<?xml version="1.0" encoding="UTF-8"?>
<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/action/doSearch?af=R">
      <title>Proceedings of the National Academy of Sciences: Plant Biology</title>
      <description>Biological Sciences / Plant Biology -- New results matching your topic search.</description>
      <link>https://www.pnas.org/action/doSearch?af=R</link>
      <dc:title>Proceedings of the National Academy of Sciences: Plant Biology</dc:title>
      <dc:publisher>Proceedings of the National Academy of Sciences</dc:publisher>
      <dc:language>en-US</dc:language>
      <prism:publicationName/>
      <items>
         <rdf:Seq>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2604539123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2424126123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2521483123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2523470123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2526714123?af=R"/>
            <rdf:li rdf:resource="https://www.pnas.org/doi/abs/10.1073/pnas.2527570123?af=R"/>
         </rdf:Seq>
      </items>
   </channel>
   <image rdf:about="http://www.atypon.com/images/atypon_logo_small.gif">
      <title>Atypon Systems</title>
      <url>http://www.atypon.com/images/atypon_logo_small.gif</url>
      <link>http://www.atypon.com</link>
   </image>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R">
      <title>Rubisco kinetic acclimation at the holoenzyme level</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceKinetic acclimation enables proteins to adjust their activity in response to environmental perturbations. For the CO2-fixing enzyme Rubisco, kinetic acclimation may be conferred by its small subunits. Plants express multiple small subunits and ...</description>
      <dc:title>Rubisco kinetic acclimation at the holoenzyme level</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519914123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Bryce AskeyMaddie CeminskyElena ScottYongsheng WangZhen Guo OhStavros AzinasArthur LaganowskyLaura Helen GunnaPlant Biology Section, School of Integrated Plant Science, Cornell University, Ithaca, NY 14853bDepartment of Chemistry, Texas A&amp;M University, College Station, TX 77843cDepartment of Molecular Medicine, Cornell University, Ithaca, NY 14853dDepartment of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Solna 171 65, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519914123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519914123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R">
      <title>Small subunit isoform diversity underlies structural heterogeneity in native plant Rubisco</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificanceRibulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the key enzyme in photosynthetic CO2fixation, has long challenged efforts to understand its assembly, regulation, and potential for enhancement. Here, we show that multiple small ...</description>
      <dc:title>Small subunit isoform diversity underlies structural heterogeneity in native plant Rubisco</dc:title>
      <dc:identifier>doi:10.1073/pnas.2519949123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Thomas ReynoldsZhemin ZhangDušan ŽivkovićSteven KellyJani R. BollaaDepartment of Biology, Univeristy of Oxford, Oxford OX1 3RB, United KingdombDepartment of Pharmacology, Case Western Reserve University, Cleveland, OH 44106cDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2519949123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2519949123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R">
      <title>Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;SignificancePlants survive drought by sensing the hormone abscisic acid (ABA), but how receptor structure converts hormone levels into precise stress responses has remained unclear. Here, we uncover a minimal five-amino acid “code” that determines whether ...</description>
      <dc:title>Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534140123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-15T07:00:00Z</dc:date>
      <dc:creator>Maria Rivera-MorenoMar BonoLourdes InfantesPedro L. RodriguezArmando AlbertaInstituto de Química-Física “Blas Cabrera”, Consejo Superior de Investigaciones Científicas, Madrid ES-28006, SpainbInstituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia, Valencia ES-46022, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534140123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534140123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R">
      <title>The next frontier: Exploring plant hypoxia sensing and response mechanisms through synthetic biology</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 16, April 2026. &lt;br/&gt;</description>
      <dc:title>The next frontier: Exploring plant hypoxia sensing and response mechanisms through synthetic biology</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606254123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-13T07:00:00Z</dc:date>
      <dc:creator>Emmanuelle GracietaBiology Department, Maynooth University, Maynooth Co. Kildare W23 XY3X, Ireland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>16</prism:number>
      <prism:coverDate>2026-04-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606254123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606254123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R">
      <title>BpFLC coordinates seasonal and age-related flowering in Betula platyphylla through environmental cues and epigenetic regulation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceThis study addresses the prolonged juvenile phase inBetulaplatyphylla(white birch) breeding by identifyingBpFLCas a central flowering-time regulator.BpFLCdelays flowering and promotes vegetative growth, thereby influencing carbon ...</description>
      <dc:title>BpFLC coordinates seasonal and age-related flowering in Betula platyphylla through environmental cues and epigenetic regulation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2518761123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Yi LiuSui WangTangchun ZhengHuiying SuoDi XiaoDong ZengXiangling YouHeike W. SederoffVincent L. ChiangXiyang ZhaoRonald R. SederoffGuanzheng QuaState Key Laboratory of Tree Genetics and Breeding, School of Forestry, Northeast Forestry University, Harbin 150040, ChinabJilin Provincial Key Laboratory of Tree and Grass Genetics and Breeding, College of Forestry and Grassland Science, Jilin Agricultural University, Changchun 130118, ChinacNational Key Laboratory of Smart Farm Technologies and Systems, Northeast Agricultural University, Harbin 150030, ChinadKey Laboratory of Soybean Biology of Chinese Education Ministry, College of Agriculture, Northeast Agricultural University, Harbin 150030, ChinaeNational Engineering Research Center for Floriculture, School of Landscape Architecture, Beijing Forestry University, Beijing 100083, ChinafCollege of Life Science, Northeast Forestry University, Harbin 150040, ChinagKey Laboratory of Horticulture Crop Genomics and Genetic Improvement in Xinjiang, Institute of Fruits and Vegetables, Xinjiang Academy of Agricultural Sciences, Urumqi 830091, ChinahDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695iForest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2518761123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2518761123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R">
      <title>An acetyltransferase family required for biosynthesis of diverse marine carotenoids</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceApproximately half of global photosynthesis occurs in oceans. Marine eukaryotic algae synthesize specialized carotenoids to facilitate efficient light capture underwater. While the multistep biosynthesis of these pigments has been partially ...</description>
      <dc:title>An acetyltransferase family required for biosynthesis of diverse marine carotenoids</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525772123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-09T07:00:00Z</dc:date>
      <dc:creator>Tianjun CaoXuechun BaiTingting YouYanyou JiangMartin LohrXiaobo LiaState Key Laboratory of Gene Expression, School of Life Sciences, Westlake University, Hangzhou 310030, ChinabInstitute of Biology, Westlake Institute for Advanced Study, Hangzhou 310030, ChinacWestlake Laboratory of Life Sciences and Biomedicine, Hangzhou 310024, ChinadInstitut für Molekulare Physiologie, Johannes Gutenberg University, 55099 Mainz, GermanyeZhejiang Key Laboratory of Low-Carbon Intelligent Synthetic Biology, Westlake University, Hangzhou 310030, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525772123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2525772123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R">
      <title>A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceHuanglongbing (HLB) is the most devastating disease of citrus with no resistance having been identified in commercial cultivars. Previous work implicated papain-like cysteine proteases (PLCPs) as an important hub of defense in citrus; however, ...</description>
      <dc:title>A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528641123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-07T07:00:00Z</dc:date>
      <dc:creator>Alexander J. McClellandBin HuYuantao XuXiaodong FangChunxia WangBenjamin L. KochAmelia H. LovelaceEva HawaraYuanchun WangZhiqian PangAgustina De FrancescoSuzanne P. van WierAndrew M. BeekmanAmit LevyNian WangRenier A. L. van der HoornQiang XuWenbo MaaThe Sainsbury Laboratory, University of East Anglia, Norwich NR4 7UH, United KingdombNational Key Laboratory for Germplasm Innovation and Utilization of Horticultural Crops, Huazhong Agricultural University, Wuhan 430070, ChinacCitrus Research and Education Center, Department of Plant Pathology, Microbiology and Cell Science, University of Florida/Institute of Food and Agricultural Sciences, Lake Alfred, FL 33850dDepartment of Microbiology and Plant Pathology, University of California Riverside, Riverside, CA 92521eSchool of Chemistry, Pharmacy and Pharmacology, University of East Anglia, Norwich NR4 7TJ, United KingdomfPlant Chemetics Laboratory, Department of Biology, University of Oxford, Oxford OX1 3RB, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528641123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528641123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R">
      <title>Hydraulic stress limits thermal acclimation in trees under chronic drought</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceFuture forest resilience depends on whether trees can acclimate to rising heat and drought. Using multiyear manipulations of soil moisture and air temperature, we tested how long-term acclimation shapes leaf cooling and damage inFagus ...</description>
      <dc:title>Hydraulic stress limits thermal acclimation in trees under chronic drought</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531865123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Alyssa T. KullbergArianna MilanoAlvaro PorettiYike MaPatrick FavreKate M. JohnsonGiovanni BortolamiMaxwell BergströmThibaut JuillardJin WuZhengfei GuoJonas GislerMarcus SchaubCharlotte GrossiordaPlant Ecology Research Laboratory, School of Architecture, Civil and Environmental Engineering, École polytechnique fédérale de Lausanne, Lausanne CH-1015, SwitzerlandbForest and Soil Ecology Research Unit, Swiss Federal Institute for Forest, Snow, and Landscape Research, Birmensdorf CH-8903, SwitzerlandcCentre for Ecological Research and Forestry Applications, Barcelona 08193, SpaindSchool of Biological Sciences and Institute for Climate and Carbon Neutrality, The University of Hong Kong, ChinaeState Key Laboratory of Agrobiotechnology, Chinese University of Hong Kong, Hong Kong, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531865123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2531865123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R">
      <title>Expanded applicability of the triple oxygen isotope composition of phytoliths as an indicator of atmospheric relative humidity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Expanded applicability of the triple oxygen isotope composition of phytoliths as an indicator of atmospheric relative humidity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534827123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Anne AlexandreJulie AlemanMinger GuoDavid Au YangRobin HavasElizabeth WebbaCentre Européen de Recherche et d’Enseignement des Géosciences de l’Environnement (CEREGE), Centre National de la Recherche Scientifique (CNRS), Aix-Marseille Université, Institut de Recherche pour le Développement (IRD), Institut National de la Recherche Agronomique (INRA), Collège de France, Aix-en-Provence 13580, FrancebTrent School of the Environment, Trent University, Peterborough, ON K9L 0G2, CanadacEarth Sciences, University of Western Ontario, London, ON N6A 5B7, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534827123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2534827123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R">
      <title>A rare glycoalkaloid biosynthetic pathway from wild potato unlocks genetic routes to Colorado potato beetle resistance</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;SignificanceSolanaceous crops such as potato produce steroidal glycoalkaloids, compounds that are toxic to humans and animals yet provide protection against pests. The Colorado potato beetle (CPB) is a destructive pest that quickly evolves insecticide ...</description>
      <dc:title>A rare glycoalkaloid biosynthetic pathway from wild potato unlocks genetic routes to Colorado potato beetle resistance</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537847123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Ryota AkiyamaYuki IkeyamaHyoung Jae LeeNaoyuki UmemotoKenji AsanoTetsuya MoriToshiya MuranakaKazuki SaitoYukihiro SugimotoMasaharu MizutaniaDepartment of Agrobioscience, Graduate School of Agricultural Science, Kobe University, Kobe, Hyogo 657-8501, JapanbMetabolomics Research Group, RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa 230-0045, JapancNational Agricultural Research Center for Hokkaido Region, National Agriculture and Food Research Organization, Hokkaido 082-0081, JapandDepartment of Biotechnology, Graduate School of Engineering, Osaka University, Osaka 565-0871, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537847123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2537847123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2604539123?af=R">
      <title>Reply to Alexandre et al.: Insensitivity of the Δ′17O value of equisetum to atmospheric relative humidity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604539123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Reply to Alexandre et al.: Insensitivity of the Δ′17O value of equisetum to atmospheric relative humidity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604539123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Zachary SharpAnthony GarganoVincent HareJordan WostbrockaDepartment of Earth and Planetary Sciences, University of New Mexico, Albuquerque, NM 87122bDepartment of Archaeology, University of Cape Town, Rondebosch 7701, South AfricacEarth and Planetary Sciences, Yale University, New Haven, CT 06511</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604539123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604539123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R">
      <title>Structural innovation and flexibility in plant chemical defenses</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. &lt;br/&gt;</description>
      <dc:title>Structural innovation and flexibility in plant chemical defenses</dc:title>
      <dc:identifier>doi:10.1073/pnas.2606250123</dc:identifier>
      <dc:source/>
      <dc:date>2026-04-06T07:00:00Z</dc:date>
      <dc:creator>Martin VolfaBiology Centre, Institute of Entomology, Czech Academy of Sciences, Ceske Budejovice 370 05, Czech RepublicbFaculty of Science, Department of Zoology, University of South Bohemia, Ceske Budejovice 370 05, Czech Republic</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>15</prism:number>
      <prism:coverDate>2026-04-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-04-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2606250123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2606250123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R">
      <title>Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacterium Anabaena sp. PCC 7120</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe light reactions of oxygenic photosynthesis are powered by Photosystem I (PSI) and Photosystem II (PSII), which consist of a core and the peripheral light-harvesting antenna complexes. In cyanobacteria, phycobilisomes (PBSs) serve as the ...</description>
      <dc:title>Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacterium Anabaena sp. PCC 7120</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530459123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Zhiyuan MaoZhenhua LiXingyue LiLiangliang ShenTingyun KuangWenda WangJian-Ren ShenGuangye HanaState Key Laboratory of Forage Breeding-by-Design and Utilization, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, ChinabUniversity of Chinese Academy of Sciences, Beijing 100049, ChinacBeijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinadChina National Botanical Garden, Beijing 100093, ChinaeAcademician Workstation of Agricultural High-Tech Industrial Area of the Yellow River Delta, National Center of Technology Innovation for Comprehensive Utilization of Saline-Alkali Land, Dongying 257300, ChinafInstitute for Interdisciplinary Science, Advanced Research Field, and Graduate School of Environmental Life, Natural Science and Technology, Okayama University, Okayama 700-8530, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530459123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530459123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R">
      <title>A conserved ethylene-triggered cell death mechanism may underlie hollow stem formation across plant species</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceHollow stems are a widespread trait that has independently evolved multiple times across the plant kingdom, representing a case of convergent evolution. This trait plays important roles in plant development and environmental adaptation, yet ...</description>
      <dc:title>A conserved ethylene-triggered cell death mechanism may underlie hollow stem formation across plant species</dc:title>
      <dc:identifier>doi:10.1073/pnas.2530957123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-25T07:00:00Z</dc:date>
      <dc:creator>Mengxiao YanWeijuan FanYinghui MengJiamin ZhaoWei YangZiyin XuYusen GaoHaiyan ZhuangWuyu ZhouYuqin WangQingjun HuangLing YuanHongxia WangJun YangaShanghai Key Laboratory of Plant Functional Genomics and Resources, Shanghai Chenshan Botanical Garden, Shanghai 201602, ChinabDepartment of Urban Construction and Ecological Technology, Shanghai Institute of Technology, Shanghai 201418, ChinacCollege of Life Sciences, Shanghai Normal University, Shanghai 200234, ChinadCAS Center for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, ChinaeUniversity of Chinese Academy of Sciences, Beijing 101408, ChinafDepartment of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312gKentucky Tobacco Research and Development Center, University of Kentucky, Lexington, KY 40546-0236</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2530957123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2530957123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R">
      <title>Specialization of independently acquired flagellar FliC proteins in plant-associated Sphingomonas balances swimming and immunogenicity</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. &lt;br/&gt;SignificanceThe bacterial flagellum controls microbial motility and surface attachment. Some flagella contain a flg22 peptide epitope that is recognized by the plant immune receptor FLS2. This immune surveillance creates a trade-off between flagellar ...</description>
      <dc:title>Specialization of independently acquired flagellar FliC proteins in plant-associated Sphingomonas balances swimming and immunogenicity</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535583123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-27T07:00:00Z</dc:date>
      <dc:creator>Dor RussChinmay SahaKarnelia PaulZhiyu ZhengTheresa F. LawManuel Anguita-MaesoDerek S. LundbergConnor R. FitzpatrickJeffery L. DanglaDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill 27599, NCbHHMI, University of North Carolina at Chapel Hill, Chapel Hill 27599, NCcDepartment of Plant Biology, Swedish University of Agricultural Sciences, Uppsala 75007, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>13</prism:number>
      <prism:coverDate>2026-03-31T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-31T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535583123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535583123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2424126123?af=R">
      <title>Condensate-mediated shape transformations of cellular membranes by capillary forces</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2424126123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. &lt;br/&gt;SignificanceCells use membraneless compartments, called condensates, to organize biochemical processes. We show that condensates can physically reshape cellular membranes, producing tubes, sheets, or cup-like structures by tuning the shape metastability ...</description>
      <dc:title>Condensate-mediated shape transformations of cellular membranes by capillary forces</dc:title>
      <dc:identifier>doi:10.1073/pnas.2424126123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-16T07:00:00Z</dc:date>
      <dc:creator>Lukas HauerKatharina SporbeckJoseph F. McKennaDmytro PuchkovAlexander I. MayLorenzo FrigerioRoland L. KnorrAmir H. BahramiaCenter for Biochemistry, Faculty of Medicine, University of Cologne, University Hospital Cologne, Cologne, GermanybInstitute of Biology, Humboldt-Universität zu Berlin, Berlin 10115, GermanycSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, United KingdomdLeibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, GermanyeInstitute for Integrated Research, Institute of Science Tokyo, Tokyo, JapanfGraduate School and Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, JapangInstitute of Materials Science and Nanotechnology, Living Matter and Biophysics, National Nanotechnology Research Center (UNAM), Bilkent University, Ankara 06800, Türkiye</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>12</prism:number>
      <prism:coverDate>2026-03-24T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-24T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2424126123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2424126123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2521483123?af=R">
      <title>The Arabidopsis FRIENDLY (FMT) protein interacts with NAC and determines where nuclear-encoded mitochondrial proteins are translated</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2521483123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. &lt;br/&gt;SignificancePrecise regulation of gene expression in response to different stimuli requires fine-tuned control at both temporal and spatial levels. Among the involved mechanisms, intracellular mRNA trafficking and localized translation have emerged as ...</description>
      <dc:title>The Arabidopsis FRIENDLY (FMT) protein interacts with NAC and determines where nuclear-encoded mitochondrial proteins are translated</dc:title>
      <dc:identifier>doi:10.1073/pnas.2521483123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-17T07:00:00Z</dc:date>
      <dc:creator>Valentina Montoya-BrachJeanne RoignantGrégory RenardJohana ChicherAnne-Marie DuchêneaInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, Strasbourg Cedex 67084, FrancebStrasbourg-Esplanade Proteomics Facility, Institut de Biologie Moléculaire et Cellulaire, UAR1589 du CNRS, Université de Strasbourg, Strasbourg Cedex 67084, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>12</prism:number>
      <prism:coverDate>2026-03-24T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-24T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2521483123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2521483123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2523470123?af=R">
      <title>Subcellular calcium dynamics and organelle perturbations in resistosome-mediated cell death</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2523470123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. &lt;br/&gt;SignificanceNucleotide-binding leucine-rich repeat (NLR) proteins form resistosomes to trigger immune responses, yet how resistosome activation leads to cell death has remained unresolved. By live-cell imaging of NLR required for cell death 4 (NRC4) ...</description>
      <dc:title>Subcellular calcium dynamics and organelle perturbations in resistosome-mediated cell death</dc:title>
      <dc:identifier>doi:10.1073/pnas.2523470123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-18T07:00:00Z</dc:date>
      <dc:creator>Yi-Feng ChenKuan-Yu LinChing-Yi HuangLiang-Yu HouEnoch Lok Him YuenWei-Che Jimmy SunBing-Jen ChiangChin-Wen ChangHung-Yu WangTolga Osman BozkurtChih-Hang WuaInstitute of Plant and Microbial Biology, Academia Sinica, Taipei 115201, TaiwanbDepartment of Plant Pathology and Microbiology, National Taiwan University, Taipei 106319, TaiwancDepartment 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>12</prism:number>
      <prism:coverDate>2026-03-24T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-24T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2523470123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2523470123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2526714123?af=R">
      <title>Intrinsic period stability of the cyanobacterial circadian oscillator across in vitro and in vivo conditions</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2526714123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. &lt;br/&gt;SignificanceThe circadian clock exhibits remarkable precision and environmental insensitivity of its period, enabling organisms to anticipate daily environmental changes. In cyanobacteria, circadian rhythm is driven by a KaiC protein-based oscillator that ...</description>
      <dc:title>Intrinsic period stability of the cyanobacterial circadian oscillator across in vitro and in vivo conditions</dc:title>
      <dc:identifier>doi:10.1073/pnas.2526714123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-18T07:00:00Z</dc:date>
      <dc:creator>Kumiko Ito-MiwaKeiko ImaiKazuki TerauchiTakao KondoaDepartment of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, JapanbInstitute for Advanced Research, Nagoya University, Nagoya 464-8602, JapancDepartment of Physics, Graduate School of Science, Nagoya University, Nagoya 464-8602, JapandLaboratory of Cell Biology, Faculty of Medicine, Kansai Medical University, 2-5-1 Shin-machi, Hirakata City, Osaka 573-1010, JapaneCollege of Life Sciences, Ritsumeikan University, Shiga 525-8577, JapanfGraduate School of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>12</prism:number>
      <prism:coverDate>2026-03-24T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-24T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2526714123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2526714123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2527570123?af=R">
      <title>N-glucosylation of indole-3-acetyl amino acids modulates auxin metabolism and growth traits in Oryza sativa</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527570123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. &lt;br/&gt;SignificanceAlthough auxin metabolism is central to the regulation of plant growth and development, the fate of conjugates beyond oxidation has remained unclear. Here, we identify a rice UDP-glucosyltransferase, IAAspGT, that catalyzes theN-glucosylation ...</description>
      <dc:title>N-glucosylation of indole-3-acetyl amino acids modulates auxin metabolism and growth traits in Oryza sativa</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527570123</dc:identifier>
      <dc:source/>
      <dc:date>2026-03-18T07:00:00Z</dc:date>
      <dc:creator>Anna ZenjiKimihiko HataShoji SegamiNobue MakitaMikiko KojimaMika Yoshino-KidaKeisuke NagaiMotoyuki AshikariKazuki MatsubaraMasahiro YanoShuichi FukuokaKen-Ichiro HayashiYutaka SatoTokunori HoboYoshiaki InukaiHitoshi SakakibaraaGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, JapanbDivision of Evolutionary Biology, National Institute for Basic Biology, Okazaki 444-8585, JapancBasic Biology Program, SOKENDAI (The Graduate University for Advanced Studies), Okazaki 444-8585, JapandRIKEN Center for Sustainable Resource Science, Yokohama 230-0045, JapaneBioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, JapanfNational Institute of Agrobiological Sciences, Tsukuba 305-8602, JapangInstitute of Crop Science, National Agricultural and Food Research Organization, Tsukuba 305-8518, JapanhDepartment of Bioscience, Okayama University of Science, Okayama 700-0005, JapaniNational Institute of Genetics, Mishima 411-8540, JapanjDepartment of Genetics, School of Life Science, SOKENDAI (The Graduate University for Advanced Studies), Mishima 411-8540, JapankInternational Center for Research and Education in Agriculture, Nagoya University, Nagoya 464-8601, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>12</prism:number>
      <prism:coverDate>2026-03-24T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-03-24T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527570123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2527570123?af=R</prism:url>
      <prism:copyright/>
   </item>
</rdf:RDF>
