{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T05:12:32Z","timestamp":1790745152574,"version":"4.1.0"},"reference-count":65,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2019,10,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Caveolae are 50\u2013100\u2005nm invaginations found within the plasma membrane of cells. Caveolae are involved in many processes that are essential for homeostasis, most notably endocytosis, mechano-protection, and signal transduction. Within these invaginations, the most important proteins are caveolins, which in addition to participating in the aforementioned processes are structural proteins responsible for caveolae biogenesis. When caveolin is misregulated or mutated, many disease states can arise which include muscular dystrophy, cancers, and heart disease. Unlike most integral membrane proteins, caveolin does not have a transmembrane orientation; instead, it is postulated to adopt an unusual topography where both the N- and C-termini lie on the cytoplasmic side of the membrane, and the hydrophobic span adopts an intramembrane loop conformation. While knowledge concerning the biology of caveolin has progressed apace, fundamental structural information has proven more difficult to obtain. In this mini-review, we curate as well as critically assess the structural data that have been obtained on caveolins to date in order to build a robust and compelling model of the caveolin secondary structure.<\/jats:p>","DOI":"10.1042\/bst20190375","type":"journal-article","created":{"date-parts":[[2019,9,24]],"date-time":"2019-09-24T16:36:19Z","timestamp":1569342979000},"page":"1489-1498","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Secondary structure of caveolins: a mini review"],"prefix":"10.1042","volume":"47","author":[{"given":"Kyle T.","family":"Root","sequence":"first","affiliation":[{"name":"Department of Chemistry, Lock Haven University, 301 E. Church Street, Lock Haven, PA 17745, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey A.","family":"Julien","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Lehigh University, 6 E. Packer Ave, Bethlehem, PA 18015, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1867-4965","authenticated-orcid":false,"given":"Kerney Jebrell","family":"Glover","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Lehigh University, 6 E. Packer Ave, Bethlehem, PA 18015, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2019,9,24]]},"reference":[{"key":"2021111915551804400_BST-2019-0375CC1","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1016\/j.bbamcr.2005.08.008","article-title":"Structure of caveolae","volume":"1746","year":"2005","journal-title":"Biochim. Biophys. Acta."},{"key":"2021111915551804400_BST-2019-0375CC2","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1146\/annurev-cellbio-100617-062737","article-title":"Caveolae: structure, function, and relationship to disease","volume":"34","year":"2018","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"2021111915551804400_BST-2019-0375CC3","doi-asserted-by":"publisher","first-page":"8655","DOI":"10.1073\/pnas.92.19.8655","article-title":"De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin","volume":"92","year":"1995","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111915551804400_BST-2019-0375CC4","doi-asserted-by":"publisher","first-page":"752","DOI":"10.1016\/j.cell.2012.06.042","article-title":"Constitutive formation of caveolae in bacterium","volume":"150","year":"2012","journal-title":"Cell"},{"key":"2021111915551804400_BST-2019-0375CC5","doi-asserted-by":"publisher","first-page":"617","DOI":"10.1083\/jcb.140.3.617","article-title":"Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells","volume":"140","year":"1998","journal-title":"J. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC6","doi-asserted-by":"publisher","first-page":"2449","DOI":"10.1126\/science.1062688","article-title":"Loss of caveolae, vascular dysfunction, and pulmonary defects in caveolin-1 gene-disrupted mice","volume":"293","year":"2001","journal-title":"Science"},{"key":"2021111915551804400_BST-2019-0375CC7","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1016\/j.biochi.2010.03.022","article-title":"Cavin proteins: new players in the caveolae field","volume":"93","year":"2011","journal-title":"Biochimie"},{"key":"2021111915551804400_BST-2019-0375CC8","doi-asserted-by":"publisher","first-page":"15160","DOI":"10.1074\/jbc.271.25.15160","article-title":"Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells \u2014 caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins","volume":"271","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC9","doi-asserted-by":"publisher","first-page":"2255","DOI":"10.1074\/jbc.271.4.2255","article-title":"Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle","volume":"271","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC10","doi-asserted-by":"publisher","first-page":"21425","DOI":"10.1074\/jbc.M100828200","article-title":"Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T-tubule abnormalities","volume":"276","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC11","doi-asserted-by":"publisher","first-page":"25708","DOI":"10.1074\/jbc.274.36.25708","article-title":"Caveolin-2 localizes to the Golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC12","doi-asserted-by":"publisher","first-page":"25718","DOI":"10.1074\/jbc.274.36.25718","article-title":"Expression of caveolin-1 is required for the transport of caveolin-2 to the plasma membrane \u2014 retention of caveolin-2 at the level of the Golgi complex","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC13","doi-asserted-by":"publisher","first-page":"1597","DOI":"10.1002\/j.1460-2075.1993.tb05804.x","article-title":"Caveolae and sorting in the trans-Golgi network of epithelial cells","volume":"12","year":"1993","journal-title":"EMBO J."},{"key":"2021111915551804400_BST-2019-0375CC14","doi-asserted-by":"publisher","first-page":"789","DOI":"10.1083\/jcb.122.4.789","article-title":"Signal-transducing molecules and glycosyl-phosphatidylinositol-Linked proteins form a caveolin-rich insoluble complex in MDCK cells","volume":"122","year":"1993","journal-title":"J. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC15","doi-asserted-by":"publisher","first-page":"9407","DOI":"10.1073\/pnas.92.20.9407","article-title":"Oligomeric structure of caveolin: implications for caveolae membrane organization","volume":"92","year":"1995","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111915551804400_BST-2019-0375CC16","doi-asserted-by":"publisher","first-page":"911","DOI":"10.1091\/mbc.6.7.911","article-title":"VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro","volume":"6","year":"1995","journal-title":"Mol. Biol. Cell"},{"key":"2021111915551804400_BST-2019-0375CC17","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1124\/pr.54.3.431","article-title":"Caveolae: from cell biology to animal physiology","volume":"54","year":"2002","journal-title":"Pharmacol. Rev."},{"key":"2021111915551804400_BST-2019-0375CC18","doi-asserted-by":"publisher","first-page":"480","DOI":"10.1016\/j.bbrc.2004.05.196","article-title":"N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes","volume":"320","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021111915551804400_BST-2019-0375CC19","doi-asserted-by":"publisher","first-page":"8301","DOI":"10.1021\/bi7002636","article-title":"A new N-terminal recognition domain in caveolin-1 interacts with sterol carrier protein-2 (SCP-2)","volume":"46","year":"2007","journal-title":"Biochemistry."},{"key":"2021111915551804400_BST-2019-0375CC20","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1016\/j.virusres.2007.02.004","article-title":"Rotavirus NSP4 interacts with both the amino- and carboxyl- termini of caveolin-1","volume":"126","year":"2007","journal-title":"Virus Res."},{"key":"2021111915551804400_BST-2019-0375CC21","doi-asserted-by":"publisher","first-page":"3863","DOI":"10.1074\/jbc.271.7.3863","article-title":"Phosphorylation of caveolin by Src tyrosine kinases \u2014 the alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo","volume":"271","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC22","doi-asserted-by":"publisher","first-page":"4398","DOI":"10.1074\/jbc.M005448200","article-title":"Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation \u2014 protein sorting at the level of the endoplasmic reticulum","volume":"276","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC23","doi-asserted-by":"publisher","first-page":"11193","DOI":"10.1073\/pnas.172196599","article-title":"Mechanism of caveolin filament assembly","volume":"99","year":"2002","journal-title":"Proc. Natl Acad. Sci. U.S.A."},{"key":"2021111915551804400_BST-2019-0375CC24","first-page":"575180","article-title":"Elucidation of the rotavirus NSP4-caveolin-1 and -cholesterol interactions using synthetic peptides","volume":"2012","year":"2011","journal-title":"J. Amino Acids."},{"key":"2021111915551804400_BST-2019-0375CC25","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1242\/jcs.02853","article-title":"Biogenesis of caveolae: a structural model for caveolin-induced domain formation","volume":"119","year":"2006","journal-title":"J. Cell Sci."},{"key":"2021111915551804400_BST-2019-0375CC26","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1016\/j.bbrc.2005.10.099","article-title":"Structural insights into the function of human caveolin 1","volume":"338","year":"2005","journal-title":"Biochem.Biophys. Res. Commun."},{"key":"2021111915551804400_BST-2019-0375CC27","doi-asserted-by":"publisher","first-page":"24875","DOI":"10.1074\/jbc.M115.644336","article-title":"Molecular characterization of caveolin-induced membrane curvature","volume":"290","year":"2015","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC28","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1083\/jcb.148.1.17","article-title":"Multiple domains in caveolin-1 control its intracellular traffic","volume":"148","year":"2000","journal-title":"J. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC29","doi-asserted-by":"publisher","first-page":"1686","DOI":"10.1016\/j.bpj.2015.08.030","article-title":"Secondary structure analysis of a functional construct of caveolin-1 reveals a long C-terminal helix","volume":"109","year":"2015","journal-title":"Biophys. J."},{"key":"2021111915551804400_BST-2019-0375CC30","doi-asserted-by":"publisher","first-page":"2475","DOI":"10.1016\/j.bpj.2016.05.004","article-title":"A pH-mediated topological switch within the N-terminal domain of human caveolin-3","volume":"110","year":"2016","journal-title":"Biophys. J."},{"key":"2021111915551804400_BST-2019-0375CC31","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1083\/jcb.126.1.111","article-title":"Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source \u2014 implications for human-disease","volume":"126","year":"1994","journal-title":"J. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC32","doi-asserted-by":"publisher","first-page":"8858","DOI":"10.1074\/jbc.274.13.8858","article-title":"Regulation of G protein-coupled receptor kinases by caveolin","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC33","doi-asserted-by":"publisher","first-page":"18522","DOI":"10.1074\/jbc.272.30.18522","article-title":"Direct interaction of endothelial nitric-oxide synthase and caveolin-1 inhibits synthase activity","volume":"272","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC34","doi-asserted-by":"publisher","first-page":"5419","DOI":"10.1074\/jbc.273.10.5419","article-title":"Caveolins, a family of scaffolding proteins for organizing \u2018preassembled signaling complexes\u2019 at the plasma membrane\u2019","volume":"273","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC35","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1038\/10067","article-title":"Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains","volume":"1","year":"1999","journal-title":"Nat. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC36","doi-asserted-by":"publisher","first-page":"478","DOI":"10.1110\/ps.051911706","article-title":"Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking","volume":"15","year":"2006","journal-title":"Protein Sci."},{"key":"2021111915551804400_BST-2019-0375CC37","doi-asserted-by":"publisher","first-page":"5301","DOI":"10.1016\/j.febslet.2006.08.075","article-title":"Role of the membrane interface on the conformation of the caveolin scaffolding domain: a CD and NMR study","volume":"580","year":"2006","journal-title":"FEBS Lett."},{"key":"2021111915551804400_BST-2019-0375CC38","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1007\/s00249-009-0548-4","article-title":"Structural and dynamic properties of juxta-membrane segments of caveolin-1 and caveolin-2 at the membrane interface","volume":"39","year":"2010","journal-title":"Eur. Biophys. J."},{"key":"2021111915551804400_BST-2019-0375CC39","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1002\/bip.20595","article-title":"Interaction of synthetic peptides corresponding to the scaffolding domain of caveolin-3 with model membranes","volume":"84","year":"2006","journal-title":"Biopolymers"},{"key":"2021111915551804400_BST-2019-0375CC40","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1021\/bi201356v","article-title":"Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes","volume":"51","year":"2012","journal-title":"Biochemistry"},{"key":"2021111915551804400_BST-2019-0375CC41","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.1016\/j.bpj.2014.02.005","article-title":"Probing the U-shaped conformation of caveolin-1 in a bilayer","volume":"106","year":"2014","journal-title":"Biophys. J."},{"key":"2021111915551804400_BST-2019-0375CC42","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1016\/j.bbamem.2011.12.033","article-title":"The transmembrane domain of caveolin-1 exhibits a helix-break-helix structure","volume":"1818","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111915551804400_BST-2019-0375CC43","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.bbamem.2011.09.009","article-title":"Caveolin-1 hydrophobic segment peptides insertion into membrane mimetic systems: role of proline residue","volume":"1818","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111915551804400_BST-2019-0375CC44","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1002\/bip.22597","article-title":"Structural study of caveolin-1 intramembrane domain by circular dichroism and nuclear magnetic resonance","volume":"104","year":"2015","journal-title":"Biopolymers"},{"key":"2021111915551804400_BST-2019-0375CC45","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/j.bbamem.2004.04.011","article-title":"Membrane proteins, lipids and detergents: not just a soap opera","volume":"1666","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111915551804400_BST-2019-0375CC46","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1038\/nrm1784","article-title":"How proteins produce cellular membrane curvature","volume":"7","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021111915551804400_BST-2019-0375CC47","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.devcel.2012.06.012","article-title":"Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?","volume":"23","year":"2012","journal-title":"Dev. Cell"},{"key":"2021111915551804400_BST-2019-0375CC48","doi-asserted-by":"publisher","first-page":"339","DOI":"10.1016\/j.jmb.2004.10.064","article-title":"Caveolin scaffolding region and cholesterol-rich domains in membranes","volume":"345","year":"2005","journal-title":"J. Mol. Biol."},{"key":"2021111915551804400_BST-2019-0375CC49","doi-asserted-by":"publisher","first-page":"e44879","DOI":"10.1371\/journal.pone.0044879","article-title":"Evaluating caveolin interactions: do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif?","volume":"7","year":"2012","journal-title":"PLoS ONE"},{"key":"2021111915551804400_BST-2019-0375CC50","doi-asserted-by":"publisher","first-page":"22660","DOI":"10.1074\/jbc.274.32.22660","article-title":"A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1 \u2014 the caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC51","doi-asserted-by":"publisher","first-page":"4398","DOI":"10.1074\/jbc.272.7.4398","article-title":"Mutational analysis of the properties of caveolin-1. A novel role for the C-terminal domain in mediating homo-typic caveolin-caveolin interactions","volume":"272","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC52","doi-asserted-by":"publisher","first-page":"21605","DOI":"10.1074\/jbc.M002558200","article-title":"A molecular dissection of caveolin-1 membrane attachment and oligomerization \u2014 two separate regions of the caveolin-1 C-terminal domain mediate membrane binding and oligomer\/oligomer interactions in vivo","volume":"275","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC53","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1016\/0092-8674(92)90143-Z","article-title":"Caveolin, a protein component of caveolae membrane coats","volume":"68","year":"1992","journal-title":"Cell"},{"key":"2021111915551804400_BST-2019-0375CC54","doi-asserted-by":"publisher","first-page":"5754","DOI":"10.1021\/bi0121656","article-title":"Connexin family members target to lipid raft domains and interact with caveolin-1","volume":"41","year":"2002","journal-title":"Biochemistry"},{"key":"2021111915551804400_BST-2019-0375CC55","doi-asserted-by":"publisher","first-page":"6838","DOI":"10.1074\/jbc.270.12.6838","article-title":"Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae","volume":"270","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC56","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1016\/j.bbamcr.2015.02.002","article-title":"Fatty acylated caveolin-2 is a substrate of insulin receptor tyrosine kinase for insulin receptor substrate-1-directed signaling activation","volume":"1853","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111915551804400_BST-2019-0375CC57","doi-asserted-by":"publisher","first-page":"25632","DOI":"10.1074\/jbc.274.36.25632","article-title":"Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C) - retention of LGMD-1C caveolin-3 mutants within the Golgi complex","volume":"274","year":"1999","journal-title":"J. Biol. Chem."},{"key":"2021111915551804400_BST-2019-0375CC58","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/S1937-6448(08)01804-2","article-title":"The biology of caveolae: achievements and perspectives","volume":"2009","year":"2009","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"2021111915551804400_BST-2019-0375CC59","doi-asserted-by":"publisher","first-page":"3911","DOI":"10.1021\/bi3001853","article-title":"Probing the caveolin-1 P132L mutant: critical insights into its oligomeric behavior and structure","volume":"51","year":"2012","journal-title":"Biochemistry"},{"key":"2021111915551804400_BST-2019-0375CC60","doi-asserted-by":"publisher","first-page":"4320","DOI":"10.1021\/bi5005238","article-title":"Modest effects of lipid modifications on the structure of caveolin-3","volume":"53","year":"2014","journal-title":"Biochemistry"},{"key":"2021111915551804400_BST-2019-0375CC61","doi-asserted-by":"publisher","first-page":"1351","DOI":"10.1016\/j.bbamem.2012.01.013","article-title":"Efficiency of detergents at maintaining membrane protein structures in their biologically relevant forms","volume":"1818","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111915551804400_BST-2019-0375CC62","doi-asserted-by":"publisher","first-page":"287","DOI":"10.3390\/biom9070287","article-title":"Caveolin-1 endows order in cholesterol-rich detergent resistant membranes","volume":"9","year":"2019","journal-title":"Biomolecules"},{"key":"2021111915551804400_BST-2019-0375CC63","doi-asserted-by":"publisher","first-page":"M110.007146","DOI":"10.1074\/mcp.M110.007146","article-title":"Differential impact of caveolae and caveolin-1 scaffolds on the membrane raft proteome","volume":"10","year":"2011","journal-title":"Mol. Cell Proteomics"},{"key":"2021111915551804400_BST-2019-0375CC64","doi-asserted-by":"publisher","first-page":"3077","DOI":"10.1242\/jcs.191262","article-title":"Architecture of the caveolar coat complex","volume":"129","year":"2016","journal-title":"J Cell Sci."},{"key":"2021111915551804400_BST-2019-0375CC65","doi-asserted-by":"publisher","first-page":"40302","DOI":"10.1074\/jbc.M112.377085","article-title":"Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptor","volume":"287","year":"2012","journal-title":"J. Biol. Chem."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/47\/5\/1489\/859149\/bst-2019-0375c.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/47\/5\/1489\/859149\/bst-2019-0375c.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,19]],"date-time":"2021-11-19T16:08:37Z","timestamp":1637338117000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/47\/5\/1489\/220552\/Secondary-structure-of-caveolins-a-mini-review"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9,24]]},"references-count":65,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2019,9,24]]},"published-print":{"date-parts":[[2019,10,31]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20190375","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,9,24]]}}}