{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T11:31:16Z","timestamp":1777462276521,"version":"3.51.4"},"reference-count":48,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2018,6,1]],"date-time":"2018-06-01T00:00:00Z","timestamp":1527811200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,6,1]],"date-time":"2018-06-01T00:00:00Z","timestamp":1527811200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,6,1]],"date-time":"2019-06-01T00:00:00Z","timestamp":1559347200000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R01GM64742"],"award-info":[{"award-number":["R01GM64742"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R01GM072701"],"award-info":[{"award-number":["R01GM072701"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["1S10OD021536"],"award-info":[{"award-number":["1S10OD021536"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R01GM27906"],"award-info":[{"award-number":["R01GM27906"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R37AG26160"],"award-info":[{"award-number":["R37AG26160"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["F31HL095361"],"award-info":[{"award-number":["F31HL095361"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000968","name":"American Heart Association","doi-asserted-by":"publisher","award":["16PRE27770056"],"award-info":[{"award-number":["16PRE27770056"]}],"id":[{"id":"10.13039\/100000968","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2018,6]]},"DOI":"10.1016\/j.bbamem.2018.02.030","type":"journal-article","created":{"date-parts":[[2018,3,2]],"date-time":"2018-03-02T03:08:44Z","timestamp":1519960124000},"page":"1335-1341","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"title":["Effects of the Arg9Cys and Arg25Cys mutations on phospholamban's conformational equilibrium in membrane bilayers"],"prefix":"10.1016","volume":"1860","author":[{"given":"Sarah E.D.","family":"Nelson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kim N.","family":"Ha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tata","family":"Gopinath","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mara H.","family":"Exline","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessandro","family":"Mascioni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David D.","family":"Thomas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gianluigi","family":"Veglia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2018.02.030_bb0005","doi-asserted-by":"crossref","DOI":"10.1038\/nrm1151","article-title":"Phospholamban: a crucial regulator of cardiac contractility","volume":"4","author":"MacLennan","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0010","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1146\/annurev.physiol.70.113006.100455","article-title":"Calcium cycling and signaling in cardiac myocytes","volume":"70","author":"Bers","year":"2008","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0015","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11010-006-9355-8","article-title":"Calcium signaling phenomena in heart diseases: a perspective","volume":"298","author":"Chakraborti","year":"2007","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0020","doi-asserted-by":"crossref","first-page":"572","DOI":"10.3109\/07853890008998837","article-title":"Phospholamban and cardiac contractility","volume":"32","author":"Frank","year":"2000","journal-title":"Ann. Med."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0025","doi-asserted-by":"crossref","first-page":"21726","DOI":"10.1074\/jbc.271.36.21726","article-title":"Phospholamban regulates the Ca2+-ATPase through intramembrane interactions","volume":"271","author":"Kimura","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0030","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1152\/physrev.1998.78.4.921","article-title":"Phospholamban: protein structure, mechanism of action, and role in cardiac function","volume":"78","author":"Simmerman","year":"1998","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0035","doi-asserted-by":"crossref","first-page":"9101","DOI":"10.1073\/pnas.1016535108","article-title":"Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method","volume":"108","author":"Verardi","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0040","doi-asserted-by":"crossref","first-page":"2960","DOI":"10.1021\/bi961955q","article-title":"Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers","volume":"36","author":"Cornea","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0045","doi-asserted-by":"crossref","DOI":"10.1021\/bi0478446","article-title":"Phospholamban pentamer quaternary conformation determined by in-gel fluorescence anisotropy","volume":"44","author":"Robia","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0050","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.272.24.15061","article-title":"Phospholamban inhibitory function is activated by depolymerization","volume":"272","author":"Kimura","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0055","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1161\/CIRCRESAHA.107.159947","article-title":"Forster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex","volume":"101","author":"Robia","year":"2007","journal-title":"Circ. Res."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0060","doi-asserted-by":"crossref","first-page":"10165","DOI":"10.1073\/pnas.0904290106","article-title":"Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach","volume":"106","author":"Traaseth","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0065","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.bbamem.2011.07.040","article-title":"Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy","volume":"1818","author":"Gustavsson","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0070","doi-asserted-by":"crossref","first-page":"17338","DOI":"10.1073\/pnas.1303006110","article-title":"Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban","volume":"110","author":"Gustavsson","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0075","doi-asserted-by":"crossref","first-page":"6684","DOI":"10.1021\/bi400517b","article-title":"Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation","volume":"52","author":"De Simone","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0080","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/j.jmb.2011.03.015","article-title":"Lipid-mediated folding\/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase","volume":"408","author":"Gustavsson","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0085","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1007\/s10974-012-9319-4","article-title":"Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function","volume":"33","author":"Ha","year":"2012","journal-title":"J. Muscle Res. Cell Motil."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0090","doi-asserted-by":"crossref","first-page":"37205","DOI":"10.1074\/jbc.M704056200","article-title":"Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics","volume":"282","author":"Ha","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0095","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.bbamem.2009.09.009","article-title":"Probing excited states and activation energy for the integral membrane protein phospholamban by NMR CPMG relaxation dispersion experiments","volume":"1798","author":"Traaseth","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0100","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1126\/science.1081578","article-title":"Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban","volume":"299","author":"Schmitt","year":"2003","journal-title":"Science"},{"issue":"10092","key":"10.1016\/j.bbamem.2018.02.030_bb0105","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/S0140-6736(16)31713-5","article-title":"Dilated cardiomyopathy","volume":"390","author":"Weintraub","year":"2017","journal-title":"Lancet"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0110","doi-asserted-by":"crossref","first-page":"16521","DOI":"10.1074\/jbc.M112.360859","article-title":"Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy","volume":"287","author":"Ceholski","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0115","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1093\/cvr\/cvv127","article-title":"A novel human R25C-phospholamban mutation is associated with super-inhibition of calcium cycling and ventricular arrhythmia","volume":"107","author":"Liu","year":"2015","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0120","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S1046-5928(03)00127-X","article-title":"Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies","volume":"30","author":"Buck","year":"2003","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0125","first-page":"3145","article-title":"NMR studies on fully hydrated membrane proteins, with emphasis on bacteriorhodopsin as a typical and prototype membrane protein","volume":"1768","author":"Saito","year":"2007","journal-title":"BBA-Bioenergetics"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0130","doi-asserted-by":"crossref","first-page":"9553","DOI":"10.1021\/jp503032h","article-title":"Solid-state NMR shows that dynamically different domains of membrane proteins have different hydration dependence","volume":"118","author":"Zhang","year":"2014","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0135","doi-asserted-by":"crossref","first-page":"4456","DOI":"10.1021\/acs.jpcb.7b03268","article-title":"Probing the conformationally excited states of membrane proteins via (1)H-detected MAS solid-state NMR spectroscopy","volume":"121","author":"Gopinath","year":"2017","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0140","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0145","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1093\/bioinformatics\/btp345","article-title":"PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy","volume":"25","author":"Lee","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0150","doi-asserted-by":"crossref","first-page":"10892","DOI":"10.1021\/bi0003543","article-title":"Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase","volume":"39","author":"Karim","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0155","doi-asserted-by":"crossref","first-page":"38814","DOI":"10.1074\/jbc.M104006200","article-title":"Role of cysteine residues in structural stability and function of a transmembrane helix bundle","volume":"276","author":"Karim","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0160","doi-asserted-by":"crossref","first-page":"12074","DOI":"10.1021\/bi980642n","article-title":"Cysteine reactivity and oligomeric structures of phospholamban and its mutants","volume":"37","author":"Karim","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0165","doi-asserted-by":"crossref","first-page":"12965","DOI":"10.1021\/ja0530164","article-title":"Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy","volume":"127","author":"Andronesi","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0170","doi-asserted-by":"crossref","first-page":"2589","DOI":"10.1016\/S0006-3495(03)74681-5","article-title":"NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles","volume":"85","author":"Zamoon","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0175","doi-asserted-by":"crossref","first-page":"4747","DOI":"10.1073\/pnas.0406039102","article-title":"Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation","volume":"102","author":"Zamoon","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0180","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1016\/j.jmb.2006.02.051","article-title":"Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA","volume":"358","author":"Karim","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0185","doi-asserted-by":"crossref","first-page":"2805","DOI":"10.1529\/biophysj.107.108910","article-title":"Rotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance","volume":"93","author":"Nesmelov","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0190","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.jmb.2012.02.011","article-title":"Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup charge","volume":"418","author":"Li","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0195","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1016\/j.bpj.2013.08.045","article-title":"Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase","volume":"105","author":"Pallikkuth","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0200","doi-asserted-by":"crossref","first-page":"10367","DOI":"10.1021\/bi200759y","article-title":"Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase\/phospholamban complex","volume":"50","author":"Gustavsson","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2018.02.030_bb0205","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.yjmcc.2014.10.005","article-title":"Phospholamban interactome in cardiac contractility and survival: a new vision of an old friend","volume":"77","author":"Haghighi","year":"2014","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0210","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.jmb.2011.06.041","article-title":"cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban","volume":"412","author":"Masterson","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0215","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1038\/nchembio.452","article-title":"Dynamics connect substrate recognition to catalysis in protein kinase A","volume":"6","author":"Masterson","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0220","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.1073\/pnas.1502299112","article-title":"Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation","volume":"112","author":"Kim","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0225","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1073\/pnas.1013987108","article-title":"Lethal Arg9Cys phospholamban mutation hinders Ca2+-ATPase regulation and phosphorylation by protein kinase A","volume":"108","author":"Ha","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0230","doi-asserted-by":"crossref","first-page":"7130","DOI":"10.1074\/jbc.M114.630319","article-title":"Acute inotropic and lusitropic effects of cardiomyopathic R9C mutation of phospholamban","volume":"290","author":"Abrol","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0235","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1529\/biophysj.103.038844","article-title":"(1)H\/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles","volume":"87","author":"Metcalfe","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2018.02.030_bb0240","doi-asserted-by":"crossref","first-page":"5984","DOI":"10.1021\/bi00185a040","article-title":"Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation","volume":"33","author":"Farrow","year":"1994","journal-title":"Biochemistry"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273618300713?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273618300713?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T08:44:36Z","timestamp":1757753076000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273618300713"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,6]]},"references-count":48,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2018,6]]}},"alternative-id":["S0005273618300713"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2018.02.030","relation":{},"ISSN":["0005-2736"],"issn-type":[{"value":"0005-2736","type":"print"}],"subject":[],"published":{"date-parts":[[2018,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effects of the Arg9Cys and Arg25Cys mutations on phospholamban's conformational equilibrium in membrane bilayers","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Biomembranes","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamem.2018.02.030","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier B.V.","name":"copyright","label":"Copyright"}]}}