Biological Sciences / Biophysics and Computational Biology -- New results matching your topic search. https://www.pnas.org/action/doSearch?af=R Proceedings of the National Academy of Sciences: Biophysics and Computational Biology Proceedings of the National Academy of Sciences en-US http://www.atypon.com/images/atypon_logo_small.gif http://www.atypon.com https://www.pnas.org/doi/abs/10.1073/pnas.2613826123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 39, September 2026. <br/>SignificanceA central question in materials science is whether permanent deformation under repeated or intense loading requires breaking the polymer backbone. Many biological materials can undergo permanent shape change while maintaining long-term ... Sliding-before-breaking governs deformation in chitinous extracellular matrices reinforced by strong, fatigue-resistant chitin doi:10.1073/pnas.2613826123 2026-09-23T07:00:00Z Zhangmin WanChris ZhouMaëva PerezJian-Wen QiuZihui ShenXin LuJie WuShuyuan CuiYan YuXun NiuRan BiJeremy C. SmithSimcha SrebnikOrlando J. Rojasahttps://ror.org/03rmrcq20Bioproducts Institute, The University of British Columbia, Vancouver, BC V6T 1Z4, Canadabhttps://ror.org/03rmrcq20Department of Chemical and Biological Engineering, The University of British Columbia, Vancouver, BC V6T 1Z3, Canadachttps://ror.org/0145fw131Department of Biology, Hong Kong Baptist University, Hong Kong SAR 999077, ChinadUniversity of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, Oak Ridge National Laboratory, Oak Ridge, TN 37831ehttps://ror.org/01qz5mb56Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831fhttps://ror.org/00pwgnh47Department of Colloid Chemistry, Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, Potsdam 14476, Germanyghttps://ror.org/03rmrcq20Department of Wood Science, The University of British Columbia, Vancouver, BC V6T 1Z4, Canadahhttps://ror.org/03rmrcq20Department of Chemistry, The University of British Columbia, Vancouver, BC V6T 1Z1, Canada Proceedings of the National Academy of Sciences 123 39 2026-09-29T07:00:00Z 2026-09-29T07:00:00Z 10.1073/pnas.2613826123 https://www.pnas.org/doi/abs/10.1073/pnas.2613826123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2616367123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 39, September 2026. <br/>SignificanceDeveloping drugs that selectively target closely related ion channel isoforms remains a major challenge because these proteins often share highly conserved drug-binding sites. Here, we show that selective activation of Kv7 potassium channel ... Voltage-sensor conformational microenvironments encode isoform-selective ion channel activation doi:10.1073/pnas.2616367123 2026-09-23T07:00:00Z Rían W. ManvilleLorenzo FogliaRyan F. YoshimuraDaniel E. SantosAlvin YuGeoffrey W. Abbottahttps://ror.org/04gyf1771Bioelectricity Laboratory, Department of Physiology and Biophysics, School of Medicine, University of California, Irvine, CA 92697bhttps://ror.org/04gyf1771Yu Lab, Department of Physiology and Biophysics, School of Medicine, University of California, Irvine, CA 92697 Proceedings of the National Academy of Sciences 123 39 2026-09-29T07:00:00Z 2026-09-29T07:00:00Z 10.1073/pnas.2616367123 https://www.pnas.org/doi/abs/10.1073/pnas.2616367123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2631666123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 39, September 2026. <br/> Correction for Lobo et al., amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome doi:10.1073/pnas.2631666123 2026-09-21T07:00:00Z Proceedings of the National Academy of Sciences 123 39 2026-09-29T07:00:00Z 2026-09-29T07:00:00Z 10.1073/pnas.2631666123 https://www.pnas.org/doi/abs/10.1073/pnas.2631666123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2534924123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. <br/>SignificanceTaste receptor type 1 (TAS1R) proteins, including sweet and umami receptors in humans, recognize nutrients such as sugars and amino acids. To detect diverse chemicals using a limited repertoire of receptors, many TAS1Rs exhibit broad substrate ... Identification and structural characterization of stereochemical promiscuity in a taste receptor doi:10.1073/pnas.2534924123 2026-09-15T07:00:00Z Rakuto MizoguchiYasuka TodaMana NagaeTakashi YoshidaHiroaki MatsuuraKunio HirataVi Toan LamDuy Phuoc TranAkio KitaoYohei MiyanoiriMaiko HosotaniYuji AshikawaChiaki ItoNaotaka TsutsumiNorihisa YasuiYoshiro IshimaruAtsuko Yamashitaahttps://ror.org/02pc6pc55Division of Pharmaceutical Sciences, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japanbhttps://ror.org/02rqvrp93Department of Agricultural Chemistry, School of Agriculture, Meiji University, Kawasaki 214-8571, Japanchttps://ror.org/05dqf9946School of Life Science and Technology, Institute of Science Tokyo, Yokohama 226-8501, Japandhttps://ror.org/035t8zc32Division of Integrative Protein Science, Institute for Protein Research, The University of Osaka, Suita 565-0871, JapaneRIKEN SPring-8 Center, Sayo 679-5148, Japanfhttps://ror.org/05dqf9946School of Life Science and Technology, Institute of Science Tokyo, Meguro, Tokyo 152-8550, Japan Proceedings of the National Academy of Sciences 123 38 2026-09-22T07:00:00Z 2026-09-22T07:00:00Z 10.1073/pnas.2534924123 https://www.pnas.org/doi/abs/10.1073/pnas.2534924123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2612191123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. <br/>SignificanceAllosteric regulation enables proteins to transmit signals over long distances, but the mechanisms linking local ligand binding to global conformational changes remain difficult to resolve. Here, we combine NMR-based chemical shift covariance ... Integrating NMR and contact-response analysis reveals the allosteric network driving domain closure in Enzyme I doi:10.1073/pnas.2612191123 2026-09-16T07:00:00Z Aayushi SinghDaniel BurnsSergey L. SedinkinSayan DasDavit A. PotoyanVincenzo Vendittiahttps://ror.org/04rswrd78Department of Chemistry, Iowa State University, Ames, IA 50011bhttps://ror.org/04rswrd78Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011 Proceedings of the National Academy of Sciences 123 38 2026-09-22T07:00:00Z 2026-09-22T07:00:00Z 10.1073/pnas.2612191123 https://www.pnas.org/doi/abs/10.1073/pnas.2612191123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2613741123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. <br/>SignificanceCurrently, there exists a huge gap between the number of available viral coat protein (CP) sequences and the experimentally determined capsid structures. Moreover, there are no resources available that provide full capsid models. By leveraging ... FoldaVirus, a knowledge-based icosahedral capsid prediction tool using AlphaFold doi:10.1073/pnas.2613741123 2026-09-17T07:00:00Z Oscar Rojas LabraDavid S. Montoya-MunozNelly Santoyo-RiveraJeffrey McDonaldDaniel Montiel-GarciaDavid A. CaseVijay S. Reddyahttps://ror.org/017zqws13The Hormel Institute, University of Minnesota, Austin, MN 55912bhttps://ror.org/01da06998Department of Computer Systems and Information Technologies, Tecnologico Nacional de Mexico and Instituto Tecnológico Superior de Irapuato, Irapuato, Guanajuato C.P. 36821, Mexicochttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037dhttps://ror.org/05vt9qd57Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, NJ 08854 Proceedings of the National Academy of Sciences 123 38 2026-09-22T07:00:00Z 2026-09-22T07:00:00Z 10.1073/pnas.2613741123 https://www.pnas.org/doi/abs/10.1073/pnas.2613741123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2616547123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. <br/>SignificanceUnderstanding enzyme mechanisms requires precise knowledge of active-site protonation states—features largely inaccessible to conventional structural biology. Here, we introduce an accelerated NMR crystallography workflow that makes practical ... NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam doi:10.1073/pnas.2616547123 2026-09-15T07:00:00Z Christopher G. WilliamsSonglin WangVeronica CartaPatricia S. LanganAlexander F. ThomeSebastian A. RamosJacob B. HolmesRittik K. GhoshKevin L. WeissGregory J. O. BeranJoshua D. HartmanLeighton CoatesChad M. RienstraLeonard J. MuelleraDepartment of Chemistry, University of California-Riverside, Riverside, CA 92521bhttps://ror.org/01y2jtd41Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706chttps://ror.org/01y2jtd41National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, Madison, WI 53706dhttps://ror.org/01qz5mb56Oak Ridge National Laboratory, Neutron Scattering Science Division, Oak Ridge, TN 37831 Proceedings of the National Academy of Sciences 123 38 2026-09-22T07:00:00Z 2026-09-22T07:00:00Z 10.1073/pnas.2616547123 https://www.pnas.org/doi/abs/10.1073/pnas.2616547123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2622980123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 38, September 2026. <br/>SignificanceRNA base-pairing enables folding and regulation, but it also creates pervasive opportunities for unintended RNA–RNA interactions in the crowded intracellular environment. We identify this as a transcriptome-scale physical problem. Simulations ... Maintaining transcriptome solubility constrains mRNA sequence composition doi:10.1073/pnas.2622980123 2026-09-14T07:00:00Z Marco TodiscoChristalyn AuslerAnkur Jainahttps://ror.org/04vqm6w82Whitehead Institute for Biomedical Research, Cambridge, MA 02142bhttps://ror.org/042nb2s44Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139 Proceedings of the National Academy of Sciences 123 38 2026-09-22T07:00:00Z 2026-09-22T07:00:00Z 10.1073/pnas.2622980123 https://www.pnas.org/doi/abs/10.1073/pnas.2622980123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2521821123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceForce generation by actin filaments is a fundamental property of Eukaryotic cells. These filaments can generate pushing forces via polymerization, pulling forces via the action of molecular motor proteins, and can generate filament sliding ... Myosin II–independent contraction of actin filaments in membrane nanotubes doi:10.1073/pnas.2521821123 2026-09-08T07:00:00Z Md Arsalan AshrafTapas SinghaSusav PradhanSerene Rose DavidPierre SensPramod Pullarkatahttps://ror.org/01qdav448Raman Research Institute, Bengaluru 560080, Indiabhttps://ror.org/04t0gwh46Institut Curie, Paris Science and Letters Research University, CNRS UMR 168, Paris F-75005, France Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2521821123 https://www.pnas.org/doi/abs/10.1073/pnas.2521821123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2532976123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceThe spatial interplay between tumor and immune cells in the tumor microenvironment is a critical yet poorly understood determinant of cancer progression and treatment response. This study bridges a key gap in cancer systems biology by ... Integrating tumor–immune mechanistic modeling with transcriptomics reveals pattern-driven prognostic biomarkers in tumors doi:10.1073/pnas.2532976123 2026-09-10T07:00:00Z Ke QiSuoqin JinHan MaTengfei WangYijun LouQing NieXiufen Zouahttps://ror.org/033vjfk17School of Mathematics and Statistics, Wuhan University, Wuhan 430072, Chinabhttps://ror.org/0030zas98Department of Applied Mathematics, Hong Kong Polytechnic University, Hong Kong 999077, Chinachttps://ror.org/04gyf1771National Science Foundation–Simons Center for Multiscale Cell Fate Research, University of California, Irvine, CA 92697dhttps://ror.org/04gyf1771Department of Developmental and Cell Biology, University of California, Irvine, CA 92697ehttps://ror.org/04gyf1771Department of Mathematics, University of California, Irvine, CA 92697 Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2532976123 https://www.pnas.org/doi/abs/10.1073/pnas.2532976123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2536532123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceIt is surprising that transthyretin (TTR) has an aggregation pathway leading to organ system deterioration in humans, because it denatures very slowly in circulation at physiological pH, and denaturation is required for aggregation. A ... Transthyretin can denature by an alternative pathway doi:10.1073/pnas.2536532123 2026-09-08T07:00:00Z Marcus JägerJan-Hannes SchäferGabriel C. LanderEvan T. PowersMartin GruebeleJeffery W. Kellyahttps://ror.org/02dxx6824Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037bhttps://ror.org/02dxx6824Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037chttps://ror.org/047426m28Department of Chemistry, University of Illinois Urbana-Champaign, Champaign, IL 61801dhttps://ror.org/047426m28Department of Physics, University of Illinois Urbana-Champaign, Champaign, IL 61801ehttps://ror.org/047426m28Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Champaign, IL 61801fhttps://ror.org/047426m28Carle-Illinois College of Medicine, University of Illinois Urbana-Champaign, Champaign, IL 61801 Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2536532123 https://www.pnas.org/doi/abs/10.1073/pnas.2536532123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2605103123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificancePotassium channels regulate electrical signaling by transporting K+across cell membranes. This activity is controlled by multiple gates, yet how these gates interact remains not entirely understood. We identify a conserved gating crosstalk ... Gating crosstalk in potassium channels doi:10.1073/pnas.2605103123 2026-09-09T07:00:00Z Lyubin HuBert L. de GrootRuo-Xu Guahttps://ror.org/0220qvk04Department of Bioinformatics and Biostatistics, College of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, Chinabhttps://ror.org/03av75f26Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2605103123 https://www.pnas.org/doi/abs/10.1073/pnas.2605103123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2607937123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceUnderstanding the molecular basis of protein aggregation disorders is essential to developing treatments. One such disease is corneal dystrophy, genetically and pathologically associated with transforming growth factor β–induced protein (... Cryo-EM structure of TGFBIp fibrils driven by a corneal dystrophy–linked mutation enables design of peptide inhibitors of aggregation doi:10.1073/pnas.2607937123 2026-09-08T07:00:00Z Yi Xiao JiangLukasz SalwinskiMichael R. SawayaPeng GeLiisa LutterXinyi ChengCarolyn J. HuHillary HernandezDavid R. BoyerConrad WangFilipe A. MeloDuilio CascioDavid S. Eisenbergahttps://ror.org/046rm7j60Department of Biological Chemistry, University of California, Los Angeles, CA 90095bhttps://ror.org/046rm7j60Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095chttps://ror.org/046rm7j60Department of Energy Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095dhttps://ror.org/046rm7j60Molecular Biology Institute, University of California, Los Angeles, CA 90095ehttps://ror.org/046rm7j60Institute for Quantitative and Computational Biosciences, University of California, Los Angeles, CA 90095 Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2607937123 https://www.pnas.org/doi/abs/10.1073/pnas.2607937123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2612002123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceBuilding quantitative models that connect genome structure to chromatin dynamics is essential for predicting chromosome motion and genome function in living cells. Using genome-wide live-cell imaging and Hi-C data-constrained polymer modeling ... Integrative modeling of the genome structure and dynamics in fission yeast doi:10.1073/pnas.2612002123 2026-09-08T07:00:00Z Soya ShinkaiToshinori NambaTakeshi SugawaraSoya HagiwaraShuichi OnamiTokuko HaraguchiYasushi HiraokaAkinori AwazuMasaru UenoShin-ichi TateaLaboratory for Developmental Dynamics, Center for Biosystems Dynamics Research, RIKEN, Kobe 650-0047, Japanbhttps://ror.org/03t78wx29Research Center for the Mathematics on Chromatin Live Dynamics, Hiroshima University, Higashi-Hiroshima 739-8530, Japanchttps://ror.org/035t8zc32Graduate School of Frontier Biosciences, University of Osaka, Suita 565-0871, Japandhttps://ror.org/03t78wx29Graduate School of Integrated Sciences for Life, Hiroshima University, Higashi-Hiroshima 739-8530, Japanehttps://ror.org/03t78wx29International Institute for Sustainability with Knotted Chiral Meta Matter, Hiroshima University, Higashi-Hiroshima 739-0046, Japan Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2612002123 https://www.pnas.org/doi/abs/10.1073/pnas.2612002123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2612170123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceCentrioles are fundamental for cell division, cilia formation, and human health, yet the molecular principles governing their earliest assembly remain incompletely understood. By resolving the native architecture of the cartwheel in situ from ... The native structure of the Trichonympha centriole cartwheel reveals a zigzag stacking pattern doi:10.1073/pnas.2612170123 2026-09-08T07:00:00Z Carlee M. RowsellShintaroh KuboAsuva ArinThibault LegalMolly Yining YuKhanh Huy Buiahttps://ror.org/01pxwe438Department of Biochemistry, McGill University, Montreal, QC H3G 0B1, Canadabhttps://ror.org/057zh3y96Department of Applied Chemistry, Graduate School of Engineering, the University of Tokyo, Tokyo 113-0033, Japanchttps://ror.org/01pxwe438Department of Anatomy and Cell Biology, McGill University, Montreal, QC H3A 0C7, Canadadhttps://ror.org/01pxwe438Centre for Structural Biology Research, McGill University, Montreal, QC H3G 0B1, Canada Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2612170123 https://www.pnas.org/doi/abs/10.1073/pnas.2612170123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2614238123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 37, September 2026. <br/>SignificanceLiving cells maintain their functions through complex networks of chemical reactions. Despite their diversity, metabolic networks share a scale-free structure across species, with highly heterogeneous connectivity. However, how this ... Starvation suppression in dense scale-free metabolic networks: Dynamical mean-field analysis of catalytic reaction networks doi:10.1073/pnas.2614238123 2026-09-10T07:00:00Z Kota MitsumotoShuji Ishiharaahttps://ror.org/057zh3y96Department of Basic Science, Graduate School of Arts and Sciences, The University of Tokyo, Meguro-ku, Tokyo 153-8902, Japanbhttps://ror.org/057zh3y96Research Center for Complex Systems Biology, Universal Biology Institute, The University of Tokyo, Meguro-ku, Tokyo 153-8902, Japan Proceedings of the National Academy of Sciences 123 37 2026-09-15T07:00:00Z 2026-09-15T07:00:00Z 10.1073/pnas.2614238123 https://www.pnas.org/doi/abs/10.1073/pnas.2614238123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2605178123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 36, September 2026. <br/>SignificanceCircular permutation—a phenomenon where proteins fold into a similar 3D shape, yet differ in their termini positioning—presents a fascinating evolutionary puzzle. However, identifying such relationships has remained challenging due to search ... Systematic discovery of circular permutations across the protein universe using CIRPIN doi:10.1073/pnas.2605178123 2026-09-04T07:00:00Z Aiden R. KolodziejS. Mazdak AbulnagaSergey Ovchinnikovahttps://ror.org/042nb2s44Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139bhttps://ror.org/042nb2s44Computer Science and Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139chttps://ror.org/002pd6e78Department of Radiology, Massachusetts General Hospital, Boston, MA 02115dHarvard Medical School, Boston, MA 02115 Proceedings of the National Academy of Sciences 123 36 2026-09-08T07:00:00Z 2026-09-08T07:00:00Z 10.1073/pnas.2605178123 https://www.pnas.org/doi/abs/10.1073/pnas.2605178123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2605886123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 36, September 2026. <br/>SignificanceHyponatremia is a major clinical problem with limited therapeutic options. The kidney chloride channel CLC-Ka is an attractive drug target, but its high sequence identity to CLC-Kb has hindered the development of isoform-selective inhibitors ... Mechanism of gating and isoform-specific inhibition in renal CLC chloride channels doi:10.1073/pnas.2605886123 2026-09-01T07:00:00Z Chih-Ta ChienBriana L. Sobecks-DohertyAlexander S. PowersAnindita DasJürgen KreiterChloe N. BarryMuyuan ChenAndrew HinmanCamille F. PetrakianBrianna WilliamsChase A. P. WoodMengyuan XuRon O. DrorWah ChiuMerritt Madukeahttps://ror.org/00f54p054Department of Bioengineering, Stanford University, Stanford, CA 94305bhttps://ror.org/00f54p054Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305chttps://ror.org/00f54p054Department of Chemical Engineering, Stanford University, Stanford, CA 94305dhttps://ror.org/00f54p054Department of Computer Science, Stanford University, Stanford, CA 94305ehttps://ror.org/00f54p054Department of Structural Biology, Stanford University, Stanford, CA 94305fhttps://ror.org/00f54p054Institute for Computational and Mathematical Engineering, Stanford University, Stanford, CA 94305ghttps://ror.org/00f54p054Department of Chemistry, Stanford University, Stanford, CA 94305hhttps://ror.org/00f54p054Innovative Medicines Accelerator, Stanford University, Stanford, CA 94305ihttps://ror.org/00f54p054Division of Cryogenic Electron Microscopy and Bioimaging, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA 94025jhttps://ror.org/00f54p054Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305 Proceedings of the National Academy of Sciences 123 36 2026-09-08T07:00:00Z 2026-09-08T07:00:00Z 10.1073/pnas.2605886123 https://www.pnas.org/doi/abs/10.1073/pnas.2605886123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2613565123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 36, September 2026. <br/>SignificanceFish often swim through fast, chaotic currents that are difficult and costly to resist. Instead of battling these flows head-on, we found that fish use a simple strategy: they slightly turn their bodies relative to the flow. This subtle change ... Fish navigate a hydrodynamic maze via yaw-mediated lateral migration doi:10.1073/pnas.2613565123 2026-09-03T07:00:00Z Michael A. CalicchiaRui Niahttps://ror.org/00za53h95Department of Mechanical Engineering, The Johns Hopkins University, Baltimore, MD 21218 Proceedings of the National Academy of Sciences 123 36 2026-09-08T07:00:00Z 2026-09-08T07:00:00Z 10.1073/pnas.2613565123 https://www.pnas.org/doi/abs/10.1073/pnas.2613565123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2618242123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 36, September 2026. <br/>SignificancePhotosynthesis and cellular respiration are key processes that power metabolism of living cells. Understanding the molecular mechanisms underlying their efficiency remains a major challenge with broad implications for biology, bioenergetics, ... Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bc1 doi:10.1073/pnas.2618242123 2026-09-01T07:00:00Z Rafał PietrasAnna Wójcik-AugustynBohun MieleckiMarcin SarewiczMarcin JaciukŁukasz KoziejSebastian GlattArtur Osyczkaahttps://ror.org/03bqmcz70Faculty of Biochemistry, Biophysics and Biotechnology, Department of Molecular Biophysics, Jagiellonian University, Kraków 30-387, Polandbhttps://ror.org/03bqmcz70Małopolska Centre of Biotechnology, Jagiellonian University, Kraków 30-387, Polandchttps://ror.org/03bqmcz70National Synchrotron Radiation Centre SOLARIS, Jagiellonian University, Kraków 30-392, Polanddhttps://ror.org/01w6qp003Department for Biological Sciences and Pathobiology, University of Veterinary Medicine Vienna, Vienna 1210, Austria Proceedings of the National Academy of Sciences 123 36 2026-09-08T07:00:00Z 2026-09-08T07:00:00Z 10.1073/pnas.2618242123 https://www.pnas.org/doi/abs/10.1073/pnas.2618242123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2526705123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 35, September 2026. <br/> Myelination sustains axonal bioenergetics by storing and consuming oxygen for aerobic metabolism doi:10.1073/pnas.2526705123 2026-08-24T07:00:00Z Isabella PanfoliGiovanni CandianoMaurizio Bruschiahttps://ror.org/0107c5v14Department of Pharmacy, University of Genoa, Genoa 16132, Italybhttps://ror.org/0424g0k78Unit of Nephrology, Dialysis and Transplantation, Laboratory of Molecular Nephrology, Istituto Giannina Gaslini, Scientific Institute for Research, Hospitalization and Healthcare, Genoa 16147, Italychttps://ror.org/0107c5v14Department of Experimental Medicine, University of Genoa, Genoa 16132, Italy Proceedings of the National Academy of Sciences 123 35 2026-09-01T07:00:00Z 2026-09-01T07:00:00Z 10.1073/pnas.2526705123 https://www.pnas.org/doi/abs/10.1073/pnas.2526705123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2531078123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 35, September 2026. <br/>SignificanceCell competition is relevant for a range of biological processes, from the elimination of malignant cells in tissues to cancer progression. It can arise through various mechanisms, including signaling pathways or ecological competition for ... Cell competition driven by secreted ligands: Modeling liver metastasis of colorectal cancer doi:10.1073/pnas.2531078123 2026-08-27T07:00:00Z Hossein NematiSaskia Jacoba Elisabeth SuijkerbuijkJoost de Graafahttps://ror.org/04pp8hn57Institute for Theoretical Physics, Department of Physics, Faculty of Science, Utrecht University, Princetonplein 5, Utrecht 3584 CC, The Netherlandsbhttps://ror.org/04pp8hn57Division of Developmental Biology, Institute of Biodynamics and Biocomplexity, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, Utrecht 3584 CH, The Netherlands Proceedings of the National Academy of Sciences 123 35 2026-09-01T07:00:00Z 2026-09-01T07:00:00Z 10.1073/pnas.2531078123 https://www.pnas.org/doi/abs/10.1073/pnas.2531078123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2604869123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 35, September 2026. <br/> Reply to Panfoli et al.: From O2 consumption in myelin to gap junctional ATP delivery in axons: An energy link needing further scrutiny doi:10.1073/pnas.2604869123 2026-08-24T07:00:00Z Katja WitschasAn GhyselsLuc Leybaertahttps://ror.org/033003e23Biophysics of the Eye - Research Group, Faculty of Medicine and Health Technology, Tampere University, Tampere 3433520, Finlandbhttps://ror.org/00cv9y106Institute of Biomedical Engineering, Biophysical Models for Medical Applications Group, Ghent University, Ghent 9000, Belgiumchttps://ror.org/00cv9y106Department of Fundamental and Applied Medical Sciences, Ghent University, Ghent 9000, Belgium Proceedings of the National Academy of Sciences 123 35 2026-09-01T07:00:00Z 2026-09-01T07:00:00Z 10.1073/pnas.2604869123 https://www.pnas.org/doi/abs/10.1073/pnas.2604869123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2618972123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 35, September 2026. <br/>SignificanceThe motility of kinesin-14 depends strongly on the ionic strength. Finding the origin of this effect is important for understanding intracellular transportation. The present work uses microscopic simulations to elucidate the origin of the ... On the origin of the ionic strength control of the motility of kinesin-14 doi:10.1073/pnas.2618972123 2026-08-25T07:00:00Z Ritaban HalderArieh Warshelahttps://ror.org/03taz7m60Department of Chemistry, University of Southern California, Los Angeles, CA 90089-1062 Proceedings of the National Academy of Sciences 123 35 2026-09-01T07:00:00Z 2026-09-01T07:00:00Z 10.1073/pnas.2618972123 https://www.pnas.org/doi/abs/10.1073/pnas.2618972123?af=R