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      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 30, July 2026. &lt;br/&gt;SignificanceHow epithelial tissues control the shape dynamics of fluid-filled epithelial cavities remains poorly understood. Using MDCK epithelial domes as a model system, we show that diverse dome behaviors, including stable growth, sudden collapse, ...</description>
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      <title>Deciphering the mechanism of protein aggregation and effects of inhibitors using single-molecule mass photometry</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536600123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 30, July 2026. &lt;br/&gt;SignificanceBecause oligomers early in the aggregation cascade are difficult to observe directly, defining therapeutic targets during aggregation and determining how inhibitors act within the cascade is challenging. Currently, aggregation mechanisms are ...</description>
      <dc:title>Deciphering the mechanism of protein aggregation and effects of inhibitors using single-molecule mass photometry</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536600123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-22T07:00:00Z</dc:date>
      <dc:creator>Aaron LyonsSimanta Sarani PaulJack E. MacArthurGrace N. HoffmanAllan YarahmadySue-Ann MokMichael T. Woodsideahttps://ror.org/0160cpw27Department of Physics, University of Alberta, Edmonton AB T6G2E1, Canadabhttps://ror.org/0160cpw27Department of Biochemistry, University of Alberta, Edmonton AB T6G2H7, Canadachttps://ror.org/0160cpw27Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton AB T6G2M8, Canadadhttps://ror.org/0160cpw27Li Ka Shing Institute of Virology, University of Alberta, Edmonton AB T6G2E1, Canada</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>30</prism:number>
      <prism:coverDate>2026-07-28T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2536600123</prism:doi>
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      <title>Classification models for KCNQ1 variants distinguish functional and trafficking effects to enhance pathogenicity interpretation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537217123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 30, July 2026. &lt;br/&gt;SignificanceMissense variants in the KCNQ1 ion channel can disrupt channel activity, resulting in cardiac arrhythmias. It is critical to understand the underlying effects of individual variants on channel activity to guide therapeutic interventions. ...</description>
      <dc:title>Classification models for KCNQ1 variants distinguish functional and trafficking effects to enhance pathogenicity interpretation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537217123</dc:identifier>
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      <dc:date>2026-07-21T07:00:00Z</dc:date>
      <dc:creator>Ana C. Chang-GonzalezEric W. BellCarlos G. VanoyeEduardo GuadarramaReshma R. DesaiJean-Marc DeKeyserKathryn R. ButcherJames ScottCharles R. SandersAlfred L. GeorgeKaitlyn V. LedwitchJens Meilerahttps://ror.org/02vm5rt34Department of Chemistry, Vanderbilt University, Nashville, TN 37240bhttps://ror.org/02vm5rt34Center for Structural Biology, Vanderbilt University, Nashville, TN 37240cDepartment of Pharmacology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611dhttps://ror.org/02vm5rt34Department of Biochemistry, Vanderbilt University, Nashville, TN 37240ehttps://ror.org/05dq2gs74Department of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232fhttps://ror.org/02vm5rt34Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37240ghttps://ror.org/03s7gtk40Institute for Drug Discovery, Institute for Computer Science, Wilhelm Ostwald Institute for Physical and Theoretical Chemistry, Leipzig University, Leipzig, SAC 04103, Germanyhhttps://ror.org/01t4ttr56Center for Scalable Data Analytics and Artificial Intelligence and School of Embedded Composite Artificial Intelligence, Dresden 01062, Germanyihttps://ror.org/02vm5rt34Center for Applied AI in Protein Dynamics, Vanderbilt University, Nashville, TN 37240</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>30</prism:number>
      <prism:coverDate>2026-07-28T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-28T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537217123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2619864123?af=R">
      <title>HUWE1 targets mitochondria via RMC1 to promote neurodevelopment</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2619864123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 30, July 2026. &lt;br/&gt;SignificanceMutations in HUWE1 are a recurrent cause of X-linked intellectual disability, yet most studies have focused on catalytic defects and the consequences for nuclear substrates. The present work identifies a mitochondrial pathway that is ...</description>
      <dc:title>HUWE1 targets mitochondria via RMC1 to promote neurodevelopment</dc:title>
      <dc:identifier>doi:10.1073/pnas.2619864123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-23T07:00:00Z</dc:date>
      <dc:creator>Jiamin YiQin YangChunzhuang ZhouYunfei ZhuYingfeng TuLin ZhaoMin TangJunhong QinTao LongTianxing LiPing LiZikang GongQilin WangXin YongDa Jiaahttps://ror.org/00x43yy22Key Laboratory of Birth Defects and Related Diseases of Women and Children, Department of Paediatrics, West China Second University Hospital, State Key Laboratory of Biotherapy, Sichuan University, Chengdu 610041, Chinabhttps://ror.org/011ashp19Development and Related Diseases of Women and Children Key Laboratory of Sichuan Province, West China Second University Hospital, Sichuan University, Chengdu 610041, China</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>30</prism:number>
      <prism:coverDate>2026-07-28T07:00:00Z</prism:coverDate>
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      <prism:doi>10.1073/pnas.2619864123</prism:doi>
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      <title>Correction for Sabzehei et al., Exploring PrPC unfolding as a critical step preceding its refolding in the context of PrPSc propagation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2623376123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 30, July 2026. &lt;br/&gt;</description>
      <dc:title>Correction for Sabzehei et al., Exploring PrPC unfolding as a critical step preceding its refolding in the context of PrPSc propagation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2623376123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-20T07:00:00Z</dc:date>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>30</prism:number>
      <prism:coverDate>2026-07-28T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-28T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2623376123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2525799123?af=R">
      <title>Quantitative calibration of a spatial QSP model identifies fibroblast impact on HCC immunotherapy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2525799123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 29, July 2026. &lt;br/&gt;SignificanceComputational models can simulate disease to generate virtual clinical trials informing therapeutic selection. Predictions depend on the tumor microenvironment (TME), yet struggle to capture its spatiotemporal complexity in individual ...</description>
      <dc:title>Quantitative calibration of a spatial QSP model identifies fibroblast impact on HCC immunotherapy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2525799123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-14T07:00:00Z</dc:date>
      <dc:creator>Shuming ZhangHanwen WangYeonju ChoHeber L. RochaWendy WongMark YarchoanElizabeth M. JaffeeWon Jin HoLuciane T. KagoharaElana J. FertigAleksander S. PopelAtul Deshpandeahttps://ror.org/00za53h95Department of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205bhttps://ror.org/00za53h95Department of Oncology, Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine, Baltimore, MD 21205chttps://ror.org/00za53h95Convergence Institute, Johns Hopkins University, Baltimore, MD 21205dDepartment of Intelligent Systems Engineering, Indiana University, Bloomington, IN 47405ehttps://ror.org/00za53h95Bloomberg-Kimmel Immunotherapy Institute for Cancer Immunotherapy, Johns Hopkins University School of Medicine, Baltimore, MD 21205fInstitute for Genome Sciences, University of Maryland School of Medicine, Baltimore, MD 21201gMarlene &amp; Stuart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201hUniversity of Maryland Institute of Health Computing, University of Maryland School of Medicine, Baltimore, MD 21201iDepartment of Medicine, University of Maryland School of Medicine, Baltimore, MD 21201jhttps://ror.org/00za53h95Department of Electrical and Computer Engineering, Johns Hopkins University, Baltimore, MD 21218khttps://ror.org/00za53h95Data Science and AI Institute, Johns Hopkins University, Baltimore, MD 21209</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>29</prism:number>
      <prism:coverDate>2026-07-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2525799123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2608896123?af=R">
      <title>Fly navigational responses exploit plume-specific odor motion and gradient cues</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2608896123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 29, July 2026. &lt;br/&gt;SignificanceMany animals navigate diverse odor plumes by smell. While upwind movement upon odor detection is well established, less is known about how animals steer crosswind to stay in the plume. We show that directional odor cues—gradient and motion—...</description>
      <dc:title>Fly navigational responses exploit plume-specific odor motion and gradient cues</dc:title>
      <dc:identifier>doi:10.1073/pnas.2608896123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-14T07:00:00Z</dc:date>
      <dc:creator>Samuel BrudnerBaohua ZhouViraaj JayaramGustavo Madeira SantanaJohn P. CrimaldiDamon A. ClarkThierry Emonetahttps://ror.org/03v76x132Department of Molecular Cellular and Developmental Biology, Yale University, New Haven, CT 06511bhttps://ror.org/03v76x132Quantitative Biology Institute, Yale University, New Haven, CT 06511chttps://ror.org/03v76x132Department of Physics, Yale University, New Haven, CT 06511dhttps://ror.org/03v76x132Department of Neuroscience, Yale University, New Haven, CT 06510ehttps://ror.org/03v76x132Wu Tsai Institute, Yale University, New Haven, CT 06510fhttps://ror.org/02ttsq026Department of Civil, Environmental and Architectural Engineering, University of Colorado, Boulder, CO 80309</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>29</prism:number>
      <prism:coverDate>2026-07-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2608896123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2609610123?af=R">
      <title>The accuracy of electrostatic interactions captured by AI protein structure prediction models</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2609610123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 29, July 2026. &lt;br/&gt;SignificanceAI-based tools for protein structure prediction have transformed structural biology, yet their limitations remain incompletely understood. This study reveals a recurring tendency of modern AI structure predictors: their limited capacity to ...</description>
      <dc:title>The accuracy of electrostatic interactions captured by AI protein structure prediction models</dc:title>
      <dc:identifier>doi:10.1073/pnas.2609610123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-17T07:00:00Z</dc:date>
      <dc:creator>George I. Makhatadzeahttps://ror.org/01rtyzb94Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180bhttps://ror.org/01rtyzb94Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180chttps://ror.org/01rtyzb94Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>29</prism:number>
      <prism:coverDate>2026-07-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2609610123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610068123?af=R">
      <title>3D nanoscale imaging of amyloid-β oligomer interactions with extracellular vesicles by cryo-ET</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610068123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 29, July 2026. &lt;br/&gt;SignificanceAlzheimer’s disease accounts for over two-thirds of dementia cases worldwide. A key factor in Alzheimer’s disease pathology is the hydrophobic peptide, amyloid-β (Aβ), which self-assembles into neurotoxic oligomers found in patients’ brains. ...</description>
      <dc:title>3D nanoscale imaging of amyloid-β oligomer interactions with extracellular vesicles by cryo-ET</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610068123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-14T07:00:00Z</dc:date>
      <dc:creator>Anum KhursheedQi ShangHui ZhangYao TianPiotr SzwedziakVladimir A. VolkovJohn H. Vilesahttps://ror.org/026zzn846Centre for Molecular and Cellular Biology, Department of Biochemistry, School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdombhttps://ror.org/03d7sax13Wuhan Institute for Neuroscience and Neuroengineering, College of Life Sciences, South-Central Minzu University, Wuhan 430074, Chinachttps://ror.org/02crff812Center for Microscopy and Image Analysis, University of Zurich, Zurich CH-8006, Switzerland</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>29</prism:number>
      <prism:coverDate>2026-07-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610068123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2610567123?af=R">
      <title>Virtual ultrasound machine operating in a GHz to MHz frequency range for particle-based biomedical simulations</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2610567123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 29, July 2026. &lt;br/&gt;SignificanceParticle-based simulations of ultrasound at mesoscopic scales are essential for understanding how acoustic waves interact with microbubbles, cells, and other soft biological structures, but existing methods struggle to achieve numerical ...</description>
      <dc:title>Virtual ultrasound machine operating in a GHz to MHz frequency range for particle-based biomedical simulations</dc:title>
      <dc:identifier>doi:10.1073/pnas.2610567123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-16T07:00:00Z</dc:date>
      <dc:creator>Urban ČokoTilen PotiskMatej Praprotnikahttps://ror.org/050mac570Theory Department, National Institute of Chemistry, Ljubljana SI-1001, Sloveniabhttps://ror.org/05njb9z20Department of Physics, Faculty of Mathematics and Physics, University of Ljubljana, Ljubljana SI-1000, Sloveniachttps://ror.org/021018s57Universitat de Barcelona Institute of Complex Systems, Barcelona 08028, Spain</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>29</prism:number>
      <prism:coverDate>2026-07-21T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-21T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2610567123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2509171123?af=R">
      <title>Provable cluster-preserving visualizations with curvature-based stochastic neighbor embeddings</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2509171123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 28, July 2026. &lt;br/&gt;SignificanceWidely adopted Stochastic Neighbor Embedding (SNE) techniques like UMAP and tSNE have been used to make inferences in a range of scientific disciplines. Despite this, they are prone to producing visualizations that fragment underlying clusters ...</description>
      <dc:title>Provable cluster-preserving visualizations with curvature-based stochastic neighbor embeddings</dc:title>
      <dc:identifier>doi:10.1073/pnas.2509171123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-10T07:00:00Z</dc:date>
      <dc:creator>Tristan Luca SaidiAbigail HickokBastian RieckAndrew J. Blumbergahttps://ror.org/00hj8s172Department of Computer Science, Columbia University, New York, NY 10027bhttps://ror.org/00hj8s172Department of Mathematics, Columbia University, New York, NY 10027cDepartment of Machine Learning, University, Fribourg 1700, Switzerlanddhttps://ror.org/00hj8s172Irving Institute for Cancer Dynamics, Columbia University, New York, NY 10027</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>28</prism:number>
      <prism:coverDate>2026-07-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2509171123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2531232123?af=R">
      <title>Vimentin promotes actin assembly by stabilizing ATP-actin subunits at the barbed end</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2531232123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 28, July 2026. &lt;br/&gt;SignificanceThe cytoskeleton is composed of three types of filaments: actin, microtubules, and intermediate filaments, which coordinate to control cell shape, mechanics, and movement. Among them, the contribution of vimentin intermediate filaments to ...</description>
      <dc:title>Vimentin promotes actin assembly by stabilizing ATP-actin subunits at the barbed end</dc:title>
      <dc:identifier>doi:10.1073/pnas.2531232123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-06T07:00:00Z</dc:date>
      <dc:creator>Lilian PatyLukas KalvodaMaritzaida Varela-SalgadoQuang D. TranMartin LenzAntoine JégouGuillaume Romet-LemonneCécile Leducahttps://ror.org/02c5gc203Université Paris Cité, CNRS, Institut Jacques Monod, Paris F-75013, Francebhttps://ror.org/00w67e447Université Paris-Saclay, CNRS, Laboratoire de Physique Théorique et Modèles Statistiques, Orsay F-91405, Francechttps://ror.org/05f82e368Physique et Mécanique des Milieux Hétérogènes, CNRS, Ecole Supérieure de Physique et de Chimie Industrielles de la Ville de Paris, Paris Science et Lettres Research University, Sorbonne Université, Université Paris Cité, Paris F-75005, France</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>28</prism:number>
      <prism:coverDate>2026-07-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2531232123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2532243123?af=R">
      <title>Topological expansion of Boehm’s brushes via structured light</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2532243123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 28, July 2026. &lt;br/&gt;SignificanceThe human eye can perceive subtle polarization patterns in light, revealing structural features of the retina without invasive imaging. We identified a visual phenomenon in which structured light manifesting a spatially varying polarization ...</description>
      <dc:title>Topological expansion of Boehm’s brushes via structured light</dc:title>
      <dc:identifier>doi:10.1073/pnas.2532243123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-09T07:00:00Z</dc:date>
      <dc:creator>Dmitry A. PushinIman SalehiAmy ChowAndrew E. SilvaPinki ChahalDavid G. CoryMukhit KulmaganbetovGary P. MissonNaume ShentevskiTaranjit SinghShelby E. TempleBenjamin ThompsonDusan Sarenacahttps://ror.org/01aff2v68Institute for Quantum Computing, University of Waterloo, Waterloo, ON N2L3G1, Canadabhttps://ror.org/01aff2v68Department of Physics and Astronomy, University of Waterloo, Waterloo, ON N2L3G1, Canadachttps://ror.org/01aff2v68School of Optometry and Vision Science, University of Waterloo, Waterloo, ON N2L3G1, CanadadIncoherent Vision Inc., Wellesley, ON N0B2T0, CanadaeCentre for Eye and Vision Research, Shatin, Hong Kongfhttps://ror.org/0162z8b04Department of Psychology, Idaho State University, Pocatello, ID 83209ghttps://ror.org/01y64my43Department of Physics, University at Buffalo, State University of New York, Buffalo, NY 14260hhttps://ror.org/01aff2v68Department of Chemistry, University of Waterloo, Waterloo, ON N2L3G1, Canadaihttps://ror.org/05j0ve876School of Optometry, Aston University, Birmingham B4 7ET, United Kingdomjhttps://ror.org/0524sp257Division of Research and Innovation, University of Bristol, Bristol BS8 1QU, United KingdomkAzul Optics Ltd., Henleaze, Bristol BS9 4QG, United Kingdom</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>28</prism:number>
      <prism:coverDate>2026-07-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2532243123</prism:doi>
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      <title>A phase oscillator model of cell cycles reveals nuclear density control in a branched fungal network</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2534542123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 28, July 2026. &lt;br/&gt;SignificanceMultinucleate cells appear in diverse biological contexts, from human tissues to filamentous fungi, yet many fundamental aspects of their cell biology are still unclear. Regulating the nuclear-to-cytoplasmic ratio is important across cell ...</description>
      <dc:title>A phase oscillator model of cell cycles reveals nuclear density control in a branched fungal network</dc:title>
      <dc:identifier>doi:10.1073/pnas.2534542123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-09T07:00:00Z</dc:date>
      <dc:creator>Grace A. McLaughlinBenjamin M. StormoAmeya P. JalihalTaylor L. PompanMadhav ManiTimothy C. ElstonAmy S. Gladfelterahttps://ror.org/0130frc33Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599bhttps://ror.org/00py81415Department of Cell Biology, Duke University, Durham, NC 27705cDepartment of Engineering Sciences and Applied Mathematics, Northwestern University, Evanston, IL 60208dhttps://ror.org/0130frc33Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599ehttps://ror.org/0130frc33Computational Medicine Program, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>28</prism:number>
      <prism:coverDate>2026-07-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2534542123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2603575123?af=R">
      <title>High-resolution structure of monomorphic Aβ1-40 fibrils</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2603575123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 28, July 2026. &lt;br/&gt;SignificanceIn Alzheimer’s disease (AD), which affects more than 50 M people worldwide, the principal component of senile plaques is the amyloid-β (Aβ) peptide, predominantly existing in two alloforms: Aβ1-40and Aβ1-42. Aβ1-42is recognized for its ...</description>
      <dc:title>High-resolution structure of monomorphic Aβ1-40 fibrils</dc:title>
      <dc:identifier>doi:10.1073/pnas.2603575123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-08T07:00:00Z</dc:date>
      <dc:creator>Salima BahriRavi Shankar PalaniRobert SilversBrian MichaelVeronica LattanziIngemar AndréSara LinseRobert G. Griffinahttps://ror.org/042nb2s44Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/05g3dte14Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306chttps://ror.org/012a77v79Biochemistry and Structural Biology, Department of Chemistry, Lund University, Lund SE 22100, Sweden</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>28</prism:number>
      <prism:coverDate>2026-07-14T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-14T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2603575123</prism:doi>
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      <title>Combinatorial decision-making driven by multicomponent surface condensates</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2527873123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceIn living cells, biomolecules self-organize into compartments called condensates that form by phase transitions, often around surfaces such as DNA and membranes. Typically viewed as concentrating mechanisms, we show that the physics underlying ...</description>
      <dc:title>Combinatorial decision-making driven by multicomponent surface condensates</dc:title>
      <dc:identifier>doi:10.1073/pnas.2527873123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-01T07:00:00Z</dc:date>
      <dc:creator>Aidan ZentnerEthan V. HalingstadCameron ChalkMichael P. BrennerArvind MuruganErik WinfreeKrishna Shrinivasahttps://ror.org/03vek6s52School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138bDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL 60208cCenter for Synthetic Biology, Northwestern University, Evanston, IL 60208dNSF-Simons National Institute for Theory and Mathematics in Biology, Chicago, IL 60611ehttps://ror.org/05dxps055Computation and Neural Systems, California Institute of Technology, Pasadena, CA 91125fhttps://ror.org/03vek6s52Department of Physics, Harvard University, Cambridge, MA 02138ghttps://ror.org/024mw5h28Department of Physics, University of Chicago, Chicago, IL 60637</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2527873123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2528109123?af=R">
      <title>Two-step mechanism of Bruton’s tyrosine kinase membrane recruitment and activation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2528109123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceSpecific recruitment of peripheral membrane proteins to the organellar membrane surface is essential for cellular signaling and maintaining organellar health. Often, these recruitments are guided by low-affinity, transient interactions with ...</description>
      <dc:title>Two-step mechanism of Bruton’s tyrosine kinase membrane recruitment and activation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2528109123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Rachel A. McAllisterAmy L. StieglerKeerthana ChariMeera ChariMoitrayee BhattacharyyaKallol Guptaahttps://ror.org/03v76x132Nanobiology Institute, Yale University, West Haven, CT 06516bhttps://ror.org/03v76x132Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510chttps://ror.org/03v76x132Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510dhttps://ror.org/03v76x132Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2528109123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2528109123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2529234123?af=R">
      <title>Thick filament molecular interfaces play a critical role in the pathogenesis of hypertrophic cardiomyopathy</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2529234123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceHeart contraction results from the interaction of thick and thin protein filaments. Pathogenic variants in thick filament proteins produce hypertrophic cardiomyopathy that impairs the heartbeat, but the underlying mechanisms are unclear. Here, ...</description>
      <dc:title>Thick filament molecular interfaces play a critical role in the pathogenesis of hypertrophic cardiomyopathy</dc:title>
      <dc:identifier>doi:10.1073/pnas.2529234123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Debabrata DuttaYuri KimCarolyn Y. HoJonathan G. SeidmanChristine E. SeidmanRoger CraigRaúl Padrónahttps://ror.org/0464eyp60Division of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Chan Medical School, Worcester, MA 01655bhttps://ror.org/04b6nzv94Cardiovascular Division, Brigham and Women’s Hospital, Boston, MA 02115cDepartment of Genetics, Harvard Medical School, Boston, MA 02115</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2529234123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2529234123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535076123?af=R">
      <title>The emergence of novel versus known three-dimensional structures from random sequences</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535076123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceThe availability of powerful and accurate programs for predicting protein three-dimensional structures enables one to ask fundamental questions concerning the origin of folded functional proteins during evolution. We show that 120-residue ...</description>
      <dc:title>The emergence of novel versus known three-dimensional structures from random sequences</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535076123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Rose YangHyunjun YangAnton DavydenkoZack MawaldiRian KormosDru MyerscoughYibing WuWilliam F. DeGradoahttps://ror.org/043mz5j54Department of Pharmaceutical Chemistry, Cardiovascular Research Institute, University of California San Francisco, San Francisco, CA 94158bhttps://ror.org/05abbep66Department of Biochemistry, Brandeis University, Waltham, MA 02453chttps://ror.org/01dq60k83Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai, Miyagi 980-8577, Japan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535076123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535076123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535494123?af=R">
      <title>Beyond native sequence recovery: Improved modeling of the sequence-energy landscape of protein structures</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535494123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceMachine learning has revolutionized the design of novel proteins by facilitating the generation of protein sequences that adopt desired structures. State-of-the-art sequence design models optimize the similarity of designed sequences to native ...</description>
      <dc:title>Beyond native sequence recovery: Improved modeling of the sequence-energy landscape of protein structures</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535494123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-02T07:00:00Z</dc:date>
      <dc:creator>Foster BirnbaumAmy E. Keatingahttps://ror.org/042nb2s44Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/042nb2s44Computational and Systems Biology, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/042nb2s44Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535494123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535494123?af=R</prism:url>
      <prism:copyright/>
   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2535920123?af=R">
      <title>Antimicrobial peptoids pass rapidly through bacterial membranes and flocculate ribosomes and DNA: A single-cell fluorescence study</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2535920123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceThis study demonstrates that natural human host defense peptides such as LL-37, known to display remarkable broad-spectrum antibacterial effects and to bind to and rigidify nucleic acids, can be mimicked by simpler “peptoid” analogues (...</description>
      <dc:title>Antimicrobial peptoids pass rapidly through bacterial membranes and flocculate ribosomes and DNA: A single-cell fluorescence study</dc:title>
      <dc:identifier>doi:10.1073/pnas.2535920123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Yanyu ZhuJosefine Eilsø NielsenNatalia MolchanovaMainak MustafiClaudine HerlanBettina FleckStefan BräseUte SchepersKristian SørensenClaudia ZielkeJennifer S. LinJames C. WeisshaarHåvard JenssenAnnelise E. Barronahttps://ror.org/01y2jtd41Department of Chemistry, University of Wisconsin–Madison, Madison, WI 53706bhttps://ror.org/00f54p054Department of Bioengineering, Schools of Medicine and of Engineering, Stanford University, Stanford, CA 94305chttps://ror.org/014axpa37Department of Science and Environment, Roskilde University, Roskilde 4000, Denmarkdhttps://ror.org/02jbv0t02The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720ehttps://ror.org/04t3en479Institute of Biological and Chemical Systems–Functional Molecular Systems, Karlsruhe Institute of Technology, Karlsruhe 76131, Germanyfhttps://ror.org/04t3en479Institute of Functional Interfaces, Karlsruhe Institute of Technology, Karlsruhe 76131, Germany</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2535920123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2535920123?af=R</prism:url>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536595123?af=R">
      <title>Dual salt bridges govern proton gating and calcium leak in BsYetJ across bilayers and live cells</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536595123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceCells tightly regulate calcium because it controls processes ranging from signaling to survival. We show that the membrane proteinBsYetJ uses two distinct electrostatic gates to couple proton sensing to calcium leak: One gate controls channel ...</description>
      <dc:title>Dual salt bridges govern proton gating and calcium leak in BsYetJ across bilayers and live cells</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536595123</dc:identifier>
      <dc:source/>
      <dc:date>2026-07-01T07:00:00Z</dc:date>
      <dc:creator>Chu-Chun ChengChieh-Chin LiYun-Shan WangChun-Wei LinYun-Wei Chiangahttps://ror.org/00zdnkx70Department of Chemistry, National Tsing Hua University, Hsinchu 300-044, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536595123</prism:doi>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2536746123?af=R">
      <title>Corkscrew motion of Trypanosoma brucei is driven by helical beating of the flagellum and facilitated by its bent shape</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2536746123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceTrypanosoma bruceiis a single-cell parasite causing sleeping sickness across 37 sub-Saharan countries, threatening ~60 million people. Revealing its locomotion mechanism is critical to understand its lifecycle in fly vectors and mammalian ...</description>
      <dc:title>Corkscrew motion of Trypanosoma brucei is driven by helical beating of the flagellum and facilitated by its bent shape</dc:title>
      <dc:identifier>doi:10.1073/pnas.2536746123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-30T07:00:00Z</dc:date>
      <dc:creator>Sizhe ChengDevadyouti DasMykhaylo BarchukRaveen ArmstrongMichele M. KlingbeilBecca ThomasesShuang Zhouahttps://ror.org/0072zz521Department of Physics, University of Massachusetts, Amherst, MA 01003bhttps://ror.org/0072zz521Department of Microbiology, University of Massachusetts, Amherst, MA 01003chttps://ror.org/0497crr92Department of Mathematical Sciences, Smith College, Northampton, MA 01063</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2536746123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2536746123?af=R</prism:url>
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   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2537345123?af=R">
      <title>BetaDescribe: Providing rich descriptions from protein sequences</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2537345123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceDetermining protein function remains a major bottleneck in biology, particularly for proteins lacking close homologs with known annotations. This work introduces BetaDescribe, a protein-to-text modeling framework that generates rich, human-...</description>
      <dc:title>BetaDescribe: Providing rich descriptions from protein sequences</dc:title>
      <dc:identifier>doi:10.1073/pnas.2537345123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Edo DotanIris LyubmanMarcelo EhrlichEran BacharachTal PupkoYonatan BelinkovaThe Henry and Marilyn Taub Faculty of Computer Science, Technion–Israel Institute of Technology, Haifa 3200003, Israelbhttps://ror.org/04mhzgx49The Shmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israelchttps://ror.org/03vek6s52Kempner Institute, Harvard University, Cambridge, MA 02134</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2537345123</prism:doi>
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   </item>
   <item rdf:about="https://www.pnas.org/doi/abs/10.1073/pnas.2601775123?af=R">
      <title>Dynamic positioning of Rpc34 winged helix in RNA polymerase III elongation complex for its stability with implications for reinitiation</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2601775123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceRNA Polymerase III (Pol III) is essential for rapid production of structural RNAs, yet how its mobile components coordinate this high-speed machinery remains unclear. Using a chemical biology strategy for site-specific labeling of large ...</description>
      <dc:title>Dynamic positioning of Rpc34 winged helix in RNA polymerase III elongation complex for its stability with implications for reinitiation</dc:title>
      <dc:identifier>doi:10.1073/pnas.2601775123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Jheng-Syong WuYu-Chun LinYi-Yu WeiHsin-Hung LinYang-Chih LiuJen-Wei ChangI-Ping TuHung-Ta ChenWei-Hau Changahttps://ror.org/04xjjma71Institute of Chemistry, Academia Sinica, Taipei 115, Taiwanbhttps://ror.org/047sbcx71Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwanchttps://ror.org/044gv5910Institute of Statistical Science, Academia Sinica, Taipei 115, TaiwandGenomic Research Center, Academia Sinica, Taipei 115, Taiwanehttps://ror.org/01tpvdq80Institute of Physics, Academia Sinica, Taipei 115, Taiwan</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2601775123</prism:doi>
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      <title>The mechanism for ligand activation of the Smoothened G protein–coupled receptor</title>
      <link>https://www.pnas.org/doi/abs/10.1073/pnas.2604658123?af=R</link>
      <description>Proceedings of the National Academy of Sciences, Volume 123, Issue 27, July 2026. &lt;br/&gt;SignificanceThe Hedgehog (Hh) signaling pathway plays a critical role in development and is frequently dysregulated in cancers such as basal cell carcinoma. However, the activation mechanism of a key component of this pathway, Smoothened (SMO), remains ...</description>
      <dc:title>The mechanism for ligand activation of the Smoothened G protein–coupled receptor</dc:title>
      <dc:identifier>doi:10.1073/pnas.2604658123</dc:identifier>
      <dc:source/>
      <dc:date>2026-06-29T07:00:00Z</dc:date>
      <dc:creator>Ryan D. YuAmy-Doan P. VoSoo-Kyung KimWilliam A. Goddardahttps://ror.org/05dxps055Materials and Process Simulation Center, Division of Chemistry &amp; Chemical Engineering, California Institute of Technology, Pasadena, CA 91125</dc:creator>
      <prism:publicationName>Proceedings of the National Academy of Sciences</prism:publicationName>
      <prism:volume>123</prism:volume>
      <prism:number>27</prism:number>
      <prism:coverDate>2026-07-07T07:00:00Z</prism:coverDate>
      <prism:coverDisplayDate>2026-07-07T07:00:00Z</prism:coverDisplayDate>
      <prism:doi>10.1073/pnas.2604658123</prism:doi>
      <prism:url>https://www.pnas.org/doi/abs/10.1073/pnas.2604658123?af=R</prism:url>
      <prism:copyright/>
   </item>
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