Biophysical reviews最新文献

{"title":"Roger Cooke: Physicist to biophysicist (1940-2024).","authors":"Cristobal Dos Remedios","doi":"10.1007/s12551-026-01431-0","DOIUrl":"https://doi.org/10.1007/s12551-026-01431-0","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"577-580"},"PeriodicalIF":5.0,"publicationDate":"2026-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486415/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788056","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Professor Roger Cooke's vision for skeletal muscle's super relaxed state: a conceptual paradigm shift for naturally managing metabolic diseases including obesity.","authors":"Clyde Wilson","doi":"10.1007/s12551-026-01442-x","DOIUrl":"https://doi.org/10.1007/s12551-026-01442-x","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"581-594"},"PeriodicalIF":5.0,"publicationDate":"2026-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486450/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>Biophysical</i> <i>R</i> <i>eviews</i>: a call for nominations to the 2027 Michèle Auger Award.","authors":"Wilma K Olson","doi":"10.1007/s12551-026-01447-6","DOIUrl":"https://doi.org/10.1007/s12551-026-01447-6","url":null,"abstract":"<p><p>This editorial describes an open the call for nominations to the 2027 Michéle Auger Award for Young Scientists' Independent Research-the single award administered by <i>Biophysical Reviews</i>.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"569-570"},"PeriodicalIF":5.0,"publicationDate":"2026-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486430/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788073","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanobiology of the diabetic cardiomyocyte: insulin signaling, titin elasticity, and multiscale mechanical dysfunction.","authors":"Mustafa Kaçmaz, Evelyn Halupka, Innas Sultana, Simin Delalat, Ibrahim El-Battrawy, Muchtiar Khan, Loek van Heerebek, Nazha Hamdani","doi":"10.1007/s12551-026-01444-9","DOIUrl":"https://doi.org/10.1007/s12551-026-01444-9","url":null,"abstract":"<p><p>Cardiomyocyte function emerges from tightly coupled electromechanical processes that span sarcomeric force generation, titin-based elasticity, excitation-contraction coupling, mitochondrial ATP supply, and mechanotransductive adaptation to load. Insulin signaling integrates these processes across molecular, cellular, and organ scales, thereby contributing to cardiomyocyte mechanical homeostasis. In cardiomyocytes, canonical insulin signaling is initiated by insulin receptor (IR) activation, recruitment of IRS-1/IRS-2, and downstream PI3K-Akt signaling. Through Akt-dependent modulation of mTOR, GSK-3β, and FOXO transcription factors, insulin aligns energy availability with mechanical demand while supporting structural integrity of sarcomeres, Z-disc/costameric networks, and intercalated disc architecture. Disruption of insulin signaling and insulin resistance in type 2 diabetes (T2DM) remodel cardiomyocyte mechanics by altering myofilament calcium sensitivity, shifting contractile protein expression, perturbing titin isoform composition and phosphorylation, impairing calcium cycling and β-adrenergic microdomain signaling, and inducing mitochondrial dysfunction with oxidative stress (Fig. 1). These changes manifest as altered force-pCa relations, reduced contractile reserve, prolonged relaxation, increased passive stiffness, and modified viscoelastic behavior, as measured by quantitative biophysical assays (Fig. 2). Here, we synthesize mechanistic pathways linking insulin signaling to cardiac mechanics; summarize evidence for T2DM-induced cardiomyocyte dysfunction across species and disease stages; describe mechanotransduction failure in diabetes involving costameres, integrins/FAK, and stretch-responsive pathways such as YAP/TAZ; and provide an overview of quantitative tools to measure cardiomyocyte mechanics including AFM, TFM, nanoindentation, optical/magnetic tweezers, skinned-cell mechanics, real-time calcium-contractility platforms, engineered heart tissues, and microphysiological heart-on-chip systems. Finally, we discuss therapeutic perspectives with emphasis on interventions that restore mechanical homeostasis through titin phosphorylation, reduction of AGE-driven stiffening, and normalization of oxidative and inflammatory stress, including SGLT2 inhibitors and GLP-1 agonists.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"689-702"},"PeriodicalIF":5.0,"publicationDate":"2026-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486435/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788075","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Roger Cooke (1940-2024): a legacy in muscle biophysics and molecular motors.","authors":"Cristobal Dos Remedios, David D Thomas, Amy Li","doi":"10.1007/s12551-026-01446-7","DOIUrl":"https://doi.org/10.1007/s12551-026-01446-7","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"565-567"},"PeriodicalIF":5.0,"publicationDate":"2026-06-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486437/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Beyond sarcomere genetics: proteomic insights into hypertrophic cardiomyopathy.","authors":"Zachery R Gregorich, Zhan Gao, Kalina J Rossler, J Carter Ralphe, Timothy J Kamp, Ying Ge","doi":"10.1007/s12551-026-01445-8","DOIUrl":"https://doi.org/10.1007/s12551-026-01445-8","url":null,"abstract":"<p><p>Hypertrophic cardiomyopathy (HCM) has long been viewed as the archetypal monogenic disorder caused by pathogenic variants in the genes encoding components of the sarcomere. However, the fact that only one-third of HCM cases are genotype-positive, as well as other factors such as incomplete disease penetrance and marked phenotypic heterogeneity, challenge this reductionist view. Recent advances in mass spectrometry-based proteomics have provided new opportunities to interrogate human HCM myocardium at unprecedented depth and are reshaping our understanding of HCM pathobiology. In this mini-review, we summarize insights from both top-down and bottom-up proteomics studies showing that HCM is characterized by broad molecular remodeling across multiple cellular compartments, including the sarcomere, sarcoplasmic reticulum, cytoskeleton, mitochondria, and nucleus. Together, these studies support a model in which diverse HCM genotypes converge on shared downstream proteomic phenotypes and highlight proteomics as a powerful approach for defining disease mechanisms, modifiers, and therapeutic targets.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"703-714"},"PeriodicalIF":5.0,"publicationDate":"2026-06-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486424/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biomolecular condensates in living systems: from function to disease. What to do next.","authors":"Laura Finzi, Jesús Pérez Gil, Sabrina Leslie, Allison Squires","doi":"10.1007/s12551-026-01439-6","DOIUrl":"https://doi.org/10.1007/s12551-026-01439-6","url":null,"abstract":"<p><p>This is a call for papers for a special issue of Biophysical Reviews devoted to Biomolecular Condensates in Living Systems. Our objective is to have under one volume a selection of articles that can give the wider scientific community a firm insight into current developments in the dynamic and rapidly evolving field of biomolecular condensates.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"255-256"},"PeriodicalIF":5.0,"publicationDate":"2026-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272735/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276049","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Correction to: A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributions.","authors":"Donald J Winzor, Peter R Wills","doi":"10.1007/s12551-026-01415-0","DOIUrl":"10.1007/s12551-026-01415-0","url":null,"abstract":"<p><p>[This corrects the article DOI: 10.1007/s12551-025-01371-1.].</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 2","pages":"563"},"PeriodicalIF":5.0,"publicationDate":"2026-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13272695/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148276062","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"MLCK as a phosphorylation switch: from molecular structure to muscle function.","authors":"Poushali Mitra, Rohit Singh, Prince Tiwari","doi":"10.1007/s12551-026-01440-z","DOIUrl":"https://doi.org/10.1007/s12551-026-01440-z","url":null,"abstract":"<p><p>Myosin light chain kinase (MLCK) serves as a central, phosphorylation-dependent molecular switch that governs myosin activation and muscle contractility. Upon binding Ca²⁺/calmodulin, it phosphorylates the regulatory light chain (RLC) of myosin, inducing conformational transitions that shift myosin from an inhibited, folded state to an extended, force-generating configuration. MLCK is a ubiquitous kinase that phosphorylates both striated and non-striated myosin, albeit through distinct regulatory mechanisms. While the structural transition from inhibited to activated myosin and the contraction-initiation pathway are well established, structural details of MLCK activation and its precise interactions remain incompletely resolved due to the absence of a high-resolution structure of full-length MLCK. Recent advances in structural biology, including cryo-electron microscopy, have significantly expanded our understanding of myosin and MLCK dynamics. However, critical challenges remain, particularly in visualizing the molecular architecture of MLCK and conformational transitions underlying myosin activation. This review integrates current knowledge of the structural and mechanistic basis of myosin regulation by MLCK, emphasizing conformational switching, phosphorylation-dependent activation, and most importantly, its unique way of functioning in the striated and non-striated muscle systems. Understanding these molecular processes will provide critical insights into muscle contractility and its implications in disease states linked to myosin activation.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"649-670"},"PeriodicalIF":5.0,"publicationDate":"2026-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486429/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788119","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Remembering Roger Cooke: a rebel with a southern charm.","authors":"Paul Marie Gerard Curmi","doi":"10.1007/s12551-026-01443-w","DOIUrl":"https://doi.org/10.1007/s12551-026-01443-w","url":null,"abstract":"<p><p>Memories of my interactions with Roger Cooke, a leader in the biophysics of muscle contraction.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":"18 3","pages":"595-596"},"PeriodicalIF":5.0,"publicationDate":"2026-05-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13486404/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148788105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}