antibody heavy chain variable region exon interacts with the 3′ regulatory region to form a stable somatic hypermutation center</dc:title>
      <dc:identifier>doi:10.1073/pnas.2625638123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Ying GuanMariia MikhovaZhuo YangKai XuShuxian XieXin LinAdam Yongxin YeTaimor WilliamsJianshu WangDavid G. SchatzFrederick W. AltXi Chenahttps://ror.org/00dvg7y05Howard Hughes Medical Institute, Boston Children's Hospital, Boston, MA 02115bhttps://ror.org/00dvg7y05Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115cDepartment of Genetics, Harvard Medical School, Boston, MA 02115dDepartment of Immunobiology, Yale School of Medicine, New Haven, CT 06520-8011</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2625638123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2625638123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622558123?af=R">
      <title>Masking phosphatidylserine prevents neuronal loss in two distinct Drosophila models of neurodegeneration</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622558123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceNeuronal loss is a defining feature of neurodegenerative diseases, yet its underlying mechanisms remain incompletely understood. Here, we demonstrate in twoDrosophilamodels of neurodegeneration that stressed but viable neurons are ...</description>
      <dc:title>Masking phosphatidylserine prevents neuronal loss in two distinct Drosophila models of neurodegeneration</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622558123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Naden KhatebMiri ShwartsburdEden GrigShelly Vogelesang-GanonTsneem FauziMalak AyoubKetty Hakim-MishnaevskiEstee Kurantahttps://ror.org/02f009v59The Herta and Paul Amir School of Medicine, Faculty of Natural Sciences, University of Haifa, Haifa 34988, Israelbhttps://ror.org/02f009v59Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 34988, Israel</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622558123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622558123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2627537123?af=R">
      <title>Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2627537123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceAlthough the mode of action of pore-forming proteins (PFPs) has been increasingly elucidated, the structural mechanisms underlying their maturation into membrane-spanning pores remain unclear. This gap is important because pore-forming toxins ...</description>
      <dc:title>Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2627537123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Tomohito YamadaRen NakanishiYukihiko SugitaYuki NinomiyaToru YoshidaTakeshi NodaHideaki Tsugeahttps://ror.org/05t70xh16Department of Frontier Life Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japanbhttps://ror.org/00pqz0q24Laboratory of Ultrastructural Virology, Institute for Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japanchttps://ror.org/02kpeqv85Laboratory of Ultrastructural Virology, Graduate School of Biostudies, Kyoto University, Kyoto 606-8507, Japandhttps://ror.org/02kpeqv85Hakubi Center for Advanced Research, Kyoto University, Kyoto 606-8507, Japanehttps://ror.org/00pqz0q24Laboratory of Supramolecular Structural Biology, Research Center for Infectious Diseases, Institute for Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japanfhttps://ror.org/04gpcyk21Department of Chemical and Biological Sciences, Faculty of Science, Japan Women’s University, Tokyo 112-8681, Japanghttps://ror.org/05t70xh16Institute for Protein Dynamics, Kyoto Sangyo University, Kyoto 603-8555, Japanhhttps://ror.org/05t70xh16Center for Molecular Research in Infectious Diseases, Kyoto Sangyo University, Kyoto 603-8555, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2627537123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2627537123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615939123?af=R">
      <title>Spatiotemporally primed coelomic epithelium and supporting-like cells establish the dual origin of granulosa cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615939123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceHow ovaries form remains poorly understood, particularly how multipotent epithelial progenitors of the coelomic epithelium generate pregranulosa and steroidogenic theca cells, the two main somatic components of the follicle. Here, we show that ...</description>
      <dc:title>Spatiotemporally primed coelomic epithelium and supporting-like cells establish the dual origin of granulosa cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615939123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Cyril DjariChloé MayèreMaëva GuyAitana Perea-GomezLaura BelluttiPaul BarreauHerta AdemiAgathe RozierAnthony S. MartinezTyler J. GibsonFrançoise KühneCassandre GuérinDagmar WilhelmGabriel LiveraJennifer McKeyMarie-Christine ChaboissierSerge Nefahttps://ror.org/01swzsf04Department of Genetic Medicine and Development, University of Geneva, Geneva 1211, Switzerlandbhttps://ror.org/01swzsf04Institute of Genetics and Genomics in Geneva, Institute of Genetics and Genomics of Geneva, University of Geneva, Geneva 1211, Switzerlandchttps://ror.org/03bnma344Université Côte d‘Azur, CNRS, Inserm, Institut de Biologie Valrose, Nice 06108, Francedhttps://ror.org/05f82e368University Paris Cité, Inserm, French Alternative Energies and Atomic Energy Commission, Genetic Stability Stem Cells and Radiation, Laboratory of Development of the Gonads, Université Paris Cité, Fontenay-aux-Roses F-92265, Franceehttps://ror.org/03xjwb503University Paris Cité, Inserm, French Alternative Energies and Atomic Energy Commission, Genetic Stability Stem Cells and Radiation, Genetic Stability, Stem Cells and Radiation, Laboratory of Development of the Gonads/Institute of Cellular and Molecular Radiobiology/François Jacob Institute of Biology, Université Paris-Saclay, Fontenay-aux-Roses F-92265, Francefhttps://ror.org/03wmf1y16Section of Developmental Biology, Department of Pediatrics, University of Colorado Anschutz Medical Campus, Aurora, CO 80045ghttps://ror.org/01ej9dk98Department of Anatomy and Physiology, University of Melbourne, Parkville, VIC 3010, Australia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615939123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615939123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613113123?af=R">
      <title>Classifying strategy use in multiattribute subjective choice: Application to conjoint experiments in political science</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613113123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceUnderstanding how individuals navigate multiattribute decisions is essential for interpreting public preferences. While researchers frequently use conjoint experiments to measure these preferences, traditional approaches in the applied social ...</description>
      <dc:title>Classifying strategy use in multiattribute subjective choice: Application to conjoint experiments in political science</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613113123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Nidhi V. BanavarKirk Bansakahttps://ror.org/01an7q238Department of Political Science, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613113123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613113123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528514123?af=R">
      <title>BAG3 coordinates astrocytic proteostasis of Alzheimer’s disease–linked proteins via proteasome, autophagy, and retromer interactions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528514123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceTaken together, these data converge on a model in which Bcl-2-associated athanogene 3 (BAG3) acts as a central regulator of astrocytic adaptation to neurodegenerative stressors such as Aβ. The integration of induced pluripotent stem cell-based ...</description>
      <dc:title>BAG3 coordinates astrocytic proteostasis of Alzheimer’s disease–linked proteins via proteasome, autophagy, and retromer interactions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528514123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Zachary M. AugurGarrett M. FogoCourtney R. BenoitMasin A. KearneyGizem TerziogluZachary R. MurphyMason R. ArberyNatacha Comandante-LouDuc M. DuongNicholas T. SeyfriedPhilip L. De JagerTracy L. Young-Pearseahttps://ror.org/04b6nzv94Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115bhttps://ror.org/01esghr10Center for Translational and Computational Neuroimmunology, Department of Neurology and the Taub Institute for the Study of Alzheimer’s Disease and the Aging Brain, Columbia University Irving Medical Center, New York, NY 10032cDepartment of Biochemistry, Emory School of Medicine, Atlanta, GA 30322</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528514123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528514123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601665123?af=R">
      <title>Nuclear cGAS inhibits stimulation-induced inflammatory gene transcription via HDAC1</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601665123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceInnate immune responses must be sufficiently robust to control infection while remaining tightly constrained to avoid tissue damage. How immune cells maintain this balance at the transcriptional level remains incompletely understood. Cyclic ...</description>
      <dc:title>Nuclear cGAS inhibits stimulation-induced inflammatory gene transcription via HDAC1</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601665123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Shangze GaoHongpeng LiShuaiting YanShengping HouHang Yinahttps://ror.org/03cve4549State Key Laboratory of Membrane Biology, School of Pharmaceutical Sciences, Tsinghua-Peking Center for Life Sciences, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/013e4n276Beijing Institute of Ophthalmology, Beijing Tongren Hospital, Capital Medical University, Beijing 100730, Chinachttps://ror.org/03cve4549School of Medicine, Tsinghua University, Beijing 100082, Chinadhttps://ror.org/022k4wk35Institute for Advanced Study, Beijing Normal University, Beijing 100875, Chinaehttps://ror.org/022k4wk35College of Chemistry, Beijing Normal University, Beijing 100875, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601665123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601665123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602542123?af=R">
      <title>Mantis: A foundation model for mechanistic disease forecasting</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602542123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceReliable infectious disease forecasts are crucial for decision-making but models often struggle when data is scarce, such as during new outbreaks. This paper presents Mantis, an AI model trained on synthetic data generated by epidemiological ...</description>
      <dc:title>Mantis: A foundation model for mechanistic disease forecasting</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602542123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Carson DudleyReiden MagdalenoChristopher HardingAnanya SharmaEmily MartinMarisa Eisenbergahttps://ror.org/00jmfr291Department of Mathematics, University of Michigan, Ann Arbor, MI 48109bhttps://ror.org/00jmfr291Department of Epidemiology for School of Public Health, University of Michigan, Ann Arbor, MI 48109chttps://ror.org/00jmfr291Department of Electrical Engineering and Computer Science, University of Michigan, Ann Arbor, MI 48109dhttps://ror.org/00jmfr291Center for the Study of Complex Systems, University of Michigan, Ann Arbor, MI 48109</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602542123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602542123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526156123?af=R">
      <title>Associative synaptic plasticity creates dynamic persistent activity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526156123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceNeurons and synapses interact through activity-dependent plasticity mechanisms. Here, we study a recurrent neural network in which ongoing plastic weight updates make small adjustments to static background connections. We show that the ...</description>
      <dc:title>Associative synaptic plasticity creates dynamic persistent activity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526156123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Albert J. WakhlooDavid G. ClarkL. F. Abbottahttps://ror.org/00hj8s172Center for Theoretical Neuroscience, Zuckerman Institute, Columbia University, New York, NY 10027bhttps://ror.org/00sekdz59Center for Computational Neuroscience, Flatiron Institute, New York, NY 10010chttps://ror.org/00hj8s172Kavli Institute for Brain Science, Columbia University, New York, NY 10027dhttps://ror.org/03vek6s52Kempner Institute for the Study of Natural and Artificial Intelligence, Harvard University, Boston, MA 02134</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526156123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526156123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534602123?af=R">
      <title>Twisted Rényi negativity as a reliable proxy for mixed-state entanglement in fermionic systems</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534602123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceEntanglement is a defining feature of quantum mechanics, yet quantifying it in realistic, finite-temperature environments (mixed states) remains a formidable challenge, particularly for fermionic systems like electrons in solids. A long-...</description>
      <dc:title>Twisted Rényi negativity as a reliable proxy for mixed-state entanglement in fermionic systems</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534602123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Fo-Hong WangXiao Yan Xuahttps://ror.org/0220qvk04Tsung-Dao Lee Institute, Key Laboratory of Artificial Structures and Quantum Control (Ministry of Education), School of Physics and Astronomy, Shanghai Jiao Tong University, Shanghai 200240, ChinabHefei National Laboratory, Hefei 230088, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534602123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534602123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615054123?af=R">
      <title>Chain organization of dimple-ended magnetite magnetosomes supports field-dependent cell linking in unicellular magnetotactic bacteria</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615054123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMagnetotactic bacteria are widely viewed as single-celled “living compasses” whose magnetosome chains orient along geomagnetic field lines. We describe a bacterium that produces comparatively large, dimple-ended magnetite magnetosomes that ...</description>
      <dc:title>Chain organization of dimple-ended magnetite magnetosomes supports field-dependent cell linking in unicellular magnetotactic bacteria</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615054123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Jinhua LiYuqin WangPeiyu LiuQianqian LanXiang ZhaoNicolas MenguyJian WangEric LeroyJiawei LiuRafal E. Dunin-BorkowskiWyn WilliamsAndrew P. RobertsRixiang ZhuYongxin Panahttps://ror.org/034t30j35Key Laboratory of Deep Petroleum Intelligent Exploration and Development, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, ChinabLaboratory for Marine Geology, Qingdao Marine Science and Technology Center, Qingdao 266061, Chinachttps://ror.org/03swgqh13Southern Marine Science and Engineering Guangdong Laboratory, Zhuhai 519082, Chinadhttps://ror.org/05qbk4x57College of Earth and Planetary Sciences, University of Chinese Academy of Sciences, Beijing 100049, Chinaehttps://ror.org/02nv7yv05Ernst Ruska-Centre for Microscopy and Spectroscopy with Electrons and Peter Grünberg Institute, Forschungszentrum Jülich GmbH, Jülich 52425, Germanyfhttps://ror.org/019wvm592Research School of Earth Sciences, Australian National University, Canberra, ACT 2601, Australiaghttps://ror.org/05abgg682Sorbonne Université, UMR CNRS 7590, Muséum national d’Histoire naturelle, Institut de Recherche pour le Développement, Institut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Paris 75005, Francehhttps://ror.org/010x8gc63Canadian Light Source Inc., University of Saskatchewan, Saskatoon S7N 2V3, Canadaihttps://ror.org/04c3cen15Institut de Chimie et des Matériaux Paris-Est, University Paris East, UMR 7182, CNRS, Thiais Cedex 94320, Francejhttps://ror.org/034t30j35Key Laboratory of Planetary Sciences and Frontier Technology, Institute of Geology and Geophysics, Chinese Academy of Sciences, Beijing 100029, Chinakhttps://ror.org/01nrxwf90School of GeoSciences, University of Edinburgh, Edinburgh EH9 3JW, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615054123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615054123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601083123?af=R">
      <title>Slc35a1-mediated endothelial sialylation controls the fate and integrity of the intestinal microvascular network in adult mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601083123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSlc35a1 transports activated sialic acids required for terminal glycan sialylation in the Golgi. Although endothelial cells are highly sialylated, whetherSlc35a1-dependent sialylation regulates vascular fate in adult tissues is unknown. Using ...</description>
      <dc:title>Slc35a1-mediated endothelial sialylation controls the fate and integrity of the intestinal microvascular network in adult mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601083123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Yizhi JiangShipra RathoreXin GengNicole KirbyChihiro ItoJ. Michael McDanielMeixiang ZhouSamuel McGeeR. Sathish SrinivasanLijun Xiaahttps://ror.org/035z6xf33Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK 73014bhttps://ror.org/0457zbj98Department of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104chttps://ror.org/04chrp450Department of Biochemistry II, Nagoya University School of Medicine, Showa-ku, Nagoya 466-0065, Japandhttps://ror.org/0457zbj98Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601083123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601083123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524371123?af=R">
      <title>PKD2-like proteins target Chlamydomonas PKD2 to distinct subciliary regions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524371123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceChlamydomonasPKD2 assembles into specific subciliary regions along the length and circumference of cilia. To establish this spatial pattern, PKD2 partners with several PKD2-like 5-transmembrane helix (5TMH) proteins. MST3 organizes PKD2 and ...</description>
      <dc:title>PKD2-like proteins target Chlamydomonas PKD2 to distinct subciliary regions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524371123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Poulomi DasHaixia ZhouSneha SureshkumarNathan ChasenJin DaiAlan BrownKarl LechtreckaDepartment of Cellular Biology, University of Georgia, Athens, GA 30602bDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524371123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524371123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613824123?af=R">
      <title>Healing cascades and infections in wounds monitored using a wearable sensor of gaseous flux</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613824123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceLimited capabilities in continuous, quantitative assessment of a wound site create challenges in early diagnosis and effective management, particularly in cases of infection that rapidly progress before symptoms appear. Noncontact approaches ...</description>
      <dc:title>Healing cascades and infections in wounds monitored using a wearable sensor of gaseous flux</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613824123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Seunghee ChoAnsen TanZixi ChenKyung Rok PyunShupeng LiFujie YinAiwa ZhangNeena FeldmanEvan J. NeuhartAmara Devi MorenoJoyce Eunsung YoonJaeho ShinJoseph Woojin SongJacob TruebYonggang HuangGuillermo A. AmeerJohn A. RogersaQuerrey-Simpson Institute for Bioelectronics, Northwestern University, Evanston, IL 60208bQuerrey Simpson Institute for Regenerative Engineering at Northwestern University, Chicago, IL 60611cDepartment of Biomedical Engineering, Northwestern University, Evanston, IL 60208dCenter for Advanced Regenerative Engineering, Northwestern University, Evanston, IL 60208eDepartment of Civil and Environmental Engineering, Northwestern University, Evanston, IL 60208fDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208gDepartment of Mechanical Engineering, Northwestern University, Evanston, IL 60208hhttps://ror.org/047426m28Department of Bioengineering, University of Illinois Urbana-Champaign, Champaign, IL 61801iExperimental Advanced Engineering and Science Lab, Molecular Recognition Research Center, Korea Institute of Science and Technology, Seoul, South Korea 02792jDepartment of Materials Science and Engineering, Northwestern University, Evanston, IL 60208kInternational Institute for Nanotechnology, Northwestern University, Evanston, IL 60208lDepartment of Dermatology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611mDepartment of Neurological Surgery, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613824123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613824123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615454123?af=R">
      <title>Biosynthetic origin of anticancer dolastatin 15 reveals a noncanonical NRPS architecture enabling 2-keto acid activation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615454123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMarine natural products have inspired important medicines, yet for many compounds the producing organisms and biosynthetic genes remain unknown, limiting mechanistic understanding and biotechnological access. Here, we identify the marine ...</description>
      <dc:title>Biosynthetic origin of anticancer dolastatin 15 reveals a noncanonical NRPS architecture enabling 2-keto acid activation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615454123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Manyun ChenJie LiuHsin-Ying TsaiCheng-Yu LiJeremiah D. BatucanCampbell W. EckhardtTam H. D. PhamEmma K. EllisRanjala RatnayakeValerie J. PaulSteven D. BrunerMohamed S. DoniaHendrik LueschYousong Dingahttps://ror.org/02y3ad647Department of Medicinal Chemistry, Center for Natural Products, Drug Discovery, and Development, University of Florida, Gainesville, FL 32610bhttps://ror.org/00hx57361Department of Molecular Biology, Princeton University, Princeton, NJ 08544chttps://ror.org/02y3ad647Department of Chemistry, University of Florida, Gainesville, FL 32611dhttps://ror.org/00ga81413Smithsonian Marine Station, Fort Pierce, FL 34949ehttps://ror.org/01tgyzw49Program in Cancer and Stem Cell Biology, Duke-National University of Singapore Medical School, Singapore 169857, Singapore</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615454123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615454123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619440123?af=R">
      <title>The phenotypic landscape of the model firmicute Bacillus subtilis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619440123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceLarge-scale chemical genomics screens facilitate the characterization of genes by generating phenotypic data across a library of gene mutants. Here, using CRISPRi, we designed a compact pooled library targeting all genes inB. subtilisand ...</description>
      <dc:title>The phenotypic landscape of the model firmicute Bacillus subtilis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619440123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Lili M. KimByoung-Mo KooHannah N. BurkhartDaniela VollmerWaldemar VollmerHoria TodorCarol A. Grossahttps://ror.org/043mz5j54Department of Microbiology and Immunology, University of California, San Francisco, CA 94158bhttps://ror.org/00rqy9422Institute for Molecular Bioscience, The University of Queensland, Brisbane 4067, QLD, Australiachttps://ror.org/043mz5j54Department of Cell and Tissue Biology, University of California, San Francisco, CA 94158dhttps://ror.org/043mz5j54Quantitative Biosciences Institute, University of California, San Francisco, CA 94158</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619440123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619440123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612869123?af=R">
      <title>The Ca2+ channel CYCLIC NUCLEOTIDE GATED CHANNEL13 regulates vasculature-mediated systemic Ca2+ and jasmonate signaling on herbivory</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612869123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificancePlants must respond to insect herbivory by activating local and systemic immunity. Calcium (Ca2+) signaling plays a central role in this defense network, yet long-distance herbivory signaling inArabidopsisis largely attributed to glutamate ...</description>
      <dc:title>The Ca2+ channel CYCLIC NUCLEOTIDE GATED CHANNEL13 regulates vasculature-mediated systemic Ca2+ and jasmonate signaling on herbivory</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612869123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Misha KumariRamgopal PrajapatiMahendra PawarBhawana SharmaBianca Maria Orlando MarchesanoYang YangYong-Fei WangAlex CostaJyothilakshmi Vadasseryahttps://ror.org/04zw11527Biotechnology Research and Innovation Council-National Institute of Plant Genome Research, New Delhi 110067, Indiabhttps://ror.org/00wjc7c48Department of Biosciences, University of Milan, Milan 20133, Italychttps://ror.org/04ew43640State Key Laboratory of Plant Trait Design, Chinese Academy of Sciences Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai 200032, ChinadInstitute of Biophysics, National Research Council of Italy, Milan 20133, Italy</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612869123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612869123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2623500123?af=R">
      <title>The PKMYT1–ALDOA axis drives chemoresistance in cholangiocarcinoma by enhancing glycolysis and MRE11 lactylation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2623500123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceChemoresistance remains a major clinical challenge for the treatment of advanced cholangiocarcinoma (CCA). Gemcitabine combined with cisplatin serves as the standard first-line chemotherapy regimen for this disease, yet it yields limited ...</description>
      <dc:title>The PKMYT1–ALDOA axis drives chemoresistance in cholangiocarcinoma by enhancing glycolysis and MRE11 lactylation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623500123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Wei WuJian WangWu YangZhen SunXiaoxiao SunYafang WangShuo LianJiaojiao ZhengYangyang ZhouWeiming ShenPei HuJianglong GuoQiangxin WuSiying WangQi JiaShengxian YuanRené BernardsWenxin QinHaojie Jinahttps://ror.org/0220qvk04State Key Laboratory of Systems Medicine for Cancer, Shanghai Cancer Institute, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200032, Chinabhttps://ror.org/03xqtf034Division of Molecular Carcinogenesis, Oncode Institute, The Netherlands Cancer Institute, Amsterdam 1066CX, The Netherlandschttps://ror.org/04tavpn47Department of Hepatobiliary Surgery, Eastern Hepatobiliary Surgery Hospital, Second Military Medical University (Naval Medical University), Shanghai 200438, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2623500123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2623500123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614926123?af=R">
      <title>Reproducible cortical links between functional hierarchy, structure, and metabolism</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614926123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThe human cortex is organized along broad functional gradients, but it remains unclear whether these large-scale patterns are tied to underlying biology. We show that the brain’s principal functional hierarchy is reproducibly coupled to ...</description>
      <dc:title>Reproducible cortical links between functional hierarchy, structure, and metabolism</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614926123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Dardo TomasiNora D. Volkowahttps://ror.org/02jzrsm59Laboratory of Neuroimaging, National Institute on Alcohol Abuse and Alcoholism, NIH, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614926123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614926123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528513123?af=R">
      <title>Phosphoproteomic dysregulation promotes tumor proliferation in Cushing’s disease</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528513123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCushing’s disease (CD) causes significant morbidity and mortality despite best medical and surgical treatment. Surgery is the mainstay of treatment, but carries perioperative risks and is sometimes followed by recurrence. There is a paucity of ...</description>
      <dc:title>Phosphoproteomic dysregulation promotes tumor proliferation in Cushing’s disease</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528513123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>David T. AsuzuDhruval BhattDustin MullaneyDebjani MandalDiana NwokoyeSheelu VargheseDaniela Tortoza LopezNikhil RamavenkatKory JohnsonAbdel G. ElkahlounZied AbdullaevKenneth AldapeDragan MaricClarisse QuignonNasir MalikJoseph P. SteinerYan LiSusan WrayChristina TatsiLynnette K. NiemanPrashant Chittiboinaahttps://ror.org/01s5ya894Neurosurgery Unit for Pituitary and Inheritable Diseases, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892bhttps://ror.org/01s5ya894Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892chttps://ror.org/0153tk833Department of Neurological Surgery, University of Virginia, Charlottesville, VA 22903dDepartment of Neurosurgery, University of Texas Southwestern, Dallas, TX 75231ehttps://ror.org/01s5ya894Division of Intramural Research, Bioinformatics Section, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892fhttps://ror.org/00baak391Cancer Genetics and Comparative Genomics Branch, National Human Genome Research Institute, Bethesda, MD20892gLaboratory of Pathology, National Cancer Institute, Bethesda, MD 20892hhttps://ror.org/01s5ya894Flow and Imaging Cytometry Core Facility, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892ihttps://ror.org/01s5ya894Cellular and Developmental Neurobiology Section, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892jhttps://ror.org/01s5ya894Translational Neuroscience Center, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892khttps://ror.org/01s5ya894Proteomics Core Facility, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892lhttps://ror.org/04byxyr05Section on Endocrinology and Genetics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892mhttps://ror.org/00adh9b73Section on Translational Endocrinology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528513123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528513123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601203123?af=R">
      <title>Functional brain networks underlying approach–avoidance conflict processing in humans and rats</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601203123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceApproach–avoidance decisions are a core feature of everyday behavior and are disrupted in psychiatric conditions such as anxiety and addiction. Despite extensive research, how the brain resolves this conflict at the level of large-scale ...</description>
      <dc:title>Functional brain networks underlying approach–avoidance conflict processing in humans and rats</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601203123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Norman R. StewartSabrina L. ValenzanoJingmin ZhangSonja ChuZhemeng WuJina Khiabani JavidAndy C. H. LeeRutsuko Itoahttps://ror.org/03dbr7087Department of Cell and Systems Biology, University of Toronto, Toronto, ON M5S 3G5, Canadabhttps://ror.org/03dbr7087Department of Psychology (St. George), University of Toronto, Toronto, ON M5S 3G3, Canadachttps://ror.org/01kvpec59Rotman Research Institute, Baycrest Academy of Research &amp; Education, Toronto, ON M6A 2E1, Canadadhttps://ror.org/03dbr7087Department of Psychology (Scarborough), University of Toronto, Toronto, ON M1C 1A4, Canadaehttps://ror.org/03dbr7087Department of Psychological Clinical Science, University of Toronto, Toronto, ON M1C 1A4, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601203123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601203123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536317123?af=R">
      <title>SRSF3 plays a key role in liver cancer sex disparity by facilitating hepatocyte expression of ERα and FOXA</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536317123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceConditional Srsf3 KO from mouse liver hepatocytes or mammary glands revealed that Srsf3 is tumor-suppressive in development of DEN-induced liver cancer but oncogenic in Erbb2-mammary tumorigenesis by differential regulation of different set of ...</description>
      <dc:title>SRSF3 plays a key role in liver cancer sex disparity by facilitating hepatocyte expression of ERα and FOXA</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536317123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Lulu YuMasahiko AjiroVladimir MajerciakAlexei LobanovYafeng HeMaggie CamBaktiar KarimDeanna GotteChuxia DengKeji ZhaoDouglas R. LowyNicholas J. G. WebsterZhi-Ming ZhengaTumor Virus RNA Biology Section, HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, NIH, Frederick, MD 21702bCenter for Cancer Research Collaborative Bioinformatics Resource, National Cancer Institute, NIH, Bethesda, MD 20892chttps://ror.org/012pb6c26Laboratory of Epigenome Biology, Systems Biology Center, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD 20892dhttps://ror.org/03v6m3209Frederick National Laboratory for Cancer Research, Frederick, MD 21702ehttps://ror.org/03hz5th67Faculty of Synthetic Biology, Shenzhen University of Advanced Technology, Shenzhen 518107, ChinafLaboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892ghttps://ror.org/0168r3w48Department of Medicine, University of California San Diego, La Jolla, CA 92093</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536317123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536317123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612904123?af=R">
      <title>TCR–mTORC1 signaling promotes epigenetic stabilization of Foxp3 expression in regulatory T cells via TET protein translation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612904123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceRegulatory T (Treg) cells are essential for immune tolerance, and their lineage identity is maintained by T cell receptor (TCR)-dependent epigenetic regulation of theFoxp3locus. Yet the underlying mechanisms remain unclear. Here, using an in ...</description>
      <dc:title>TCR–mTORC1 signaling promotes epigenetic stabilization of Foxp3 expression in regulatory T cells via TET protein translation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612904123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Tomohide KinoshitaAkira NakajimaToru KobayashiMai OhnoYuxi WeiTatsumasa HasegawaNorihito HayatsuShoshiro HirayamaYu-ichi TsukadaAtsushi HiraoShigeo MurataShohei Horiahttps://ror.org/057zh3y96Laboratory of Immunology and Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japanbhttps://ror.org/04mb6s476Formerly Laboratory for Immune Homeostasis, RIKEN Center for Integrative Medical Sciences, Kanagawa 230-0045, Japanchttps://ror.org/057zh3y96Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japandhttps://ror.org/00p4k0j84Formerly Advanced Biological Information Research Division, INAMORI Frontier Research Center, Kyushu University, Fukuoka 819-0395, JapaneDivision of Molecular Genetics, Cancer and Stem Cell Research Program, Cancer Research Institute, World Premier International Research Center Initiative, Nano Life Science Institute, Kanazawa University, Ishikawa 920-1192, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612904123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612904123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620354123?af=R">
      <title>Deletions in variable region 1 of the HIV envelope accelerate V3-glycan bNAb induction in SHIV-infected rhesus macaques</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620354123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceAn effective HIV-1 vaccine will need to elicit broadly neutralizing antibodies (bNAbs) that protect against the extensive diversity of globally circulating strains. Potent bNAbs rarely develop during natural infection, in large part due to ...</description>
      <dc:title>Deletions in variable region 1 of the HIV envelope accelerate V3-glycan bNAb induction in SHIV-infected rhesus macaques</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620354123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Michael P. HogartyHui LiChengyan ZhaoChristian L. MartellaAshwin N. SkellyRumi HabibAndrew Jesse ConnellFrederic Bibollet-RucheWeimin LiuJohn W. CareyKasirajan AyyanathanWenge DingJinery LoraYounghoon ParkEmily LewisJuliette RandoNeha ChohanAjay SinghShuyi WangAlexander MurphyMacy J. AkeleyKatayoun MansouriTaylor N. SpenceKevin J. WieheWilton B. WilliamsKevin O. SaundersKshitij WaghMichael S. SeamanRobert J. EdwardsBarton F. HaynesBeatrice H. HahnGeorge M. Shawahttps://ror.org/00b30xv10Department of Medicine, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104bhttps://ror.org/00b30xv10Department of Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104chttps://ror.org/00py81415Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710dhttps://ror.org/04drvxt59Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Boston, MA 02215</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620354123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620354123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607382123?af=R">
      <title>Mechanisms of substrate recognition and catalysis in a mammalian phosphatidylserine synthase 2</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607382123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificancePhosphatidylserine (PS) is a major negatively charged lipid in cell membranes and a key signaling molecule for important cellular processes such as apoptosis and blood coagulation. In mammals, PS is mainly produced by two homologous ...</description>
      <dc:title>Mechanisms of substrate recognition and catalysis in a mammalian phosphatidylserine synthase 2</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607382123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Lie WangZhen ZhangHongyuan YangArthur LaganowskyMing Zhouahttps://ror.org/02pttbw34Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030bhttps://ror.org/03gds6c39Department of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030chttps://ror.org/01f5ytq51Department of Chemistry, Texas A&amp;M University, College Station, TX 77843</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607382123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607382123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610600123?af=R">
      <title>Distribution and voltage dependence of ion channels shape single-neuron computations</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610600123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThe computations performed by a single neuron depend on the function and the subcellular localization of voltage-gated ion channels. We develop inDrosophilaa set of tools to map endogenous channels in genetically defined cells and ...</description>
      <dc:title>Distribution and voltage dependence of ion channels shape single-neuron computations</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610600123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Renée M. VieiraMichael DeistlerClémentine GuillemetTabea SchillingJakob H. MackeAlexander BorstLukas N. Groschnerahttps://ror.org/03g267s60Max Planck Institute for Biological Intelligence, Martinsried 82152, Germanybhttps://ror.org/03a1kwz48Machine Learning in Science, University of Tübingen, Tübingen 72076, Germanychttps://ror.org/0107nyd78Tübingen AI Center, Tübingen 72076, Germanydhttps://ror.org/04fq9j139Department Empirical Inference, Max Planck Institute for Intelligent Systems, Tübingen 72076, Germanyehttps://ror.org/02n0bts35Gottfried Schatz Research Center, Molecular Biology and Biochemistry, Medical University of Graz, Graz 8010, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610600123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610600123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534566123?af=R">
      <title>Loss of cerebral autoregulation drives abnormal perfusion patterns after stroke</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534566123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCerebral autoregulation is essential for maintaining stable brain perfusion, yet the vascular mechanisms that coordinate blood flow regulation across cerebrovascular networks remain incompletely understood. Using an in silico framework applied ...</description>
      <dc:title>Loss of cerebral autoregulation drives abnormal perfusion patterns after stroke</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534566123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Chryso LambrideMohamad El AmkiSusanne WegenerFranca Schmidahttps://ror.org/02crff812Department of Neurology, University Hospital and University of Zurich, Zurich 8057, Switzerlandbhttps://ror.org/02crff812Neuroscience Center Zurich, University of Zurich and ETH Zurich, Zurich 8091, Switzerlandchttps://ror.org/02k7v4d05ARTificial ORGan Center for Biomedical Engineering Research, University of Bern, Bern 3010, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534566123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534566123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620180123?af=R">
      <title>Desulfinylation of the deubiquitinase USP7 by SRXN1 attenuates oxidative acute liver injury</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620180123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceProteinS-sulfinylation is a reversible oxidative cysteine modification, but its role in acute liver injury remains poorly understood. We identify sulfiredoxin-1 (SRXN1), a key regulator of proteinS-sulfinylation, as a critical ...</description>
      <dc:title>Desulfinylation of the deubiquitinase USP7 by SRXN1 attenuates oxidative acute liver injury</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620180123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Mengyun KeJong-Won KimMeishu XuJingyuan WangLingyi LiuSyamprasad N. P.Bin YangXiaofei WangHuatian LiSongrong RenKate S. CarrollSong LiWen Xieahttps://ror.org/01an3r305Center for Pharmacogenetics, Department of Pharmaceutical Sciences, University of Pittsburgh, Pittsburgh, PA 15261bDepartment of Chemistry and Biochemistry, Florida Atlantic University, Jupiter, FL 33458chttps://ror.org/01an3r305Department of Pharmacology and Chemical Biology, University of Pittsburgh, Pittsburgh, PA 15261</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620180123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620180123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2624702123?af=R">
      <title>Loss of CsrA in Acinetobacter baumannii leads to lethal dysregulation of alanine metabolism</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624702123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceIn the pathogenAcinetobacter baumannii, the posttranscriptional regulator CsrA is required for growth under certain environmental conditions, including rich growth media and infection-relevant conditions like human serum. However, CsrA is ...</description>
      <dc:title>Loss of CsrA in Acinetobacter baumannii leads to lethal dysregulation of alanine metabolism</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624702123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-29T07:00:00Z</dc:date>
      <dc:creator>Rosa L. SavaMichael J. Gebhardtahttps://ror.org/036jqmy94Department of Microbiology and Immunology, University of Iowa, Iowa City, IA 52242</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2624702123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2624702123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536158123?af=R">
      <title>Mathematical discovery and exploration can be done at scale</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536158123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThis research represents an advancement in mathematical discovery by demonstrating that AI systems can autonomously improve on algorithms tackling mathematical questions at a much larger scale than traditional mathematics. We establish this ...</description>
      <dc:title>Mathematical discovery and exploration can be done at scale</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536158123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Bogdan GeorgievJavier Gómez-SerranoTerence TaoAdam Zsolt Wagnerahttps://ror.org/00971b260Google DeepMind, London N1C 4UZ, United Kingdombhttps://ror.org/05gq02987Department of Mathematics, Brown University, Providence, RI 02912cSchool of Mathematics, Institute for Advanced Study, Princeton, NJ 08540dhttps://ror.org/046rm7j60Department of Mathematics, University of California, Los Angeles, CA 90095-1555</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536158123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536158123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614237123?af=R">
      <title>Genome stability disrupted by the circRBM39(4,5,6)–RPA2 axis represses breast tumorigenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614237123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCircular RNAs (circRNAs) are natural outputs of transcription and RNA processing, which have been implicated in physiology and human diseases. We have identifiedcircRBM39(4,5,6)as a tumor suppressor in breast cancer (BC), which directly ...</description>
      <dc:title>Genome stability disrupted by the circRBM39(4,5,6)–RPA2 axis represses breast tumorigenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614237123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Xing BianMaoyi XuNa LiChuanbo SunXu LiuYuqi DengDun LiuGuozhen CaoWenchu LinBo HongGe ShanXiaolin Wangahttps://ror.org/04c4dkn09Department of Obstetrics and Gynecology, The First Affiliated Hospital of University of Science and Technology of China, The Ribonucleic Acid Institute, School of Basic Medical Sciences, Division of Life Science and Medicine, University of Science and Technology of China, Hefei 230027, Chinabhttps://ror.org/04c4dkn09Center for Advanced Interdisciplinary Science and Biomedicine of Institute of Healthand Medicine, Division of Life Science and Medicine, University of Science and Technology of China, Hefei 230027, Chinachttps://ror.org/046ft6c74College of Life and Health, West Anhui University, Lu’an 237012, Chinadhttps://ror.org/00j2a7k55Department of Medical Oncology, The Affiliated Hospital of Jiaxing University, Jiaxing 314001, Chinaehttps://ror.org/00j2a7k55Department of Pathology, Jiaxing Maternity and Child Health Hospital, Affiliated Women and Children’s Hospital of Jiaxing University, Jiaxing Affiliated Women and Children’s Hospital of Wenzhou Medical University, Jiaxing 314000, Chinafhttps://ror.org/02d5ks197Institute of Digestive Disease, The Second Affiliated Hospital, School of Medicine, The Chinese University of Hong Kong, Shenzhen and Longgang District People’s Hospital of Shenzhen, Shenzhen 518172, Chinaghttps://ror.org/034t30j35Hefei Cancer Hospital of Chinese Academy of Sciences, Institute of Health and Medical Technology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614237123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601715123?af=R">
      <title>Repeated marine-to-freshwater fish transitions reveal paleoenvironmental modulation of adaptive radiation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601715123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceTropical rivers in Australia and New Guinea host one of the most unusual continental freshwater fish assemblages on Earth, composed almost entirely of marine-derived lineages. This system allows asking why some colonizing lineages diversify ...</description>
      <dc:title>Repeated marine-to-freshwater fish transitions reveal paleoenvironmental modulation of adaptive radiation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601715123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Aline P. M. MedeirosMelissa Rincon-SandovalAaron DavisAintzane SantaquiteriaChristine E. ThackerJoshua P. EganJonathan KimAlfred Ko’ouDahiana ArcilaWilliam B. LudtLily C. HughesDevin BloomRicardo Betancur-Rahttps://ror.org/0168r3w48Scripps Institution of Oceanography, Marine Biology Research Division, University of California San Diego, La Jolla, CA 92037bhttps://ror.org/02aqsxs83Department of Biology, The University of Oklahoma, Norman, OK 73019chttps://ror.org/04gsp2c11Centre for Tropical Water and Aquatic Ecosystem Research (TropWATER), Australian Tropical Sciences and Innovation Precint (ATSIP), School of Marine and Tropical Biology, James Cook University, Townsville, QLD 4811, Australiadhttps://ror.org/00y4zzh67Department of Biological Sciences, The George Washington University, Washington, DC 20052ehttps://ror.org/05psc8795Department of Vertebrate Zoology, Vertebrate Zoology, Santa Barbara Museum of Natural History, Santa Barbara, CA 93105fhttps://ror.org/00p9h0053Department of Ichthyology, Natural History Museum of Los Angeles County, Los Angeles, CA 90007ghttps://ror.org/05sfwv538Science and Research Division, Great Lakes Fishery Commission, Ann Arbor, MI 48105hhttps://ror.org/017zqws13Bell Museum of Natural History, University of Minnesota, 100 Ecology, 1987 Upper Buford Circle, Saint Paul, MN 55108ihttps://ror.org/04j198w64Department of Biological Sciences, Western Michigan University, Kalamazoo, MI 49008jhttps://ror.org/05jxf0p38School of Natural &amp; Physical Sciences, The University of Papua New Guinea University, National Capital District Port Moresby 134, Papua New Guineakhttps://ror.org/04tj63d06Department of Marine, Earth, and Atmospheric Sciences, North Carolina State University, Raleigh, NC 27607lhttps://ror.org/01bqnjh41Ichthyology Collection, North Carolina Museum of Natural Sciences, Raleigh, NC 27601mhttps://ror.org/04j198w64School of the Environment, Geography, and Sustainability Western Michigan University, Kalamazoo, MI 49008</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601715123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601715123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604233123?af=R">
      <title>Passive sampling for grazer cues incorporates top-down effects in harmful algal bloom monitoring and toxin prediction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604233123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceHarmful algal blooms (HABs) ofPseudo-nitzschiacan introduce the neurotoxin domoic acid into marine food webs, posing a serious threat to seafood safety and wildlife conservation. Accurate HAB forecasting is challenging, and current ...</description>
      <dc:title>Passive sampling for grazer cues incorporates top-down effects in harmful algal bloom monitoring and toxin prediction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604233123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Aubrey TrappAda Behncké-SerraErik SelanderMelissa B. PeacockRaphael M. Kudelaahttps://ror.org/03s65by71Ocean Sciences Department, University of California Santa Cruz, Santa Cruz, CA 95064bhttps://ror.org/02c235t25Salish Sea Research Center, Northwest Indian College, Bellingham, WA 98226chttps://ror.org/012a77v79Biology Department, Lund University, Lund 223 62, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604233123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604233123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616216123?af=R">
      <title>Metabolite ratiomics: Rapid diagnosis and classification of gliomas for intraoperative application during brain surgery</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616216123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceGliomas are highly infiltrative brain tumors whose molecular heterogeneity complicates diagnosis and treatment. Maximal safe surgical resection offers the best chance for durable disease control, yet tumor cells often extend beyond MRI-defined ...</description>
      <dc:title>Metabolite ratiomics: Rapid diagnosis and classification of gliomas for intraoperative application during brain surgery</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616216123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Mahdiyeh ShahiKenneth Lane VirginLoizos MichaelidesDiogo Moniz GarciaAleeshba N. BasilAlfredo Quiñones-HinojosaR. Graham Cooksahttps://ror.org/02dqehb95Department of Chemistry, Purdue University, West Lafayette, IN 47907bhttps://ror.org/02ets8c94Indiana University School of Medicine, Indianapolis, IN 46202chttps://ror.org/02qp3tb03Department of Neurosurgery, Mayo Clinic, Jacksonville, FL 32224</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616216123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616216123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616692123?af=R">
      <title>MrtR of Mesorhizobium tianshanense reveals both activation and inhibition mechanisms of a LuxR-type quorum sensing receptor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616692123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceQuorum sensing (QS) regulates diverse bacterial behaviors, and LuxR-type receptors are attractive targets for applications ranging from antivirulence strategies to synthetic biology and agriculture. Despite intense interest in developing ...</description>
      <dc:title>MrtR of Mesorhizobium tianshanense reveals both activation and inhibition mechanisms of a LuxR-type quorum sensing receptor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616692123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Irene M. StoutlandHelen E. Blackwellahttps://ror.org/01y2jtd41Department of Chemistry, University of Wisconsin–Madison, Madison, WI 53706</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616692123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616692123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614593123?af=R">
      <title>The circSNX6 restricts dengue virus replication in association with PARP1 and ferroptosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614593123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceDengue virus (DENV) is among the most significant mosquito-borne viral diseases, with an estimated 100 to 400 million infections occurring annually. No specific antiviral therapy exists. Using transcriptomic profiling of patient blood cells ...</description>
      <dc:title>The circSNX6 restricts dengue virus replication in association with PARP1 and ferroptosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614593123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Ruixia TangJianyu XuHaiting LongJiahong GaoJunying ChenYue PanZhengcun WuQiangming Sunahttps://ror.org/02drdmm93Institute of Medical Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Kunming 650118, People’s Republic of Chinabhttps://ror.org/0040axw97College of Life Sciences, Yunnan University, Kunming 650000, People’s Republic of Chinachttps://ror.org/02drdmm93National Kunming High-level Biosafety Primate Research Center, Institute of Medical Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Kunming 650118, People’s Republic of ChinadYunnan Key Laboratory of Cross-Border Infectious Disease Control and Prevention and Novel Drug Development, Kunming 650118, People’s Republic of ChinaeState Key Laboratory of Respiratory Health and Multimorbidity, Beijing 100000, People’s Republic of ChinafYunnan Key Laboratory of Vaccine Research and Development on Severe Infectious Diseases, Kunming 650118, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614593123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614593123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612455123?af=R">
      <title>Scaling laws for massively parallel microfluidics enable rapid construction of ten-million-scale natively paired antibody libraries</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612455123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSingle-cell immune profiling of rare populations may require hundreds of millions of droplets, exceeding conventional single-nozzle throughput. Parallelization increases throughput but can compromise flow uniformity. We derive a scaling law ...</description>
      <dc:title>Scaling laws for massively parallel microfluidics enable rapid construction of ten-million-scale natively paired antibody libraries</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612455123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Hongyu ChenYing LinZhongfu ChenDakun ZhangJiancheng DingRongwei ZhangZhichao WuYulin ZhangWangheng HouKunyu YangMujin FangYingbing WangJun ZhangShiyin ZhangShengxiang GeDahou YangNingshao Xiaahttps://ror.org/00mcjh785State Key Laboratory of Vaccines for Infectious Diseases, Xiang An Biomedicine Laboratory, School of Public Health, Xiamen University, Xiamen 361102, Fujian, Chinabhttps://ror.org/00mcjh785National Institute of Diagnostics and Vaccine Development in Infectious Diseases, National Innovation Platform for Industry-Education Integration in Vaccine Research, Xiamen University, Xiamen 361102, Fujian, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612455123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612455123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605220123?af=R">
      <title>Tandem RNA-binding domain architecture drives PKR activation through an intramolecular interface</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605220123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceRNA-binding proteins often contain tandem repeats of RNA-binding domains (RBDs) connected by intrinsically disordered sequences, yet how this flexible arrangement contributes to biological function remains unclear. Here, we show that in ...</description>
      <dc:title>Tandem RNA-binding domain architecture drives PKR activation through an intramolecular interface</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605220123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Chong HanChen LiYi-Feng XuMing RaoShao-Qing ZhangLing-Ling ChenJiaquan Liuahttps://ror.org/05qbk4x57State Key Laboratory of RNA Innovation, Science and Engineering, Shanghai Key Laboratory of Molecular Andrology, Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai 200031, ChinabNew Cornerstone Science Laboratory, Shenzhen 518054, Chinachttps://ror.org/0220qvk04School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, Chinadhttps://ror.org/031vgn537Shanghai Academy of Natural Sciences, Shanghai 200031, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605220123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605220123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610486123?af=R">
      <title>Functional similarity shapes global patterns of fish naturalization and invasion richness</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610486123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceIdentifying the factors determining successful invasions is critical for managing exotic species, yet the relative role of ecological similarity, native diversity, and human pressure remains debated. Using global fish community data and trait-...</description>
      <dc:title>Functional similarity shapes global patterns of fish naturalization and invasion richness</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610486123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Zhijun XiaJuanjuan ChenErik JeppesenKun GuoGuohuan SuGuohao LiuFandong YuBeata MessyaszJialin LiDavid Z. ZhuNaicheng Wuahttps://ror.org/03et85d35School of Civil Engineering and Future Cities, Ningbo University, Ningbo 315211, Chinabhttps://ror.org/03et85d35School of Geography and Remote Sensing, Ningbo University, Ningbo 315211, Chinachttps://ror.org/03et85d35Zhejiang-Germany Joint Laboratory on Remote Sensing of Coastal Ecosystem, Ningbo University, Ningbo 315211, Chinadhttps://ror.org/01aj84f44Department of Ecoscience and Centre for Water Technology, Aarhus University, Aarhus 8000, Denmarkehttps://ror.org/05qbk4x57Sino-Danish Centre for Education and Research (SDC), University of Chinese Academy of Sciences, Beijing 100190, ChinafInstitute for Ecological Research and Pollution Control of Plateau Lakes, School of Ecology and Environmental Science, Yunnan University, Kunming 650228, Chinaghttps://ror.org/034t30j35State Key Laboratory of Black Soils Conservation and Utilization, Northeast Institute of Geography and Agroecology, Chinese Academy of Sciences, Changchun 130102, Chinahhttps://ror.org/034t30j35State Key Laboratory of Breeding Biotechnology and Sustainable Aquaculture, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, Chinaihttps://ror.org/040af2s02Department of Geosciences and Geography, University of Helsinki, Helsinki 00014, Finlandjhttps://ror.org/05ckt8b96Pearl River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Key Laboratory of Prevention and Control for Aquatic Invasive Alien Species, Ministry of Agriculture and Rural Affairs, Guangzhou 510380, Chinakhttps://ror.org/04and7w57Key Laboratory of Alien Species and Ecological Security (CAFS), Pearl River Fisheries Research Institute, Chinese Academy of Fisheries Science, Guangzhou 510380, Chinalhttps://ror.org/04g6bbq64Department of Hydrobiology, Institute of Environmental Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, Poznan 61-614, Polandmhttps://ror.org/0160cpw27Department of Civil and Environmental Engineering, University of Alberta, Edmonton, AB T6G 2H5, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610486123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2610486123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613799123?af=R">
      <title>A highly potent bispecific antibody confers complete protection against SFTSV in preclinical models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613799123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSevere fever with thrombocytopenia syndrome virus (SFTSV) causes severe human disease with a case fatality rate of up to 30%, representing a substantial threat to public health. Currently, no specific therapeutics have been approved for ...</description>
      <dc:title>A highly potent bispecific antibody confers complete protection against SFTSV in preclinical models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613799123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Xiaoping GuoFujian WanWujian LiQingcui ZouEntao LiWeiqi WangFangxu LiZunhao ZhouXiaoman YangQiyuan YangXinyu WangXiang GaoHaoyi HeWenyu XieAiqing HouYanan SuHongliang HeMinghua LiBo ShuSandra Chiuahttps://ror.org/04c4dkn09Department of Infectious Disease, The First Affiliated Hospital of University of Science and Technology of China, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230031, Chinabhttps://ror.org/04c4dkn09Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui 230026, ChinacKey Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases, Hefei, Anhui 230026, Chinadhttps://ror.org/034t30j35State Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, Hubei 430062, Chinaehttps://ror.org/05qbk4x57University of Chinese Academy of Sciences, Beijing 100049, Chinafhttps://ror.org/034t30j35Kunming National High-level Biosafety Research Center for Non-Human Primates, Center for Biosafety Mega-Science, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650201, Chinaghttps://ror.org/034t30j35State Key Laboratory of Genetic Evolution &amp; Animal Models, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650201, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613799123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613799123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2616933123?af=R">
      <title>Targeted extracellular degradation of LRP8 promotes ferroptosis in cancer cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2616933123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMany therapy-resistant cancers depend on the selenium-containing enzyme glutathione peroxidase 4 (GPX4) to suppress ferroptosis, an iron-dependent form of cell death driven by lipid peroxidation. Direct inhibition of GPX4 has proven ...</description>
      <dc:title>Targeted extracellular degradation of LRP8 promotes ferroptosis in cancer cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2616933123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Fangzhu ZhaoAlex InagueTrenton M. Peters-ClarkeYifei ChenSnehal D. GanjaveYun ZhangKun MiaoZi YaoYan WuMadison K. C. SetoKevin K. LeungJames A. OlzmannJames A. Wellsahttps://ror.org/043mz5j54Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, CA 94158bhttps://ror.org/01an7q238Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720chttps://ror.org/01an7q238Department of Metabolic Biology and Nutrition, University of California Berkeley, Berkeley, CA 94720dhttps://ror.org/043mz5j54Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA 94158</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2616933123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2616933123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622416123?af=R">
      <title>Pressure-induced Lifshitz and quantum phase transitions in electron-doped cuprate superconductors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622416123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceTuning the electronic ground state of high-temperature superconducting cuprates is a key issue for understanding the underlying mechanism of superconductivity. Here, we present evidence of two distinct pressure-induced electronic transitions ...</description>
      <dc:title>Pressure-induced Lifshitz and quantum phase transitions in electron-doped cuprate superconductors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622416123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Jinyu ZhaoShu CaiZhaoyu LiuJianfeng ZhangShuaihang SunPengyu WangJing GuoYazhou ZhouShiliang LiFuyang LiuLuhong WangHaozhe LiuYang DingQi WuTao XiangRichard L. GreeneLiling SunaCenter for High Pressure Science &amp; Technology Advanced Research, Beijing 100193, Chinabhttps://ror.org/034t30j35Institute of Physics, Chinese Academy of Sciences, Beijing 100190, Chinachttps://ror.org/03wcck081Shanghai Key Laboratory of Material Frontiers Research in Extreme Environments, Shanghai Advanced Research in Physical Sciences, Shanghai 201203, Chinadhttps://ror.org/047s2c258Maryland Quantum Materials Center, Department of Physics, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622416123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606579123?af=R">
      <title>α-aminobutyric acid promotes tumor progression by polarizing macrophages through the ASNS–mTORC2 axis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606579123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceIdentifying metabolic barriers within the tumor microenvironment is essential for advancing immunotherapy. We found that the metabolite α-aminobutyric acid (AABA) acts as a critical checkpoint, driving immunosuppressive macrophage polarization ...</description>
      <dc:title>α-aminobutyric acid promotes tumor progression by polarizing macrophages through the ASNS–mTORC2 axis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606579123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Fei LiXiaorong XieTongran XuYu TangYuting XiaYali TangShijie YuanMengdi ZhuXuwei WuLan HeShu-Hai LinRan Heahttps://ror.org/00p991c53Department of Immunology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, ChinabSchool of Medical Technology, Jiangsu College of Nursing, Huai’an 223005, Jiangsu, Chinachttps://ror.org/00mcjh785State Key Laboratory for Cellular Stress Biology, School of Life Sciences, Faculty of Medicine and Life Sciences, Xiamen University, Xiamen 361102, Chinadhttps://ror.org/05htk5m33School of Biomedical Sciences, Hunan University, Changsha 410082, Chinaehttps://ror.org/00p991c53Department of Dermatology, Affiliated Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606579123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606579123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620353123?af=R">
      <title>Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620353123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSegments of the nucleus and endoplasmic reticulum (ER) are degraded by autophagy in response to starvation or the accumulation of misfolded proteins. These pathways are crucial for cellular homeostasis and defects lead to accelerated ...</description>
      <dc:title>Atg39-dependent nucleophagy and Atg40-dependent ER-phagy require the Apq12/Brr6/Brl1 complex</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620353123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Dongmei LiuShuliang ChenHua YuanSusan Ferro-NovickPeter Novickahttps://ror.org/0168r3w48Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0668</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620353123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620353123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617741123?af=R">
      <title>Ufd4p-mediated Sum1p clearance ensures proper chromosome organization during cell division</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617741123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMaintaining proper chromosome architecture is a universal requirement for genome integrity across all cellular divisions, yet the upstream regulatory networks controlling this process remain largely elusive. This study uncovers an unexpected ...</description>
      <dc:title>Ufd4p-mediated Sum1p clearance ensures proper chromosome organization during cell division</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617741123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Taicong TanYali MiPeng DuZhaojie LiuShuyun HeShenli YuanRenjie JiaoChao LiuWei Liahttps://ror.org/00zat6v61Institute of Reproductive Health and Perinatology, Women and Children’s Medical Center, GMU-GIBH Joint School of Life Sciences, Sino-French Hoffmann Institute, School of Basic Medical Sciences, Guangzhou Medical University, Guangzhou 510623, Chinabhttps://ror.org/00zat6v61Joint School of Life Sciences, Guangzhou Medical University and Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangdong Provincial Key Laboratory of Protein Modification and Disease, The Guangdong-Hong Kong-Macao Joint Laboratory for Cell Fate Regulation and Diseases, Guangzhou Medical University, Guangzhou 510182, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617741123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617741123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613911123?af=R">
      <title>Thermosensor OsTT3.1 enhances rice thermotolerance by degrading OsGSK2 to reduce OsHsfB2c phosphorylation and nuclear translocation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613911123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceRising global temperatures pose an escalating threat to rice yield. While heat-shock transcription factors (HSFs) are recognized as central regulators of heat stress responses, the mechanisms underlying their precise posttranslational ...</description>
      <dc:title>Thermosensor OsTT3.1 enhances rice thermotolerance by degrading OsGSK2 to reduce OsHsfB2c phosphorylation and nuclear translocation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613911123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Jiaqi HouJin YangTingyu ChenYating ZhaoDaoyi TuZetian GuoMutian YangZiyi WangYan ZengNachuan ZhangLijia Liahttps://ror.org/033vjfk17State Key Laboratory of Hybrid Rice, College of Life Sciences, Wuhan University, Wuhan 430072, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613911123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613911123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614738123?af=R">
      <title>LAT condensation gates PLCγ1 activation via bimodal LAT phosphorylation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614738123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceT cells are sensitive sensors capable of detecting and responding to trace amounts of foreign antigen. Understanding how they achieve such sensitivity while maintaining accurate antigen discrimination remains a key challenge. Here, through ...</description>
      <dc:title>LAT condensation gates PLCγ1 activation via bimodal LAT phosphorylation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614738123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>He RenHyun-Ro LeeYannick A. D. OmarJoseph B. DeGrandchampChien-Lun HungTimothy J. EisenDimitrios StamouJohn KuriyanArup K. ChakrabortyJay T. Grovesahttps://ror.org/01an7q238Department of Chemistry, University of California, Berkeley, CA 94720bhttps://ror.org/042nb2s44Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/02vm5rt34Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37240dhttps://ror.org/035b05819Department of Chemistry, University of Copenhagen, Copenhagen DK-2100, Denmark</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614738123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614738123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602013123?af=R">
      <title>Deep-earth water transport beyond the transition zone via subducted feldspars</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602013123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThe transport of water into Earth’s deep mantle plays a fundamental role in controlling mantle rheology, melting processes, and seismic structure, yet the mineralogical pathways enabling water to traverse the mantle transition zone remain ...</description>
      <dc:title>Deep-earth water transport beyond the transition zone via subducted feldspars</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602013123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Yeonhak JungStella CharitonVitali B. PrakapenkaNico GiordanoZhenxian LiuSung-Hyun ParkYongjae Leeahttps://ror.org/01wjejq96Department of Earth System Science, Yonsei University, Seoul 03722, Republic of Koreabhttps://ror.org/024mw5h28GeoSoilEnviroCARS, Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 60637cDeutsches Elektronen-Synchrotron, Hamburg 22607, Germanydhttps://ror.org/02mpq6x41Department of Physics, University of Illinois Chicago, Chicago, IL 60607ehttps://ror.org/00n14a494Division of Glacier and Earth Sciences, Korea Polar Research Institute, Incheon 21990, Republic of KoreafKorea Polar Research Institute School, University of Science and Technology, Incheon 21990, Republic of Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602013123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602013123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2620626123?af=R">
      <title>A conserved β-sheet motif mediates PIN2 hydrophilic loop–loop interactions to regulate PIN2 dynamics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2620626123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificancePIN auxin transporters are critical for generating morphogenic gradients that govern plant development. While their central hydrophilic loop (HL) is known to recruit diverse trans-acting effectors, the structural coordination within the loop ...</description>
      <dc:title>A conserved β-sheet motif mediates PIN2 hydrophilic loop–loop interactions to regulate PIN2 dynamics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2620626123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <dc:creator>Kwang-Ho MaengHyung-Taeg Choahttps://ror.org/04h9pn542Department of Biological Sciences, Seoul National University, Seoul 08826, Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2620626123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2620626123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605806123?af=R">
      <title>T–B interactions yield CD3+ B cells and CD20+ T cells with pathogenic features in multiple sclerosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605806123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceThe precise identification of immune cell subsets based on surface markers and their selective targeting is a corner-stone in current precision medicine. The surface markers CD3 and CD20 are typically used to identify B and T cells, but a ...</description>
      <dc:title>T–B interactions yield CD3+ B cells and CD20+ T cells with pathogenic features in multiple sclerosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605806123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Selia BaierZhongyi WangNathalie LollSimone MaderStephan WinklmeierFady ShenoudaSamantha HoEva OswaldSelen ÜnlüArek KendirliAtay VuralCeren ÖzdemirChristoph A. ReichelJan KranichJan SchmidtJulie BoisclairRachel CuttatWalter GeorgescuYoann GilbartMagali JivkovUlrike NaumannEddie A. JamesJosé M. CarballidoTania KümpfelValérie DubostPhilippe CouttetEdgar Meinlahttps://ror.org/05591te55Institute of Clinical Neuroimmunology, LMU University Hospital, LMU Medizin, Ludwig-Maximilians-Universität München, Munich 81377, Germanybhttps://ror.org/05591te55Biomedical Center (BMC), LMU Medizin, Ludwig-Maximilians-Universität München, Martinsried 82152, Germanychttps://ror.org/05591te55Graduate School of Systemic Neuroscience, Ludwig-Maximilians-Universität München, Martinsried 82152, GermanydNovartis Biomedical Research, Basel 4056, SwitzerlandeDepartment of Translational Immunology, Department of Medicine 3 - Rheumatology and Immunology, Nikolaus-Fiebiger Center for Molecular Medicine, Friedrich-Alexander-Universität (FAU) Erlangen-Nürnberg and Uniklinikum Erlangen, Erlangen 91054, GermanyfDeutsches Zentrum Immuntherapie, Friedrich-Alexander-Universität (FAU) Erlangen-Nürnberg and Uniklinikum Erlangen, Erlangen 91054, Germanyghttps://ror.org/00jzwgz36Research Center for Translational Medicine, Koç University, İstanbul 34010, Türkiyehhttps://ror.org/025z3z560Munich Cluster for Systems Neurology (SyNergy), Munich 81377, Germanyihttps://ror.org/00jzwgz36Department of Neurology, Koç University School of Medicine, İstanbul 34010, Türkiyejhttps://ror.org/05591te55Department of Otorhinolaryngology, University Hospital, Ludwig-Maximilians-Universität München, Munich 81377, Germanykhttps://ror.org/05591te55Institute of Immunology, Faculty of Medicine, Ludwig-Maximilians-Universität München, Martinsried 82152, Germanylhttps://ror.org/04j9rp686Benaroya Research Institute, Seattle, WA 98101mhttps://ror.org/02s6k3f65Division of Molecular and Systems Toxicology, Department of Pharmaceutical Sciences, University of Basel, Basel 4056, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605806123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529250123?af=R">
      <title>The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529250123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceDiderm bacteria in the Mycobacteriales order have a distinctive outer layer called the mycomembrane. Proteins that reside within the mycomembrane play critical roles in virulence and cell viability. However, how proteins are assembled into the ...</description>
      <dc:title>The mycomembrane proteins PorH and ProtX are inserted at polar growth zones and linked to the cell wall</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529250123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Elizabeth M. HartDieuwertje A. de BruinVictoria M. MarandoMarina Arnau AlemanyEric D. SnowBailey J. SchultzErkin KuruSuzanne WalkerAndrea VettigerThomas G. BernhardtaDepartment of Microbiology, Harvard Medical School, Boston, MA 02115bHHMI, Harvard Medical School, Boston, MA 02115chttps://ror.org/019whta54Department of Fundamental Microbiology, University of Lausanne, Lausanne CH-1015, SwitzerlanddDepartment of Genetics, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529250123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529250123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611888123?af=R">
      <title>Generalized Taylor’s law for infinite-mean heavy-tailed data under dependence and heterogeneity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611888123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMany phenomena exhibit rare but extremely large fluctuations. Examples include financial losses, epidemic outbreaks, and measurements on networked systems. In such settings, classical assumptions of finite mean, finite variance, and ...</description>
      <dc:title>Generalized Taylor’s law for infinite-mean heavy-tailed data under dependence and heterogeneity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611888123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Pok Him ChengJoel E. CohenHok Kan LingSheung Chi Phillip Yamahttps://ror.org/00hj8s172Department of Statistics, Columbia University, New York, NY 10027bhttps://ror.org/0420db125Laboratory of Populations, The Rockefeller University, New York, NY 10065-6399chttps://ror.org/00hj8s172Climate School, Columbia University, New York, NY 10027dhttps://ror.org/024mw5h28Department of Statistics, University of Chicago, Chicago, IL 60637ehttps://ror.org/02y72wh86Department of Mathematics and Statistics, Queen’s University, Kingston, ON K7L 3N6, Canadafhttps://ror.org/00t33hh48Department of Statistics and Data Science, The Chinese University of Hong Kong, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611888123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618715123?af=R">
      <title>Climate-driven adaptive microevolution in wild yeasts</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618715123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceUnderstanding how environmental gradients shape biodiversity is a central challenge in biology, particularly for microorganisms, whose natural populations remain poorly characterized. UsingSaccharomyces eubayanus, the wild ancestor of lager-...</description>
      <dc:title>Climate-driven adaptive microevolution in wild yeasts</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618715123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Christian I. OportoLuis A. SaonaPablo QuintrelKamila UrbinaJosé Benavides-ParraFrancisca GrenePablo VillarrealJuliana A. ViannaFrida I. PiperRoberto F. NespoloFrancisco A. Cubillosahttps://ror.org/02ma57s91Facultad de Química y Biología, Departamento de Biología, Universidad de Santiago de Chile, Santiago 9170022, Chilebhttps://ror.org/05btm5233Agencia Nacional de Investigación y Desarrollo-Millennium Nucleus of Patagonian Limit of Life, Valdivia 5110566, Chilechttps://ror.org/010r9dy59Facultad de Ingeniería, Instituto de Ciencias Aplicadas, Centro de Investigación e Innovación, Universidad Autónoma de Chile, Santiago 8581151, Chiledhttps://ror.org/05xcmte05Agencia Nacional de Investigación y Desarrollo-Millennium Science Initiative-Millennium Institute for Integrative Biology, Santiago 7500574, Chileehttps://ror.org/04jrwm652Facultad de Medicina, Universidad San Sebastián, Providencia 7510157, Chilefhttps://ror.org/01qq57711One Health Institute, Faculty of Life Sciences, Universidad Andrés Bello, Santiago 8370134, ChilegMillennium Institute Center for Genome Regulation, Santiago 7500000, ChilehMillennium Institute Biodiversity of Antarctic and Subantarctic Ecosystems, Santiago 7800003, Chileihttps://ror.org/01s4gpq44Instituto de Ciencias Biológicas, Universidad de Talca, Talca 3460000, ChilejInstituto de Ecología y Biodiversidad, Victoria 631, Barrio Universitario, Concepción 4030000, Chilekhttps://ror.org/029ycp228Instituto de Ciencias Ambientales y Evolutivas, Universidad Austral de Chile, Valdivia 5090000, Chilelhttps://ror.org/01p6hjg61Centro Científico y Tecnológico de Excelencia Ciencia and Vida, Fundación Ciencia and Vida, Santiago 8580702, Chile</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618715123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607529123?af=R">
      <title>Impaired control of autoimmunity increases pediatric multiple sclerosis risk in EBNA-1-seropositives and -seronegatives</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607529123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceMultiple sclerosis (MS) is associated with Epstein–Barr virus (EBV) infection and EBNA-1-specific immunity, yet the mechanisms linking EBV to central nervous system (CNS) autoimmunity remain incompletely understood. We demonstrate that CNS-...</description>
      <dc:title>Impaired control of autoimmunity increases pediatric multiple sclerosis risk in EBNA-1-seropositives and -seronegatives</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607529123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Hannes VietzenEmmanuelle L. WaubantT. Charles CasperLeslie A. BensonTanuja ChitnisTeri SchreinerAmy T. WaldmanSoe MarBianca Weinstock-GuttmanLaura M. KühnerSarah M. BergerMarianne GraningerKevin RostásyHenrieke SauckeFranziska KauthGeorgia KoukouSimon SommerEva-Maria WendelGabriel BstehMarkus PonleitnerMarkus ReindlBarbara KornekMarkus BreuElisabeth Puchhammer-StöcklPaulus RommerThomas Bergerahttps://ror.org/05n3x4p02Center for Virology, Medical University of Vienna, Vienna 1090, Austriabhttps://ror.org/043mz5j54Department of Neurology, University of California San Francisco, San Francisco, CA 94158chttps://ror.org/03r0ha626Department of Pediatrics, University of Utah School of Medicine, Salt Lake City, UT 84132dhttps://ror.org/00dvg7y05Department of Neurology, Department of Neurology, Boston Children’s Hospital, Boston, MA 02115ehttps://ror.org/002pd6e78Department of Pediatric Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114fhttps://ror.org/03wmf1y16Children’s Hospital Colorado, University of Colorado School of Medicine, Aurora, CO 80045ghttps://ror.org/01z7r7q48Children’s Hospital of Philadelphia, Philadelphia, PA 19104hhttps://ror.org/01yc7t268Department of Neurology, Department of Neurology, Washington University in St. Louis, St. Louis, MO 63110ihttps://ror.org/01y64my43Department of Neurology, Department of Neurology, Jacobs School of Medicine and Biomedical Sciences, University of Buffalo Jacobs School of Medicine, Buffalo, NY 14203jhttps://ror.org/00yq55g44Department of Pediatric Neurology, Children´s Hospital Datteln, Witten/Herdecke University, Datteln 45711, Germanykhttps://ror.org/00yq55g44Chair of Biochemistry and Molecular Medicine, Center for Biomedical Education and Research, School of Life Sciences, Witten/Herdecke University, Witten 58448, GermanylDivision of Pediatric Neurology, Department of Pediatrics, Olgahospital, Stuttgart 70174, Germanymhttps://ror.org/05n3x4p02Department of Neurology, Medical University of Vienna, Vienna 1090, Austrianhttps://ror.org/05n3x4p02Comprehensive Center for Clinical Neurosciences and Mental Health, Medical University of Vienna, Vienna 1090, Austriaohttps://ror.org/054pv6659Clinical Department of Neurology, Medical University of Innsbruck, Innsbruck 6020, Austria</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607529123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607475123?af=R">
      <title>Constitutive sporulation in wild fission yeast enhances insect-mediated survival</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607475123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceSex is costly for single-celled organisms, and yeast reproduce sexually only under starvation. We report that many wild strains ofSchizosaccharomyces japonicusisolated in Japan undergo constitutive sporulation even in nutrient-rich ...</description>
      <dc:title>Constitutive sporulation in wild fission yeast enhances insect-mediated survival</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607475123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Hironori NikiShunsuke NodaKeigo FujiwaraTakuya MiyakeKoichiro AkiyamaTaisuke Seikeahttps://ror.org/02xg1m795Department of Gene Function and Phenomics, National Institute of Genetics, Mishima, Shizuoka 411-8540, JapanbGraduate Institute for Advanced Studies, Graduate University for Advanced Studies, Mishima, Shizuoka 411-8540, Japanchttps://ror.org/02278tr80Department of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka 820-8502, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607475123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607475123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617622123?af=R">
      <title>Defensive networks provide basis for late pre-Hispanic Andean polities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617622123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceHow large political communities formed without centralized governments remains a major question in archaeology. Before the rise of the Inca Empire in the Andes (1000 to 1450 CE), people built thousands of hilltop fortifications. Archaeologists ...</description>
      <dc:title>Defensive networks provide basis for late pre-Hispanic Andean polities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617622123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Lauren E. KohutElizabeth ArkushRyan D. SmithRomuald HousseNicholas SuarezSteven A. Wernkeahttps://ror.org/04mpzkf73Department of Chemistry, Physics, Geology and the Environment, Winthrop University, Rock Hill, SC 29733bhttps://ror.org/01an3r305Department of Anthropology, University of Pittsburgh, Pittsburgh, PA 15260cInstituto Francés de Estudios Andinos, Lima 15063, PerúdArchaïos, Paris 75004, Franceehttps://ror.org/02vm5rt34Department of Anthropology, Vanderbilt University, Nashville, TN 37235</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617622123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617622123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613915123?af=R">
      <title>Development of A10P3C, an isoform-selective inhibitor of EGLN2, for targeting breast cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613915123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceOxygen-sensing enzymes help cells adapt to low oxygen and are involved in many diseases, including cancer. Among these enzymes, EGLN2 expression and hydroxylation activity promotes breast cancer growth, but no highly selective inhibitor has ...</description>
      <dc:title>Development of A10P3C, an isoform-selective inhibitor of EGLN2, for targeting breast cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613915123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Qian LiangHuimin ZhuBan-Chieh HuangTzu-Kuan LinYayoi AdachiYing XueChengheng LiaoXiaodong LvXufen YuLee-Wei YangXijuan LiuQing Zhangahttps://ror.org/05byvp690Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390bhttps://ror.org/01rxvg760Institute of Modern Biology, State Key Laboratory of Pharmaceutical Biotechnology, Department of Ultrasound Medicine of Nanjing Drum Tower Hospital, Nanjing University, Nanjing, Jiangsu 210023, ChinacPraexisio Inc., San Diego, CA 92121dhttps://ror.org/013q1eq08School of Pharmacy, Key Laboratory of Smart Drug Delivery (Ministry of Education), Fudan University, Shanghai 201203, Chinaehttps://ror.org/00zdnkx70Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300044, Taiwanfhttps://ror.org/00zdnkx70Biomedical Artificial Intelligence PhD Program, National Tsing Hua University, Hsinchu 300044, Taiwanghttps://ror.org/02mh1d616Physics Division, National Center for Theoretical Sciences, Taipei 106319, TaiwanhJiangsu Provincial Key Laboratory of Cancer Immunology and Metabolism, Nanjing, Jiangsu 210023, Chinaihttps://ror.org/05byvp690Simmons Comprehensive Cancer Center, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613915123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613915123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2622107123?af=R">
      <title>Signaling by a tyrosine-sulfated peptide balances growth and osmotic stress response in rice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2622107123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceCrop survival during drought depends on the ability to transition from growth to stress adaptation. Plant peptide hormones have emerged as important regulators of this critical transition, highlighting the importance of investigating their ...</description>
      <dc:title>Signaling by a tyrosine-sulfated peptide balances growth and osmotic stress response in rice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2622107123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-01T07:00:00Z</dc:date>
      <dc:creator>Yejin ShimEllen Y. RimJin C.-Y. LiaoMyeong-Je ChoGeorge AustinPatrick W. CarlosSameer S. KulkarniRichard J. PayneMaria Florencia ErcoliPamela C. Ronaldahttps://ror.org/05rrcem69Department of Plant Pathology, University of California, Davis, CA 95616bhttps://ror.org/00f54p054Department of Chemical Engineering, Stanford University, CA 94305chttps://ror.org/01an7q238Innovative Genomics Institute, University of California, Berkeley, CA 94720dhttps://ror.org/0384j8v12School of Chemistry, The University of Sydney, Sydney, NSW 2006, Australiaehttps://ror.org/0384j8v12Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australiafhttps://ror.org/05rrcem69The Genome Center, 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>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2622107123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2622107123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536086123?af=R">
      <title>PAK4 exacerbates melanoma immunosuppression by promoting exosome release</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536086123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceImmunotherapy resistance remains a major challenge in melanoma. We identify PAK4 as a key driver of this resistance by promoting the release of PD-L1-enriched exosomes that suppress antitumor immunity. We describe a dual mechanism by which ...</description>
      <dc:title>PAK4 exacerbates melanoma immunosuppression by promoting exosome release</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536086123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Ruizhi ZhouTong XuZeming ShenYiheng ZhangShengrui LiChen LiuJiabin LiHao WangMeisi RenXinghua GaoGuangxiang ZangDanni LiFeng LiaDepartment of Cell Biology, Key Laboratory of Cell Biology, National Health Commission of China and Key Laboratory of Medical Cell Biology, Ministry of Education of China, China Medical University, Shenyang, Liaoning 110122, ChinabLiaoning Provincial Key Laboratory of Oral Disease, Department of Oral Pathology, School and Hospital of Stomatology, China Medical University, Shenyang City 110002, Chinachttps://ror.org/04wjghj95Department of Dermatology, The First Hospital of China Medical University, Shenyang, Liaoning 110001, ChinadKey Laboratory of Immunodermatology, Ministry of Education and National Health Commission of China, National Joint Engineering Research Center for Theranostics of Immunological Skin Diseases, Shenyang, Liaoning 110001, Chinaehttps://ror.org/04wjghj95Department of Medical Oncology, The First Hospital of China Medical University, Shenyang 110001, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536086123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536086123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2515233123?af=R">
      <title>Children from six cultures reliably help their peers—but in different ways</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2515233123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceAll over the world people routinely help one another. Helping provides valuable opportunities to affiliate with others—the foundation of human sociality. Focusing on peer interactions, we tested 4- to 9-y-old children in an experimental task ...</description>
      <dc:title>Children from six cultures reliably help their peers—but in different ways</dc:title>
      <dc:identifier>doi:10.1073/pnas.2515233123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Henriette ZeidlerMarie SchäferEsther HerrmannPatricia KanngiesserLuke MauritsDaniel HaunMichael TomaselloaDepartment of Dynamic and Clinical Psychology and Health, Sapienza University, Rome 00185, Italybhttps://ror.org/03s7gtk40Wilhelm Wundt Institute for Psychology, Leipzig University, Leipzig 04109, Germanychttps://ror.org/03ykbk197School of Psychology, Sport and Health Sciences, University of Portsmouth, Portsmouth PO1 2DY, United Kingdomdhttps://ror.org/008n7pv89School of Psychology, University of Plymouth, Plymouth PL4 8AA, United Kingdomehttps://ror.org/02a33b393Department of Comparative Cultural Psychology, Max Planck Institute for Evolutionary Anthropology, Leipzig 04103, Germanyfhttps://ror.org/00py81415Department of Psychology and Neuroscience, Duke University, Durham, NC 27708</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2515233123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2515233123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607883123?af=R">
      <title>Cell size modulates SBF and Whi5 chromatin association to regulate the Start of the budding yeast cell cycle</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607883123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceFor cells to function, they must divide only after growing enough to keep cell size constant across generations. How cells measure their own size to decide when to divide remains unclear. In budding yeast, this decision is governed by the ...</description>
      <dc:title>Cell size modulates SBF and Whi5 chromatin association to regulate the Start of the budding yeast cell cycle</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607883123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Huan ZhengAna Paulina Gutierrez AlejandreMasoumeh ShafieidarabiMatthew P. SwafferZiad W. El-HajjMaria VeraJan M. SkotheimRodrigo Reyes-Lamotheahttps://ror.org/01pxwe438Department of Biology, McGill University, Montreal, QC H3G 0B1, Canadabhttps://ror.org/00f54p054Department of Biology, Stanford University, Stanford, CA 94158chttps://ror.org/01nrxwf90Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, United Kingdomdhttps://ror.org/01pxwe438Department of Biochemistry, McGill University, Montreal, QC H3G 0B1, Canadaehttps://ror.org/01pxwe438Centre de Recherche en Biologie Structurale, McGill University, Montreal, QC H3G 0B1, CanadafChan Zuckerberg Biohub, San Francisco, CA 94158ghttps://ror.org/01pxwe438Department of Microbiology and Immunology, McGill University, Montreal, QC H3A 2B4, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607883123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607883123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536965123?af=R">
      <title>A structure-aware generative AI framework for revealing functional relationships in protein families</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536965123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceProtein databases contain millions of rapidly accumulating sequences, while increasingly accurate 3D structure predictions provide unprecedented data for analysis. Predicted structures can also be encoded using a structure-focused alphabet ...</description>
      <dc:title>A structure-aware generative AI framework for revealing functional relationships in protein families</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536965123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Divyanshu ShuklaJonathan MartinFaruck MorcosDavit A. Potoyanahttps://ror.org/04rswrd78Bioinformatics and Computational Biology Program, Iowa State University, Ames, IA 50011bhttps://ror.org/049emcs32Department of Biological Sciences, The University of Texas at Dallas, Dallas, TX 75080chttps://ror.org/049emcs32Department of Bioengineering, The University of Texas at Dallas, Dallas, TX 75080dhttps://ror.org/049emcs32Department of Physics, The University of Texas at Dallas, Dallas, TX 75080ehttps://ror.org/049emcs32Center for Systems Biology, The University of Texas at Dallas, Dallas, TX 75080fhttps://ror.org/04rswrd78Department of Chemistry, Iowa State University, Ames, IA 50011ghttps://ror.org/04rswrd78Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, 50011, Ames, IA</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536965123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536965123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615985123?af=R">
      <title>Dynamic tRNA modification programs align codon usage with growth-phase-specific gene expression in Pseudomonas aeruginosa</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615985123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceBacteria fine-tune gene expression not only by controlling which genes are switched on, but also by regulating how efficiently their encoded proteins are produced. Transfer RNAs (tRNAs) carry chemical modifications that can alter their ...</description>
      <dc:title>Dynamic tRNA modification programs align codon usage with growth-phase-specific gene expression in Pseudomonas aeruginosa</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615985123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Yannick Noah FrommeyerJingjing SunJunzhou WuBenedikt KennepohlJulius WitteNicolas Oswaldo GomezJana BattermannLeon BeckerPierina CetraroRuth VerstratenJürgen TomaschAndreas PichDaniel P. DepledgePeter C. DedonSusanne Häusslerahttps://ror.org/04bya8j72Institute of Molecular Bacteriology, TWINCORE, Centre for Experimental and Clinical Infection Research GmbH, Hanover 30625, Germanybhttps://ror.org/042nb2s44Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139cAntimicrobial Resistance Interdisciplinary Research Group, Singapore-Massachusetts Institute of Technology Alliance for Research and Technology Centre, Singapore 138602, Singaporedhttps://ror.org/03d0p2685Institute of Molecular Bacteriology, Helmholtz Centre for Infection Research, Braunschweig 38124, GermanyeInstitute of Virology, Hanover Medical School, Hanover 30625, Germanyfhttps://ror.org/02p1jz666Institute of Microbiology of the Czech Academy of Science, Center Algatech, Třeboň 37981, Czech Republicghttps://ror.org/00f2yqf98Research Core Unit Proteomics and Institute of Toxicology, Hannover Medical School, Hanover 30625, Germanyhhttps://ror.org/00f2yqf98Excellence Cluster 2155 RESIST, Hannover Medical School, Hanover 30625, Germanyihttps://ror.org/028s4q594German Center for Infection Research, partner site Hanover-Braunschweig, Hanover 30625, GermanyjDepartment of Clinical Microbiology, Rigshospitalet, Copenhagen 2100, Denmark</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615985123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615985123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2615179123?af=R">
      <title>Lineage and renewal dynamics of sebaceous glands govern skin barrier integrity in mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2615179123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceToday it remains challenging to study Sebaceous Glands (SGs) in vivo owing to the lack of SG-specific tool mouse models. Here we generated tool mouse models and decoded the cellular dynamics of typical and atypical SGs in vivo. Cell tracing ...</description>
      <dc:title>Lineage and renewal dynamics of sebaceous glands govern skin barrier integrity in mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2615179123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-10-02T07:00:00Z</dc:date>
      <dc:creator>Xichen GuoCaiwei ZhenZhijing WuXinyu WangAoyang TuChong ShangZhuowei ZhaoZifan FuHaoran ZhangYilin ZhouShanshan ChenZixin LiuWenjuan YiQiong Annabel WangYong LiuBao-Liang SongLihua ZhangZhuzhen ZhangaState Key Laboratory of Metabolism and Regulation in Complex Organisms, Taikang Center for Life and Medical Sciences, Hubei Provincial Research Center for Basic Biological Sciences, Hubei Key Laboratory of Cell Homeostasis, Department of Biochemistry, College of Life Sciences, Wuhan University, Wuhan 430072, Chinabhttps://ror.org/033vjfk17School of Computer Science and School of Artificial Intelligence, Wuhan University, Wuhan 430072, Chinachttps://ror.org/01v5mqw79Department of Dermatology, Zhongnan Hospital of Wuhan University, Wuhan 430072, ChinadDepartment of Molecular and Cellular Endocrinology, Arthur Riggs Diabetes and Metabolism Research Institute, City of Hope Medical Center, Duarte, CA 91010ehttps://ror.org/05fazth07Comprehensive Cancer Center, Beckman Research Institute, City of Hope Medical Center, Duarte, CA 91010</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2615179123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2615179123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536061123?af=R">
      <title>Cellular remodeling during reversible life-stage transition in sessile ciliates: Genomic and transcriptomic insights</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536061123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;SignificanceLife-stage transitions require cells to rapidly reorganize architecture, metabolism, and energy allocation in response to environmental change. Here, we combine chromosome-level genomes, stage-resolved transcriptomics, and live-cell imaging to ...</description>
      <dc:title>Cellular remodeling during reversible life-stage transition in sessile ciliates: Genomic and transcriptomic insights</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536061123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-25T07:00:00Z</dc:date>
      <dc:creator>Chao LiZhaorui ZhouTong WuZheng WangZhongyu JiBorong LuXue ZhangMichael LynchYing Yanahttps://ror.org/04rdtx186Institute of Evolution and Marine Biodiversity, Ocean University of China, Qingdao 266003, Chinabhttps://ror.org/04rdtx186Key Laboratory of Evolution and Marine Biodiversity (Ministry of Education), Ocean University of China, Qingdao 266003, Chinachttps://ror.org/03efmqc40Biodesign Center for Mechanisms of Evolution, Arizona State University, Tempe AZ 85287</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536061123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536061123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2618666123?af=R">
      <title>Uneven attention to climate tipping points</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2618666123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;Climate tipping points have moved from theoretical concern to a practical challenge for climate-risk assessment and governance. Yet whether scientific attention is aligned with risk-relevant characteristics of climate tipping elements (CTEs) has not been ...</description>
      <dc:title>Uneven attention to climate tipping points</dc:title>
      <dc:identifier>doi:10.1073/pnas.2618666123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Heming WangBingyu ChenFengmei MaNico WunderlingTimothy M. LentonAsaf Tzachorahttps://ror.org/04gwbew76Key Laboratory of Eco-Industry (Ministry of Ecology and Environment), School of Metallurgy, Northeastern University, Shenyang, Liaoning 110819, Chinabhttps://ror.org/03qn8fb07Commonwealth Scientific and Industrial Research Organisation, Canberra, ACT 2601, Australiachttps://ror.org/01vxfm326Center for Collective Learning, Corvinus Institute for Advanced Studies, Corvinus University of Budapest, Budapest 1093, Hungarydhttps://ror.org/034t30j35State Key Laboratory of Regional and Urban Ecology, Institute of Urban Environment, Chinese Academy of Sciences, Xiamen 361021, Chinaehttps://ror.org/01n6r0e97Potsdam Institute for Climate Impact Research, Member of the Leibniz Association, Potsdam 14473, Germanyfhttps://ror.org/04cvxnb49Center for Critical Computational Studies, Goethe University Frankfurt, Frankfurt am Main 60629, Germanyghttps://ror.org/01n6r0e97Senckenberg Research Institute and Natural History Museum, Member of the Leibniz Association, Frankfurt am Main 60325, Germanyhhttps://ror.org/03yghzc09Global Systems Institute, University of Exeter, Exeter EX4 4QE, United Kingdomihttps://ror.org/01px5cv07School of Sustainability, Aviram Sustainability and Climate Program, Reichman University, Herzliya 4610101, Israeljhttps://ror.org/013meh722Institute for Technology and Humanity, Centre for the Study of Existential Risk, University of Cambridge, Cambridge CB2 1SB, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2618666123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2618666123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2630040123?af=R">
      <title>Twist in the fibril: Structure guides inhibition of TGFBIp amyloid formation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2630040123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Twist in the fibril: Structure guides inhibition of TGFBIp amyloid formation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2630040123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Jan J. Enghildahttps://ror.org/01aj84f44Department of Molecular Biology and Genetics, Aarhus University, Aarhus 8000C, Denmark</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2630040123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2630040123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2629158123?af=R">
      <title>The other immune landscape of SARS-CoV-2 evolution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2629158123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>The other immune landscape of SARS-CoV-2 evolution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2629158123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Mahan Ghafariahttps://ror.org/052gg0110Department of Biology, University of Oxford, Oxford OX1 3EL, United Kingdombhttps://ror.org/052gg0110Pandemic Sciences Institute, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2629158123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2629158123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2630482123?af=R">
      <title>A 40-y-old model of muscle metabolism, finally open to scrutiny</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2630482123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>A 40-y-old model of muscle metabolism, finally open to scrutiny</dc:title>
      <dc:identifier>doi:10.1073/pnas.2630482123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Juliano MorimotoaPrograma de Pós-graduação em Ecologia e Conservação, Department of Biological Sciences, Federal University of Paraná, Curitiba 82590-300, Brazilbhttps://ror.org/016476m91Institute of Mathematics, School of Natural and Computing Sciences, University of Aberdeen, King’s College, Aberdeen AB24 3FX, United Kingdomchttps://ror.org/036rp1748Department of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo 14040-900, Brazil</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2630482123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2630482123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2621014123?af=R">
      <title>Unexplained rapid bill-size changes in an urban bird during the COVID-19 anthropause</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2621014123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Unexplained rapid bill-size changes in an urban bird during the COVID-19 anthropause</dc:title>
      <dc:identifier>doi:10.1073/pnas.2621014123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Samson Acoca-PidolleLaurine A. Mathieuahttps://ror.org/001tmjg57Department of Ecology and Evolutionary Biology, University of Kansas, Lawrence, KS 66045bhttps://ror.org/051escj72Centre d‘Ecologie Fonctionnelle et Evolutive, CNRS, Ecole Pratique des Hautes Etudes, Institut de Recherche pour le Developpement, Université de Montpellier, Montpellier 34090, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2621014123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2621014123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619004123?af=R">
      <title>Potential vascular confound in GPR84-PET imaging following systemic LPS administration</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619004123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Potential vascular confound in GPR84-PET imaging following systemic LPS administration</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619004123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Sami S. ZoghbiRobert B. InnisaMolecular Imaging Branch, National Institute of Mental Health, NIH, Bethesda, MD 20892-1026</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2619004123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2619004123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2624547123?af=R">
      <title>Reply to Acoca-Pidolle and Mathieu: Rapid phenotypic change in an urban bird likely driven by resource changes during COVID-19</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2624547123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Acoca-Pidolle and Mathieu: Rapid phenotypic change in an urban bird likely driven by resource changes during COVID-19</dc:title>
      <dc:identifier>doi:10.1073/pnas.2624547123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Eleanor S. DiamantPamela J. Yehahttps://ror.org/046rm7j60Department of Ecology and Evolutionary Biology, University of California Los Angeles, Los Angeles, CA 90095bhttps://ror.org/04yrgt058Division of Science, Mathematics, and Computing, Bard College, Annandale-on-Hudson, NY 12504chttps://ror.org/01arysc35Santa Fe Institute, Santa Fe, NM 87501</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2624547123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2624547123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2623658123?af=R">
      <title>Reply to Zoghbi and Innis: Clarifying the cellular basis of GPR84-PET signal in neuroinflammation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2623658123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Zoghbi and Innis: Clarifying the cellular basis of GPR84-PET signal in neuroinflammation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623658123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-28T07:00:00Z</dc:date>
      <dc:creator>Mausam KalitaRenesmee C. KuoSamantha T. ReyesPeter J. H. ScottGraeme MilliganMichelle L. Jamesahttps://ror.org/00f54p054Department of Radiology, Stanford University, Stanford, CA 94305bhttps://ror.org/00f54p054Department of Electrical Engineering, Stanford University, Stanford, CA 94305chttps://ror.org/00jmfr291Division of Nuclear Medicine, Department of Radiology, University of Michigan Medical School, Ann Arbor, MI 48109dhttps://ror.org/00vtgdb53Centre for Translational Pharmacology, School of Molecular Biosciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, Scotland G12 8QQ, United Kingdomehttps://ror.org/00f54p054Department of Neurology and Neurological Sciences, Stanford University, Stanford, CA 94304</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2623658123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2623658123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2632674123?af=R">
      <title>Retraction for Lin and Lee, A dual self-regulatory platform for programmable biosynthesis of L-lysine-derived alkaloids</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2632674123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 40, October 2026. &lt;br/&gt;</description>
      <dc:title>Retraction for Lin and Lee, A dual self-regulatory platform for programmable biosynthesis of L-lysine-derived alkaloids</dc:title>
      <dc:identifier>doi:10.1073/pnas.2632674123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-09-30T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>40</prism:number>
      <prism:coverDate>2026-10-06T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-10-06T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2632674123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2632674123?af=R</prism:url>
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   </item>
</rdf:RDF>