{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,17]],"date-time":"2026-04-17T10:12:08Z","timestamp":1776420728698,"version":"3.51.2"},"reference-count":45,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,10,1]],"date-time":"2024-10-01T00:00:00Z","timestamp":1727740800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100002341","name":"Research Council of Finland","doi-asserted-by":"publisher","award":["350636"],"award-info":[{"award-number":["350636"]}],"id":[{"id":"10.13039\/501100002341","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100001377","name":"Walther Cancer Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100001377","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"publisher","award":["HL122416"],"award-info":[{"award-number":["HL122416"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"publisher","award":["HL071818"],"award-info":[{"award-number":["HL071818"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"publisher","award":["F32HL131288"],"award-info":[{"award-number":["F32HL131288"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["molpharm.aspetjournals.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Pharmacology"],"published-print":{"date-parts":[[2024,10]]},"DOI":"10.1124\/molpharm.124.000932","type":"journal-article","created":{"date-parts":[[2024,8,16]],"date-time":"2024-08-16T19:50:14Z","timestamp":1723837814000},"page":"188-197","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"title":["Rescue of Familial Lecithin:Cholesterol Acyltranferase Deficiency Mutations with an Allosteric Activator"],"prefix":"10.1016","volume":"106","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3874-8228","authenticated-orcid":false,"given":"Kelly A.","family":"Manthei","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Grace E.","family":"Tremonti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Louise","family":"Chang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8679-3712","authenticated-orcid":false,"given":"Akseli","family":"Niemel\u00e4","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laura","family":"Giorgi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Artturi","family":"Koivuniemi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1125-3727","authenticated-orcid":false,"given":"John Joseph Grubb","family":"Tesmer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1124\/molpharm.124.000932_bib1","first-page":"19","article-title":"Gromacs: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1-2","author":"Abraham","year":"2015","journal-title":"Software X"},{"key":"10.1124\/molpharm.124.000932_bib2","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0010-4655(95)00042-E","article-title":"GROMACS: A message-passing parallel molecular dynamics implementation","volume":"91","author":"Berendsen","year":"1995","journal-title":"Comput Phys Commun"},{"key":"10.1124\/molpharm.124.000932_bib3","doi-asserted-by":"crossref","DOI":"10.1063\/1.2408420","article-title":"Canonical sampling through velocity rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J Chem Phys"},{"key":"10.1124\/molpharm.124.000932_bib400","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1161\/CIRCULATIONAHA.108.848143","article-title":"Functional lecithin: cholesterol acyltransferase is not required for efficient atheroprotection in humans","volume":"120","author":"Calabresi","year":"2009","journal-title":"Circulation"},{"key":"10.1124\/molpharm.124.000932_bib4","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1161\/01.ATV.0000175751.30616.13","article-title":"The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families","volume":"25","author":"Calabresi","year":"2005","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1124\/molpharm.124.000932_bib5","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.atherosclerosis.2011.11.034","article-title":"Genetic lecithin:cholesterol acyltransferase deficiency and cardiovascular disease","volume":"222","author":"Calabresi","year":"2012","journal-title":"Atherosclerosis"},{"key":"10.1124\/molpharm.124.000932_bib6","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1194\/jlr.M082685","article-title":"Interaction of lecithin:cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I-derived peptides","volume":"59","author":"Casteleijn","year":"2018","journal-title":"J Lipid Res"},{"key":"10.1124\/molpharm.124.000932_bib7","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1177\/1087057106292746","article-title":"Universal screening methods and applications of ThermoFluor","volume":"11","author":"Cummings","year":"2006","journal-title":"J Biomol Screen"},{"key":"10.1124\/molpharm.124.000932_bib8","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: An N\u00b7log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J Chem Phys"},{"key":"10.1124\/molpharm.124.000932_bib9","unstructured":"Dassuex J-L, Sekul R, Buttner K, Cornut I, Metz G, Dufourcq J. (1999) Apolipoprotein A-I agonists and their use to treat dyslipidemic disorders, US Patent 6,004,925."},{"key":"10.1124\/molpharm.124.000932_bib10","first-page":"375","article-title":"LCAT deficiency: molecular and phenotypic characterization of an Italian family","volume":"19","author":"Gigante","year":"2006","journal-title":"J Nephrol"},{"key":"10.1124\/molpharm.124.000932_bib11","doi-asserted-by":"crossref","first-page":"6250","DOI":"10.1038\/ncomms7250","article-title":"Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase","volume":"6","author":"Glukhova","year":"2015","journal-title":"Nat Commun"},{"key":"10.1124\/molpharm.124.000932_bib12","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/0140-6736(91)90665-C","article-title":"Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency","volume":"338","author":"Gotoda","year":"1991","journal-title":"Lancet"},{"key":"10.1124\/molpharm.124.000932_bib13","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0021-9150(97)06079-6","article-title":"Familial lecithin: cholesterol acyltransferase deficiency: molecular analysis of a compound heterozygote: LCAT (Arg147\u2192 Trp) and LCAT (Tyr171\u2192 Stop)","volume":"131","author":"Guerin","year":"1997","journal-title":"Atherosclerosis"},{"key":"10.1124\/molpharm.124.000932_bib14","doi-asserted-by":"crossref","first-page":"2799","DOI":"10.1074\/jbc.M115.672790","article-title":"Agonistic Human Antibodies Binding to Lecithin-Cholesterol Acyltransferase Modulate High Density Lipoprotein Metabolism","volume":"291","author":"Gunawardane","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1124\/molpharm.124.000932_bib15","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1186\/1472-6807-8-49","article-title":"HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures","volume":"8","author":"Ho","year":"2008","journal-title":"BMC Struct Biol"},{"key":"10.1124\/molpharm.124.000932_bib16","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J Mol Graph"},{"key":"10.1124\/molpharm.124.000932_bib17","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J Chem Phys"},{"key":"10.1124\/molpharm.124.000932_bib18","doi-asserted-by":"crossref","first-page":"9443","DOI":"10.1074\/jbc.270.16.9443","article-title":"In vitro expression of structural defects in the lecithin-cholesterol acyltransferase gene","volume":"270","author":"Klein","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1124\/molpharm.124.000932_bib19","series-title":"5-hydroxy-4-(trifluoromethyl)pyrazolopyridine derivative. U.S. patent 9796709","author":"Kobayashi","year":"2016"},{"key":"10.1124\/molpharm.124.000932_bib20","series-title":"Piperidinylpyrazolopyridine derivative, U.S. patent 9150575","author":"Kobayashi","year":"2015"},{"key":"10.1124\/molpharm.124.000932_bib21","series-title":"Condensed Pyrazole Derivative. U.S. patent 2015111545","author":"Kobayashi","year":"2015"},{"key":"10.1124\/molpharm.124.000932_bib22","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0022-2275(20)37433-2","article-title":"The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes","volume":"38","author":"Kuivenhoven","year":"1997","journal-title":"J Lipid Res"},{"key":"10.1124\/molpharm.124.000932_bib23","series-title":"Progress in Medicinal Chemistry","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/bs.pmch.2018.01.001","article-title":"Chapter Four - Recent Progress in the Discovery and Development of Small-Molecule Modulators of CFTR","author":"Kym","year":"2018"},{"key":"10.1124\/molpharm.124.000932_bib24","series-title":"Apolipoprotein Mimetics in the Management of Human Disease","first-page":"29","article-title":"Apolipoprotein Mimetic Peptides for Stimulating Cholesterol Efflux","author":"Li","year":"2015"},{"key":"10.1124\/molpharm.124.000932_bib25","doi-asserted-by":"crossref","first-page":"1950","DOI":"10.1002\/prot.22711","article-title":"Improved side-chain torsion potentials for the Amber ff99SB protein force field","volume":"78","author":"Lindorff-Larsen","year":"2010","journal-title":"Proteins"},{"key":"10.1124\/molpharm.124.000932_bib26","doi-asserted-by":"crossref","first-page":"20313","DOI":"10.1074\/jbc.M117.802736","article-title":"A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I","volume":"292","author":"Manthei","year":"2017","journal-title":"J Biol Chem"},{"key":"10.1124\/molpharm.124.000932_bib27","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.41604","article-title":"Molecular basis for activation of lecithin:cholesterol acyltransferase by a compound that increases HDL cholesterol","volume":"7","author":"Manthei","year":"2018","journal-title":"Elife"},{"key":"10.1124\/molpharm.124.000932_bib28","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1161\/01.ATV.15.4.460","article-title":"Two different allelic mutations in a Finnish family with lecithin:cholesterol acyltransferase deficiency","volume":"15","author":"Miettinen","year":"1995","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1124\/molpharm.124.000932_bib29","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1161\/01.ATV.18.4.591","article-title":"Molecular Genetic Study of Finns With Hypoalphalipoproteinemia and Hyperalphalipoproteinemia: A Novel Gly230Arg Mutation (LCATFin) of Lecithin:Cholesterol Acyltransferase (LCAT) Accounts for 5% of Cases With Very Low Serum HDL Cholesterol Levels","volume":"18","author":"Miettinen","year":"1998","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1124\/molpharm.124.000932_bib30","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0021-9150(03)00241-7","article-title":"A novel LCAT mutation (Phe382\u2192Val) in a kindred with familial LCAT deficiency and defective apolipoprotein B-100","volume":"170","author":"Nanjee","year":"2003","journal-title":"Atherosclerosis"},{"key":"10.1124\/molpharm.124.000932_bib31","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1008426","article-title":"Positive allosteric modulators of lecithin: Cholesterol acyltransferase adjust the orientation of the membrane-binding domain and alter its spatial free energy profile","volume":"17","author":"Niemel\u00e4","year":"2021","journal-title":"PLoS Comput Biol"},{"key":"10.1124\/molpharm.124.000932_bib32","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1161\/CIRCULATIONAHA.118.034706","article-title":"Complete and Partial Lecithin: Cholesterol Acyltransferase Deficiency is Differentially Associated with Atherosclerosis","volume":"138","author":"Oldoni","year":"2018","journal-title":"Circulation"},{"key":"10.1124\/molpharm.124.000932_bib33","series-title":"Imidazopyridine Derivative, (Organization WIP ed)","author":"Onoda","year":"2015"},{"key":"10.1124\/molpharm.124.000932_bib34","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0150083","article-title":"Lipoprotein X Causes Renal Disease in LCAT Deficiency","volume":"11","author":"Ossoli","year":"2016","journal-title":"PLoS One"},{"key":"10.1124\/molpharm.124.000932_bib35","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: A new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J Appl Phys"},{"key":"10.1124\/molpharm.124.000932_bib36","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1124\/jpet.120.000159","article-title":"Activation of Naturally Occurring Lecithin: Cholesterol Acyltransferase Mutants by a Novel Activator Compound","volume":"375","author":"Pavanello","year":"2020","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1124\/molpharm.124.000932_bib37","doi-asserted-by":"crossref","first-page":"1711","DOI":"10.1194\/jlr.M059873","article-title":"The high-resolution crystal structure of human LCAT","volume":"56","author":"Piper","year":"2015","journal-title":"J Lipid Res"},{"key":"10.1124\/molpharm.124.000932_bib38","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.jacl.2011.07.002","article-title":"Homozygous lecithin:cholesterol acyltransferase (LCAT) deficiency due to a new loss of function mutation and review of the literature","volume":"5","author":"Roshan","year":"2011","journal-title":"J Clin Lipidol"},{"key":"10.1124\/molpharm.124.000932_bib39","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1097\/MED.0b013e328329233b","article-title":"Lecithin: cholesterol acyltransferase\u2013from biochemistry to role in cardiovascular disease","volume":"16","author":"Rousset","year":"2009","journal-title":"Curr Opin Endocrinol Diabetes Obes"},{"key":"10.1124\/molpharm.124.000932_bib40","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.jacl.2015.12.007","article-title":"Familial lecithin:cholesterol acyltransferase deficiency: First-in-human treatment with enzyme replacement","volume":"10","author":"Shamburek","year":"2016","journal-title":"J Clin Lipidol"},{"key":"10.1124\/molpharm.124.000932_bib41","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/0014-5793(92)80795-I","article-title":"The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families","volume":"309","author":"Skretting","year":"1992","journal-title":"FEBS Lett"},{"key":"10.1124\/molpharm.124.000932_bib42","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/BF00193195","article-title":"Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele","volume":"85","author":"Taramelli","year":"1990","journal-title":"Hum Genet"},{"key":"10.1124\/molpharm.124.000932_bib43","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1016\/S0022-2275(20)32384-1","article-title":"Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease","volume":"41","author":"Vanloo","year":"2000","journal-title":"J Lipid Res"},{"key":"10.1124\/molpharm.124.000932_bib44","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1002\/jcc.20035","article-title":"Development and testing of a general amber force field","volume":"25","author":"Wang","year":"2004","journal-title":"J Comput Chem"}],"container-title":["Molecular Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026895X24018194?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026895X24018194?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1124\/molpharm.124.000932","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,26]],"date-time":"2025-02-26T02:36:20Z","timestamp":1740537380000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0026895X24018194"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10]]},"references-count":45,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2024,10]]}},"alternative-id":["S0026895X24018194"],"URL":"https:\/\/doi.org\/10.1124\/molpharm.124.000932","relation":{},"ISSN":["0026-895X"],"issn-type":[{"value":"0026-895X","type":"print"}],"subject":[],"published":{"date-parts":[[2024,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Rescue of Familial Lecithin:Cholesterol Acyltranferase Deficiency Mutations with an Allosteric Activator","name":"articletitle","label":"Article Title"},{"value":"Molecular Pharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1124\/molpharm.124.000932","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2024 American Society for Pharmacology and Experimental Therapeutics. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}