<?xml version="1.0" encoding="UTF-8" standalone="no"?><rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns="http://purl.org/rss/1.0/" xmlns:cc="http://web.resource.org/cc/" xmlns:content="http://purl.org/rss/1.0/modules/content/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:prism="http://prismstandard.org/namespaces/basic/2.0/">
   <channel rdf:about="https://www.pnas.org/loi/pnas?af=R">
      <title>Current Issue</title>
      <description></description>
      <link>https://www.pnas.org/loi/pnas?af=R</link>
      <dc:title>Proceedings of the National Academy of Sciences: Proceedings of the National Academy of Sciences: Table of Contents</dc:title>
      <dc:publisher>Proceedings of the National Academy of Sciences</dc:publisher>
      <dc:language>en-US</dc:language>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <items>
         <rdf:Seq>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/iti2426123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2611387123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617960123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607144123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535524123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603271123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524614123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612171123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536870123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604088123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2529903123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535689123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534793123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531253123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2523612123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601925123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2609325123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535879123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524065123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2533437123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535430123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2522000123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2538081123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602147123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2520331123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537770123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528009123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2612003123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535299123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537686123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2538139123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605237123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602209123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606892123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524866123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603105123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607035123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2520997123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603966123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2607573123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605725123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535777123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2603926123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2424788123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2511427123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2529786123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528970123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535199123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2526271123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602470123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2530690123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536368123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606552123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2518957123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534946123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2536989123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524671123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531054123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601061123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528450123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604929123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605288123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528668123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2523043123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2538027123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537884123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2609054123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531481123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2601472123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524190123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2525378123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531280123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604369123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2524496123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2517639123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2523183123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2602575123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531602123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2609202123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605694123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604814123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2529341123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604082123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2611096123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2605838123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2614646123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2613743123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606967123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606646123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535289123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617334123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617330123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617803123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2617340123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2613406123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2613719123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2609802123?af=R"/>
         </rdf:Seq>
      </items>
   </channel>
   <image rdf:about="https://www.pnas.org/cms/asset/433b8ee2-291a-4032-a821-9a689e8fcaa8/default_cover.png">
      <title>Proceedings of the National Academy of Sciences</title>
      <url>https://www.pnas.org/cms/asset/433b8ee2-291a-4032-a821-9a689e8fcaa8/default_cover.png</url>
      <link>https://www.pnas.org/loi/pnas?af=R</link>
   </image>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/iti2426123?af=R">
      <title>In This Issue</title>
      <link>https://www.pnas.org/doi/abs/10.1073/iti2426123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>In This Issue</dc:title>
      <dc:identifier>doi:10.1073/iti2426123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-16T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/iti2426123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/iti2426123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611387123?af=R">
      <title>Madhav Gadgil (1942–2026): A pioneering Indian ecologist’s legacy of biodiversity conservation and human coexistence</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611387123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Madhav Gadgil was an evolutionary ecologist and champion of governmental and intergovernmental policies for biodiversity conservation, human coexistence with nature, and indigenous rights to land, natural resources, and self-governance. He made ...</description>
      <dc:title>Madhav Gadgil (1942–2026): A pioneering Indian ecologist’s legacy of biodiversity conservation and human coexistence</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611387123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Krushnamegh KunteUtkarsh GhateK. A. Subramanianahttps://ror.org/03ht1xw27National Centre Biological Sciences, Tata Institute of Fundamental Research, Bengaluru, Karnataka 560065, Indiabhttps://ror.org/011pwcp79Research and Action in Natural Wealth Administration, Ganesh Nagar, Pune, Maharashtra 411038, Indiachttps://ror.org/00h6p6a20Zoological Survey of India, Chennai, Tamil Nadu 600028, India</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611387123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611387123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617960123?af=R">
      <title>Driven by climate change, sudden swings between wet and dry create “hydrologic whiplash”</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617960123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Driven by climate change, sudden swings between wet and dry create “hydrologic whiplash”</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617960123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Amy McDermott</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617960123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617960123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607144123?af=R">
      <title>Quantum algorithms for viscosity solutions to nonlinear Hamilton–Jacobi equations based on an entropy penalization method</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607144123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceWe developed quantum algorithms for nonlinear Hamilton–Jacobi equations that obviated several major obstacles for nonlinear partial differential equations:valid for general convex and strongly nonlinear Hamiltonian with small dissipation;valid ...</description>
      <dc:title>Quantum algorithms for viscosity solutions to nonlinear Hamilton–Jacobi equations based on an entropy penalization method</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607144123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Shi JinNana Liuahttps://ror.org/0220qvk04Institute of Natural Sciences, Shanghai Jiao Tong University, Shanghai 200240, Chinabhttps://ror.org/0220qvk04School of Mathematical Sciences, Shanghai Jiao Tong University, Shanghai 200240, Chinachttps://ror.org/0220qvk04Ministry of Education Key Laboratory in Scientific and Engineering Computing, Shanghai Jiao Tong University, Shanghai 200240, Chinadhttps://ror.org/0220qvk04Global College, Shanghai Jiao Tong University, Shanghai 200240, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607144123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607144123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535524123?af=R">
      <title>Enhanced global storm surges by tropical cyclone poleward migration</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535524123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceTropical cyclone–induced storm surges are among the most destructive coastal hazards in the world, yet their long-term trends under climate change have remained poorly quantified. This study reveals a robust increase in tropical cyclone–...</description>
      <dc:title>Enhanced global storm surges by tropical cyclone poleward migration</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535524123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-01T07:00:00Z</dc:date>
      <dc:creator>Yi-Peng GuoZhe-Min Tanahttps://ror.org/03d2yag39State Key Laboratory of Severe Weather Meteorological Science and Technology, Key Laboratory of Mesoscale Severe Weather/Ministry of Education, and School of Atmospheric Sciences, Nanjing University, Nanjing 210023, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535524123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535524123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603271123?af=R">
      <title>New climate regime restructures the ecology of Canada’s Northern Great Lakes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603271123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe effects of anthropogenic climate change on large, deep Arctic lakes have been historically buffered by their extensive ice covers. However, recent accelerated warming has now triggered a pronounced response in the algal communities of ...</description>
      <dc:title>New climate regime restructures the ecology of Canada’s Northern Great Lakes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603271123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-01T07:00:00Z</dc:date>
      <dc:creator>Kathleen M. RühlandNeal MicheluttiMarlene S. EvansKimberly L. HowlandJohn P. Smolahttps://ror.org/02y72wh86Department of Biology, Paleoecological Environmental Assessment and Research Lab, Queen’s University, Kingston, ON K7L 3N6, Canadabhttps://ror.org/026ny0e17Environment and Climate Change Canada, Saskatoon, SK S7N 3H5, Canadachttps://ror.org/02qa1x782Arctic Fisheries and Marine Mammal Science Division, Freshwater Institute, Fisheries and Oceans Canada, Winnipeg, MB R3T 2N6, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603271123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603271123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524614123?af=R">
      <title>An aquaglyceroporin governs cellular water and CO2 conductance relevant for vesicular mineral formation in a marine calcifier</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524614123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceMany marine calcifiers initiate skeleton formation by producing a mineral precursor inside cells via endocytotic uptake of seawater-like fluids. To concentrate the substrates required for mineralization, cells must remove both water and ions (...</description>
      <dc:title>An aquaglyceroporin governs cellular water and CO2 conductance relevant for vesicular mineral formation in a marine calcifier</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524614123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Ann-Sophie MattSmilla TetzlaffSima JonusaiteAlex Quijada-RodriguezMarcus ScheweSönke CordeiroDirk WeihrauchMarian Y. Huahttps://ror.org/00v8kcx92Institute of Physiology, Christian-Albrechts-University, Kiel 24118, Germanybhttps://ror.org/04wn28048Department of Biological Sciences, University of Tulsa, Tulsa, OK 74101chttps://ror.org/00fn7gb05Department of Biology, Wilfrid Laurier University, Waterloo N2L 3C5, Ontaria, Canadadhttps://ror.org/02gfys938Department of Biological Sciences, University of Manitoba, Winnipeg R3T 2N2, Manitoba, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524614123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524614123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612171123?af=R">
      <title>Arabidopsis YEATS domain proteins facilitate DNA double-strand break repair via homology-directed pathways</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612171123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceDetecting and repairing damaged DNA is critical for maintaining cellular function. These processes occur within chromatin, yet how chromatin effectors (proteins that modulate the properties and compositions of chromatin) facilitate this ...</description>
      <dc:title>Arabidopsis YEATS domain proteins facilitate DNA double-strand break repair via homology-directed pathways</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612171123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Neeraja VegesnaLaura Bouza-MorcilloClara BourbousseYasaman Jami-AlahmadiEn LiMaherun NisaAna Marie S. PalancaJames A. WohlschlegelJulie A. Lawahttps://ror.org/03xez1567Plant Molecular and Cellular Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037bhttps://ror.org/046rm7j60Department of Biological Chemistry, University of California, Los Angeles, CA 90095chttps://ror.org/0168r3w48Division of Biological Sciences, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612171123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612171123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536870123?af=R">
      <title>mRNA delivery of a class 1/4 SARS-CoV-2 neutralizing antibody protects against diverse sarbecoviruses in a lethal mouse challenge model</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536870123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificancePan-sarbecovirus broadly neutralizing antibodies (bNAbs) are urgently needed to combat SARS-CoV-2 variants, mitigate future zoonotic spillover, and inform vaccine design. Here, we describe the isolation of bNAb lineages from a participant with ...</description>
      <dc:title>mRNA delivery of a class 1/4 SARS-CoV-2 neutralizing antibody protects against diverse sarbecoviruses in a lethal mouse challenge model</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536870123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Ashwin N. SkellyChengcheng FanJennifer R. KeeffeArya B. ÖktenEdem GavorMaddy L. NewbyJoel D. AllenEdward F. KreiderWenge DingRebecca A. OsbaldestonYounghoon ParkAndrew J. ConnellMelinda G. LituchyFrederic Bibollet-RucheKatelyn M. RadfordAnthony P. WestMario A. Peña-HernándezKendra CruickshankWeimin LiuYingying LiAmie AlbertusBrieyanna McWilliamsRonnie M. RussellKylie M. KonrathJonathan L. TorresMeng YuanHongmei GaoDavid C. MontefioriMichael S. SaagPaul A. GoepfertDaniel W. KulpAndrew B. WardIan A. WilsonGeorge M. ShawRaiees AndrabiMax CrispinDrew WeissmanCraig B. WilenPamela J. BjorkmanBeatrice H. Hahnahttps://ror.org/00b30xv10Department of Medicine, University of Pennsylvania, Philadelphia, PA 19104bhttps://ror.org/00b30xv10Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104chttps://ror.org/05dxps055Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125dDepartment of Laboratory Medicine, Yale School of Medicine, New Haven, CT 06510eDepartment of Immunobiology, Yale School of Medicine, New Haven, CT 06510fhttps://ror.org/01ryk1543School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, United Kingdomghttps://ror.org/04wncat98Vaccine and Immunotherapy Center, The Wistar Institute, Philadelphia, PA 19104hhttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037ihttps://ror.org/03njmea73Duke Human Vaccine Institute, Duke University Medical Center, Durham, NC 27710jhttps://ror.org/03njmea73Department of Surgery, Duke University Medical Center, Durham, NC 27710khttps://ror.org/008s83205Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35233lhttps://ror.org/008s83205Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35233mhttps://ror.org/008s83205O’Neal Comprehensive Cancer Center, University of Alabama at Birmingham, Birmingham, AL 35233</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536870123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536870123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604088123?af=R">
      <title>Functional asymmetry and essential structural roles of PDE6α and PDE6β subunits in rod–photoreceptor integrity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604088123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Significancephosphodiesterase-6 (PDE6) is a rod-specific enzyme critical for phototransduction, comprised of a dimeric αβ catalytic core and two inhibitory γ subunits. Using transgenic mice with PDE6-subunit-specific inactivating mutations, biochemical ...</description>
      <dc:title>Functional asymmetry and essential structural roles of PDE6α and PDE6β subunits in rod–photoreceptor integrity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604088123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Roman SmidakDeepak PoriaFangyuan GaoZhiqian DongJianye ZhangMarco BassettoEleonora RisalitiAleksander TworakWeijing LiuVladimir J. KefalovKrzysztof Palczewskiahttps://ror.org/04gyf1771Brunson Center for Translational Vision Research, Department of Ophthalmology and Visual Sciences, Gavin Herbert Eye Institute, University of California, Irvine, CA 92697bChromatography and Mass Spectrmetry Division, Thermo Fisher Scientific, San Jose, CA 95134chttps://ror.org/04gyf1771Department of Physiology and Biophysics, University of California, Irvine, CA 92697dhttps://ror.org/04gyf1771Department of Chemistry, University of California, Irvine, CA 92697ehttps://ror.org/04gyf1771Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604088123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604088123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529903123?af=R">
      <title>A census of anti-CRISPR proteins reveals AcrIE9 and AcrIE13 as inhibitors of the Escherichia coli K12 type IE CRISPR-Cas system</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529903123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceA census of Acrs withinEnterobacteriaceaereveals that the most widespread anti-CRISPR cluster in this order consists ofacrIE9,acrIE10, andacrIE13protein, identified in this study. Mechanistically, AcrIE9 binds to the Cas7 subunit of the ...</description>
      <dc:title>A census of anti-CRISPR proteins reveals AcrIE9 and AcrIE13 as inhibitors of the Escherichia coli K12 type IE CRISPR-Cas system</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529903123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Dmitry TaranenkoOksana KotovskayaKonstantin KuznedelovDaria YanovskayaAlina DemkinaSofya FardeevaViktor MamontovKaiya VierraNathaniel BurmanDan LiMinggui WangBlake WiedenheftKonstantin SeverinovEkaterina SemenovaArtem Isaevahttps://ror.org/03f9nc143Skolkovo Institute of Science and Technology, Moscow 143028, Russiabhttps://ror.org/05vt9qd57Waksman Institute for Microbiology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854cShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow 117997, Russiadhttps://ror.org/02w0trx84Montana State University, Bozeman, Department of Microbiology and Cell Biology, Bozeman, MT 59717ehttps://ror.org/013q1eq08Institute of Antibiotics, Huashan Hospital, Fudan University, Shanghai 200040, Chinafhttps://ror.org/01yq9ya27Institute of Gene Biology, Moscow 119334, Russia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529903123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529903123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535689123?af=R">
      <title>Circular and athermal atmospheric CO2 capture by food waste-derived amyloid sorbents</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535689123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCurrent amine-based direct air capture technologies often exhibit low CO2capacity under ambient air, require energy-intensive thermal regeneration, and suffer from chemical degradation that can generate hazardous by-products. Here, we develop ...</description>
      <dc:title>Circular and athermal atmospheric CO2 capture by food waste-derived amyloid sorbents</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535689123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Zhou DongMing DaiFelix DonatDominik RichertBin DaiPaweł P. ZiemiańskiJiangtao ZhouMilad RadiomMohammad PeydayeshYanwen LiXiuhuai LiHui WuChristoph R. MüllerWenshuai ChenRaffaele MezzengaaSwiss Federal Institute of Technology in Zurich, Department of Health Sciences and Technology, Zürich 8092, Switzerlandbhttps://ror.org/02yxnh564Key Laboratory of Bio-based Material Science and Technology, Ministry of Education, Northeast Forestry University, Harbin 150040, People’s Republic of Chinachttps://ror.org/05a28rw58Swiss Federal Institute of Technology in Zurich, Department of Mechanical and Process Engineering, Zürich CH-8092, Switzerlanddhttps://ror.org/0220qvk04School of Automation and Intelligent Sensing, Shanghai Jiao Tong University, Shanghai 200240, People’s Republic of ChinaeBuilding Energy Materials and Components, Empa, Dübendorf 8600, Switzerlandfhttps://ror.org/01tgyzw49Department of Food Science and Technology, National University of Singapore, 2 Science Drive 2 117542, Singaporeghttps://ror.org/0530pts50College of Food Science and Engineering, South China University of Technology, Guangzhou 510640, People’s Republic of Chinahhttps://ror.org/05a28rw58Swiss Federal Institute of Technology in Zurich, Department of Materials, Zürich 8093, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535689123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535689123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534793123?af=R">
      <title>Dissecting hydrogen bond energetics to answer the age-old question: “How much do hydrogen bonds contribute to enzymatic catalysis?”</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534793123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceEnzymes enable the fast and specific reactions needed to sustain life, and enzyme engineering holds great promise for industry and medicine. Highlighting our limited understanding, we cannot design enzymes that rival those from nature. ...</description>
      <dc:title>Dissecting hydrogen bond energetics to answer the age-old question: “How much do hydrogen bonds contribute to enzymatic catalysis?”</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534793123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Margaux M. PinneyCorey LiuDaniel Herschlagahttps://ror.org/00f54p054Department of Biochemistry, Stanford University, Stanford, CA 94305bhttps://ror.org/01an7q238Department of Chemistry, University of California Berkeley, Berkeley, CA 94720chttps://ror.org/04n1n3n22California Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA 94720dBiohub San Francisco, San Francisco, CA 94158ehttps://ror.org/00f54p054Sarafan ChEM-H, Stanford University, Stanford, CA 94305fhttps://ror.org/00f54p054Stanford Magnetic Resonance Laboratory, Stanford University, Stanford, CA 94305ghttps://ror.org/00f54p054Department of Chemical 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534793123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534793123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531253123?af=R">
      <title>Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531253123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceDiverse bacterial species use filamentous surface appendages called type IV pili (T4P) to move along surfaces, take up DNA for horizontal gene transfer, and stick to biotic and abiotic surfaces. The forceful retraction of these filaments is ...</description>
      <dc:title>Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531253123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Abigail E. TeipenJacob D. HoltDiane L. LynchYixuan PengTriana N. DaliaJames C. GumbartCarey D. NadellAnkur B. DaliaaDepartment of Biology, Indiana University, Bloomington, IN 47405bDepartment of Biological Sciences, Dartmouth, Hanover, NH 03755cDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755dhttps://ror.org/01zkghx44School of Physics, Georgia Institute of Technology, Atlanta, GA 30332ehttps://ror.org/01zkghx44School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531253123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531253123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523612123?af=R">
      <title>A pericyte chloride clamp mechanism governs capillary control of cerebral blood flow</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523612123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceXiang et al. demonstrate that thin-strand pericytes found in the deepest parts of the capillary bed of the brain express functional TMEM16A calcium-activated chloride channels. They show that L- and T-type voltage-dependent calcium channels in ...</description>
      <dc:title>A pericyte chloride clamp mechanism governs capillary control of cerebral blood flow</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523612123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Liuruimin XiangAshwini HariharanDominic IsaacsNick WeirThomas A. LongdenaDepartment of Pharmacology and Physiology, University of Maryland School of Medicine, Baltimore, MD 21201bProgram in Neuroscience, University of Maryland School of Medicine, Baltimore, MD 21201</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523612123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523612123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601925123?af=R">
      <title>Avoidance of MAIT cells is an essential determinant of Listeria monocytogenes pathogenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601925123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceListeriamonocytogenesis a bacterial pathogen that grows freely in the environment but can become intracellular following ingestion of contaminated food. AlthoughL. monocytogenescan synthesize most metabolites required for growth, it lacks ...</description>
      <dc:title>Avoidance of MAIT cells is an essential determinant of Listeria monocytogenes pathogenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601925123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Rafael Rivera-LugoJesse Garcia CastilloMariya LobanovskaEugene TangAndrea Anaya-SanchezScott EspichSarah A. StanleyMichel DuPageDaniel A. Portnoyahttps://ror.org/01an7q238Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720bhttps://ror.org/01an7q238Graduate Group in Microbiology, University of California Berkeley, Berkeley, CA 94720chttps://ror.org/01an7q238Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA 94720dhttps://ror.org/01an7q238Division of Infectious Disease and Vaccinology, School of Public Health, University of California Berkeley, Berkeley, CA 94720</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601925123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601925123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609325123?af=R">
      <title>A long-distance signaling loop promotes soybean nodulation and productivity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609325123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceLegumes rely on symbiotic nitrogen fixation to sustain productivity in both agricultural and natural ecosystems, yet the mechanisms that promote the formation of nitrogen-fixing root nodules remain poorly understood. This study uncovers a ...</description>
      <dc:title>A long-distance signaling loop promotes soybean nodulation and productivity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609325123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Jingbo DuanJinbin WangRunze GuoChancelor B. ClarkZhuojun LuoXiaochong LiLeonie TrabertXing-Qi HuangW. Andy TaoNatalia DudarevaGary StaceyBlake C. MeyersJianxin Maahttps://ror.org/02dqehb95Department of Agronomy, Purdue University, West Lafayette, IN 47907bhttps://ror.org/02dqehb95Center for Plant Biology, Purdue University, West Lafayette, IN 47907chttps://ror.org/02dqehb95Department of Biochemistry, Purdue University, West Lafayette, IN 47907dhttps://ror.org/02ymw8z06Division of Plant Science &amp; Technology, University of Missouri, Columbia, MO 65211ehttps://ror.org/05rrcem69Genome Center and Department of Plant Sciences, University of California, Davis, CA 95616</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609325123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609325123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535879123?af=R">
      <title>Targeting the cGAS–STING pathway mitigates Huntington disease pathogenesis in a knock-in mouse model</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535879123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceHuntington disease (HD) is a hereditary neurodegenerative disorder with prominent inflammation and no disease-modifying therapies. We identify the DNA-sensing cGAS–STING pathway as a key driver of HD-related inflammation and cellular stress. ...</description>
      <dc:title>Targeting the cGAS–STING pathway mitigates Huntington disease pathogenesis in a knock-in mouse model</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535879123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Anuradha KesharwaniSunayana DagarIsabella ZunigaMarianne Charlene MonetGanesh HaladeGunjan UpadhyayUri Nimrod Ramírez-JarquínVioleta Gisselle Lopez-HuertaEmaad MirzaNing QuanSrinivasa SubramaniamaDepartment of Chemistry and Biochemistry, Florida Atlantic University, Jupiter, FL 33458bFlorida Atlantic University, Stiles-Nicholson Brain Institute, Jupiter, FL 33458cDavid and Lynn Nicholson Center for Neuroscience Research, Jupiter, FL 33458dFAU Honors College, Jupiter, FL 33458eThe International Max Planck Research School for Synapses and Circuits, Max Planck Florida Institute for Neuroscience, Jupiter, FL 33458fDepartment of Biological Sciences, Charles E. Schmidt College of Science, Florida Atlantic University, Boca Raton, FL 33431ghttps://ror.org/032db5x82Heart Institute, Division of Cardiovascular Sciences, Department of Internal Medicine, University of South Florida, Tampa, FL 33602hhttps://ror.org/032db5x82Hypertension and Kidney Research Center, Heart Institute, University of South Florida, Tampa, FL 33602ihttps://ror.org/046e90j34National Institute of Cardiology Ignacio Chavez, Mexico City 14080, Mexicojhttps://ror.org/01tmp8f25Institute of Cellular Physiology, National Autonomous University of Mexico, Mexico City 04510, MexicokDepartment of Biomedical Science, Charles E. Schmidt College of Medicine, Florida Atlantic University, Boca Raton, FL 33431lCenter for Molecular Biology and Biotechnology, Jupiter, FL 33458</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535879123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535879123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524065123?af=R">
      <title>Active zone plasticity couples sleep need to presynaptic hypophosphorylation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524065123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceSynaptic plasticity has been causally linked to homeostatic sleep regulation. However, how synaptic plasticity governs the dynamic accumulation and dissipation of sleep pressure remains elusive. Using synapse-enriched proteomics and phospho-...</description>
      <dc:title>Active zone plasticity couples sleep need to presynaptic hypophosphorylation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524065123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Chengji PiaoEwelina P. DutkiewiczLaxmikanth KolliparaAlbert SickmannSheng HuangStephan J. Sigristahttps://ror.org/046ak2485Institute for Biology/Genetics, Freie Universität Berlin, Berlin 14195, GermanybNeuroCure Cluster of Excellence, Charité Universitätsmedizin, Berlin 10117, GermanycLeibniz-Institut für Analytische Wissenschaften, Dortmund 44139, Germanydhttps://ror.org/04tsk2644Medizinische Fakultät, Ruhr-Universität Bochum, Bochum 44801, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524065123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524065123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2533437123?af=R">
      <title>A biomineralized light-guiding structure in the porous calcitic skeleton of the sea star Protoreaster nodosus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2533437123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceEngineering cellular solids are typically designed for structural applications and rarely incorporate optical functionality, yet efficient optical control is essential for lightweight sensors, displays, and energy systems. Although biological ...</description>
      <dc:title>A biomineralized light-guiding structure in the porous calcitic skeleton of the sea star Protoreaster nodosus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2533437123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Liuni ChenHannah FeldsteinZian JiaChenhao HuHongshun ChenYang GengEmily M. PetermanCarla SlebodnickDaniel I. SpeiserDaniel BaumMathias KolleLing Liahttps://ror.org/00b30xv10Department of Materials Science and Engineering, University of Pennsylvania, Philadelphia, PA 19104bhttps://ror.org/02smfhw86Department of Mechanical Engineering, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061chttps://ror.org/042nb2s44Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139dhttps://ror.org/03gh96r95Department of Earth and Oceanographic Science, Bowdoin College, Brunswick, ME 04011ehttps://ror.org/02smfhw86Department of Chemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061fhttps://ror.org/02b6qw903Department of Biological Sciences, University of South Carolina, Columbia, SC 29208ghttps://ror.org/02eva5865Department of Visual and Data-Centric Computing, Zuse Institute Berlin, Berlin 14195, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2533437123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2533437123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535430123?af=R">
      <title>Chemical neighborhood exploration for substrate discovery in biocatalysis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535430123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceComputational methods in biocatalysis are mostly focused on biocatalytic matrix engineering, whereas identifying the most reactive substrates for a given catalyst remains much less developed. By quantitatively reproducing the experimentally ...</description>
      <dc:title>Chemical neighborhood exploration for substrate discovery in biocatalysis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535430123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Yaroslav V. SolovevNikita N. KostinYuri A. ProkopenkoPatrick MassonIvan V. SmirnovHongkai ZhangWei ZhengIgor A. YaroshevichAlexey V. StepanovPetr A. PopovAlexander G. Gabibovahttps://ror.org/05qrfxd25Department of Peptide and Protein Technologies, M.M. Shemyakin and Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russiabhttps://ror.org/05256ym39Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, RussiacThe National Key Laboratory of Intelligent Tracking and Forecasting for Infectious Diseases, School of Statistics and Data Science, Academy for Advanced Interdisciplinary Studies, Key Laboratory of Pure Mathematics and Combinatorics and Key Laboratory for Medical Data Analysis and Statistical Research, Nankai University, Tianjin 300071, People’s Republic of Chinadhttps://ror.org/010pmpe69Department of Biophysics, Faculty of Biology, Lomonosov Moscow State University, Moscow 119991, Russiaehttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037fhttps://ror.org/02yrs2n53School of Science, Constructor University Bremen, Bremen 28759, GermanygConstructor Labs, Bremen 28759, Germanyhhttps://ror.org/010pmpe69Department of Industrial Pharmacology, Faculty of Fundamental Medicine, Lomonosov Moscow State University, Moscow 119991, Russia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535430123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535430123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2522000123?af=R">
      <title>Psychedelics disrupt hierarchical cortical propagations in the default mode network of humans and mice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2522000123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificancePsychedelic substances are increasingly recognized for both their therapeutic potential and risks. Dissensus in how psychedelics impact macroscale brain function is one barrier to understanding risks and benefits at a neurobiological level. ...</description>
      <dc:title>Psychedelics disrupt hierarchical cortical propagations in the default mode network of humans and mice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2522000123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Adam R. PinesXue ZhangJohn KochalkaSam S. VesunaIsaac V. KauvarDivya RajasekharanT. Rick ReneauTeddy J. AkikiLaura M. HackJoshua S. SiegelLeanne M. Williamsahttps://ror.org/00f54p054Department of Psychiatry and Behavioral Sciences, Stanford University, Palo Alto, CA 94305bhttps://ror.org/00f54p054Department of Bioengineering, Stanford University, Palo Alto, CA 94305cDepartment of Education, Graduate School of Education, Stanford University, Palo Alto, CA 94305dDepartment of Radiology, Mallinckrodt Institute of Radiology, Washington University School of Medicine, St. Louis, MO 63110ehttps://ror.org/02hd1sz82Sierra-Pacific Mental Illness Research, Education and Clinical Center, Veterans Affairs Palo Alto Health Care System, Palo Alto, CA 94304fhttps://ror.org/0190ak572Department of Psychiatry, New York University, Langone Center for Psychedelic Medicine, New York University Grossman School of Medicine, New York, NY 10016ghttps://ror.org/01s434164Nathan Kline Institute for Psychiatric Research, New York, NY 10962</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2522000123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2522000123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2538081123?af=R">
      <title>Shaping chaos in bilayer graphene cavities</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2538081123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceQuantum chaos plays a central role in mesoscopic physics, quantum information, and wavefunction engineering, yet solid-state platforms that allow continuous control of chaotic dynamics have been lacking. Bilayer graphene cavities provide a ...</description>
      <dc:title>Shaping chaos in bilayer graphene cavities</dc:title>
      <dc:identifier>doi:10.1073/pnas.2538081123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Jucheng LinYicheng ZhuangAnton M. GrafEric J. HellerJoonas Keski-Rahkonenahttps://ror.org/03vek6s52Department of Physics, Harvard University, Cambridge, MA 02138bhttps://ror.org/03vek6s52Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138chttps://ror.org/0220qvk04Department of Physics and Astronomy, Shanghai Jiao Tong University, Shanghai 200240, Chinadhttps://ror.org/02v51f717Department of Physics, School of Physics, Peking University, Beijing 100871, Chinaehttps://ror.org/03vek6s52Department of Applied Mathematics, Harvard John A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2538081123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2538081123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602147123?af=R">
      <title>Programmable DNA hydrogels for dual-mode PD-L1 suppression via polyvalent LYTAC mimics and transcriptional silencing</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602147123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceOvercoming resistance to immune checkpoint therapies requires targeting not just the proteins on the cell surface, but the genetic machinery that replenishes them. We developed a smart DNA hydrogel that acts as a dual-action therapeutic ...</description>
      <dc:title>Programmable DNA hydrogels for dual-mode PD-L1 suppression via polyvalent LYTAC mimics and transcriptional silencing</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602147123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Rui ZhangJing WangShuo WuXinghong ShenFeng XiaoXingyu JiangChi YaoDayong YangaDepartment of Chemistry, State Key Laboratory of Molecular Engineering of Polymers, Fudan University, Shanghai 200438, People’s Republic of ChinabState Key Laboratory of Synthetic Biology, Frontiers Science Center for Synthetic Biology, Key Laboratory of Systems Bioengineering Ministry of Education, School of Synthetic Biology and Biomanufacturing, Tianjin University, Tianjin 300350, People’s Republic of ChinacShenzhen Key Laboratory of Smart Healthcare Engineering, Guangdong Provincial Key Laboratory of Advanced Biomaterials, Department of Biomedical Engineering, Southern University of Science and Technology, Shenzhen, Guangdong 518055, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602147123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602147123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520331123?af=R">
      <title>Dysregulation of autophagosome–mitochondria contacts contributes to autophagy dysfunction and neurodegeneration in tauopathy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520331123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceMitochondria interact with other organelles by forming membrane contacts that serve as critical signaling hubs. In this study, we revealed the dysregulation of an autophagosome–mitochondria contact in tauopathy neurons. Such defects are caused ...</description>
      <dc:title>Dysregulation of autophagosome–mitochondria contacts contributes to autophagy dysfunction and neurodegeneration in tauopathy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520331123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Nuo JiaHongyuan GuanYantao ZuoYu Young JeongNiharika AmireddyGavesh RajapakshaCuauhtemoc Ulises GonzalezNora JaberYun-Kyung LeeMarialaina NissenbaumDavid J. MargolisWei DaiAlexander W. KusnecovQian Caiahttps://ror.org/05vt9qd57Division of Life Sciences, Department of Cell Biology and Neuroscience, School of Arts and Sciences, Rutgers, The State University of New Jersey, Piscataway, NJ 08854bhttps://ror.org/05vt9qd57Institute for Quantitative Biomedicine, Rutgers, The State University of New Jersey, Piscataway, NJ 08854chttps://ror.org/05vt9qd57Graduate School of Biochemistry, Rutgers, The State University of New Jersey, Piscataway, NJ 08854dhttps://ror.org/05vt9qd57Department of Psychology, School of Arts and Sciences, Rutgers, The State University of New Jersey, Piscataway, NJ 08854</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520331123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520331123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537770123?af=R">
      <title>The Urban Pulse: Diagnosing the urbanization process as spiky, cyclical, and asynchronous</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537770123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceUrbanization is traditionally measured as a static outcome. Here we propose the concept of Urban Pulse to capture urbanization as a dynamic process. Inspired by the human pulse, where an electrocardiogram renders invisible activity visible, we ...</description>
      <dc:title>The Urban Pulse: Diagnosing the urbanization process as spiky, cyclical, and asynchronous</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537770123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Zhe ZhuMichail FragkiasJi Won SuhElla McCoshanLelin ChenKexin SongJuwon KongTian LiKaren C. Setoahttps://ror.org/02der9h97Department of Natural Resources and the Environment, University of Connecticut, Storrs, CT 06269bhttps://ror.org/02e3zdp86Department of Economics, College of Business and Economics, Boise State University, Boise, ID 83725chttps://ror.org/04s5mat29Department of Geography, University of Victoria, Victoria, BC V8P 5C2, Canadadhttps://ror.org/03v76x132Yale School of the Environment, Yale University, New Haven, CT 06511ehttps://ror.org/05bnh6r87School of Integrative Plant Science, Cornell University, Ithaca, NY 14853</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537770123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537770123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528009123?af=R">
      <title>Bridging national climate targets and firm-level decisions: An agent-based model of China’s steel decarbonization pathways</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528009123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceDecarbonizing China’s steel industry is critical for achieving global climate goals, yet conventional models often fail to capture the complex, firm-level decisions that drive this transition. We developed an agent-based model to bridge this ...</description>
      <dc:title>Bridging national climate targets and firm-level decisions: An agent-based model of China’s steel decarbonization pathways</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528009123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Xiao LiuJinhong DuLingling LvJingnan HuXingang Liuahttps://ror.org/05t8xvx87State Key Laboratory of Environmental Criteria and Risk Assessment, Chinese Research Academy of Environmental Sciences, Beijing 100012, Chinabhttps://ror.org/022k4wk35School of Environment, Beijing Normal University, Beijing 100875, Chinachttps://ror.org/026drga03China National Environmental Monitoring Centre, Beijing 100012, Chinadhttps://ror.org/03jc41j30School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang 212013, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528009123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528009123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2612003123?af=R">
      <title>Mechanisms of ubiquitylation of the mitotic regulatory protein Cdc20</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2612003123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCdc20 regulates the activity of the ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) in mitosis. All actions of Cdc20 are terminated by its degradation on exit from mitosis. It was known that Cdc20 is targeted for degradation by ...</description>
      <dc:title>Mechanisms of ubiquitylation of the mitotic regulatory protein Cdc20</dc:title>
      <dc:identifier>doi:10.1073/pnas.2612003123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Danielle Sitry-ShevahShirly Miniowitz-ShemtovTania Liburkin DanDavid BarfordAvram HershkoaDepartment of Biochemistry, The Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa 31096, Israelbhttps://ror.org/03x94j517Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 OQH, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2612003123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2612003123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535299123?af=R">
      <title>Tuning bubble coalescence rates over orders of magnitude in liquid mixtures of simple surface thermodynamics: Experiments and theory</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535299123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceWhen two bubbles touch, they usually merge instantly. However, in multicomponent liquids, this process can be significantly delayed by Gibbs elasticity, a thermodynamic property that allows liquid interfaces to resist stretching. Understanding ...</description>
      <dc:title>Tuning bubble coalescence rates over orders of magnitude in liquid mixtures of simple surface thermodynamics: Experiments and theory</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535299123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Ange CombrouzeAnjishnu ChoudhuryAlexandra KlimenkoPascal PanizzaLaurent DucheminFrançois LequeuxEmilie VerneuilLaurence TaliniaSoft Matter Sciences and Engineering (SIMM), Ecole Supérieure de Physique et de Chimie Industrielles Paris, Paris Sciences et Lettres University, Sorbonne Université, CNRS, Paris F-75005, FrancebLaboratoire Physico-Chimie des Interfaces Complexes, Ecole Supérieure de Physique et de Chimie Industrielles Paris, Paris F-75231, FrancecTotalEnergies One Tech, Pôle d’Etudes et de Recherches de Lacq, Lacq F-64170, Francedhttps://ror.org/02qyf5152Department of Mechanical Engineering, Indian Institute of Technology Bombay, Mumbai 400076, Indiaehttps://ror.org/022b0h879Univ. Rennes, CNRS, Institut de Physique de Rennes, Rennes F-35000, Francefhttps://ror.org/02en5vm52Physique et Mécanique des Milieux Hétérogénes, CNRS, Ecole Supérieure de Physique et de Chimie Industrielles Paris, Université Paris Sciences et Lettres, Sorbonne Université, Université Paris-Cité, Paris F-75005, Franceghttps://ror.org/04kadgz77CNRS, Surface du Verre et Interfaces, Saint-Gobain, Aubervilliers F-93300, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535299123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535299123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537686123?af=R">
      <title>Spin-state engineering of cobalt(IV)-oxo enables direct oxygen atom transfer for high-efficiency olefin epoxidation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537686123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceOxygen atom transfer (OAT) is crucial in synthesis, yet balancing activity and selectivity remains challenging. Notably, high-valent cobalt-oxo species (CoIV=O), are principal reactive species in OAT. However, their typical square-pyramidal ...</description>
      <dc:title>Spin-state engineering of cobalt(IV)-oxo enables direct oxygen atom transfer for high-efficiency olefin epoxidation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537686123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Xue LiYufan ZhangJie YangJikun LiXiaohui WangTiantian ChenGuangming ZhanChuncheng ChenMingce LongLizhi Zhangahttps://ror.org/0220qvk04State Key Laboratory of Green Papermaking and Resource Recycling, School of Environmental Science and Engineering, Shanghai Jiao Tong University, Shanghai 200240, People’s Republic of Chinabhttps://ror.org/034t30j35Key Laboratory of Photochemistry, Research/Education Center for Excellence in Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537686123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537686123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2538139123?af=R">
      <title>Cognition does not automatically influence perception: Evidence from neural encoding of colors belonging to different categories</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2538139123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe Whorfian hypothesis posits that basic language categories alter one’s perception of the world in a fundamental manner. Some of the most compelling evidence in favor of this hypothesis came from electrophysiological responses that indicated ...</description>
      <dc:title>Cognition does not automatically influence perception: Evidence from neural encoding of colors belonging to different categories</dc:title>
      <dc:identifier>doi:10.1073/pnas.2538139123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Jasna MartinovicAlexey A. DelovJana TomastikovaJoel T. MartinGalina V. ParameiYulia A. Griberahttps://ror.org/01nrxwf90Department of Psychology, School of Philosophy, Psychology and Language Sciences, University of Edinburgh, Edinburgh EH8 9JZ, United Kingdombhttps://ror.org/04gmqtx37Department of Sociology and Philosophy, Smolensk State University, Smolensk 214000, Russiachttps://ror.org/03ctjbj91School of Psychology, Liverpool Hope University, Liverpool L16 9JD, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2538139123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2538139123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605237123?af=R">
      <title>Integrating trophic importance into conservation of terrestrial vertebrates</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605237123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCurrent conservation strategies prioritize species diversity and extinction risk while neglecting species’ roles in food webs. We introduce a framework that integrates species’ trophic importance and IUCN threat status into a Trophic ...</description>
      <dc:title>Integrating trophic importance into conservation of terrestrial vertebrates</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605237123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Xiyang HaoMarcel HolyoakZhicheng ZhangChuan Yanahttps://ror.org/01mkqqe32State Key Laboratory of Herbage Improvement and Grassland Agro-Ecosystems, College of Ecology, Lanzhou University, Lanzhou 730000, Chinabhttps://ror.org/05rrcem69Department of Environmental Science and Policy, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605237123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605237123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602209123?af=R">
      <title>Dual enhancement of superconductivity in FeSe/SrTiO3 via orbital and correlation synergy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602209123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceIn iron-based superconductors, thedz2orbital band lies deep below the Fermi energy and is conventionally excluded from the superconducting pairing process. This work overturns this view. Using a scanning tunneling microscope tip to apply ...</description>
      <dc:title>Dual enhancement of superconductivity in FeSe/SrTiO3 via orbital and correlation synergy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602209123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Guihao JiaJingming YanYucong PengShendong SuPei OuyangXiaopeng HuQi-Kun XueWei Liahttps://ror.org/03cve4549State Key Laboratory of Low-Dimensional Quantum Physics, Department of Physics, Tsinghua University, Beijing 100084, ChinabFrontier Science Center for Quantum Information, Beijing 100084, Chinachttps://ror.org/04nqf9k60Beijing Academy of Quantum Information Sciences, Beijing 100193, Chinadhttps://ror.org/049tv2d57Southern University of Science and Technology, Shenzhen 518055, ChinaeHefei 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602209123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602209123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606892123?af=R">
      <title>A polymerase ribozyme increases copying fidelity through pyrophosphate-mediated RNA repair</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606892123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceA key step in the emergence of life on Earth likely involved copying of an informational polymer, such as RNA, by an early polymerase enzyme. Under partial equilibrium conditions, when pyrophosphate—the coproduct of RNA polymerization—is ...</description>
      <dc:title>A polymerase ribozyme increases copying fidelity through pyrophosphate-mediated RNA repair</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606892123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Alexandra D. KentLucy L. YangKyle H. ColeIvee A. LeeAndrej LuptákaDepartment of Chemistry, University of California at Irvine, Irvine, CA 92697bDepartment of Pharmaceutical Sciences, University of California at Irvine, Irvine, CA 92697cDepartment of Molecular Biology and Biochemistry, University of California at Irvine, Irvine, CA 92697</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606892123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606892123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524866123?af=R">
      <title>G-protein regulatory network governs receptor internalization dynamics</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524866123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceAll biological systems require regulatory precision for proper function. Many of these functions are guided by G proteins, whose activity is regulated by a vast molecular network. At the forefront, G protein–coupled receptors serve to initiate ...</description>
      <dc:title>G-protein regulatory network governs receptor internalization dynamics</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524866123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Jacob B. RoweShubhi PandeyRyan A. MayerW. Grant LudlamJulia DrubeAsuka InoueCarsten HoffmannKirill A. Martemyanovahttps://ror.org/02dgjyy92Department of Physiology and Biophysics, University of Miami Miller School of Medicine, Miami, FL 33136bhttps://ror.org/02y3ad647Department of Neuroscience, The Herbert Wertheim UF Scripps Institute for Biomedical Innovation and Technology, University of Florida, Jupiter, FL 33458chttps://ror.org/05qpz1x62Institute for Molecular Cell Biology, Center for Molecular Biomedicine, Universitätsklinikum Jena, Friedrich-Schiller-Universität Jena, Jena 07745, Germanydhttps://ror.org/01dq60k83Molecular and Cellular Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japanehttps://ror.org/02kpeqv85Department of Molecular Pharmacology, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524866123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524866123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603105123?af=R">
      <title>The Campylobacter jejuni flagellar V-ring discerns viscosity levels to alter swimming velocity, metabolic gene expression, and fitness</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603105123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceBacterial commensals and pathogens likeCampylobacter jejuniexperience ranges of external viscosity during migration in hosts and establishing residence in the mucus layer lining the lower intestinal tract. We identified a structure in the ...</description>
      <dc:title>The Campylobacter jejuni flagellar V-ring discerns viscosity levels to alter swimming velocity, metabolic gene expression, and fitness</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603105123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Deborah A. RibardoNanki K. SinghMorgan BeebyDavid R. Hendrixsonahttps://ror.org/05byvp690Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390bhttps://ror.org/041kmwe10Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603105123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603105123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607035123?af=R">
      <title>Void-X: A generative void-filling model for predicting atomic packing in proteins</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607035123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceComputational protein design is advancing rapidly from designing protein folds to designing specific protein–protein and protein–drug interactions for expediting drug discovery. The majority of the recent design studies employ a top–down ...</description>
      <dc:title>Void-X: A generative void-filling model for predicting atomic packing in proteins</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607035123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Jing YangJunying YuanJames J. Chouahttps://ror.org/034t30j35Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201203, Chinabhttps://ror.org/034t30j35State Key Laboratory of Chemical Biology, Chinese Academy of Sciences, Shanghai 200032, ChinacShanghai Key Laboratory of Aging Studies, Shanghai 201203, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607035123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607035123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2520997123?af=R">
      <title>A GTP synthase ribozyme with increased GTP turnover</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2520997123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceAn early stage of life must have used catalytic RNAs (ribozymes) to self-replicate in a prebiotic environment. Self-replication would have required RNA polymerization from chemically activated nucleotides, which exist in today’s biology as ...</description>
      <dc:title>A GTP synthase ribozyme with increased GTP turnover</dc:title>
      <dc:identifier>doi:10.1073/pnas.2520997123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Xu HanZoe J. PepperJoshua T. ArriolaUlrich F. Müllerahttps://ror.org/0168r3w48Department of Chemistry and Biochemistry, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2520997123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2520997123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603966123?af=R">
      <title>Oxytocin selectively biases sensory–prefrontal communication through network-level suppression and theta coupling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603966123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceOxytocin is known to influence social behavior, yet how its local synaptic actions shape communication across distributed brain networks remains poorly understood. Using multisite local field potential recordings in mice, we show that oxytocin ...</description>
      <dc:title>Oxytocin selectively biases sensory–prefrontal communication through network-level suppression and theta coupling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603966123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>DaYoung JungHio-Been HanJungyoung KimJi Hyung KimRobert C. FroemkeJee Hyun ChoiaComputational Cognitive &amp; Systems Neuroscience Laboratory, Brain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of KoreabDepartment of Biotechnology, Korea University, Seoul 02841, Republic of Koreachttps://ror.org/0190ak572Department of Neuroscience, New York University, Grossman School of Medicine, New York University, New York, NY 10016dhttps://ror.org/00chfja07School of Convergence, Seoul National University of Science and Technology, Seoul 01811, Republic of Koreaehttps://ror.org/05apxxy63Department of Bio and Brain Engineering Program, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Koreafhttps://ror.org/0190ak572Department of Otolaryngology–Head and Neck Surgery, New York University Grossman School of Medicine, Neuroscience Institute, New York University, New York, NY 10016gDivision of Artificial Intelligence and Robotics, University of Science and Technology, Daejeon 34113, Republic of Korea</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603966123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603966123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2607573123?af=R">
      <title>Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2607573123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceTip links gate mechanotransduction channels in cochlear hair cells and have been proposed to be the gating springs for the transduction channel. The ultrastructure of the tip link remains not well defined. Here we have used cryo-electron ...</description>
      <dc:title>Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15</dc:title>
      <dc:identifier>doi:10.1073/pnas.2607573123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Xiaoping LiangRoshan PathakXufeng QiuLucas DillardEdward C. TwomeyUlrich Müllerahttps://ror.org/00za53h95The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205bhttps://ror.org/00za53h95Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2607573123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2607573123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605725123?af=R">
      <title>Consecutive catalytic steps of viral RNA polymerase and exonuclease suggest a way to overcome intrinsic nucleotide analogue resistance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605725123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceTreatment of coronavirus infections with nucleoside analogue antivirals is complicated by the presence of a virally encoded proofreading exonuclease domain. Using 5′ α-thiophosphate modified nucleotides, we followed the stereochemical course ...</description>
      <dc:title>Consecutive catalytic steps of viral RNA polymerase and exonuclease suggest a way to overcome intrinsic nucleotide analogue resistance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605725123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Ashleigh ShannonVéronique FattoriniCandice SartreAurélie ChazotAdel MoussaJean-Pierre SommadossiYingxiao ZhuManfu WangHui ShiFrançois FerronKarine AlvarezBruno Canardahttps://ror.org/04jm8zw14Aix-Marseille University, Centre National de la Recherche Scientifique, Architecture et Fonction des Macromolécules Biologiques UMR7257, Marseille 13009, FrancebAtea Pharmaceuticals, Inc., Boston, MA 02110cBiortus Discovery Co. Ltd., Wuxi, Jiangsu 214142, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605725123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605725123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535777123?af=R">
      <title>RNF126 is a peroxisomal fate switch enabling redifferentiation therapy in hepatocellular carcinoma</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535777123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe dedifferentiation of cancer cells is a major hallmark of malignancy and a challenge for therapy. Here, we reveal that hypoxia drives HCC dedifferentiation by actively eliminating peroxisomes, the organelles that help define liver cell ...</description>
      <dc:title>RNF126 is a peroxisomal fate switch enabling redifferentiation therapy in hepatocellular carcinoma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535777123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Qi SuYichun YangJiayan RenYu ZhangLijuan FuQing WuXu HanYanmin Zhangahttps://ror.org/017zhmm22School of Pharmacy, Health Science Center, Xi’an Jiaotong University, Xi’an 710061, PR ChinabState Key Laboratory of Shaanxi for Natural Medicines Research and Engineering, Xi’an 710061, PR China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535777123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535777123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603926123?af=R">
      <title>Risk prediction of Helicobacter pylori strains across Correa’s cascade via intelligent analysis of genome-wide SNPs</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603926123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceMost individuals infected withHelicobacter pylori(H. pylori) do not develop gastric cancer, and bacterial “high-risk” markers explain only a fraction of outcome variability. We analyzedH. pylorigenomes across Correa’s cascade and developed ...</description>
      <dc:title>Risk prediction of Helicobacter pylori strains across Correa’s cascade via intelligent analysis of genome-wide SNPs</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603926123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Xiuling SongXiangyu WangShuzhen ZhangHong LiChao WuHuifang LiuChin Yen TayCong MaBarry J. MarshallBing GuLiang Wangahttps://ror.org/01vjw4z39Department of Clinical Laboratory Medicine, Guangdong Provincial People’s Hospital (Guangdong Academy of Medical Sciences), Southern Medical University, Guangzhou, Guangdong 510080, Chinabhttps://ror.org/01vy4gh70Department of Gastroenterology, Shenzhen Second People’s Hospital, The First Affiliated Hospital of Shenzhen University, Shenzhen, Guangdong 518000, Chinachttps://ror.org/01vy4gh70Marshall Laboratory of Biomedical Engineering, Shenzhen University Medical School, Shenzhen University, Shenzhen, Guangdong 518000, ChinadDepartment of Clinical Laboratory, Shenzhen Dapeng New District Kuichong People’s Hospital, Shenzhen, Guangdong 518000, Chinaehttps://ror.org/011ashp19Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, Chinafhttps://ror.org/007mrxy13Laboratory of Infectious and Liver Diseases, Institution of Infectious Diseases, West China Hospital of Sichuan University, Chengdu, Sichuan 610041, Chinaghttps://ror.org/00xjwyj62Department of Laboratory Medicine, The Eighth Affiliated Hospital of Sun Yat-Sen University, Shenzhen, Guangdong 518033, ChinahCenter for Infectious Diseases, Vision Medicals Co., Ltd, Guangzhou, Guangdong 510000, Chinaihttps://ror.org/047272k79Marshall Center for Intervention of Infectious Diseases, University of Western Australia, Perth, WA 6009, Australiajhttps://ror.org/047272k79School of Molecular Sciences, School of Biomedical Sciences, University of Western Australia, Perth, WA 6009, Australiakhttps://ror.org/0030zas98Marshall Research Centre for Medical Microbial Biotechnology, Department of Applied Biology and Chemical Technology, Faculty of Science, The Hong Kong Polytechnic University, Hong Kong Special Administrative Region 999077, Chinalhttps://ror.org/0530pts50School of Medicine, South China University of Technology, Guangzhou, Guangdong 510006, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603926123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2603926123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2424788123?af=R">
      <title>The tyrosine phosphatase STEP is a developmental suppressor of synaptogenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2424788123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe balance between phosphorylation and dephosphorylation is essential for the signaling pathways that control synapse formation and maturation. Here, we identify Striatal-Enriched Protein Tyrosine Phosphatase (STEP) as a developmental brake ...</description>
      <dc:title>The tyrosine phosphatase STEP is a developmental suppressor of synaptogenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2424788123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Joel P. PiresDiogo ToméMiranda MeleAna Caulino-RochaElisa CortiIra MilosevicGraça F. BaltazarRamiro D. Almeidaahttps://ror.org/04z8k9a98Center for Neuroscience and Cell Biology, University of Coimbra, Coimbra 3004-504, Portugalbhttps://ror.org/04z8k9a98Center for Innovative Biomedicine and Biotechnology, University of Coimbra, Coimbra 3004-504, Portugalchttps://ror.org/03nf36p02Health Sciences Research Centre, University of Beira Interior, Covilhã 6200-506, Portugaldhttps://ror.org/03nf36p02RISE-Health, Department of Medical Sciences, Faculty of Health Sciences, University of Beira Interior, Covilhã 6200-506, Portugalehttps://ror.org/00nt41z93Institute of Biomedicine, Department of Medical Sciences, University of Aveiro, Aveiro 3810-193, Portugalfhttps://ror.org/04z8k9a98Multidisciplinary Institute of Aging, Center for Innovative Biomedicine and Biotechnology, University of Coimbra, Coimbra 3004-504, Portugalghttps://ror.org/04z8k9a98Faculty of Pharmacy, University of Coimbra, Coimbra 3000-548, Portugalhhttps://ror.org/04z8k9a98Institute for Interdisciplinary Research, University of Coimbra, Coimbra 3030-789, Portugalihttps://ror.org/04z8k9a98Institute for Interdisciplinary Research, Doctoral Programme in Experimental Biology and Biomedicine, University of Coimbra, Coimbra 3030-789, Portugaljhttps://ror.org/052gg0110Centre for Human Genetics, Nuffield Department of Medicine, University of Oxford, Oxford OX3-7BN, UK</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2424788123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2424788123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2511427123?af=R">
      <title>Drp1-driven fragmentation of scleral mitochondria promotes myopia development</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2511427123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceScleral collagen reduction constitutes a primary determinant of ocular axial elongation and myopia development, yet the molecular underpinnings remain elusive. This study demonstrated that scleral mitochondrial fragmentation, driven by ...</description>
      <dc:title>Drp1-driven fragmentation of scleral mitochondria promotes myopia development</dc:title>
      <dc:identifier>doi:10.1073/pnas.2511427123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Zhenqi GuanWenting LiShengcong LiuXingxing YangYuejia PengLong YeLuyao WangYuan LuSisi DongHuihui LiuJian YuanJianzhong SuJia QuXianqun FanFei ZhaoMiaozhen PanXiangtian Zhouahttps://ror.org/00rd5t069State Key Laboratory of Eye Health, Oujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision and Brain Health), Eye Hospital, Wenzhou Medical University, Wenzhou 325027, Chinabhttps://ror.org/02drdmm93Research Unit of Myopia Basic Research and Clinical Prevention and Control, Chinese Academy of Medical Sciences (2019RU025), Wenzhou, Zhejiang 325027, Chinachttps://ror.org/0220qvk04State Key Laboratory of Eye Health, Department of Ophthalmology, Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2511427123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2511427123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529786123?af=R">
      <title>GREM1/FGFR1-activated myofibroblasts induce immunosuppression and accelerate metastasis in high-grade serous ovarian cancer</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529786123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceExtensive metastasis remains the predominant cause of mortality in patients with high-grade serous ovarian cancer (HGSOC). Our investigation reveals that Gremlin1 (GREM1)+myofibroblasts (myCAFs), enriched in HGSOC metastatic lesions, drive ...</description>
      <dc:title>GREM1/FGFR1-activated myofibroblasts induce immunosuppression and accelerate metastasis in high-grade serous ovarian cancer</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529786123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Runrong LiXizhan HuangYue ChenXiaowen ChenYue YangYurui LiuBinyi BaiFanliang MengYan LiYunshan Ningahttps://ror.org/01vjw4z39School of Laboratory Medicine and Biotechnology, Southern Medical University, Guangzhou 510515, Chinabhttps://ror.org/01vjw4z39Guangdong Provincial Key Laboratory of Immune Regulation and Immunotherapy, Southern Medical University, Guangzhou 510515, Chinachttps://ror.org/01vjw4z39The First School of Clinical Medicine, Southern Medical University, Guangzhou 510515, Chinadhttps://ror.org/01vjw4z39Department of Obstetrics and Gynecology, Nanfang Hospital, Southern Medical University, Guangzhou 510515, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529786123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529786123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528970123?af=R">
      <title>Structural basis of long-range transcription–translation coupling</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528970123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceIn bacteria, transcription and translation can be physically coupled processes. In previous work, structures have been reported of a coupled transcription–translation complex—“TTC-B”—in which RNA polymerase (RNAP) directly interacts with a ...</description>
      <dc:title>Structural basis of long-range transcription–translation coupling</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528970123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Chengyuan WangVadim MolodtsovShashank ShandilyaLinlin YouJing ZhangKonstantin KuznedelovBryce E. NickelsJason T. KaelberGregor BlahaRichard H. Ebrightahttps://ror.org/05vt9qd57Waksman Institute and Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854bhttps://ror.org/034t30j35Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 200032, Chinachttps://ror.org/02dn9h927Research Institute of Molecular and Cellular Medicine, RUDN University, Moscow 115093, Russiadhttps://ror.org/03f9nc143Skolkovo Institute of Science and Technology, Moscow 121205, Russiaehttps://ror.org/05vt9qd57Waksman Institute and Department of Genetics, Rutgers University, Piscataway, NJ 08854fhttps://ror.org/05vt9qd57Rutgers CryoEM and Nanoimaging Facility and Institute for Quantitative Biomedicine, Rutgers University, Piscataway, NJ 08854ghttps://ror.org/03nawhv43Department of Biochemistry, University of California, Riverside, CA 92521</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528970123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528970123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535199123?af=R">
      <title>A gustatory receptor–Akt axis couples nutrient sensing to hematopoiesis in the silkworm</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535199123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceNutrient availability profoundly influences immune and hematopoietic activity, yet the molecular sensors that translate metabolic cues into blood cell production remain poorly defined. We identify the gustatory receptor BmGr9 as an internal ...</description>
      <dc:title>A gustatory receptor–Akt axis couples nutrient sensing to hematopoiesis in the silkworm</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535199123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Wenjing ZhangShogo UnoRyoichi SatoDingze MangaCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding 071002, Chinabhttps://ror.org/00qg0kr10Graduate School of Bio-Application and Systems Engineering, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japanchttps://ror.org/01p884a79Hebei Basic Science Center for Biotic Interactions, Hebei University, Baoding 071002, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535199123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535199123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526271123?af=R">
      <title>Telocyte-derived pentraxin 3 enables vascular pruning as a key driver in infantile hemangioma regression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526271123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceFor some tumors, including infantile hemangioma, spontaneous regression occurs naturally, though the cellular actors driving this process have generally remained unknown. Here, we identified a mechanism by which specialized stromal cells, ...</description>
      <dc:title>Telocyte-derived pentraxin 3 enables vascular pruning as a key driver in infantile hemangioma regression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526271123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Léa PechtimaldjianMarie-Laure JulliéChloé RoussonFaiza LaananiJulie ClachetYamina IdrissiMaya LootMuriel Cario-AndreSorilla PreyAlain TaiebChristine Leauté-LabrèzeThomas MathivetFrançois Moisanahttps://ror.org/02gezhp66University of Bordeaux, Inserm, Bordeaux Institute of Oncology, UMR 1312, Bordeaux F-33076, Francebhttps://ror.org/01hq89f96Service de Pathologie, Centre Hospitalier Universitaire de Bordeaux, Bordeaux F-33000, Francechttps://ror.org/01hq89f96Service de Chirurgie Pédiatrique, Centre Hospitalier Universitaire de Bordeaux, Bordeaux F-33000, FrancedCentre de Référence Maladies Rares de la Peau et des Muqueuses d’origine Génétique Sud, Bordeaux F-33000, FranceeAquiderm, Bordeaux F-33000, Francefhttps://ror.org/01hq89f96Service de dermatologie pédiatrique et adulte, Centre Hospitalier Universitaire de Bordeaux, Bordeaux F-33000, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526271123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526271123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602470123?af=R">
      <title>High-throughput screening identifies a critical role of the SPOP–PABPC1 axis in lung adenocarcinoma progression</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602470123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceLung adenocarcinoma (LUAD) is a lethal subtype of lung cancer with limited therapeutic options. Through an integrated screening combining bioinformatics, transcriptomics, and clinical prognostic analysis, we have identified the E3 ubiquitin ...</description>
      <dc:title>High-throughput screening identifies a critical role of the SPOP–PABPC1 axis in lung adenocarcinoma progression</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602470123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Jiahui ZhangRan LiuXue HanYutong JiaoYun PengZizhang ZhouYanran DengLianggeng Gongahttps://ror.org/042v6xz23Department of Radiology, The Second Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang 330006, Chinabhttps://ror.org/042v6xz23Department of Thoracic Surgery, the First Affiliated Hospital, Jiangxi Medical College, Nanchang University, Nanchang 330006, Chinachttps://ror.org/05nkgk822Key Laboratory of Biodiversity Conservation and Bioresource Utilization of Jiangxi Province, College of Life Sciences, Jiangxi Normal University, Nanchang 330006, Chinadhttps://ror.org/042v6xz23Queen Mary College, Nanchang University, Nanchang 330006, Chinaehttps://ror.org/02ke8fw32College of Life Sciences, Shandong Agricultural University, Tai’an 271018, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602470123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602470123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530690123?af=R">
      <title>Opportunities to strengthen US phosphorus supply resilience through circular pathways</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530690123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe United States is a major producer and consumer of phosphate rock but faces growing dependence on mineral P imports. This study provides a spatiotemporal assessment of “avoidable” mineral P use across the United States. We find that soil ...</description>
      <dc:title>Opportunities to strengthen US phosphorus supply resilience through circular pathways</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530690123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Jiaxin WangJames J. ElserRebecca L. MuenichJustin S. BakerJacob L. JonesDeyi Houahttps://ror.org/03cve4549Division of Soil and Groundwater Environment, School of Environment, Tsinghua University, Beijing 100084, Chinabhttps://ror.org/03efmqc40School of Life Sciences and School of Sustainability, Arizona State University, Tempe, AZ 85281chttps://ror.org/0078xmk34Flathead Lake Biological Station, Division of Biological Sciences, University of Montana, Polson, MT 59860dDepartment of Biological and Agricultural Engineering, University of Arkansas, Fayetteville, AR 72701ehttps://ror.org/04tj63d06Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695fhttps://ror.org/04tj63d06Department of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695gState Key Laboratory of Regional Environment and Sustainability, School of Environment, Tsinghua University, Beijing 100084, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530690123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530690123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536368123?af=R">
      <title>IL-4 peptide hydrogel reprograms MSC heterogeneity toward the CD106+ population for enhanced renal repair</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536368123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThis bioengineered culture method using interleukin-4 peptide hydrogel holds strong prospective for clinical translation, enabling scalable preconditioning of Mesenchymal stem cells to overcome heterogeneity and boost potency for acute kidney ...</description>
      <dc:title>IL-4 peptide hydrogel reprograms MSC heterogeneity toward the CD106+ population for enhanced renal repair</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536368123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Kai PanEnze FuWenlong WangRui LiJiansheng YangHongyan TaoZhibo HanZhong-Chao HanQiong LiZhikun GuoZongjin Liahttps://ror.org/047hegk60Department of Cardiology, Zhengzhou Seventh People’s Hospital, Zhengzhou 450016, Chinabhttps://ror.org/01y1kjr75Department of Pathophysiology, School of Medicine, Nankai University, Tianjin 300071, Chinachttps://ror.org/038hzq450Henan Key Laboratory of Medical Tissue Regeneration, Department of Anatomy, Henan Medical University, Xinxiang 453003, Chinadhttps://ror.org/021cj6z65Qingdao Medical College, Qingdao University, Qingdao 266100, ChinaeTianjin Key Laboratory of Engineering Technologies for Cell Pharmaceutical, National Engineering Research Center of Cell Products, AmCellGene Co. Ltd., Tianjin 300457, ChinafBeijing Engineering Laboratory of Perinatal Stem Cells, Beijing Institute of Health and Stem Cells, Health Biotech Co. Ltd., Beijing 100176, Chinaghttps://ror.org/038hzq450School of Nursing, North Henan Medical University, Xinxiang 453003, Chinahhttps://ror.org/05tf9r976National Key Laboratory of Kidney Diseases, Chinese People‘s Liberation Army General Hospital, Beijing 100853, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536368123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536368123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606552123?af=R">
      <title>Adaptive self-organization of global swidden forests</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606552123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceSwidden or “slash-and-burn” agriculture is used throughout human history in Europe, Asia, Africa, and the Americas. We present evidence from a global sample of more than 18,000 forest patches that swidden can manifest adaptive self-...</description>
      <dc:title>Adaptive self-organization of global swidden forests</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606552123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Sean S. DowneyDenis TverskoiShane A. ScaggsXinyi WuZaarah SyedJensan LebowitzRongjun QinStefan Thurnerahttps://ror.org/00rs6vg23Department of Anthropology, The Ohio State University, Columbus, OH 43210bhttps://ror.org/00rs6vg23The Sustainability Institute, The Ohio State University, Columbus, OH 43210chttps://ror.org/00rs6vg23The Translational Data Analytics Institute, The Ohio State University, Columbus, OH 43210dhttps://ror.org/00rs6vg23Division of Biostatistics, College of Public Health, The Ohio State University, Columbus, OH 43210ehttps://ror.org/00rs6vg23School of Environment and Natural Resources, The Ohio State University, Columbus, OH 43210fhttps://ror.org/00rs6vg23Department of Civil, Environmental and Geodetic Engineering, The Ohio State University, Columbus, OH 43210ghttps://ror.org/00rs6vg23Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210hhttps://ror.org/00rs6vg23Department of Electrical and Computer Engineering, The Ohio State University, Columbus, OH 43210ihttps://ror.org/023dz9m50Complexity Science Hub, Vienna 1030, Austriajhttps://ror.org/05n3x4p02Institute of the Science of Complex Systems, Center for Medical Data Science, Medical University of Vienna, Vienna 1090, Austriakhttps://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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606552123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606552123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518957123?af=R">
      <title>Social immunity can be a consequence and cause of social evolution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518957123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceSocial immunity, the defensive response of social groups against pathogens, is a striking example of cooperation, which has been argued to be functionally analogous to the immune response in multicellular organisms. Using mathematical models, ...</description>
      <dc:title>Social immunity can be a consequence and cause of social evolution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518957123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Ming LiuThomas W. ScottGeorge ShillcockChristopher D. PullStuart A. Westahttps://ror.org/052gg0110Department of Biology, University of Oxford, Oxford OX1 3SZ, United Kingdombhttps://ror.org/052gg0110Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518957123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518957123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534946123?af=R">
      <title>Expression of four mitochondrial tRNAs from only two loci</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534946123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceMitochondrial genomes have been reduced to only a handful of genes over the roughly two billion years since the origin of the organelle. Despite this extreme gene loss, bilaterian animal mitochondrial genomes still retain a complete, minimal ...</description>
      <dc:title>Expression of four mitochondrial tRNAs from only two loci</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534946123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Jessica M. WarrenKasavajhala V. S. K. PrasadAnistynn M. MendezStephanie TemnykJohn P. McCutcheonahttps://ror.org/03efmqc40Biodesign Institute and School of Life Sciences, Arizona State University, Tempe, AZ 85281bHHMI, Chevy Chase, MD 20815chttps://ror.org/03k1gpj17Department of Biology, Colorado State University, Fort Collins, CO 80521</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534946123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534946123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536989123?af=R">
      <title>Loss of erythrocyte sialic acid in sepsis disrupts inhibitory Siglec interactions, driving neutrophil hyperactivation and NET outspread</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536989123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceSepsis is a life-threatening systemic inflammation with poorly understood mechanisms and no specific therapy. It is associated with overactivated neutrophils that overrelease neutrophil extracellular traps (NETs), leading to bystander ...</description>
      <dc:title>Loss of erythrocyte sialic acid in sepsis disrupts inhibitory Siglec interactions, driving neutrophil hyperactivation and NET outspread</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536989123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Anna SuchWeronika OrtmannGabriela BurczykJacek CzepielMonika Bociaga-JasikPaweł Link-LenczowskiElzbieta Kolaczkowskaahttps://ror.org/03bqmcz70Department of Experimental Hematology, Faculty of Biology, Jagiellonian University, Krakow 30-387, Polandbhttps://ror.org/03bqmcz70Doctoral School of Exact and Natural Sciences, Jagiellonian University, Krakow 30-348, Polandchttps://ror.org/03bqmcz70Department of Infectious Diseases, Faculty of Medicine, Jagiellonian University Medical College, Krakow 30-688, Polanddhttps://ror.org/03bqmcz70Department of Medical Physiology, Faculty of Health Sciences, Jagiellonian University Medical College, Krakow 31-126, Polandehttps://ror.org/03bqmcz70Center for the Development of Therapies for Civilization and Age-Related Diseases, Jagiellonian University Medical College, Krakow 31-066, Poland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536989123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536989123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524671123?af=R">
      <title>Nf2 orchestrates β-arrestin2-biased PTH1R signaling to couple bone mass with skeletal integrity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524671123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThis study identifies neurofibromin 2 (Nf2) as a critical regulator of parathyroid hormone (PTH) and PTH-related peptide (PTHrP) signaling. Nf2 specifically promotes β-arrestin2-coupled receptor internalization, decoupling this endocytic ...</description>
      <dc:title>Nf2 orchestrates β-arrestin2-biased PTH1R signaling to couple bone mass with skeletal integrity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524671123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Junguang LiaoYiliang HeChenyang ZhangQitao QianYuping HuangQi ZhangPanpan ShenChenhe ZhouMengrui WuGuiqian Chenahttps://ror.org/03893we55Department of Biopharmaceutics, Zhejiang Provincial Engineering Research Center of New Technologies and Applications for Targeted Therapy of Major Diseases, College of Life Science and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, ChinabDepartment of Orthopedics, Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310009, Chinachttps://ror.org/00a2xv884Department of Cell and Developmental Biology, College of Life Sciences, Zhejiang University, Hangzhou 310027, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524671123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524671123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531054123?af=R">
      <title>The autophagy protein ATG-9 promotes aversive learning in Caenorhabditis elegans through trafficking neuropeptide receptors</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531054123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceAutophagy is long considered a disposal system for cellular wastes. Autophagy also occurs at neuronal synapses and its biogenesis there is coupled with synaptic vesicle release, but whether synaptic autophagy has a nondegradative function in ...</description>
      <dc:title>The autophagy protein ATG-9 promotes aversive learning in Caenorhabditis elegans through trafficking neuropeptide receptors</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531054123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Wai Hou TamYu-Cheng TangHao-Han ShiuShang-Heng TsaiPei-Shu JaoChun-Liang Panahttps://ror.org/05bqach95Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 10002, Taiwanbhttps://ror.org/05bqach95Center for Precision Medicine, College of Medicine, National Taiwan University, Taipei 10002, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531054123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531054123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601061123?af=R">
      <title>Hp1bp3 loss links chromatin reorganization to metabolic vulnerability in glioma</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601061123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceHigh-grade gliomas (HGGs) are aggressive brain tumors that rely on metabolic adaptations to sustain proliferation and survival. Using an immunocompetent mouse model of HGG, we show that dietary methionine restriction reduces tumor ...</description>
      <dc:title>Hp1bp3 loss links chromatin reorganization to metabolic vulnerability in glioma</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601061123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Brittney LozziTaylor A. GatesmanPushan DasguptaDebosmita SardarYeunjung KoChenyu MaoHsiao-Chi ChenRachel N. CurryDongjoo ChoiCarrie A. MohilaMelissa L. BondyGanesh RaoMarco GalloSameer AgnihotriBenjamin Deneenahttps://ror.org/02pttbw34Program in Genetics and Genomics, Baylor College of Medicine, Houston, TX 77030bhttps://ror.org/02pttbw34Center for Cell and Gene Therapy, Baylor College of Medicine, Houston, TX 77030chttps://ror.org/02pttbw34Center for Cancer Neuroscience, Baylor College of Medicine, Houston, TX 77030dhttps://ror.org/01an3r305Department of Neurological Surgery, University of Pittsburgh, Pittsburgh, PA 15261ehttps://ror.org/02pttbw34Department of Neurology, Baylor College of Medicine, Houston, TX 77030fhttps://ror.org/02pttbw34Dan L. Duncan Comprehensive Cancer Center, Baylor College of Medicine, Houston, TX 77030ghttps://ror.org/02pttbw34Program in Immunology and Microbiology, Baylor College of Medicine, Houston, TX 77030hhttps://ror.org/02pttbw34Program in Cancer and Cell Biology, Baylor College of Medicine, Houston, TX 77030ihttps://ror.org/02pttbw34Integrative Molecular and Biomedical Sciences Graduate Program, Baylor College of Medicine, Houston, TX 77030jhttps://ror.org/05cz92x43Department of Pathology, Texas Children’s Hospital, Houston, TX 77030khttps://ror.org/00f54p054Department of Epidemiology and Population Science, Stanford University, Palo Alto, CA 94305lhttps://ror.org/02pttbw34Department of Neurosurgery, Baylor College of Medicine, Houston, TX 77030mhttps://ror.org/02pttbw34Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030nhttps://ror.org/05cz92x43Cancer and Hematology Center, Texas Children’s Hospital, Houston, TX 77030</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601061123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601061123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528450123?af=R">
      <title>Differential Wnt/β-catenin signaling via TCF7L2/LEF1 binding specificity shapes cellular and tumor phenotypes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528450123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceWnt/β-catenin signaling is crucial for development and cancer, yet how it drives different gene programs across tissues is unclear. Using patient-derived liver tumor organoids, we show that β-catenin’s transcriptional output depends on its ...</description>
      <dc:title>Differential Wnt/β-catenin signaling via TCF7L2/LEF1 binding specificity shapes cellular and tumor phenotypes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528450123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Thomas A. KluiverAnna NordinYuyan LuXuan GuoStephanie A. SchubertDarien YeungArif Ibrahim ArdisasmitaWessel TerpstraChang ZhangXiaochen DuanRishi SavurMarius C. van den HeuvelVincent E. de MeijerRuben H. de KleineKathelijne KraalRonald R. de KrijgerJózsef ZsirosClaudio CantùWeng Chuan Pengahttps://ror.org/02aj7yc53Princess Máxima Center for Pediatric Oncology, Utrecht 3584 CH, The Netherlandsbhttps://ror.org/05ynxx418Wallenberg Centre for Molecular Medicine, Linköping University, Linköping SE-581 83, Swedenchttps://ror.org/05ynxx418Department of Biomedical and Clinical Sciences, Division of Molecular Medicine and Virology, Faculty of Medicine and Health Sciences, Linköping University, Linköping SE-581 83, Swedendhttps://ror.org/05ynxx418Science for Life Laboratory, Linköping University, Linköping SE-581 83, Swedenehttps://ror.org/02z125451Department of Oncology, Zhongshan Hospital of Xiamen University, School of Medicine, Xiamen University, Xiamen 361004, Chinafhttps://ror.org/03cv38k47Department of Surgery, Section of Hepatobiliary Surgery and Liver Transplantation, University of Groningen, University Medical Center Groningen, Groningen 9713 GZ, The Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528450123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528450123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604929123?af=R">
      <title>Dark diversity framework reconciles Darwin’s naturalization conundrum for freshwater fish invasions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604929123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificancePredicting which exotic species will establish in new environments is a central challenge for invasion ecology. Since Darwin first posed his naturalization conundrum, ecologists have long debated whether exotic species similar or dissimilar to ...</description>
      <dc:title>Dark diversity framework reconciles Darwin’s naturalization conundrum for freshwater fish invasions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604929123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Wen-gang ZhangMeng XuShu-ya FanJonathan A. BennettRoss N. CuthbertJaimie T. A. DickMeelis PärtelShao-peng Liahttps://ror.org/02n96ep67Research Center for Global Change and Ecological Forecasting, Zhejiang Tiantong Forest Ecosystem National Observation and Research Station, Institute of Eco-Chongming, School of Ecological and Environmental Sciences, East China Normal University, Shanghai 200241, Chinabhttps://ror.org/034t30j35Key Laboratory of Lake and Watershed Science for Water Security, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, Chinachttps://ror.org/04and7w57Key Laboratory of Prevention and Control for Aquatic Invasive Alien Species, Ministry of Agriculture and Rural Affairs, Pearl River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510380, Chinadhttps://ror.org/0546hnb39Ecology, Department of Biology, University of Konstanz, Konstanz 78457, Germanyehttps://ror.org/0415vcw02The Forest Risk Research Centre, Faculty of Forestry and Wood Sciences, Czech University of Life Sciences Prague, Prague 16500, Czech Republicfhttps://ror.org/010x8gc63Department of Plant Sciences, University of Saskatchewan, Saskatoon, SK S7N5A8, Canadaghttps://ror.org/00hswnk62Research Centre in Sustainable Energy, Institute for Global Food Security, School of Biological Sciences, Queen’s University Belfast, Belfast BT95DL, United Kingdomhhttps://ror.org/03z77qz90Department of Botany, Institute of Ecology and Earth Science, University of Tartu, Tartu 50409, Estonia</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604929123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604929123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605288123?af=R">
      <title>Ultrarapid MC1R protein and associated plumage color evolution in the domestic chicken</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605288123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceHow new alleles with large phenotypic effects evolve remains a central question in evolutionary biology. Using genome sequence data from more than 10,000 chickens, we show that the pigmentation genemelanocortin-1 receptor(MC1R) has evolved ...</description>
      <dc:title>Ultrarapid MC1R protein and associated plumage color evolution in the domestic chicken</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605288123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Cheng MaAenne-Dorothea LiebingGunnar KleinauAntje KampradLouisa CalabreseMichal SzczepekZheng LiMårten LarssonPatrick ScheererClaudia StäubertLeif Anderssonahttps://ror.org/048a87296Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala SE-751 23, Swedenbhttps://ror.org/048a87296SciLifeLab, Uppsala University, Uppsala SE-751 23, Swedenchttps://ror.org/03s7gtk40Rudolf Schönheimer Institute of Biochemistry, Faculty of Medicine, Leipzig University, Leipzig 04103, Germanydhttps://ror.org/01hcx6992Charité—Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics, Group Structural Biology of Cellular Signaling, Berlin D-10117, Germanyehttps://ror.org/022k4wk35Ministry of Education Key Laboratory for Biodiversity and Ecological Engineering, College of Life Sciences, Beijing Normal University, Beijing 100875, Chinafhttps://ror.org/01f5ytq51Department of Veterinary Integrative Biosciences, College of Veterinary Medicine and Biomedical Sciences, Texas A&amp;M University, College Station, TX 77843-4461</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605288123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605288123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528668123?af=R">
      <title>Disruption to TFEB signaling and autophagy in newly formed oligodendrocytes leads to aberrant generation of CNS myelin</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528668123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe cellular and molecular mechanisms governing myelin integrity during axon ensheathment remain poorly understood. Using volume electron microscopy and a knock-in mouse line labeling newly formed oligodendrocytes and their myelin sheaths, we ...</description>
      <dc:title>Disruption to TFEB signaling and autophagy in newly formed oligodendrocytes leads to aberrant generation of CNS myelin</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528668123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Daniela BarbosaAksheev BhambriMiguel VasquezYihe ZhangGabrielle SanchezKatherine J. WertNatalia V GounkoMark H. EllismanLu O. Sunahttps://ror.org/05byvp690Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390bhttps://ror.org/0168r3w48National Center for Microscopy and Imaging Research, Department of Neuroscience, University of California San Diego, La Jolla, CA 92039chttps://ror.org/05byvp690Department of Ophthalmology, University of Texas Southwestern Medical Center, Dallas, TX 75390dhttps://ror.org/05byvp690Hamon Center for Regenerative Science and Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390ehttps://ror.org/05byvp690Peter O’Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390fhttps://ror.org/05byvp690Electron Microscopy Core Facility, Department of Cell Biology, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528668123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528668123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523043123?af=R">
      <title>LARP1 integrates MYC and mTOR signaling to enable anabolic growth during tumor initiation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523043123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceMany cancers are driven by oncogenes—mutated genes that reprogram cells toward uncontrolled growth. How and when this genetic reprogramming is turned into actual tumor mass remains unclear. Here, we show that cancer-driving mutations (MYC ...</description>
      <dc:title>LARP1 integrates MYC and mTOR signaling to enable anabolic growth during tumor initiation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523043123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Pedro FuentesFlavia IannizzottoElisa BattagliaChiara BalzamoCarla TolaBerta ForcadaPau Bosch-i-CrespoFrancisco D. Morón-DuranBrandon E. FrankCarolina Martínez-HerráezZoi MastoraGabriella Manfili-MarinhoAlbert TaulerCristina SantosRamón SalazarAntonio Gentilellaahttps://ror.org/0008xqs48Laboratory of Cancer Metabolism, ONCOBELL Program, Bellvitge Biomedical Research Institute, Barcelona 08908, SpainbDepartment of Biology, University of Napoli “Federico II”, Napoli 80125, Italychttps://ror.org/01j1eb875Oncology Data Analytics Program, Catalan Institute of Oncology, L’Hospitalet de Llobregat, Barcelona 08908, Spaindhttps://ror.org/021018s57Department of Clinical Sciences, Faculty of Medicine and Universitat de Barcelona Institute of Complex Systems, University of Barcelona, Barcelona 08908, SpaineConsortium for Biomedical Research in Epidemiology and Public Health, Madrid 28029, Spainfhttps://ror.org/021018s57Department of Biochemistry and Physiology, Faculty of Pharmacy and Food Science, University of Barcelona, Barcelona 08028, Spainghttps://ror.org/021018s57Department of Clinical Sciences, Faculty of Medicine, University of Barcelona, Barcelona 08908, SpainhConsortium for Biomedical Research in Oncology, Madrid 28029, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523043123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523043123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2538027123?af=R">
      <title>Phase-selective Floquet engineering in a charge density wave material</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2538027123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceFloquet engineering provides an emerging approach to tailor quantum materials using time-periodic drives. Here, we demonstrate Floquet engineering of TiSe2which is enabled by the spatially periodic charge density wave (CDW) transition. We ...</description>
      <dc:title>Phase-selective Floquet engineering in a charge density wave material</dc:title>
      <dc:identifier>doi:10.1073/pnas.2538027123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Fei WangXuanxi CaiTeng XiaoChanghua BaoHaoyuan ZhongWanying ChenTianyun LinTianshuang ShengXiao TangHongyun ZhangPu YuZhiyuan SunShuyun Zhouahttps://ror.org/03cve4549Department of Physics, Tsinghua University, Beijing 100084, People’s Republic of Chinabhttps://ror.org/016g9tg59State Key Laboratory of Low-Dimensional Quantum Physics, Department of Physics, Tsinghua University, Beijing 100084, People’s Republic of Chinachttps://ror.org/01dq60k83Advanced Institute for Materials Research (WPI-AIMR), Tohoku University, Sendai 980-8577, Japandhttps://ror.org/03cve4549Frontier Science Center for Quantum Information, Tsinghua University, Beijing 100084, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2538027123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2538027123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537884123?af=R">
      <title>Development of a robust method to derive human trophoblast stem cells from late-gestation placentas and its application to preeclampsia</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537884123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceTrophoblasts play central roles in placental development and function. Although trophoblast dysfunction underlies many pregnancy complications, the molecular pathogenesis remains poorly understood due to the scarcity of appropriate ...</description>
      <dc:title>Development of a robust method to derive human trophoblast stem cells from late-gestation placentas and its application to preeclampsia</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537884123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Akira OikeEri H. KobayashiYasuhiro YamamotoHirotaka HamadaSota TakahashiTakanori ShimizuAkane KitamuraAsato SekiyaNorio KobayashiShun ShibataShun EndoTetsuya SatoNaoto KubotaChie KikutakeMikita SuyamaTakahiro ArimaHiroaki Okaeahttps://ror.org/02cgss904Department of Trophoblast Research, Institute of Molecular Embryology and Genetics, Kumamoto University, Kumamoto 860-0811, Japanbhttps://ror.org/01dq60k83Department of Informative Genetics, Environment and Genome Research Center, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japanchttps://ror.org/01dq60k83Division of Molecular Physiology and Metabolism, Tohoku University Graduate School of Medicine, Sendai, 980-8575, Japandhttps://ror.org/01dq60k83Department of Obstetrics and Gynecology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japanehttps://ror.org/00jmfr291Department of Mechanical Engineering, University of Michigan, Ann Arbor, MI 48109fhttps://ror.org/04zb31v77Biomedical Research Center, Saitama Medical University, Saitama 350-1241, Japanghttps://ror.org/00p4k0j84Division of Bioinformatics, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japanhhttps://ror.org/03nawhv43Division of Biomedical Sciences, School of Medicine, University of California, Riverside, CA 92521ihttps://ror.org/03nawhv43Center for RNA Biology and Medicine, University of California, Riverside, CA 92521jhttps://ror.org/01dq60k83Department of Molecular Oncology, Institute of Development, Aging and Cancer, Tohoku University, Sendai 980-8575, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537884123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537884123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609054123?af=R">
      <title>Strain-specific propagation of variant Creutzfeldt–Jakob disease prions in humanized neural cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609054123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificancePrions are infectious protein assemblies in which conformation encodes heritable strain information. Mechanistic study of human prion propagation has been limited by the lack of suitable cell models. Here, we establish humanized neural cells ...</description>
      <dc:title>Strain-specific propagation of variant Creutzfeldt–Jakob disease prions in humanized neural cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609054123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Melissa L. D. RaynerParineeta AroraJacqueline M. LinehanHelena RosAkin NihatFabio ArgentinaConnor PrestonChristian SchmidtJuan M. RibesPeter-Christian KlöhnSimon MeadSebastian BrandnerJohn CollingeParmjit S. Jatahttps://ror.org/03x94j517Medical Research Council Prion Unit at UCL, UCL Institute of Prion Diseases, London W1W 7FF, United Kingdombhttps://ror.org/02jx3x895Department of Pharmacology, UCL School of Pharmacy, University College London, London WC1N 1AX, United Kingdomchttps://ror.org/02jx3x895National Health Service National Prion Clinic, National Hospital for Neurology and Neurosurgery, University College London Hospitals National Health Service Foundation Trust, London WC1N 3BG, United Kingdomdhttps://ror.org/02wnqcb97Division of Neuropathology, The National Hospital for Neurology and Neurosurgery, University College National Health Service Foundation Trust, London WC1N 3BG, United Kingdomehttps://ror.org/0370htr03Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 3BG, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609054123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609054123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531481123?af=R">
      <title>Glycosylation-independent functions for distinct glypican core proteins drive cell-specific responses in corticogenesis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531481123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceBrain development relies on precise signaling in the extracellular space, which is regulated by proteoglycans, including glypicans. It was long thought that these molecules acted solely through their sugar extensions (GAG chains). Our research ...</description>
      <dc:title>Glycosylation-independent functions for distinct glypican core proteins drive cell-specific responses in corticogenesis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531481123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Sara DouceauTanya Deutsch GuerreroChloé BorowskiChloé LourençoMargot WeberHanna KavaliovaEmma BraultCamille PonsAnne RoumierRebekka WildJulien Ferentahttps://ror.org/02en5vm52Institut du Fer à Moulin, Inserm, Sorbonne Université, Paris 75005, Francebhttps://ror.org/02en5vm52Sorbonne Université, CNRS, Inserm, Center for Neuroscience Sorbonne Université (Neuro-SU), Paris 75005, Francechttps://ror.org/01c2cjg59Sorbonne Université, CNRS, Inserm, Institut de Biologie Paris-Seine (IBPS), Paris 75005, Francedhttps://ror.org/00jjx8s55Institut de Biologie Structurale, UMR 5075, University Grenoble Alpes, CNRS, Commissariat à l’énergie atomique et aux énergies alternatives (CEA), Grenoble 38000, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531481123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531481123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601472123?af=R">
      <title>Subcellular metallomic networks orchestrate physiological outcomes: Single-cell mapping via an integrated SEM-FIB-TOF-SIMS platform</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601472123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThis study introduces an integrated scanning electron microscopy–focused ion beam–time-of-flight-secondary ion mass spectrometry (SEM-FIB-TOF-SIMS) platform combining full-spectrum elemental detection, nanometer-scale resolution, and precise ...</description>
      <dc:title>Subcellular metallomic networks orchestrate physiological outcomes: Single-cell mapping via an integrated SEM-FIB-TOF-SIMS platform</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601472123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Mengzhu ChengLihong WangZiwei WangTianjiao WangJun ZhaoBin XuPing QiuTiantian LiuXiaohua HuangXing Wang DengaPeking University Institute of Advanced Agricultural Sciences, Shandong Laboratory of Advanced Agriculture Sciences in Weifang, Shandong 261325, Chinabhttps://ror.org/02v51f717School of Advanced Agricultural Sciences and School of Life Sciences, Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601472123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2601472123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524190123?af=R">
      <title>A protective role for APP in nuclear waste clearance via lysosomal exocytosis</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524190123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceResearch on Alzheimer’s disease (AD) has largely focused on amyloid-β, a fragment of the amyloid precursor protein (APP). However, the physiological functions of APP remain poorly understood. Here, we show that APP protects cells by clearing ...</description>
      <dc:title>A protective role for APP in nuclear waste clearance via lysosomal exocytosis</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524190123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-11T07:00:00Z</dc:date>
      <dc:creator>Godfried DougnonTakayoshi OtsukaYuka NakamuraAkiko SakaiTomoyuki YamanakaNoriko MatsuiAsa NakaharaAi ItoAtsushi HatanoMasaki MatsumotoHironaka IgarashiAkiyoshi KakitaMasaki UenoHideaki Matsuiahttps://ror.org/04ww21r56Department of Neuroscience of Disease, Brain Research Institute, Niigata University, Niigata 951-8585, Japanbhttps://ror.org/04ww21r56Department of System Pathology for Neurological Disorders, Brain Research Institute, Niigata University, Niigata 951-8585, Japanchttps://ror.org/04ww21r56Department of Pathology, Brain Research Institute, Niigata University, Niigata 951-8585, Japandhttps://ror.org/04ww21r56Department of Omics and Systems Biology, Graduate School of Medical and Dental Sciences, Niigata University, Niigata 951-8510, Japanehttps://ror.org/04ww21r56Department of Biological Magnetic Resonance, Center for Integrated Human Brain Science, Brain Research Institute, Niigata University, Niigata 951-8585, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524190123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524190123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525378123?af=R">
      <title>Amazon deforestation reduces precipitation and soybean yields across Southern Brazil</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525378123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceAgricultural expansion typically involves clearing forests to create new croplands, but this approach may be self-defeating. We demonstrate that Amazon deforestation substantially reduces crop productivity in Brazil’s established agricultural ...</description>
      <dc:title>Amazon deforestation reduces precipitation and soybean yields across Southern Brazil</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525378123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Hao LiCorey S. LeskLei ZhuThomas W. CrowtherMin ChenDeepak K. RayNathaniel D. Muellerahttps://ror.org/02zhqgq86Department of Geography, The University of Hong Kong, Hong Kong 999077, Chinabhttps://ror.org/00cv9y106Department of Environment, Ghent University, Ghent 9000, Belgiumchttps://ror.org/002rjbv21Department of Earth and Atmospheric Science, Université du Québec á Montréal, Montréal, QC H3C 3P8, Canadadhttps://ror.org/049s0rh22Department of Geography, Dartmouth College, Hanover, NH 03755ehttps://ror.org/03cve4549Department of Earth System Science, Tsinghua University, Beijing 100084, Chinafhttps://ror.org/01q3tbs38Environmental Sciences and Engineering, Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology, Thuwal 23955, Kingdom of Saudi ArabiagBRANCH Institute, Zug 6300, Switzerlandhhttps://ror.org/01y2jtd41Department of Forest and Wildlife Ecology, University of Wisconsin-Madison, Madison, WI 53706ihttps://ror.org/017zqws13Institute on the Environment, University of Minnesota, St Paul, MN 55108jhttps://ror.org/03k1gpj17Department of Ecosystem Science and Sustainability, Colorado State University, Fort Collins, CO 80523</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525378123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525378123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531280123?af=R">
      <title>Experimental evolution of cellular miniaturization reveals a putative mechanism for cell size evolution</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531280123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCell size influences nearly every aspect of cellular physiology and varies drastically among eukaryotes, yet how such diversity evolves without compromising cellular function remains unclear. Using experimental evolution in budding yeast, we ...</description>
      <dc:title>Experimental evolution of cellular miniaturization reveals a putative mechanism for cell size evolution</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531280123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Ana GaroñaMorgane V. LemosAndrea GiomettoMarco Fumasoniahttps://ror.org/0346k0491Gulbenkian Institute for Molecular Medicine, Oeiras 2780-156, Portugalbhttps://ror.org/05bnh6r87School of Civil and Environmental Engineering, Cornell University, Ithaca, NY 14853chttps://ror.org/01c27hj86Faculdade de Medicina da Universidade de Lisboa, Lisbon 1649-028, Portugal</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531280123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531280123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604369123?af=R">
      <title>Conceptual priorities shape individual gaze patterns during naturalistic visual attention</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604369123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceStepping into a new visual environment, we immediately start to explore that environment with our eyes. What factors shape how we selectively allocate our attention? Participants explored 360°, real-world environments while their gaze was ...</description>
      <dc:title>Conceptual priorities shape individual gaze patterns during naturalistic visual attention</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604369123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Amanda J. HaskinsKatherine O. PackardCaroline E. Robertsonahttps://ror.org/049s0rh22Department of Psychological and Brain Sciences, Dartmouth College, Hanover, NH 03755bhttps://ror.org/0168r3w48Department of Psychology, University of California, San Diego, CA 92093</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604369123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604369123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2524496123?af=R">
      <title>Heterotypic intercellular adhesion tunes efficiency of cell-on-cell migration</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2524496123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCell adhesion is important for cell migration, and when cells migrate on a substrate of other cells (rather than on extracellular matrix), the adhesive properties of both cell types must be considered. However, whether and how dynamic changes ...</description>
      <dc:title>Heterotypic intercellular adhesion tunes efficiency of cell-on-cell migration</dc:title>
      <dc:identifier>doi:10.1073/pnas.2524496123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Chandrashekar KuyyamudiSuhrid GhoshCassandra G. Extavourahttps://ror.org/03vek6s52Department of Organismic and Organismic Biology, Harvard University, Cambridge, MA 02138bHHMI, Chevy Chase, MD 20815chttps://ror.org/03vek6s52Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2524496123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2524496123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2517639123?af=R">
      <title>Transformations of the spatial activity manifold convey aversive information in CA3</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2517639123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceThe hippocampus helps us remember where we are and how we feel in different situations. We studied how the hippocampus combines location and affective experiences by recording activity from specific hippocampal connections in mice exploring a ...</description>
      <dc:title>Transformations of the spatial activity manifold convey aversive information in CA3</dc:title>
      <dc:identifier>doi:10.1073/pnas.2517639123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Albert Miguel-LópezNegar NikbahktCarlos Wert-CarvajalLena Johanna GschossmannMartin PofahlHeinz BeckTatjana Tchumatchenkoahttps://ror.org/01xnwqx93Universität Bonn, Universitätsk-linikum Bonn, Institute for Experimental Epileptology and Cognition Research, Bonn 53127, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2517639123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2517639123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523183123?af=R">
      <title>Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523183123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceProtein phosphorylation regulates nearly every aspect of biology and is dynamically controlled by the opposing activities of writer and eraser enzymes. While the sequences preferences of writer enzymes have been characterized extensively, ...</description>
      <dc:title>Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523183123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Katarzyna RadziwonLaura A. CampbellLauren E. MazurkiewiczSopo JalalishviliIzabelle EppingerAanika ParikhAmy M. Weeksahttps://ror.org/01y2jtd41Department of Biochemistry, University of Wisconsin–Madison, Madison, WI 53706bhttps://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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523183123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523183123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2602575123?af=R">
      <title>A fungal natural product that inhibits plant cellulose biosynthesis by disrupting cellulose synthase complexes</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2602575123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceCellulose, a fundamental structural component of plant cell walls, is synthesized by cellulose synthase complexes (CSCs) and represents a critical herbicide target. While synthetic cellulose biosynthesis inhibitors (CBIs) like isoxaben and ...</description>
      <dc:title>A fungal natural product that inhibits plant cellulose biosynthesis by disrupting cellulose synthase complexes</dc:title>
      <dc:identifier>doi:10.1073/pnas.2602575123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Zhongshou WuLu LiuWenyu HanXingbo CaiPixian XiaoZuodong SunChunsheng YanSilvana ReidYun ChenZhonghua MaYi TangSteven E. Jacobsenahttps://ror.org/05s5qx907State Key Laboratory of Rice Biological Breeding, Key Laboratory of Molecular Biology of Crop Pathogens and Insects, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, Chinabhttps://ror.org/046rm7j60Department of Molecular, Cell and Developmental Biology, University of California at Los Angeles, Los Angeles, CA 90095chttps://ror.org/046rm7j60HHMI, University of California at Los Angeles, Los Angeles, CA 90095dhttps://ror.org/046rm7j60Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095ehttps://ror.org/046rm7j60Department of Chemical and Biomolecular Engineering, University of California at Los Angeles, Los Angeles, CA 90095fhttps://ror.org/046rm7j60Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, University of California at Los Angeles, Los Angeles, CA 90095</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2602575123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2602575123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531602123?af=R">
      <title>Female dolphins use individual vocal labels to track coercive males</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531602123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;SignificanceHumans use accumulated social knowledge to guide decision-making, classifying individual relationships according to their social payoffs. A central component of this ability is the use of individually distinctive vocal labels, allowing ...</description>
      <dc:title>Female dolphins use individual vocal labels to track coercive males</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531602123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-01T07:00:00Z</dc:date>
      <dc:creator>Alice BouchardSimon J. AllenPernille M. SørensenMichael KrützenSvenja M. MarfurtRichard C. ConnorStephanie L. Kingahttps://ror.org/0524sp257School of Biological Sciences, University of Bristol, Bristol BS8 1TQ, United Kingdombhttps://ror.org/02crff812Evolutionary Genetics Group, Department of Evolutionary Anthropology, University of Zurich, Zurich CH-8057, Switzerlandchttps://ror.org/047272k79School of Biological Sciences, Oceans Institute, University of Western Australia, Perth, WA 6009, Australiadhttps://ror.org/01aj84f44Department of Biology, Aarhus University, Aarhus C 8000, Denmarkehttps://ror.org/02gz6gg07Institute of Environment and Department of Biological Sciences, Florida International University, Miami, FL 33181</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531602123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531602123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609202123?af=R">
      <title>General inverse-cube thickness scaling of projectile penetration energy in ultrathin films</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609202123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Ultrathin films of widely different materials exhibit a dramatic enhancement of projectile penetration resistance under high–velocity impact. Despite extensive simulations and experiments, a unifying physical explanation has remained elusive. Here we show ...</description>
      <dc:title>General inverse-cube thickness scaling of projectile penetration energy in ultrathin films</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609202123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Alessio ZacconeTimothy W. Sirkahttps://ror.org/00wjc7c48Department of Physics “A. Pontremoli”, University of Milan, Milan 20133, Italybhttps://ror.org/011hc8f90Polymers Branch, DEVCOM Army Research Laboratory, Aberdeen Proving Ground, Aberdeen, MD 21005</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609202123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609202123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605694123?af=R">
      <title>Mapping ammonia emission plumes using shortwave infrared imaging spectroscopy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605694123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Atmospheric ammonia emissions are harmful to ecosystems and human health. These emissions have traditionally been monitored using thermal infrared spectrometers, though such techniques are limited by thermal contrast requirements, the coarse spatial ...</description>
      <dc:title>Mapping ammonia emission plumes using shortwave infrared imaging spectroscopy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605694123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <dc:creator>Nicholas BalasusDaniel H. CusworthJinsol KimDaniel J. VaronCharles E. MillerRiley M. DurenaCarbon Mapper, Pasadena, CA 91101bhttps://ror.org/042nb2s44Department of Aeronautics and Astronautics, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/05dxps055Jet Propulsion Laboratory, California Institute of Technology, Pasadena, CA 91101</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605694123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605694123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604814123?af=R">
      <title>The 2025–2030 Dietary Guidelines for Americans are associated with higher land, water and nitrogen use, and greenhouse gas emissions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604814123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Dietary guidelines form the foundation of federal food policy, informing programs such as the Supplemental Nutrition Assistance Program (SNAP), government food procurement, school meals, and military and hospital food services. The most recent guidelines, ...</description>
      <dc:title>The 2025–2030 Dietary Guidelines for Americans are associated with higher land, water and nitrogen use, and greenhouse gas emissions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604814123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-01T07:00:00Z</dc:date>
      <dc:creator>Alon SheponTamar MakovDavid L. KatzGidon Eshelahttps://ror.org/04mhzgx49The Steinhardt Museum of Natural History, Tel Aviv University, Tel Aviv 6139001, Israelbhttps://ror.org/04mhzgx49The Department of Public Policy, Social Sciences Faculty, Tel Aviv University, Tel Aviv 6997801, Israelchttps://ror.org/05tkyf982Management Department, Ben-Gurion University of the Negev, Beer Sheva 8410501, Israeldhttps://ror.org/05tkyf982School of Sustainability and Climate Change, Ben-Gurion University of the Negev, Beer Sheva 8410501, IsraeleDietID, Detroit, MI 48226fhttps://ror.org/04yrgt058Department of Environmental Physics, Bard College, Annandale-on-Hudson, NY 12504-5000</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604814123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604814123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529341123?af=R">
      <title>Ancient oaks reveal rewilding of Mediterranean forests after the Black Death</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529341123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;In Italy, evergreen holm oaks (Quercus ilex) and deciduous sessile oaks (Quercus petraea) experienced a synchronized establishment pulse starting at the beginning of 1400s CE, consistent with a release from anthropogenic pressure following demographic ...</description>
      <dc:title>Ancient oaks reveal rewilding of Mediterranean forests after the Black Death</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529341123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-01T07:00:00Z</dc:date>
      <dc:creator>Gianluca PiovesanMichele BalivaFranco BiondiJordan PalliLucio CalcagnileAlessandro ChiarucciRaffaele ManiconeGianluca QuartaGiovanni QuilghiniAntonino SiclariCharles H. Cannonahttps://ror.org/03svwq685Department of Ecological and Biological Sciences, University of Tuscia, Viterbo 01100, Italybhttps://ror.org/01keh0577DendroLab, Department of Natural Resources and Environmental Science, University of Nevada, Reno, NV 89557chttps://ror.org/03fc1k060Department of Mathematics and Physics “Ennio De Giorgi”, Centre of Applied Physics, Dating and Diagnostics, University of Salento, Lecce 73100, Italydhttps://ror.org/01111rn36Department of Biological, Geological, and Environmental Sciences, Alma Mater Studiorum University of Bologna, Bologna 40126, ItalyeComando Unità Forestali Ambientali ed Agroalimentari, Raggruppamento Carabinieri Biodiversità, Roma 00187, ItalyfCittà Metropolitana di Reggio Calabria, Reggio Calabria 89100, Italyghttps://ror.org/02rz58g17Applied Research Center for Tropical Plant Conservation, Xishuangbanna Tropical Botanical Garden (XTBG), Menglun 666303, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529341123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529341123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604082123?af=R">
      <title>Alpha-synuclein fibrils induce budding of mitochondrial-derived vesicles</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604082123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;α-synuclein (α-syn) aggregation is a hallmark of synucleinopathies, a class of neurodegenerative disorders such as Parkinson’s disease (PD). Several lines of evidence indicate the involvement of mitochondria in the disease pathology. Despite extensive ...</description>
      <dc:title>Alpha-synuclein fibrils induce budding of mitochondrial-derived vesicles</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604082123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Thomas BraunViviane ReberCinzia TiberiAndri FränklDhiman GhoshRoland RiekTetiana Serdiukahttps://ror.org/02s6k3f65Biozentrum, University of Basel, Basel 4056, SwitzerlandbDepartment of Biology, Institute of Molecular Systems Biology, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerlandchttps://ror.org/02s6k3f65BioEM Lab, Biozentrum, University of Basel, Basel 4058, Switzerlanddhttps://ror.org/01m0th787Department of Chemistry and Applied Biosciences, Institute of Molecular Physical Science, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604082123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604082123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2611096123?af=R">
      <title>Testicular origin of epigenetic inheritance independent of sperm mitochondrial DNA and epididymal exposure</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2611096123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;Paternal epigenetic inheritance remains mechanistically unresolved. Recent studies propose that environmental exposures induce mitochondrial DNA (mtDNA)-dependent transcription in sperm during epididymal transit, altering small RNA content and offspring ...</description>
      <dc:title>Testicular origin of epigenetic inheritance independent of sperm mitochondrial DNA and epididymal exposure</dc:title>
      <dc:identifier>doi:10.1073/pnas.2611096123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <dc:creator>Zhuqing WangYasuhiro YamauchiSheng ChenHuili ZhengMonika A. WardWei Yanahttps://ror.org/05dk0ce17School of Molecular Biosciences, Washington State University, Pullman, WA 99164bhttps://ror.org/046rm7j60The Lundquist Institute for Biomedical Innovation at Harbor-University of California, Los Angeles Medical Center, Torrance, CA 90502chttps://ror.org/03tzaeb71Yanagimachi Institute for Biogenesis Research, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI 96822dhttps://ror.org/046rm7j60Department of Medicine, David Geffen School of Medicine at University of California, Los Angeles, Los Angeles, CA 90095</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2611096123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2611096123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2605838123?af=R">
      <title>Cryopreservation through vitrification enables functional recovery of the mouse hippocampus</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2605838123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Cryopreservation through vitrification enables functional recovery of the mouse hippocampus</dc:title>
      <dc:identifier>doi:10.1073/pnas.2605838123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Alex Maya-RomeroRoberto Zoncuahttps://ror.org/01an7q238Department of Molecular and Cell Biology, 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>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2605838123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2605838123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2614646123?af=R">
      <title>One target across kingdoms: Chemical inhibition of conserved copper pumps</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2614646123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>One target across kingdoms: Chemical inhibition of conserved copper pumps</dc:title>
      <dc:identifier>doi:10.1073/pnas.2614646123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Eva J. Geahttps://ror.org/04dawnj30Department of Chemistry, University of North Carolina at Charlotte, Charlotte, NC 28223</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2614646123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2614646123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613743123?af=R">
      <title>Two-component plant defenses are better than one</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613743123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Two-component plant defenses are better than one</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613743123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Tam Duc MaiJonathan Gershenzonahttps://ror.org/02ks53214Department of Biochemistry, Max Planck Institute for Chemical Ecology, Jena D-07745, GermanybFaculty of Forestry and Wood Sciences, University of Life Sciences, Prague 165 21, Czech Republic</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613743123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613743123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606967123?af=R">
      <title>The co-occurrence of ingroup and outgroup prosociality requires cross-group partner choice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606967123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>The co-occurrence of ingroup and outgroup prosociality requires cross-group partner choice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606967123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Qinyu XiaoHirotaka Imadaahttps://ror.org/03prydq77Department of Occupational, Economic, and Social Psychology, Faculty of Psychology, University of Vienna, Vienna 1010, AustriabDepartment of Psychology, Royal Holloway, University of London, Egham TW20 0EX, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606967123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606967123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606646123?af=R">
      <title>Bacterial biofilms in calcium oxalate kidney stones: Where do we stand?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606646123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Bacterial biofilms in calcium oxalate kidney stones: Where do we stand?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606646123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>Carlos González GonzálezFederico ZorziMichel DaudonOlivier Traxerahttps://ror.org/018pp1107Endolase Lab, Groupe de Recherche Clinique n°20–Sorbonne Université, Procédés et Ingénierie en Mécanique et Matériaux Lab Arts et Métiers ParisTech, Paris 75020, Francebhttps://ror.org/02en5vm52Service d’Urologie, Assistance Publique–Hôpitaux de Paris, Hôpital Tenon, Sorbonne Université, Paris 75020, Francechttps://ror.org/018pp1107Procédés et Ingénierie en Mécanique et Matériaux, UMR 8006 CNRS–Arts et Métiers ParisTech, Paris 75013, Francedhttps://ror.org/05h5v3c50INSERM, UMR S 1155, Physiology Unit, Hôpital Tenon, Paris 75020, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606646123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606646123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535289123?af=R">
      <title>Regulation of gut epithelial barrier and tuft/goblet cell responses by microbiome repair: Opportunities and future directions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535289123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Regulation of gut epithelial barrier and tuft/goblet cell responses by microbiome repair: Opportunities and future directions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535289123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Zian WangJiahao XieShujing LiuMei HanLiang Wangahttps://ror.org/04c8eg608Research and Teaching Department of Comparative Medicine, Dalian Medical University, Dalian City, Liaoning Province 116044, Chinabhttps://ror.org/04c8eg608Department of Gastroenterology, The Second Hospital of Dalian Medical University, Dalian City, Liaoning Province 116023, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535289123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535289123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617334123?af=R">
      <title>Correction for McDonald et al., Can auxiliary indicators improve COVID-19 forecasting and hotspot prediction?</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617334123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Correction for McDonald et al., Can auxiliary indicators improve COVID-19 forecasting and hotspot prediction?</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617334123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617334123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617334123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617330123?af=R">
      <title>Correction for Salomon et al., The US COVID-19 Trends and Impact Survey: Continuous real-time measurement of COVID-19 symptoms, risks, protective behaviors, testing, and vaccination</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617330123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Salomon et al., The US COVID-19 Trends and Impact Survey: Continuous real-time measurement of COVID-19 symptoms, risks, protective behaviors, testing, and vaccination</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617330123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617330123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617330123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617803123?af=R">
      <title>Correction for Forrest et al., Early evidence for a stable and flexible foraging niche in the evolution of Homo</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617803123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Forrest et al., Early evidence for a stable and flexible foraging niche in the evolution of Homo</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617803123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-10T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617803123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617803123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2617340123?af=R">
      <title>Correction for Ajourlou et al., Upper mantle temperatures illuminate the Iceland hotspot track and understanding of ice–Earth interactions in Greenland</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2617340123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Ajourlou et al., Upper mantle temperatures illuminate the Iceland hotspot track and understanding of ice–Earth interactions in Greenland</dc:title>
      <dc:identifier>doi:10.1073/pnas.2617340123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-12T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2617340123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2617340123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613406123?af=R">
      <title>Reply to Wang et al.: Linking microbial metabolites and gut epithelial responses to microbiome-directed therapeutic foods</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613406123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Wang et al.: Linking microbial metabolites and gut epithelial responses to microbiome-directed therapeutic foods</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613406123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Yi WangHao-Wei ChangMichael J. BarrattJeffrey I. Gordonahttps://ror.org/031e8jz65The Edison Family Center for Genome Sciences and Systems Biology, Washington University School of Medicine, St. Louis, MO 63110bNewman Center for Gut Microbiome and Nutrition Research, Washington University School of Medicine, St. Louis, MO 63110cDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613406123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613406123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2613719123?af=R">
      <title>Reply to Xiao and Imada: Prosociality across group boundaries is possible without partner choice</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2613719123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Xiao and Imada: Prosociality across group boundaries is possible without partner choice</dc:title>
      <dc:identifier>doi:10.1073/pnas.2613719123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-08T07:00:00Z</dc:date>
      <dc:creator>Kasper OttenaAsylum and Migration Group, WODC Research and Data Centre, The Hague 2500 EH, The Netherlandsbhttps://ror.org/057w15z03Erasmus School of Social and Behavioural Sciences, Erasmus University Rotterdam, Rotterdam 3000 DR, The Netherlands</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2613719123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2613719123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609802123?af=R">
      <title>Reply to González González et al.: The contribution of bacteria to kidney stone formation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609802123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 24, June 2026. &lt;br/&gt;</description>
      <dc:title>Reply to González González et al.: The contribution of bacteria to kidney stone formation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609802123</dc:identifier>
      <dc:source>Proceedings of the National Academy of Sciences</dc:source>
      <dc:date>2026-06-09T07:00:00Z</dc:date>
      <dc:creator>William C. SchmidtRena YangHenry L. SchreiberAaron CelestianGerard C. L. WongKymora B. Scotlandahttps://ror.org/046rm7j60Department of Bioengineering, University of California Los Angeles, Los Angeles, CA 90095bhttps://ror.org/046rm7j60Department of Chemistry and Biochemistry, University of California Los Angeles. Los Angeles, CA 90095chttps://ror.org/046rm7j60Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095dhttps://ror.org/046rm7j60California NanoSystems Institute, University of California Los Angeles, Los Angeles, CA 90095eDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63130fhttps://ror.org/00p9h0053Department of Mineral Sciences, Natural History Museum of Los Angeles County, Los Angeles, CA 90036ghttps://ror.org/046rm7j60Department of Urology, University of California Los Angeles, Los Angeles, CA 90095</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>24</prism:number>
      <prism:coverDate>2026-06-16T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-06-16T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609802123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2609802123?af=R</prism:url>
      <prism:copyright/>
   </item>
</rdf:RDF>