{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T05:11:02Z","timestamp":1778735462027,"version":"3.51.4"},"reference-count":55,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T00:00:00Z","timestamp":1772755200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100024370","name":"Ministero dell&apos;Istruzione dell&apos;Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100024370","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jlr.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Lipid Research"],"published-print":{"date-parts":[[2026,4]]},"DOI":"10.1016\/j.jlr.2026.101017","type":"journal-article","created":{"date-parts":[[2026,3,10]],"date-time":"2026-03-10T06:58:58Z","timestamp":1773125938000},"page":"101017","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["S-nitrosylation contributes to ER stress and aggresome formation in secosterol-B-mediated endothelial dysfunction"],"prefix":"10.1016","volume":"67","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2078-7774","authenticated-orcid":false,"given":"Maria Gemma","family":"Nasoni","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-1088-0729","authenticated-orcid":false,"given":"Erik","family":"Bargagni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francesca","family":"Monittola","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pasquale","family":"Creanza","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-2158-0369","authenticated-orcid":false,"given":"Elisa","family":"Maricchiolo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sofia","family":"Masini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anastasia","family":"Ricci","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9719-2381","authenticated-orcid":false,"given":"Serena","family":"Benedetti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3634-3454","authenticated-orcid":false,"given":"Silvia","family":"Carloni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sabrina","family":"Burattini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessandra","family":"Fraternale","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrea","family":"Pompa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michele","family":"Menotta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0027-9326","authenticated-orcid":false,"given":"Luigi","family":"Iuliano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1235-8910","authenticated-orcid":false,"given":"Rita","family":"Crinelli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8225-3129","authenticated-orcid":false,"given":"Francesca","family":"Luchetti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jlr.2026.101017_bib1","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.chemphyslip.2011.06.006","article-title":"Pathways of cholesterol oxidation via non-enzymatic mechanisms","volume":"164","author":"Iuliano","year":"2011","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jlr.2026.101017_bib2","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.biochi.2018.06.006","article-title":"Implication of oxysterols in chronic inflammatory human diseases","volume":"153","author":"Testa","year":"2018","journal-title":"Biochimie"},{"key":"10.1016\/j.jlr.2026.101017_bib3","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.redox.2012.12.001","article-title":"Oxysterols in the pathogenesis of major chronic diseases","volume":"1","author":"Poli","year":"2013","journal-title":"Redox Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0021-9150(98)00196-8","article-title":"Oxysterols and atherosclerosis","volume":"142","author":"Brown","year":"1999","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.jlr.2026.101017_bib5","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/S0891-5849(96)00626-0","article-title":"Characterization of cholesterol oxidation products formed by oxidative modification of low density lipoprotein","volume":"23","author":"Chang","year":"1997","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib6","doi-asserted-by":"crossref","first-page":"107","DOI":"10.3164\/jcbn.17-109","article-title":"Biochemical properties of cholesterol aldehyde secosterol and its derivatives","volume":"62","author":"Miyoshi","year":"2018","journal-title":"J. Clin. Biochem. Nutr."},{"key":"10.1016\/j.jlr.2026.101017_bib7","doi-asserted-by":"crossref","first-page":"2802","DOI":"10.1016\/j.jchromb.2011.08.004","article-title":"A highly sensitive LC\u2013ESI-MS\/MS method for the quantification of cholesterol ozonolysis products secosterol-A and secosterol-B after derivatization with 2-hydrazino-1-methylpyridine","volume":"879","author":"Tomono","year":"2011","journal-title":"J. Chromatogr. B"},{"key":"10.1016\/j.jlr.2026.101017_bib8","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.jsbmb.2019.04.014","article-title":"Secosterol-B affects endoplasmic reticulum structure in endothelial cells","volume":"190","author":"Luchetti","year":"2019","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib9","doi-asserted-by":"crossref","DOI":"10.3389\/fcvm.2024.1413441","article-title":"Recent progress of endoplasmic reticulum stress in the mechanism of atherosclerosis","volume":"11","author":"Ni","year":"2024","journal-title":"Front Cardiovasc. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib10","first-page":"1","article-title":"Role of endoplasmic reticulum stress in atherosclerosis and its potential as a therapeutic target","volume":"2020","author":"Yang","year":"2020","journal-title":"Oxid Med. Cell Longev."},{"key":"10.1016\/j.jlr.2026.101017_bib11","doi-asserted-by":"crossref","first-page":"1818","DOI":"10.1038\/s41598-018-19584-8","article-title":"3\u2032,4\u2032-dihydroxyflavonol ameliorates endoplasmic reticulum stress-induced apoptosis and endothelial dysfunction in mice","volume":"8","author":"Lau","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jlr.2026.101017_bib12","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1080\/15548627.2016.1147667","article-title":"Cytosolic PINK1 promotes the targeting of ubiquitinated proteins to the aggresome-autophagy pathway during proteasomal stress","volume":"12","author":"Gao","year":"2016","journal-title":"Autophagy"},{"key":"10.1016\/j.jlr.2026.101017_bib13","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.2337\/db09-1637","article-title":"Activation of AMP-Activated protein kinase inhibits oxidized LDL-Triggered endoplasmic reticulum stress in vivo","volume":"59","author":"Dong","year":"2010","journal-title":"Diabetes"},{"key":"10.1016\/j.jlr.2026.101017_bib14","first-page":"868","article-title":"- role of PERK\/eIF2\u03b1\/CHOP endoplasmic reticulum stress pathway in oxidized low-density lipoprotein mediated induction of endothelial apoptosis","volume":"29","author":"Yong","year":"2016","journal-title":"Biomed. Environ. Sci."},{"key":"10.1016\/j.jlr.2026.101017_bib15","doi-asserted-by":"crossref","first-page":"1439","DOI":"10.1161\/01.ATV.0000223900.67024.15","article-title":"Nitric oxide and endoplasmic reticulum stress","volume":"26","author":"Gotoh","year":"2006","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib16","article-title":"Mitochondrial protein translation: emerging roles and clinical significance in disease","volume":"9","author":"Wang","year":"2021","journal-title":"Front Cell Dev. Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib17","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.neuron.2013.05.005","article-title":"Aberrant protein S-Nitrosylation in neurodegenerative diseases","volume":"78","author":"Nakamura","year":"2013","journal-title":"Neuron"},{"key":"10.1016\/j.jlr.2026.101017_bib18","doi-asserted-by":"crossref","DOI":"10.1038\/srep14812","article-title":"Regulation of the unfolded protein response via S-nitrosylation of sensors of endoplasmic reticulum stress","volume":"5","author":"Nakato","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jlr.2026.101017_bib19","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/0039-128X(93)90023-G","article-title":"The ozonation of cholesterol: separation and identification of 2,4-dinitrophenulhydrazine derivatization products of 3\u03b2-hydroxy-5-oxo-5,6-secocholestan-6-al","volume":"58","author":"Wang","year":"1993","journal-title":"Steroids"},{"key":"10.1016\/j.jlr.2026.101017_bib20","doi-asserted-by":"crossref","first-page":"1148","DOI":"10.3390\/antiox11061148","article-title":"3\u03b2-Hydroxy-5\u03b2-hydroxy-B-norcholestane-6\u03b2-carboxaldehyde (SEC-B) induces proinflammatory activation of human endothelial cells associated with nitric oxide production and endothelial nitric oxide Synthase\/Caveolin-1 dysregulation","volume":"11","author":"Nasoni","year":"2022","journal-title":"Antioxidants"},{"key":"10.1016\/j.jlr.2026.101017_bib21","doi-asserted-by":"crossref","DOI":"10.1096\/fj.202201157RR","article-title":"Targeting SARS-CoV -2 by synthetic dual-acting thiol compounds that inhibit Spike\/ACE2 interaction and viral protein production","volume":"37","author":"Fraternale","year":"2023","journal-title":"FASEB J."},{"key":"10.1016\/j.jlr.2026.101017_bib22","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.plantsci.2018.03.020","article-title":"Expression of CLAVATA3 fusions indicates rapid intracellular processing and a role of ERAD","volume":"271","author":"De Marchis","year":"2018","journal-title":"Plant Sci."},{"key":"10.1016\/j.jlr.2026.101017_bib23","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1242\/jcs.045625","article-title":"ATF6\u03b1 induces XBP1-independent expansion of the endoplasmic reticulum","volume":"122","author":"Bommiasamy","year":"2009","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jlr.2026.101017_bib24","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.immuni.2004.06.010","article-title":"XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation","volume":"21","author":"Shaffer","year":"2004","journal-title":"Immunity"},{"key":"10.1016\/j.jlr.2026.101017_bib25","doi-asserted-by":"crossref","first-page":"3290","DOI":"10.1016\/j.jtha.2024.07.015","article-title":"Small molecules targeting GRP78 mitigate anti-GRP78 autoantibody\u2013mediated tissue factor procoagulant activity in cultured endothelial cells","volume":"22","author":"Chen","year":"2024","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.jlr.2026.101017_bib26","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/s10020-024-00808-9","article-title":"Endoplasmic reticulum stress and therapeutic strategies in metabolic, neurodegenerative diseases and cancer","volume":"30","author":"Yuan","year":"2024","journal-title":"Mol. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib27","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.molmed.2009.06.007","article-title":"Protein S-nitrosylation in health and disease: a current perspective","volume":"15","author":"Foster","year":"2009","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib28","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.molcel.2014.01.004","article-title":"Protein disulfide isomerase A6 controls the decay of IRE1\u03b1 signaling via disulfide-dependent Association","volume":"53","author":"Eletto","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jlr.2026.101017_bib29","doi-asserted-by":"crossref","first-page":"e2986","DOI":"10.1038\/cddis.2017.369","article-title":"PDI is an essential redox-sensitive activator of PERK during the unfolded protein response (UPR)","volume":"8","author":"Kranz","year":"2017","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.jlr.2026.101017_bib30","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/355033a0","article-title":"Protein folding in the cell","volume":"355","author":"Gething","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.jlr.2026.101017_bib31","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1083\/jcb.200907074","article-title":"Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response","volume":"187","author":"Schuck","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib32","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1083\/jcb.200406136","article-title":"XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum","volume":"167","author":"Sriburi","year":"2004","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib33","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1007\/s11906-017-0762-x","article-title":"Endoplasmic Reticulum stress, a driver or an innocent bystander in endothelial dysfunction associated with hypertension?","volume":"19","author":"Cunard","year":"2017","journal-title":"Curr. Hypertens. Rep."},{"key":"10.1016\/j.jlr.2026.101017_bib34","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1091\/mbc.e07-06-0587","article-title":"Sequestration of mutated \u03b11-Antitrypsin into inclusion bodies is a cell-protective mechanism to maintain endoplasmic reticulum function","volume":"19","author":"Granell","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jlr.2026.101017_bib35","doi-asserted-by":"crossref","first-page":"884","DOI":"10.1038\/nature02261","article-title":"Protein folding and misfolding","volume":"426","author":"Dobson","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.jlr.2026.101017_bib36","doi-asserted-by":"crossref","DOI":"10.1016\/j.snb.2024.136713","article-title":"Imaging nitric oxide dynamics in endoplasmic reticulum stress with a tailor-made near-infrared fluorescence probe","volume":"423","author":"Wang","year":"2025","journal-title":"Sens Actuators B Chem."},{"key":"10.1016\/j.jlr.2026.101017_bib37","doi-asserted-by":"crossref","first-page":"330","DOI":"10.14740\/cr1700","article-title":"The role of inducible nitric oxide synthase in assessing the functional level of coronary artery lesions in chronic coronary syndrome","volume":"15","author":"Senderovic","year":"2024","journal-title":"Cardiol. Res."},{"key":"10.1016\/j.jlr.2026.101017_bib38","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2020\/4751803","article-title":"5 \u03b1 ,6 \u03b1 -Epoxyphytosterols and 5 \u03b1 ,6 \u03b1 -Epoxycholesterol increase nitrosative stress and inflammatory cytokine production in rats on low-cholesterol diet","volume":"2020","author":"Wielkoszy\u0144ski","year":"2020","journal-title":"Oxid Med. Cell Longev."},{"key":"10.1016\/j.jlr.2026.101017_bib39","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1007\/s00018-024-05130-5","article-title":"Functional role of Ash2l in oxLDL induced endothelial dysfunction and atherosclerosis","volume":"81","author":"Su","year":"2024","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/j.jlr.2026.101017_bib40","doi-asserted-by":"crossref","first-page":"404","DOI":"10.3390\/antiox8090404","article-title":"S-Nitrosylation: an emerging paradigm of Redox Signaling","volume":"8","author":"Fernando","year":"2019","journal-title":"Antioxidants"},{"key":"10.1016\/j.jlr.2026.101017_bib41","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.nbd.2015.03.017","article-title":"Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases","volume":"84","author":"Nakamura","year":"2015","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jlr.2026.101017_bib42","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1038\/s41419-019-2144-6","article-title":"Extensive protein S-nitrosylation associated with human pancreatic ductal adenocarcinoma pathogenesis","volume":"10","author":"Tan","year":"2019","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.jlr.2026.101017_bib43","doi-asserted-by":"crossref","first-page":"4452","DOI":"10.1038\/s41467-021-24736-y","article-title":"S-nitrosylation-mediated coupling of G-protein alpha-2 with CXCR5 induces Hippo\/YAP-dependent diabetes-accelerated atherosclerosis","volume":"12","author":"Chao","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jlr.2026.101017_bib44","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.3892\/ijmm.2014.1920","article-title":"Homocysteine reduces protein S-nitrosylation in endothelium","volume":"34","author":"Chen","year":"2014","journal-title":"Int. J. Mol. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib45","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1161\/ATVBAHA.119.313440","article-title":"S-Nitrosylation of Plastin-3 exacerbates thoracic aortic dissection Formation via endothelial barrier dysfunction","volume":"40","author":"Pan","year":"2020","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib46","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1054\/ceca.1999.0099","article-title":"Effect of nitric oxide on endoplasmic reticulum calcium homeostasis, protein synthesis and energy metabolism","volume":"27","author":"Doutheil","year":"2000","journal-title":"Cell Calcium."},{"key":"10.1016\/j.jlr.2026.101017_bib47","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.freeradbiomed.2023.08.008","article-title":"When nitrosative stress hits the endoplasmic reticulum: possible implications in oxLDL\/oxysterols-induced endothelial dysfunction","volume":"208","author":"Nasoni","year":"2023","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jlr.2026.101017_bib48","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1016\/j.bbadis.2018.02.009","article-title":"eNOS S-nitrosylation mediated OxLDL-induced endothelial dysfunction via increasing the interaction of eNOS with \u03b2-catenin","volume":"1865","author":"Wang","year":"2019","journal-title":"Biochim. Biophys. Acta BBA - Mol. Basis Dis."},{"key":"10.1016\/j.jlr.2026.101017_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102087","article-title":"Critical roles of protein disulfide isomerases in balancing proteostasis in the nervous system","volume":"298","author":"Medinas","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jlr.2026.101017_bib50","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.tibs.2017.10.006","article-title":"How are proteins reduced in the endoplasmic reticulum?","volume":"43","author":"Ellgaard","year":"2018","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jlr.2026.101017_bib51","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.jprot.2019.01.001","article-title":"The protein S-nitrosylation of splicing and translational machinery in vascular endothelial cells is susceptible to oxidative stress induced by oxidized low-density lipoprotein","volume":"195","author":"Xu","year":"2019","journal-title":"J. Proteomics"},{"key":"10.1016\/j.jlr.2026.101017_bib52","doi-asserted-by":"crossref","first-page":"2715","DOI":"10.2337\/db06-1294","article-title":"High glucose attenuates protein S-Nitrosylation in endothelial cells: role of oxidative stress","volume":"56","author":"Wadham","year":"2007","journal-title":"Diabetes"},{"key":"10.1016\/j.jlr.2026.101017_bib53","doi-asserted-by":"crossref","first-page":"2105","DOI":"10.1080\/15548627.2024.2340417","article-title":"Massive ER protein disposal by reticulophagy receptors and selective disposal by TOLLIP","volume":"20","author":"Hayashi","year":"2024","journal-title":"Autophagy"},{"key":"10.1016\/j.jlr.2026.101017_bib54","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1128\/MCB.00103-14","article-title":"Proteasome failure promotes positioning of lysosomes around the aggresome via local block of microtubule-dependent transport","volume":"34","author":"Zaarur","year":"2014","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jlr.2026.101017_bib55","doi-asserted-by":"crossref","first-page":"32667","DOI":"10.1074\/jbc.M404992200","article-title":"Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum","volume":"279","author":"Molteni","year":"2004","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Lipid Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002222752600043X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002222752600043X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T04:31:53Z","timestamp":1778733113000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002222752600043X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4]]},"references-count":55,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2026,4]]}},"alternative-id":["S002222752600043X"],"URL":"https:\/\/doi.org\/10.1016\/j.jlr.2026.101017","relation":{},"ISSN":["0022-2275"],"issn-type":[{"value":"0022-2275","type":"print"}],"subject":[],"published":{"date-parts":[[2026,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"S-nitrosylation contributes to ER stress and aggresome formation in secosterol-B-mediated endothelial dysfunction","name":"articletitle","label":"Article Title"},{"value":"Journal of Lipid Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jlr.2026.101017","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101017"}}