{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,19]],"date-time":"2026-08-19T17:43:44Z","timestamp":1787161424080,"version":"build-2736575974"},"reference-count":56,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,8,18]],"date-time":"2023-08-18T00:00:00Z","timestamp":1692316800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM067260"],"award-info":[{"award-number":["GM067260"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM135158"],"award-info":[{"award-number":["GM135158"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001659","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":[[2023,9]]},"DOI":"10.1016\/j.jlr.2023.100429","type":"journal-article","created":{"date-parts":[[2023,8,19]],"date-time":"2023-08-19T17:07:28Z","timestamp":1692464848000},"page":"100429","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"title":["Lipid clearance and amyloid formation by serum amyloid A: exploring the links between beneficial and pathologic actions of an enigmatic protein"],"prefix":"10.1016","volume":"64","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1616-5347","authenticated-orcid":false,"given":"Shobini","family":"Jayaraman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angela","family":"Urdaneta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2447-6209","authenticated-orcid":false,"given":"Esther","family":"Bullitt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2123-6816","authenticated-orcid":false,"given":"Marcus","family":"F\u00e4ndrich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8598-4824","authenticated-orcid":false,"given":"Olga","family":"Gursky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jlr.2023.100429_bib1","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3109\/13506129.2011.654294","article-title":"Acute-phase serum amyloid A: perspectives on its physiological and pathological roles","volume":"19","author":"Kisilevsky","year":"2012","journal-title":"Amyloid"},{"key":"10.1016\/j.jlr.2023.100429_bib2","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1615\/CritRevImmunol.v32.i4.40","article-title":"Immune functions of serum amyloid A","volume":"32","author":"Eklund","year":"2012","journal-title":"Crit. Rev. Immunol."},{"key":"10.1016\/j.jlr.2023.100429_bib3","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1189\/jlb.3VMR0315-080R","article-title":"Emerging functions of serum amyloid A in inflammation","volume":"98","author":"Ye","year":"2015","journal-title":"J.\u00a0Leukoc. Biol."},{"key":"10.1016\/j.jlr.2023.100429_bib4","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.2174\/0929867323666160418114600","article-title":"Structure and expression of different serum amyloid A (SAA) Variants and their concentration-dependent functions during host insults","volume":"23","author":"De Buck","year":"2016","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib5","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/s10020-018-0047-0","article-title":"Serum amyloid A - a review","volume":"24","author":"Sack","year":"2018","journal-title":"Mol. Med."},{"key":"10.1016\/j.jlr.2023.100429_bib6","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s11883-020-00901-4","article-title":"High-density lipoproteins and serum amyloid A (SAA)","volume":"23","author":"Webb","year":"2021","journal-title":"Curr. Atheroscler. Rep."},{"key":"10.1016\/j.jlr.2023.100429_bib7","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1146\/annurev-pathol-020712-163913","article-title":"AA amyloidosis: pathogenesis and targeted therapy","volume":"10","author":"Westermark","year":"2015","journal-title":"Annu. Rev. Pathol."},{"key":"10.1016\/j.jlr.2023.100429_bib8","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1194\/jlr.M054015","article-title":"A\u00a0brief elevation of serum amyloid A is sufficient to increase atherosclerosis","volume":"56","author":"Thompson","year":"2015","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jlr.2023.100429_bib9","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1093\/jnen\/nlab086","article-title":"Serum amyloid a is present in human saccular intracranial aneurysm walls and associates with aneurysm rupture","volume":"80","author":"Huuska","year":"2021","journal-title":"J.\u00a0Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.jlr.2023.100429_bib10","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1097\/MOL.0000000000000616","article-title":"Role of serum amyloid A in atherosclerosis","volume":"30","author":"Shridas","year":"2019","journal-title":"Curr. Opin. Lipidol."},{"key":"10.1016\/j.jlr.2023.100429_bib11","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1161\/ATVBAHA.118.310979","article-title":"Serum amyloid A is an exchangeable apolipoprotein","volume":"38","author":"Wilson","year":"2018","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.jlr.2023.100429_bib12","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1097\/MOL.0000000000000330","article-title":"The central role of arterial retention of cholesterol-rich apolipoprotein-B-containing lipoproteins in the pathogenesis of atherosclerosis: a triumph of simplicity","volume":"27","author":"Bor\u00e9n","year":"2016","journal-title":"Curr. Opin. Lipidol."},{"key":"10.1016\/j.jlr.2023.100429_bib13","doi-asserted-by":"crossref","first-page":"25669","DOI":"10.1074\/jbc.M112.363895","article-title":"Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation","volume":"287","author":"Noborn","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib14","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/nm0295-143","article-title":"Arresting amyloidosis in\u00a0vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer\u2019s disease","volume":"1","author":"Kisilevsky","year":"1995","journal-title":"Nat. Med."},{"key":"10.1016\/j.jlr.2023.100429_bib15","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s11883-020-00888-y","article-title":"Structural basis for vital function and malfunction of serum amyloid A: an acute-phase protein that wears hydrophobicity on its sleeve","volume":"22","author":"Gursky","year":"2020","journal-title":"Curr. Atheroscler. Rep."},{"key":"10.1016\/j.jlr.2023.100429_bib16","doi-asserted-by":"crossref","first-page":"19077","DOI":"10.1073\/pnas.1910713116","article-title":"Molecular basis for retinol binding by serum amyloid A during infection","volume":"116","author":"Hu","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jlr.2023.100429_bib17","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1080\/13506129.2016.1270930","article-title":"Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks","volume":"24","author":"Frame","year":"2017","journal-title":"Amyloid"},{"key":"10.1016\/j.jlr.2023.100429_bib18","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1002\/oby.20126","article-title":"Serum amyloid A is found on ApoB-containing lipoproteins in obese humans with diabetes","volume":"21","author":"Jahangiri","year":"2013","journal-title":"Obesity (Silver Spring)"},{"key":"10.1016\/j.jlr.2023.100429_bib19","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/978-3-319-17344-3_8","article-title":"Amyloid-forming properties of human apolipoproteins: sequence analyses and structural insights","volume":"855","author":"Das","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jlr.2023.100429_bib20","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.1016\/S0022-2275(20)33513-6","article-title":"SAA-only HDL formed during the acute phase response in apoA-I+\/+ and apoA-I-\/- mice","volume":"40","author":"Cabana","year":"1999","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jlr.2023.100429_bib21","doi-asserted-by":"crossref","first-page":"1542","DOI":"10.1194\/jlr.M600145-JLR200","article-title":"Serum amyloid A generates high density lipoprotein with cellular lipid in an ABCA1- or ABCA7-dependent manner","volume":"47","author":"Abe-Dohmae","year":"2006","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jlr.2023.100429_bib22","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1194\/jlr.RA119000329","article-title":"Serum amyloid A is not incorporated into HDL during HDL biogenesis","volume":"61","author":"Ji","year":"2020","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jlr.2023.100429_bib23","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.bbrc.2004.07.052","article-title":"Serum amyloid A promotes ABCA1-dependent and ABCA1-independent lipid efflux from cells","volume":"321","author":"Stonik","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jlr.2023.100429_bib24","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1074\/jbc.RA119.010626","article-title":"Serum amyloid A exhibits pH dependent antibacterial action and contributes to host defense against Staphylococcus aureus cutaneous infection","volume":"295","author":"Zheng","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib25","doi-asserted-by":"crossref","first-page":"5189","DOI":"10.1073\/pnas.1322357111","article-title":"Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis","volume":"111","author":"Lu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jlr.2023.100429_bib26","doi-asserted-by":"crossref","first-page":"1978","DOI":"10.1016\/j.jmb.2020.01.029","article-title":"Structural basis for lipid binding and function by an evolutionarily conserved protein, serum amyloid A","volume":"432","author":"Frame","year":"2020","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jlr.2023.100429_bib27","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.jsb.2017.06.007","article-title":"Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: a hypothetical function of SAA as a \u201cmolecular mop\u201d in immune response","volume":"200","author":"Frame","year":"2017","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.jlr.2023.100429_bib28","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.46630","article-title":"Synergy between serum amyloid A and secretory phospholipase A2","volume":"8","author":"Jayaraman","year":"2019","journal-title":"Elife"},{"key":"10.1016\/j.jlr.2023.100429_bib29","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1042\/bj3090461","article-title":"Serum amyloid A protein enhances the activity of secretory non-pancreatic phospholipase A2","volume":"309","author":"Pruzanski","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.jlr.2023.100429_bib30","doi-asserted-by":"crossref","first-page":"3532","DOI":"10.1039\/C8CC01424H","article-title":"Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner","volume":"54","author":"Jayaraman","year":"2018","journal-title":"Chem. Commun. (Camb)."},{"key":"10.1016\/j.jlr.2023.100429_bib31","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.chemphyslip.2016.11.004","article-title":"Effect of lipid environment on amyloid fibril formation of human serum amyloid A","volume":"202","author":"Tanaka","year":"2017","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jlr.2023.100429_bib32","doi-asserted-by":"crossref","first-page":"E6507","DOI":"10.1073\/pnas.1707120114","article-title":"Serum amyloid A forms stable oligomers that disrupt vesicles at lysosomal pH and contribute to the pathogenesis of reactive amyloidosis","volume":"114","author":"Jayaraman","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jlr.2023.100429_bib33","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.15252\/embr.201643411","article-title":"Cellular mechanism of fibril formation from serum amyloid A1 protein","volume":"18","author":"Claus","year":"2017","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jlr.2023.100429_bib34","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1016\/j.bbalip.2016.03.015","article-title":"CD36 actions in the heart: lipids, calcium, inflammation, repair and more?","volume":"1861","author":"Abumrad","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jlr.2023.100429_bib35","doi-asserted-by":"crossref","first-page":"8492","DOI":"10.1074\/jbc.M109.007526","article-title":"CD36 is a novel serum amyloid A (SAA) receptor mediating SAA binding and SAA-induced signaling in human and rodent cells","volume":"285","author":"Baranova","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib36","doi-asserted-by":"crossref","first-page":"8765","DOI":"10.1074\/jbc.M709195200","article-title":"Mapping and characterization of the binding site for specific oxidized phospholipids and oxidized low density lipoprotein of scavenger receptor CD36","volume":"283","author":"Kar","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib37","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/s41586-021-03818-3","article-title":"APRIL limits atherosclerosis by binding to heparan sulfate proteoglycans","volume":"597","author":"Tsiantoulas","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jlr.2023.100429_bib38","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1016\/j.febslet.2015.02.028","article-title":"Structural stability and functional remodeling of high-density lipoproteins","volume":"589","author":"Gursky","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jlr.2023.100429_bib39","article-title":"Binding to heparin triggers deleterious structural and biochemical changes in human low-density lipoprotein, which are amplified in hyperglycemia","volume":"1865","author":"Jayaraman","year":"2020","journal-title":"Biochim. Biophys. Acta Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.jlr.2023.100429_bib40","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1038\/s41467-019-09033-z","article-title":"Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids","volume":"10","author":"Liberta","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jlr.2023.100429_bib41","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1038\/s41467-021-27688-5","article-title":"Cryo-EM demonstrates the in\u00a0vitro proliferation of an ex\u00a0vivo amyloid fibril morphology by seeding","volume":"13","author":"Heerde","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jlr.2023.100429_bib42","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1042\/bj2560775","article-title":"Circular-dichroism studies on two murine serum amyloid A proteins","volume":"256","author":"McCubbin","year":"1988","journal-title":"Biochem. J."},{"key":"10.1016\/j.jlr.2023.100429_bib43","doi-asserted-by":"crossref","first-page":"15947","DOI":"10.1073\/pnas.252508399","article-title":"Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel","volume":"99","author":"Wang","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jlr.2023.100429_bib44","doi-asserted-by":"crossref","first-page":"3015","DOI":"10.1042\/BCJ20210146","article-title":"Per aspera ad chaos: a personal journey to the wonderland of intrinsic disorder","volume":"478","author":"Uversky","year":"2021","journal-title":"Biochem. J."},{"key":"10.1016\/j.jlr.2023.100429_bib45","doi-asserted-by":"crossref","first-page":"3203","DOI":"10.1111\/febs.16738","article-title":"Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1-42 aggregates","volume":"290","author":"Zhaliazka","year":"2023","journal-title":"FEBS J."},{"key":"10.1016\/j.jlr.2023.100429_bib46","doi-asserted-by":"crossref","first-page":"6810","DOI":"10.1038\/s41467-022-34552-7","article-title":"The 3D structure of lipidic fibrils of \u03b1-synuclein","volume":"13","author":"Frieg","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jlr.2023.100429_bib47","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1016\/j.tibs.2021.05.003","article-title":"Protein amyloid cofactors: charged side-chain arrays meet their match?","volume":"46","author":"Lewkowicz","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jlr.2023.100429_bib48","doi-asserted-by":"crossref","first-page":"5604","DOI":"10.1073\/pnas.1523496113","article-title":"Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits","volume":"113","author":"Kollmer","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jlr.2023.100429_bib49","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.3390\/vaccines10071119","article-title":"The big potential of small particles: lipid-based nanoparticles and exosomes in vaccination","volume":"10","author":"Shimon","year":"2022","journal-title":"Vaccines (Basel)"},{"key":"10.1016\/j.jlr.2023.100429_bib50","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/S0022-2275(20)38496-0","article-title":"Regulation of the metabolism of lipid emulsion model lipoproteins by a saturated acyl chain at the 2-position of triacylglycerol","volume":"29","author":"Mortimer","year":"1988","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.jlr.2023.100429_bib51","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/S0021-9258(18)64849-5","article-title":"A simple method for the isolation and purification of totallipides from animal tissues","volume":"226","author":"Folch","year":"1957","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib52","doi-asserted-by":"crossref","first-page":"6412","DOI":"10.1074\/jbc.M008128200","article-title":"Amyloid-beta interactions with chondroitin sulfate-derived monosaccharides and disaccharides. Implications for drug development","volume":"276","author":"Fraser","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jlr.2023.100429_bib53","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1110\/ps.073007207","article-title":"Cd36, a class B scavenger receptor, functions as a monomer to bind acetylated and oxidized low-density lipoproteins","volume":"16","author":"Martin","year":"2007","journal-title":"Protein Sci."},{"key":"10.1016\/j.jlr.2023.100429_bib54","doi-asserted-by":"crossref","first-page":"W90","DOI":"10.1093\/nar\/gkac345","article-title":"BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy","volume":"50","author":"Micsonai","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jlr.2023.100429_bib55","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.chemphyslip.2018.03.003","article-title":"Phase behavior of palmitoyl and egg sphingomyelin","volume":"213","author":"Arsov","year":"2018","journal-title":"Chem. Phys. Lipids"},{"key":"10.1016\/j.jlr.2023.100429_bib56","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.chemphyslip.2011.10.002","article-title":"Phosphatidylinositol induces fluid phase formation and packing defects in phosphatidylcholine model membranes","volume":"165","author":"Peng","year":"2012","journal-title":"Chem. Phys. Lipids"}],"container-title":["Journal of Lipid Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227523001025?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227523001025?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T18:33:16Z","timestamp":1758306796000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022227523001025"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,9]]},"references-count":56,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2023,9]]}},"alternative-id":["S0022227523001025"],"URL":"https:\/\/doi.org\/10.1016\/j.jlr.2023.100429","relation":{},"ISSN":["0022-2275"],"issn-type":[{"value":"0022-2275","type":"print"}],"subject":[],"published":{"date-parts":[[2023,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Lipid clearance and amyloid formation by serum amyloid A: exploring the links between beneficial and pathologic actions of an enigmatic protein","name":"articletitle","label":"Article Title"},{"value":"Journal of Lipid Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jlr.2023.100429","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"100429"}}