{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T03:06:00Z","timestamp":1791515160430,"version":"4.3.4"},"reference-count":90,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,6,17]],"date-time":"2026-06-17T00:00:00Z","timestamp":1781654400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Swiss National Science Foundation","doi-asserted-by":"publisher","award":["310030_207870"],"award-info":[{"award-number":["310030_207870"]}],"id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,8]]},"DOI":"10.1016\/j.jbc.2026.113268","type":"journal-article","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T16:17:27Z","timestamp":1781885847000},"page":"113268","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Phosphatidylethanolamine binds to human perilipins via a hydrophobic cleft in their 4-helix bundle domain for lipid droplet targeting"],"prefix":"10.1016","volume":"302","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2449-3167","authenticated-orcid":false,"given":"Jiri","family":"Stribny","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9102-8396","authenticated-orcid":false,"given":"Roger","family":"Schneiter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113268_bib1","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1161\/CIRCULATIONAHA.118.033704","article-title":"Deciphering the role of lipid droplets in cardiovascular disease: a report from the 2017 national heart, lung, and blood institute workshop","volume":"138","author":"Goldberg","year":"2018","journal-title":"Circulation"},{"key":"10.1016\/j.jbc.2026.113268_bib2","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/s12974-025-03334-5","article-title":"Lipid droplets in central nervous system and functional profiles of brain cells containing lipid droplets in various diseases","volume":"22","author":"Zhang","year":"2025","journal-title":"J. Neuroinflammation"},{"key":"10.1016\/j.jbc.2026.113268_bib3","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1146\/annurev-cellbio-012624-031419","article-title":"Lipid droplets big and small: basic mechanisms that make them all","volume":"40","author":"Klemm","year":"2024","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib4","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1186\/s12944-024-02212-y","article-title":"Roles of lipid droplets and related proteins in metabolic diseases","volume":"23","author":"Zhang","year":"2024","journal-title":"Lipids Health Dis."},{"key":"10.1016\/j.jbc.2026.113268_bib5","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2025.102758","article-title":"Lipid droplets: emerging therapeutic targets for age-related metabolic diseases","volume":"108","author":"Ma","year":"2025","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.jbc.2026.113268_bib6","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1146\/annurev-biochem-091724-013733","article-title":"Essential biology of lipid droplets","volume":"94","author":"Farese","year":"2025","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2026.113268_bib7","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202406019","article-title":"Lipid droplets: open questions and conceptual advances around a unique organelle","volume":"224","author":"Henne","year":"2025","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib8","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-nutr-071813-105410","article-title":"The perilipins: major cytosolic lipid droplet-associated proteins and their roles in cellular lipid storage, mobilization, and systemic homeostasis","volume":"36","author":"Kimmel","year":"2016","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.jbc.2026.113268_bib9","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.bbalip.2017.07.009","article-title":"The perilipin family of lipid droplet proteins: gatekeepers of intracellular lipolysis","volume":"1862","author":"Sztalryd","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.jbc.2026.113268_bib10","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1002\/1873-3468.14792","article-title":"Molecular mechanisms of perilipin protein function in lipid droplet metabolism","volume":"598","author":"Griseti","year":"2024","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.113268_bib11","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1194\/jlr.R700014-JLR200","article-title":"Thematic review series: adipocyte biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis","volume":"48","author":"Brasaemle","year":"2007","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib12","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1038\/s42255-021-00493-6","article-title":"Lipolysis: cellular mechanisms for lipid mobilization from fat stores","volume":"3","author":"Grabner","year":"2021","journal-title":"Nat. Metab."},{"key":"10.1016\/j.jbc.2026.113268_bib13","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/s41467-023-44559-3","article-title":"ApoL6 associates with lipid droplets and disrupts Perilipin1-HSL interaction to inhibit lipolysis","volume":"15","author":"Wang","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113268_bib14","doi-asserted-by":"crossref","DOI":"10.1002\/jcb.30579","article-title":"Perilipins: a family of five fat-droplet storing proteins that play a significant role in fat homeostasis","volume":"125","author":"Chandrasekaran","year":"2024","journal-title":"J. Cell Biochem."},{"key":"10.1016\/j.jbc.2026.113268_bib15","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1007\/s00335-01-2055-5","article-title":"The murine perilipin gene: the lipid droplet-associated perilipins derive from tissue-specific, mRNA splice variants and define a gene family of ancient origin","volume":"12","author":"Lu","year":"2001","journal-title":"Mamm. Genome"},{"key":"10.1016\/j.jbc.2026.113268_bib16","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.biochi.2013.08.026","article-title":"Perilipins: lipid droplet coat proteins adapted for tissue-specific energy storage and utilization, and lipid cytoprotection","volume":"96","author":"Sztalryd","year":"2014","journal-title":"Biochimie"},{"key":"10.1016\/j.jbc.2026.113268_bib17","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1093\/cvr\/cvae005","article-title":"Perilipin 1: a systematic review on its functions on lipid metabolism and atherosclerosis in mice and humans","volume":"120","author":"Desgrouas","year":"2024","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.jbc.2026.113268_bib18","doi-asserted-by":"crossref","first-page":"eaay8085","DOI":"10.1126\/science.aay8085","article-title":"Mammalian lipid droplets are innate immune hubs integrating cell metabolism and host defense","volume":"370","author":"Bosch","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113268_bib19","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1194\/jlr.R000034","article-title":"Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins","volume":"51","author":"Kimmel","year":"2010","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib20","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1016\/j.devcel.2023.05.006","article-title":"PLIN5 interacts with FATP4 at membrane contact sites to promote lipid droplet-to-mitochondria fatty acid transport","volume":"58","author":"Miner","year":"2023","journal-title":"Dev. Cell"},{"key":"10.1016\/j.jbc.2026.113268_bib21","first-page":"4067","article-title":"Perilipin family members preferentially sequester to either triacylglycerol-specific or cholesteryl-ester-specific intracellular lipid storage droplets","volume":"125","author":"Hsieh","year":"2012","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113268_bib22","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41467-018-03717-8","article-title":"A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets","volume":"9","author":"Copic","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113268_bib23","article-title":"Exceptional stability of a perilipin on lipid droplets depends on its polar residues, suggesting multimeric assembly","volume":"10","author":"Gim\u00e9nez-Andr\u00e9s","year":"2021","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2026.113268_bib24","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1091\/mbc.E18-08-0534","article-title":"Dual binding motifs underpin the hierarchical association of perilipins1-3 with lipid droplets","volume":"30","author":"Ajjaji","year":"2019","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113268_bib25","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2023.1116491","article-title":"Perilipin 3 promotes the formation of membrane domains enriched in diacylglycerol and lipid droplet biogenesis proteins","volume":"11","author":"Khaddaj","year":"2023","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib26","doi-asserted-by":"crossref","first-page":"3204","DOI":"10.1038\/s41467-023-38725-w","article-title":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation","volume":"14","author":"Choi","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.113268_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.105384","article-title":"Binding of perilipin 3 to membranes containing diacylglycerol is mediated by conserved residues within its PAT domain","volume":"299","author":"Stribny","year":"2023","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib28","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1016\/j.str.2004.04.021","article-title":"Structure of a lipid droplet protein; the PAT family member TIP47","volume":"12","author":"Hickenbottom","year":"2004","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.113268_bib29","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2215371120","article-title":"Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms","volume":"120","author":"Stuchell-Brereton","year":"2023","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113268_bib30","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbalip.2009.04.002","article-title":"PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores","volume":"1791","author":"Bickel","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113268_bib31","article-title":"Surface tension\u2013driven sorting of human perilipins on lipid droplets","volume":"223","author":"Ara\u00fajo","year":"2024","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib32","doi-asserted-by":"crossref","first-page":"5101","DOI":"10.1074\/jbc.M006775200","article-title":"TIP47 associates with lipid droplets","volume":"276","author":"Wolins","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib33","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1083\/jcb.200812042","article-title":"TIP47 functions in the biogenesis of lipid droplets","volume":"185","author":"Bulankina","year":"2009","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib34","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1194\/jlr.M086249","article-title":"Perilipin-2 deletion promotes carbohydrate-mediated browning of white adipose tissue at ambient temperature","volume":"59","author":"Libby","year":"2018","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib35","doi-asserted-by":"crossref","first-page":"1465","DOI":"10.1194\/jlr.M068205","article-title":"Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species","volume":"57","author":"Mirheydari","year":"2016","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib36","doi-asserted-by":"crossref","first-page":"265","DOI":"10.3390\/membranes11040265","article-title":"The C-Terminus of perilipin 3 shows distinct lipid binding at phospholipid-oil-aqueous interfaces","volume":"11","author":"Titus","year":"2021","journal-title":"Membranes (Basel)"},{"key":"10.1016\/j.jbc.2026.113268_bib37","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.molstruc.2014.03.009","article-title":"MicroScale Thermophoresis: interaction analysis and beyond","volume":"1077","author":"Jerabek-Willemsen","year":"2014","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.jbc.2026.113268_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.102834","article-title":"Validating an artificial organelle: studies of lipid droplet-specific proteins on adiposome platform","volume":"24","author":"Ma","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2026.113268_bib39","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1091\/mbc.12.4.997","article-title":"Roles of phosphatidylethanolamine and of its several biosynthetic pathways in Saccharomyces cerevisiae","volume":"12","author":"Birner","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113268_bib42","doi-asserted-by":"crossref","first-page":"27","DOI":"10.12688\/f1000research.21508.1","article-title":"Identifying orthologs with OMA: a primer","volume":"9","author":"Zahn-Zabal","year":"2020","journal-title":"F1000Res"},{"key":"10.1016\/j.jbc.2026.113268_bib43","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1093\/molbev\/mst010","article-title":"MAFFT multiple sequence alignment software version 7: improvements in performance and usability","volume":"30","author":"Katoh","year":"2013","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jbc.2026.113268_bib44","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2--a multiple sequence alignment editor and analysis workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2026.113268_bib45","doi-asserted-by":"crossref","first-page":"3891","DOI":"10.1021\/acs.jcim.1c00203","article-title":"AutoDock Vina 1.2.0: new docking methods, expanded force field, and Python bindings","volume":"61","author":"Eberhardt","year":"2021","journal-title":"J. Chem. Inf. Model"},{"key":"10.1016\/j.jbc.2026.113268_bib40","doi-asserted-by":"crossref","first-page":"W463","DOI":"10.1093\/nar\/gkaf361","article-title":"Plip 2025: introducing protein-protein interactions to the protein-ligand interaction profiler","volume":"53","author":"Schake","year":"2025","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113268_bib41","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.bbamem.2004.06.010","article-title":"Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile","volume":"1666","author":"van den Brink-van der Laan","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113268_bib46","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1002\/yea.320101105","article-title":"Characterization of lipid particles of the yeast, Saccharomyces cerevisiae","volume":"10","author":"Leber","year":"1994","journal-title":"Yeast"},{"key":"10.1016\/j.jbc.2026.113268_bib47","doi-asserted-by":"crossref","first-page":"6062","DOI":"10.1074\/jbc.270.11.6062","article-title":"Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae","volume":"270","author":"Trotter","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib48","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/j.bbalip.2009.12.008","article-title":"Phosphatidylethanolamine synthesized by four different pathways is supplied to the plasma membrane of the yeast Saccharomyces cerevisiae","volume":"1801","author":"Schuiki","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113268_bib52","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1186\/1471-2105-7-339","article-title":"Tools for integrated sequence-structure analysis with UCSF Chimera","volume":"7","author":"Meng","year":"2006","journal-title":"BMC Bioinform."},{"key":"10.1016\/j.jbc.2026.113268_bib53","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.114093","article-title":"Perilipin membrane integration determines lipid droplet heterogeneity in differentiating adipocytes","volume":"43","author":"Majchrzak","year":"2024","journal-title":"Cell Rep."},{"key":"10.1016\/j.jbc.2026.113268_bib54","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.cub.2018.02.020","article-title":"Architecture of lipid droplets in endoplasmic reticulum is determined by Phospholipid intrinsic curvature","volume":"28","author":"Choudhary","year":"2018","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib55","doi-asserted-by":"crossref","first-page":"7051","DOI":"10.1021\/bi500918m","article-title":"Structural and functional assessment of perilipin 2 lipid binding domain(s)","volume":"53","author":"Najt","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113268_bib56","doi-asserted-by":"crossref","DOI":"10.1242\/bio.058516","article-title":"Conditional targeting of phosphatidylserine decarboxylase to lipid droplets","volume":"10","author":"Kumar","year":"2021","journal-title":"Biol. Open"},{"key":"10.1016\/j.jbc.2026.113268_bib57","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.devcel.2017.11.023","article-title":"Lipid homeostasis is maintained by dual targeting of the mitochondrial PE biosynthesis enzyme to the ER","volume":"44","author":"Friedman","year":"2018","journal-title":"Dev. Cell"},{"key":"10.1016\/j.jbc.2026.113268_bib58","doi-asserted-by":"crossref","first-page":"ar11","DOI":"10.1091\/mbc.E21-11-0558-T","article-title":"ER-localized phosphatidylethanolamine synthase plays a conserved role in lipid droplet formation","volume":"33","author":"Gok","year":"2022","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2026.113268_bib59","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1083\/jcb.201610013","article-title":"Pet10p is a yeast perilipin that stabilizes lipid droplets and promotes their assembly","volume":"216","author":"Gao","year":"2017","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib60","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2024.1491815","article-title":"Molecular mechanisms of lipid droplets-mitochondria coupling in obesity and metabolic syndrome: insights and pharmacological implications","volume":"15","author":"Zhang","year":"2024","journal-title":"Front. Physiol."},{"key":"10.1016\/j.jbc.2026.113268_bib61","doi-asserted-by":"crossref","first-page":"230","DOI":"10.3390\/cells7120230","article-title":"Decreasing phosphatidylcholine on the surface of the lipid droplet correlates with altered protein binding and steatosis","volume":"7","author":"Listenberger","year":"2018","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2026.113268_bib62","article-title":"Changing the phospholipid composition of lipid droplets alters localization of select lipid droplet proteins","volume":"2023","author":"Renier","year":"2023","journal-title":"Micropubl. Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib63","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1002\/hep.22268","article-title":"Differential pattern of lipid droplet-associated proteins and de novo perilipin expression in hepatocyte steatogenesis","volume":"47","author":"Straub","year":"2008","journal-title":"Hepatology"},{"key":"10.1016\/j.jbc.2026.113268_bib64","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1111\/j.1530-0277.2008.00624.x","article-title":"Adipose differentiation-related protein is a reliable lipid droplet marker in alcoholic fatty liver of rats","volume":"32","author":"Mak","year":"2008","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.jbc.2026.113268_bib65","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1111\/acer.12075","article-title":"Temporal effects of ethanol consumption on energy homeostasis, hepatic steatosis, and insulin sensitivity in mice","volume":"37","author":"Carr","year":"2013","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.jbc.2026.113268_bib66","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1111\/j.1530-0277.2011.01434.x","article-title":"Chronic ethanol consumption in mice alters hepatocyte lipid droplet properties","volume":"35","author":"Orlicky","year":"2011","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.jbc.2026.113268_bib67","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1111\/acer.12271","article-title":"Rab GTPases associate with isolated lipid droplets (LDs) and show altered content after ethanol administration: potential role in alcohol-impaired LD metabolism","volume":"38","author":"Rasineni","year":"2014","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.jbc.2026.113268_bib68","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1111\/acer.15446","article-title":"Lipid droplet-associated proteins in alcohol-associated fatty liver disease: a proteomic approach","volume":"48","author":"Perumal","year":"2024","journal-title":"Alcohol. Clin. Exp. Res. (Hoboken)"},{"key":"10.1016\/j.jbc.2026.113268_bib69","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1194\/jlr.M035063","article-title":"Perilipin-2-null mice are protected against diet-induced obesity, adipose inflammation, and fatty liver disease","volume":"54","author":"McManaman","year":"2013","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib70","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0097118","article-title":"Absence of perilipin 2 prevents hepatic steatosis, glucose intolerance and ceramide accumulation in alcohol-fed mice","volume":"9","author":"Carr","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113268_bib71","doi-asserted-by":"crossref","DOI":"10.1016\/j.jlr.2024.100635","article-title":"Therapeutic siRNA targeting PLIN2 ameliorates steatosis, inflammation, and fibrosis in steatotic liver disease models","volume":"65","author":"Wang","year":"2024","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113268_bib72","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1056\/NEJMoa1007487","article-title":"Perilipin deficiency and autosomal dominant partial lipodystrophy","volume":"364","author":"Gandotra","year":"2011","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.jbc.2026.113268_bib73","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2020.101569","article-title":"Lipid droplets maintain energy homeostasis and glioblastoma growth via Autophagic release of stored fatty acids","volume":"23","author":"Wu","year":"2020","journal-title":"iScience"},{"key":"10.1016\/j.jbc.2026.113268_bib74","doi-asserted-by":"crossref","first-page":"4013","DOI":"10.3390\/cancers15154013","article-title":"Challenges in pharmacological intervention in perilipins (PLINs) to modulate lipid droplet dynamics in obesity and cancer","volume":"15","author":"Bombarda-Rocha","year":"2023","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.jbc.2026.113268_bib75","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1111\/liv.15775","article-title":"Perilipin 5 protects the mitochondrial oxidative functions and improves the alcoholic liver injury in mice","volume":"44","author":"Gao","year":"2024","journal-title":"Liver Int."},{"key":"10.1016\/j.jbc.2026.113268_bib79","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1111\/1574-6968.12351","article-title":"Recombinant protein expression in Lactococcus lactis using the P170 expression system","volume":"351","author":"J\u00f8rgensen","year":"2014","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.jbc.2026.113268_bib80","first-page":"5198","article-title":"Expression of oleosin and perilipins in yeast promotes formation of lipid droplets from the endoplasmic reticulum","volume":"126","author":"Jacquier","year":"2013","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.jbc.2026.113268_bib81","doi-asserted-by":"crossref","first-page":"3312","DOI":"10.1021\/acsnano.5b06852","article-title":"Construction of Nanodroplet\/Adiposome and artificial lipid droplets","volume":"10","author":"Wang","year":"2016","journal-title":"ACS Nano"},{"key":"10.1016\/j.jbc.2026.113268_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.xpro.2022.101214","article-title":"Protocol for using artificial lipid droplets to study the binding affinity of lipid droplet-associated proteins","volume":"3","author":"Zhi","year":"2022","journal-title":"STAR Protoc."},{"key":"10.1016\/j.jbc.2026.113268_bib83","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1002\/jcc.20945","article-title":"CHARMM-GUI: a web-based graphical user interface for CHARMM","volume":"29","author":"Jo","year":"2008","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib84","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.bpj.2009.04.013","article-title":"CHARMM-GUI membrane builder for mixed bilayers and its application to yeast membranes","volume":"97","author":"Jo","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2026.113268_bib85","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","article-title":"Accurate structure prediction of biomolecular interactions with AlphaFold 3","volume":"630","author":"Abramson","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113268_bib86","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein modelling by satisfaction of spatial restraints","volume":"234","author":"Sali","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113268_bib87","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1021\/acs.jctc.5b00935","article-title":"CHARMM-GUI input generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM\/OpenMM simulations using the CHARMM36 additive force field","volume":"12","author":"Lee","year":"2016","journal-title":"J. Chem. Theor. Comput"},{"key":"10.1016\/j.jbc.2026.113268_bib88","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1021\/acs.jpcb.3c06662","article-title":"OpenMM 8: molecular dynamics simulation with machine learning potentials","volume":"128","author":"Eastman","year":"2024","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jbc.2026.113268_bib89","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an N\u22c5log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jbc.2026.113268_bib90","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1002\/jcc.21787","article-title":"MDAnalysis: a toolkit for the analysis of molecular dynamics simulations","volume":"32","author":"Michaud-Agrawal","year":"2011","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib91","doi-asserted-by":"crossref","first-page":"98","DOI":"10.25080\/Majora-629e541a-00e","article-title":"MDAnalysis: a python package for the rapid analysis of molecular dynamics simulations","author":"Gowers","year":"2016","journal-title":"Proc. Python Sci. Conf."},{"key":"10.1016\/j.jbc.2026.113268_bib92","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2026.113268_bib93","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib94","doi-asserted-by":"crossref","first-page":"D1373","DOI":"10.1093\/nar\/gkac956","article-title":"PubChem 2023 update","volume":"51","author":"Kim","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113268_bib95","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jbc.2026.113268_bib96","doi-asserted-by":"crossref","first-page":"W299","DOI":"10.1093\/nar\/gki370","article-title":"ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures","volume":"33","author":"Landau","year":"2005","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582602140X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582602140X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T19:36:17Z","timestamp":1787254577000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582602140X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8]]},"references-count":90,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2026,8]]}},"alternative-id":["S002192582602140X"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113268","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phosphatidylethanolamine binds to human perilipins via a hydrophobic cleft in their 4-helix bundle domain for lipid droplet targeting","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113268","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":"113268"}}