{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T03:37:56Z","timestamp":1792813076133,"version":"4.5.0"},"reference-count":81,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,7]],"date-time":"2025-01-07T00:00:00Z","timestamp":1736208000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100023581","name":"National Science Foundation Graduate Research Fellowship Program","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100023581","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000009","name":"Foundation for the National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000009","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":[[2025,2]]},"DOI":"10.1016\/j.jbc.2025.108168","type":"journal-article","created":{"date-parts":[[2025,1,8]],"date-time":"2025-01-08T23:52:24Z","timestamp":1736380344000},"page":"108168","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"title":["Liver fatty acid binding protein FABP1 transfers substrates to cytochrome P450 4A11 for catalysis"],"prefix":"10.1016","volume":"301","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0027-9120","authenticated-orcid":false,"given":"Kevin D.","family":"McCarty","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7458-3048","authenticated-orcid":false,"given":"F. Peter","family":"Guengerich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.108168_bib1","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/1479-7364-5-3-170","article-title":"The human fatty acid-binding protein family: evolutionary divergences and functions","volume":"5","author":"Smathers","year":"2011","journal-title":"Hum. Genomics."},{"key":"10.1016\/j.jbc.2025.108168_bib2","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev.nutr.27.061406.093710","article-title":"The emerging functions and mechanisms of mammalian fatty acid-binding proteins","volume":"28","author":"Storch","year":"2008","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.jbc.2025.108168_bib3","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1002\/path.2440","article-title":"The human protein atlas\u2013a tool for pathology","volume":"216","author":"Pont\u00e9n","year":"2008","journal-title":"J.\u00a0Pathol."},{"key":"10.1016\/j.jbc.2025.108168_bib4","doi-asserted-by":"crossref","first-page":"2238","DOI":"10.1194\/jlr.R056705","article-title":"Recent insights into the biological functions of liver fatty acid binding protein 1","volume":"56","author":"Wang","year":"2015","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2025.108168_bib5","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.plefa.2010.02.029","article-title":"Fatty acid transport across the cell membrane: regulation by fatty acid transporters","volume":"82","author":"Schwenk","year":"2010","journal-title":"Prostaglandins Leukot. Essent. Fatty. Acids."},{"key":"10.1016\/j.jbc.2025.108168_bib6","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1016\/S0021-9258(19)56992-7","article-title":"Role of hemoprotein P-450 in fatty acid \u03c9-hydroxylation in a soluble enzyme system from liver microsomes","volume":"243","author":"Lu","year":"1968","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib7","series-title":"Cytochrome P450: Structure, Mechanism, and Biochemistry","first-page":"523","article-title":"Human cytochromes P450","author":"Guengerich","year":"2015"},{"key":"10.1016\/j.jbc.2025.108168_bib8","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.3390\/nu14091784","article-title":"CRABPs alter all-trans-retinoic acid metabolism by CYP26A1 via protein-protein interactions","volume":"14","author":"Yabut","year":"2022","journal-title":"Nutrients"},{"key":"10.1016\/j.jbc.2025.108168_bib9","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1002\/1873-3468.12303","article-title":"Direct protein-protein interactions and substrate channeling between cellular retinoic acid binding proteins and CYP26B1","volume":"590","author":"Nelson","year":"2016","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2025.108168_bib10","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1124\/mol.117.111039","article-title":"CYP26C1 Is a hydroxylase of multiple active retinoids and interacts with cellular retinoic acid binding proteins","volume":"93","author":"Zhong","year":"2018","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.jbc.2025.108168_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.101142","article-title":"Cellular retinoid-binding proteins transfer retinoids to human cytochrome P450 27C1 for desaturation","volume":"297","author":"Glass","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib12","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1124\/molpharm.124.000878","article-title":"Drugs form ternary complexes with human liver fatty acid binding protein 1 (FABP1) and FABP1 binding alters drug metabolism","volume":"105","author":"Yabut","year":"2024","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.jbc.2025.108168_bib13","doi-asserted-by":"crossref","DOI":"10.1016\/j.bcp.2024.116191","article-title":"CYP2C9, CYP3A and CYP2C19 metabolize \u03949-tetrahydrocannabinol to multiple metabolites but metabolism is affected by human liver fatty acid binding protein (FABP1)","volume":"228","author":"Yabut","year":"2024","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.jbc.2025.108168_bib14","doi-asserted-by":"crossref","first-page":"5435","DOI":"10.1016\/j.bbagen.2013.05.005","article-title":"Albumin-drug interaction and its clinical implication","volume":"1830","author":"Yamasaki","year":"2013","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.jbc.2025.108168_bib15","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1080\/13543776.2016.1182500","article-title":"Fatty acid binding protein (FABP) inhibitors: a patent review (2012-2015)","volume":"26","author":"Wang","year":"2016","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.jbc.2025.108168_bib16","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1038\/nrd2589","article-title":"Fatty acid-binding proteins: role in metabolic diseases and potential as drug targets","volume":"7","author":"Furuhashi","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.jbc.2025.108168_bib17","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116358","article-title":"Design, synthesis, and biological evaluation of first-in-class FABP1 inhibitors for the treatment of NASH","volume":"270","author":"Chen","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.drudis.2023.103560","article-title":"Exploring human CYP4 enzymes: physiological roles, function in diseases and focus on inhibitors","volume":"28","author":"Zhou","year":"2023","journal-title":"Drug. Discov. Today."},{"key":"10.1016\/j.jbc.2025.108168_bib19","doi-asserted-by":"crossref","first-page":"309s","DOI":"10.18433\/jpps30246","article-title":"The antioxidant activity of recombinant rat hepatic fatty acid binding protein T94A variant","volume":"21","author":"Le","year":"2018","journal-title":"J.\u00a0Pharm. Pharm. Sci."},{"key":"10.1016\/j.jbc.2025.108168_bib20","doi-asserted-by":"crossref","first-page":"3523","DOI":"10.1194\/jlr.D040782","article-title":"LC\/ESI-MS\/MS detection of FAs by charge reversal derivatization with more than four orders of magnitude improvement in sensitivity","volume":"54","author":"Bollinger","year":"2013","journal-title":"J.\u00a0Lipid. Res."},{"key":"10.1016\/j.jbc.2025.108168_bib21","doi-asserted-by":"crossref","first-page":"3544","DOI":"10.1021\/acs.analchem.3c05431","article-title":"Studies of labware contamination during lipid extraction in mass spectrometry-based lipidome analysis","volume":"96","author":"Canez","year":"2024","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib22","doi-asserted-by":"crossref","first-page":"5947","DOI":"10.1038\/s41598-021-85288-1","article-title":"Development of an optimized sample preparation method for quantification of free fatty acids in food using liquid chromatography-mass spectrometry","volume":"11","author":"Park","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2025.108168_bib23","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1042\/bj2380419","article-title":"Studies on fatty acid-binding proteins. The detection and quantification of the protein from rat liver by using a fluorescent fatty acid analogue","volume":"238","author":"Wilkinson","year":"1986","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2025.108168_bib24","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0006-3495(96)79592-9","article-title":"Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein","volume":"70","author":"Kirk","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2025.108168_bib25","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1016\/j.chembiol.2014.08.015","article-title":"Versatility of acyl-acyl carrier protein synthetases","volume":"21","author":"Beld","year":"2014","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2025.108168_bib26","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0026-895X(25)14748-2","article-title":"Spectral studies of drug interaction with hepatic microsomal cytochrome","volume":"3","author":"Schenkman","year":"1967","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.jbc.2025.108168_bib27","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2023.104841","article-title":"Processive kinetics in the three-step lanosterol 14\u03b1-demethylation reaction catalyzed by human cytochrome P450 51A1","volume":"299","author":"McCarty","year":"2023","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib28","article-title":"The multistep oxidation of cholesterol to pregnenolone by human cytochrome P450 11A1 is highly processive","volume":"300","author":"McCarty","year":"2023","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100571","article-title":"Tight binding of cytochrome b5 to cytochrome P450 17A1 is a critical feature of stimulation of C21 steroid lyase activity and androgen synthesis","volume":"296","author":"Kim","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib30","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2021.109076","article-title":"Binding of cytochrome P450 27C1, a retinoid desaturase, to its accessory protein adrenodoxin","volume":"714","author":"Glass","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.108168_bib31","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1021\/tx00016a015","article-title":"Mechanism-based inactivation of human liver microsomal cytochrome P-450 IIIA4 by gestodene","volume":"3","author":"Guengerich","year":"1990","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.jbc.2025.108168_bib32","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1124\/dmd.122.001010","article-title":"Impact of intracellular lipid binding proteins on endogenous and xenobiotic ligand metabolism and disposition","volume":"51","author":"Yabut","year":"2023","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.jbc.2025.108168_bib33","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.jchromb.2008.04.011","article-title":"A\u00a0protocol for the combined sub-fractionation and delipidation of lipid binding proteins using hydrophobic interaction chromatography","volume":"867","author":"Velkov","year":"2008","journal-title":"J.\u00a0Chromatogr. B. Analyt. Technol. Biomed. Life Sci."},{"key":"10.1016\/j.jbc.2025.108168_bib34","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1002\/jms.3237","article-title":"Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein","volume":"48","author":"Santambrogio","year":"2013","journal-title":"J.\u00a0Mass. Spectrom."},{"key":"10.1016\/j.jbc.2025.108168_bib35","doi-asserted-by":"crossref","first-page":"31924","DOI":"10.1074\/jbc.M111.270165","article-title":"Fatty acid induced remodeling within the human liver fatty acid-binding protein","volume":"286","author":"Sharma","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib36","doi-asserted-by":"crossref","first-page":"7140","DOI":"10.1074\/jbc.272.11.7140","article-title":"The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates","volume":"272","author":"Thompson","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib37","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/0005-2760(95)00170-0","article-title":"Analysis of the ligand binding properties of recombinant bovine liver-type fatty acid binding protein","volume":"1259","author":"Rolf","year":"1995","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.108168_bib38","doi-asserted-by":"crossref","first-page":"31068","DOI":"10.1074\/jbc.271.49.31068","article-title":"Thermodynamic and kinetic properties of fatty acid interactions with rat liver fatty acid-binding protein","volume":"271","author":"Richieri","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib39","doi-asserted-by":"crossref","first-page":"7197","DOI":"10.1021\/bi000314z","article-title":"Fatty acid binding proteins from different tissues show distinct patterns of fatty acid interactions","volume":"39","author":"Richieri","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.108168_bib40","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1021\/bi001602y","article-title":"Binding of cytochrome P450 monooxygenase and lipoxygenase pathway products by heart fatty acid-binding protein","volume":"40","author":"Widstrom","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.108168_bib41","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1177\/0115426592007004179","article-title":"The essential fatty acids","volume":"7","author":"Sardesai","year":"1992","journal-title":"Nutr. Clin. Pract."},{"key":"10.1016\/j.jbc.2025.108168_bib42","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1111\/febs.12780","article-title":"Structural and functional interaction of fatty acids with human liver fatty acid-binding protein (L-FABP) T94A variant","volume":"281","author":"Huang","year":"2014","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2025.108168_bib43","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/S0022-2275(20)31495-4","article-title":"Very long chain n-3 and n-6 polyunsaturated fatty acids bind strongly to liver fatty acid-binding protein","volume":"43","author":"Norris","year":"2002","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2025.108168_bib44","doi-asserted-by":"crossref","first-page":"6161","DOI":"10.1021\/bi500710e","article-title":"Kinetic analysis of lauric acid hydroxylation by human cytochrome P450 4A11","volume":"53","author":"Kim","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.108168_bib45","doi-asserted-by":"crossref","first-page":"10928","DOI":"10.1074\/jbc.RA119.009305","article-title":"Human cytochrome P450 enzymes bind drugs and other substrates mainly through conformational-selection modes","volume":"294","author":"Guengerich","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib46","doi-asserted-by":"crossref","first-page":"23055","DOI":"10.1074\/jbc.273.36.23055","article-title":"The catalytic site of cytochrome P450 4A11 (CYP4A11) and its L131F mutant","volume":"273","author":"Dierks","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib47","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1006\/abbi.1996.0429","article-title":"Effects of steric bulk and conformational rigidity on fatty acid omega hydroxylation by a cytochrome P450 4A1 fusion protein","volume":"334","author":"Bambal","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.108168_bib48","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.105688","article-title":"Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase","volume":"300","author":"Tateishi","year":"2024","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib49","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1006\/abbi.1994.1435","article-title":"Influence of ionic strength on the P450 monooxygenase reaction and role of cytochrome b5 in the process","volume":"314","author":"Schenkman","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.108168_bib50","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1006\/bbrc.1999.0455","article-title":"Electrostatic interaction between cytochrome P450 and NADPH-P450 reductase: comparison of mixed and fused systems consisting of rat cytochrome P450 1A1 and yeast NADPH-P450 reductase","volume":"257","author":"Kondo","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2025.108168_bib51","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.abb.2010.10.002","article-title":"Simultaneous measurement of CYP1A2 activity, regioselectivity, and coupling: implications for environmental sensitivity of enzyme-substrate binding","volume":"505","author":"Traylor","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.108168_bib52","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1002\/jbt.10054","article-title":"Biochemical characteristics of purified beef liver NADPH-cytochrome P450 reductase","volume":"16","author":"Arinc","year":"2002","journal-title":"J.\u00a0Biochem. Mol. Toxicol."},{"key":"10.1016\/j.jbc.2025.108168_bib53","doi-asserted-by":"crossref","first-page":"12768","DOI":"10.1021\/bi00039a037","article-title":"Effect of ionic strength on the kinetic mechanism and relative rate limitation of steps in the model NADPH-cytochrome P450 oxidoreductase reaction with cytochrome c","volume":"34","author":"Sem","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.108168_bib54","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0021-9258(18)48461-X","article-title":"Free fatty acid transfer from rat liver fatty acid-binding protein to phospholipid vesicles. Effect of ligand and solution properties","volume":"267","author":"Kim","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib55","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S1388-1981(99)00146-8","article-title":"Liver fatty acid binding protein: species variation and the accommodation of different ligands","volume":"1441","author":"Thompson","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2025.108168_bib56","doi-asserted-by":"crossref","first-page":"11230","DOI":"10.1074\/jbc.M117.792200","article-title":"Heme-thiolate sulfenylation of human cytochrome P450 4A11 functions as a redox switch for catalytic inhibition","volume":"292","author":"Albertolle","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib57","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.RA120.016855","article-title":"Kinetics of cytochrome P450 3A4 inhibition by heterocyclic drugs defines a general sequential multistep binding process","volume":"296","author":"Guengerich","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib58","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100969","article-title":"Stepwise binding of inhibitors to human cytochrome P450 17A1 and rapid kinetics of inhibition of androgen biosynthesis","volume":"297","author":"Guengerich","year":"2021","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib59","doi-asserted-by":"crossref","first-page":"7827","DOI":"10.1016\/S0021-9258(19)39004-0","article-title":"Transfer of fluorescent fatty acids from liver and heart fatty acid-binding proteins to model membranes","volume":"265","author":"Storch","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib60","doi-asserted-by":"crossref","first-page":"48395","DOI":"10.1074\/jbc.M208141200","article-title":"Effect of charge reversal mutations on the ligand- and membrane-binding properties of liver fatty acid-binding protein","volume":"277","author":"Davies","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib61","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1021\/bi991638u","article-title":"Binding of fatty acids and peroxisome proliferators to orthologous fatty acid binding proteins from human, murine, and bovine liver","volume":"39","author":"Wolfrum","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2025.108168_bib62","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1194\/jlr.M900058-JLR200","article-title":"L-FABP directly interacts with PPAR\u03b1 in cultured primary hepatocytes","volume":"50","author":"Hostetler","year":"2009","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.jbc.2025.108168_bib63","doi-asserted-by":"crossref","first-page":"27475","DOI":"10.1074\/jbc.270.46.27475","article-title":"Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c","volume":"270","author":"Shen","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib64","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1161\/01.CIR.0000151309.82473.59","article-title":"Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension","volume":"111","author":"Gainer","year":"2005","journal-title":"Circulation"},{"key":"10.1016\/j.jbc.2025.108168_bib65","doi-asserted-by":"crossref","first-page":"40319","DOI":"10.1074\/jbc.M508171200","article-title":"Analysis of coumarin 7-hydroxylation activity of cytochrome P450 2A6 using random mutagenesis","volume":"280","author":"Kim","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib66","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1006\/abbi.1997.0534","article-title":"Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities","volume":"350","author":"Hanna","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.108168_bib67","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1021\/acscatal.0c04455","article-title":"Kinetic evidence for an induced fit mechanism in the binding of the substrate camphor by cytochrome P450cam","volume":"11","author":"Guengerich","year":"2021","journal-title":"ACS. Catal."},{"key":"10.1016\/j.jbc.2025.108168_bib68","doi-asserted-by":"crossref","first-page":"4371","DOI":"10.1021\/acs.biochem.7b00564","article-title":"Putidaredoxin binds to the same site on cytochrome P450cam in the open and closed conformation","volume":"56","author":"Liou","year":"2017","journal-title":"Biochemistry."},{"key":"10.1016\/j.jbc.2025.108168_bib69","doi-asserted-by":"crossref","first-page":"2370","DOI":"10.1016\/S0021-9258(20)82244-3","article-title":"The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature","volume":"239","author":"Omura","year":"1964","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib70","series-title":"The Proteomics Protocols Handbook","first-page":"571","article-title":"Protein identification and analysis tools on the ExPASy server","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.jbc.2025.108168_bib71","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0076-6879(72)25041-8","article-title":"Reaction of protein sulfhydryl groups with Ellman's reagent","volume":"25","author":"Habeeb","year":"1972","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2025.108168_bib72","doi-asserted-by":"crossref","first-page":"15016","DOI":"10.1021\/ja508185d","article-title":"Mechanism of the third oxidative step in the conversion of androgens to estrogens by cytochrome P450 19A1 steroid aromatase","volume":"136","author":"Yoshimoto","year":"2014","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2025.108168_bib73","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202317711","article-title":"Oxygen-18 labeling reveals a dominant ferric peroxide mechanism and Baeyer-Villiger intermediate in cytochrome P450 51A lanosterol 14\u03b1-demethylation","volume":"63","author":"McCarty","year":"2024","journal-title":"Angew. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib74","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1042\/bj3140943","article-title":"Mutations of recombinant rat liver fatty acid-binding protein at residues 102 and 122 alter its structural integrity and affinity for physiological ligands","volume":"314","author":"Thumser","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2025.108168_bib75","series-title":"Kinetic Analysis for the New Enzymology","first-page":"108","author":"Johnson","year":"2019"},{"key":"10.1016\/j.jbc.2025.108168_bib76","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.ab.2008.12.024","article-title":"Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data","volume":"387","author":"Johnson","year":"2009","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2025.108168_bib77","series-title":"Physical Chemistry","first-page":"330","author":"Daniels","year":"1966"},{"key":"10.1016\/j.jbc.2025.108168_bib78","series-title":"Hayes' Principles and Methods of Toxicology","first-page":"1905","article-title":"Analysis and characterization of enzymes and nucleic acids relevant to toxicology","author":"Guengerich","year":"2014"},{"key":"10.1016\/j.jbc.2025.108168_bib79","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/0003-2697(92)90279-G","article-title":"Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins","volume":"200","author":"Mach","year":"1992","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jbc.2025.108168_bib80","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3762\/bjoc.15.2","article-title":"New standards for collecting and fitting steady state kinetic data","volume":"15","author":"Johnson","year":"2019","journal-title":"Beilstein J. Org. Chem."},{"key":"10.1016\/j.jbc.2025.108168_bib81","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1038\/nprot.2009.121","article-title":"Measurement of cytochrome P450 and NADPH-cytochrome P450 reductase","volume":"4","author":"Guengerich","year":"2009","journal-title":"Nat. Protoc."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825000158?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825000158?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,2,25]],"date-time":"2025-02-25T20:09:01Z","timestamp":1740514141000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925825000158"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":81,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2025,2]]}},"alternative-id":["S0021925825000158"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.108168","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Liver fatty acid binding protein FABP1 transfers substrates to cytochrome P450 4A11 for catalysis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.108168","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology\u00e9","name":"copyright","label":"Copyright"}],"article-number":"108168"}}