{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T00:19:22Z","timestamp":1775175562882,"version":"3.50.1"},"reference-count":55,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2017,5,1]],"date-time":"2017-05-01T00:00:00Z","timestamp":1493596800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,5,23]],"date-time":"2018-05-23T00:00:00Z","timestamp":1527033600000},"content-version":"vor","delay-in-days":387,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100012538","name":"Swedish Cancer Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100012538","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Kempe Foundation"},{"DOI":"10.13039\/501100004063","name":"Knut and Alice Wallenberg Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004063","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100009252","name":"SciLifeLab","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100009252","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Ume\u00e5 Insamlingsstiftelse"},{"DOI":"10.13039\/501100001824","name":"Czech\u00a0Science Foundation","doi-asserted-by":"crossref","award":["P208\/12\/G016"],"award-info":[{"award-number":["P208\/12\/G016"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Praemium Academie Award"}],"content-domain":{"domain":["biophysj.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2017,5]]},"DOI":"10.1016\/j.bpj.2017.04.019","type":"journal-article","created":{"date-parts":[[2017,5,23]],"date-time":"2017-05-23T18:00:02Z","timestamp":1495562402000},"page":"2147-2158","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"title":["Apoptotic Bax at Oxidatively Stressed Mitochondrial Membranes: Lipid Dynamics and Permeabilization"],"prefix":"10.1016","volume":"112","author":[{"given":"Artur Peter G\u00fcnther","family":"Dingeldein","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"\u0160\u00e1rka","family":"Pokorn\u00e1","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Lidman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tobias","family":"Sparrman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Radek","family":"\u0160achl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"Hof","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerhard","family":"Gr\u00f6bner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2017.04.019_bib1","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1038\/nrd3137","article-title":"Targeting mitochondria for cancer therapy","volume":"9","author":"Fulda","year":"2010","journal-title":"Nat. Drug. Discov."},{"key":"10.1016\/j.bpj.2017.04.019_bib2","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1972.33","article-title":"Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics","volume":"26","author":"Kerr","year":"1972","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.bpj.2017.04.019_bib3","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1002\/cbf.1774","article-title":"Apoptosis: why and how does it occur in biology?","volume":"29","author":"Ulukaya","year":"2011","journal-title":"Cell Biochem. Funct."},{"key":"10.1016\/j.bpj.2017.04.019_bib4","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/j.coi.2007.05.004","article-title":"Bcl-2-regulated apoptosis: mechanism and therapeutic potential","volume":"19","author":"Adams","year":"2007","journal-title":"Curr. Opin. Immunol."},{"key":"10.1016\/j.bpj.2017.04.019_bib5","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/nrm2308","article-title":"The BCL-2 protein family: opposing activities that mediate cell death","volume":"9","author":"Youle","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpj.2017.04.019_bib6","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrm3722","article-title":"Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy","volume":"15","author":"Czabotar","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.bpj.2017.04.019_bib7","doi-asserted-by":"crossref","first-page":"5221","DOI":"10.1038\/onc.2010.283","article-title":"Still embedded together binding to membranes regulates Bcl-2 protein interactions","volume":"29","author":"Leber","year":"2010","journal-title":"Oncogene"},{"key":"10.1016\/j.bpj.2017.04.019_bib8","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.devcel.2011.06.017","article-title":"Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics","volume":"21","author":"Martinou","year":"2011","journal-title":"Dev. Cell"},{"key":"10.1016\/j.bpj.2017.04.019_bib9","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.molcel.2014.10.028","article-title":"Mitochondrial shape governs BAX-induced membrane permeabilization and apoptosis","volume":"57","author":"Renault","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpj.2017.04.019_bib10","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1038\/cdd.2008.9","article-title":"Contributions to Bax insertion and oligomerization of lipids of the mitochondrial outer membrane","volume":"15","author":"Lucken-Ardjomande","year":"2008","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.bpj.2017.04.019_bib11","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.molcel.2012.12.022","article-title":"Bax exists in a dynamic equilibrium between the cytosol and mitochondria to control apoptotic priming","volume":"49","author":"Schellenberg","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpj.2017.04.019_bib12","doi-asserted-by":"crossref","first-page":"2718","DOI":"10.1016\/j.bbamem.2012.06.005","article-title":"The oxidized phospholipid PazePC modulates interactions between Bax and mitochondrial membranes","volume":"1818","author":"Wallgren","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib13","doi-asserted-by":"crossref","first-page":"E4076","DOI":"10.1073\/pnas.1415142111","article-title":"Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane","volume":"111","author":"Westphal","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.04.019_bib14","series-title":"Membrane Structural Biology","author":"Luckey","year":"2008"},{"key":"10.1016\/j.bpj.2017.04.019_bib15","doi-asserted-by":"crossref","first-page":"18797","DOI":"10.1016\/S0021-9258(17)30583-5","article-title":"Mitochondrial contact sites. Lipid composition and dynamics","volume":"265","author":"Ardail","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.04.019_bib16","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1038\/sj.cdd.4401260","article-title":"Dynamics of mitochondrial morphology in healthy cells and during apoptosis","volume":"10","author":"Karbowski","year":"2003","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.bpj.2017.04.019_bib17","doi-asserted-by":"crossref","first-page":"26334","DOI":"10.1074\/jbc.M110.188516","article-title":"Permeabilization of the mitochondrial outer membrane by Bax\/truncated Bid (tBid) proteins as sensitized by cardiolipin hydroperoxide translocation: mechanistic implications for the intrinsic pathway of oxidative apoptosis","volume":"286","author":"Korytowski","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.04.019_bib18","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1007\/s10495-007-0718-8","article-title":"Cardiolipin: setting the beat of apoptosis","volume":"12","author":"Gonzalvez","year":"2007","journal-title":"Apoptosis"},{"key":"10.1016\/j.bpj.2017.04.019_bib19","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.bbamem.2008.12.014","article-title":"How does the Bax-\u03b11 targeting sequence interact with mitochondrial membranes? The role of cardiolipin","volume":"1788","author":"Sani","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib20","doi-asserted-by":"crossref","first-page":"8042","DOI":"10.1038\/ncomms9042","article-title":"Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species","volume":"6","author":"Subburaj","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bpj.2017.04.019_bib21","doi-asserted-by":"crossref","first-page":"32871","DOI":"10.1074\/jbc.M114.593897","article-title":"Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch","volume":"289","author":"Gahl","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2017.04.019_bib22","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1042\/BJ20141291","article-title":"Distinct lipid effects on tBid and Bim activation of membrane permeabilization by pro-apoptotic Bax","volume":"467","author":"Shamas-Din","year":"2015","journal-title":"Biochem.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib23","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/978-1-4020-8831-5_13","article-title":"Mediation of apoptosis by oxidized phospholipids","volume":"49","author":"Fruhwirth","year":"2008","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.bpj.2017.04.019_bib24","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1016\/j.bbadis.2007.04.009","article-title":"Oxidized phospholipids: from molecular properties to disease","volume":"1772","author":"Fruhwirth","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib25","doi-asserted-by":"crossref","first-page":"2806","DOI":"10.1111\/febs.12247","article-title":"Oxidized phosphatidylcholines in membrane-level cellular signaling: from biophysics to physiology and molecular pathology","volume":"280","author":"Volinsky","year":"2013","journal-title":"FEBS\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib26","doi-asserted-by":"crossref","first-page":"2734","DOI":"10.1016\/j.bpj.2009.01.007","article-title":"Lipid gymnastics: evidence of complete acyl chain reversal in oxidized phospholipids from molecular simulations","volume":"96","author":"Khandelia","year":"2009","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib27","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1039\/C2FD20089A","article-title":"Impact of oxidized phospholipids on the structural and dynamic organization of phospholipid membranes: a combined DSC and solid state NMR study","volume":"161","author":"Wallgren","year":"2013","journal-title":"Faraday Discuss."},{"key":"10.1016\/j.bpj.2017.04.019_bib28","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1016\/j.bbamem.2012.06.009","article-title":"Oxidized phospholipids-their properties and interactions with proteins","volume":"1818","author":"Hermetter","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib29","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1016\/j.bbamem.2016.03.003","article-title":"The oxidized phospholipid PazePC promotes permeabilization of mitochondrial membranes by Bax","volume":"1858","author":"Lidman","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib30","doi-asserted-by":"crossref","first-page":"249a","DOI":"10.1016\/j.bpj.2012.11.1403","article-title":"Impact of oxidized phospholipids on membrane organization","volume":"104","author":"Wallgren","year":"2013","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib31","doi-asserted-by":"crossref","first-page":"6610","DOI":"10.1021\/ja042325b","article-title":"Molecular insight into the electrostatic membrane surface potential by 14N\/31P MAS NMR spectroscopy: nociceptin-lipid association","volume":"127","author":"Lindstr\u00f6m","year":"2005","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.bpj.2017.04.019_bib32","doi-asserted-by":"crossref","first-page":"11425","DOI":"10.1021\/bi0001170","article-title":"Interaction of the lantibiotic nisin with mixed lipid bilayers: a 31P and 2H NMR study","volume":"39","author":"Bonev","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2017.04.019_bib33","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/0005-2736(83)90065-2","article-title":"Biological membranes are rich in low-frequency motion","volume":"732","author":"Cornell","year":"1983","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib34","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/S0092-8674(00)00167-7","article-title":"Structure of Bax: coregulation of dimer formation and intracellular localization","volume":"103","author":"Suzuki","year":"2000","journal-title":"Cell"},{"issue":"1 Pt. B","key":"10.1016\/j.bpj.2017.04.019_bib35","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.bbamem.2014.05.003","article-title":"Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy","volume":"1848","author":"Banigan","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib36","series-title":"Trends in Colloid and Interface Science VI","article-title":"Preparation of giant vesicles by external AC electric fields\u2014kinetics and applications","author":"Angelova","year":"1992"},{"key":"10.1016\/j.bpj.2017.04.019_bib37","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.bbamem.2014.10.038","article-title":"Membrane activity of the\u00a0pentaene macrolide didehydroroflamycoin in model lipid bilayers","volume":"1848","author":"Koukalov\u00e1","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib38","doi-asserted-by":"crossref","first-page":"2872","DOI":"10.1096\/fj.09-134114","article-title":"Magic-angle phosphorus NMR of functional mitochondria: in\u00a0situ monitoring of lipid response under apoptotic-like stress","volume":"23","author":"Sani","year":"2009","journal-title":"FASEB\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib39","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1063\/1.461417","article-title":"Collective lipid motions in bilayer-membranes studied by transverse deuteron spin relaxation","volume":"95","author":"Stohrer","year":"1991","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.bpj.2017.04.019_bib40","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.bbamem.2011.10.007","article-title":"Interaction of the full-length Bax protein with biomimetic mitochondrial liposomes: a small-angle neutron scattering and fluorescence study","volume":"1818","author":"Satsoura","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib41","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.molcel.2014.09.022","article-title":"Structural model of active Bax at the membrane","volume":"56","author":"Bleicken","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bpj.2017.04.019_bib42","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.bbamem.2009.09.002","article-title":"A calorimetric and spectroscopic comparison of the effects of ergosterol and cholesterol on the thermotropic phase behavior and organization of dipalmitoylphosphatidylcholine bilayer membranes","volume":"1798","author":"Mannock","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib43","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/S0006-3495(92)81814-3","article-title":"Dynamics of phosphate head groups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements","volume":"61","author":"Dufourc","year":"1992","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib44","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1021\/bi00119a019","article-title":"Deuteron nuclear magnetic resonance study of the dynamic organization of phospholipid\/cholesterol bilayer membranes: molecular properties and viscoelastic behavior","volume":"31","author":"Weisz","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bpj.2017.04.019_bib45","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1039\/C2FD20117H","article-title":"Computer simulations of the phase separation in model membranes","volume":"161","author":"Baoukina","year":"2013","journal-title":"Faraday Discuss."},{"key":"10.1016\/j.bpj.2017.04.019_bib46","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1007\/s10495-007-0746-4","article-title":"Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes","volume":"12","author":"Leber","year":"2007","journal-title":"Apoptosis"},{"key":"10.1016\/j.bpj.2017.04.019_bib47","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1016\/j.bpj.2010.08.068","article-title":"Pores formed by Bax\u03b15 relax to a smaller size and keep at equilibrium","volume":"99","author":"Fuertes","year":"2010","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib48","doi-asserted-by":"crossref","first-page":"9460","DOI":"10.1073\/pnas.1102356108","article-title":"Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity","volume":"108","author":"Last","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2017.04.019_bib49","doi-asserted-by":"crossref","first-page":"3619","DOI":"10.1016\/j.bpj.2010.09.027","article-title":"All-or-none versus graded: single-vesicle analysis reveals lipid composition effects on membrane permeabilization","volume":"99","author":"Apell\u00e1niz","year":"2010","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib50","series-title":"Solid-State NMR Spectroscopy: Principles and Applications","author":"Duer","year":"2002"},{"key":"10.1016\/j.bpj.2017.04.019_bib51","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.chemphys.2005.01.028","article-title":"Static CP P-31 NMR multilamellar bilayer broadlines in the absence and presence of the bioactive dipeptide beta-Ala-Tyr or Glu","volume":"314","author":"Benetis","year":"2005","journal-title":"Chem. Phys."},{"key":"10.1016\/j.bpj.2017.04.019_bib52","doi-asserted-by":"crossref","first-page":"4248","DOI":"10.1529\/biophysj.105.077289","article-title":"Distinguishing individual lipid headgroup mobility and phase transitions in raft-forming lipid mixtures with 31P MAS NMR","volume":"90","author":"Holland","year":"2006","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib53","doi-asserted-by":"crossref","first-page":"2427","DOI":"10.1016\/S0006-3495(03)75047-4","article-title":"Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A","volume":"84","author":"Ivanova","year":"2003","journal-title":"Biophys.\u00a0J."},{"key":"10.1016\/j.bpj.2017.04.019_bib54","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/0005-2736(82)90267-X","article-title":"Low-frequency motion in membranes. The effect of cholesterol and proteins","volume":"689","author":"Cornell","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bpj.2017.04.019_bib55","doi-asserted-by":"crossref","first-page":"6524","DOI":"10.1021\/acs.langmuir.6b00788","article-title":"Acyl chain disorder and azelaoyl orientation in lipid membranes containing oxidized lipids","volume":"32","author":"Mendes Ferreira","year":"2016","journal-title":"Langmuir"}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349517304356?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349517304356?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,6,22]],"date-time":"2022-06-22T12:27:31Z","timestamp":1655900851000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349517304356"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,5]]},"references-count":55,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2017,5]]}},"alternative-id":["S0006349517304356"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2017.04.019","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2017,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Apoptotic Bax at Oxidatively Stressed Mitochondrial Membranes: Lipid Dynamics and Permeabilization","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bpj.2017.04.019","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Biophysical Society.","name":"copyright","label":"Copyright"}]}}