{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T22:48:38Z","timestamp":1789512518807,"version":"build-2803163510"},"reference-count":52,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,8,13]],"date-time":"2025-08-13T00:00:00Z","timestamp":1755043200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002367","name":"Chinese Academy of Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002367","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100019958","name":"Shanghai Advanced Research Institute, Chinese Academy of Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100019958","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003021","name":"East China University of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003021","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2021YFA0911000"],"award-info":[{"award-number":["2021YFA0911000"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009666","name":"Salt Science Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009666","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003399","name":"Science and Technology Commission of Shanghai Municipality","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003399","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004921","name":"Shanghai Jiao Tong University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004921","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002855","name":"Ministry of Science and Technology of the People's Republic of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002855","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":[[2025,9]]},"DOI":"10.1016\/j.jbc.2025.110599","type":"journal-article","created":{"date-parts":[[2025,8,15]],"date-time":"2025-08-15T05:29:18Z","timestamp":1755235758000},"page":"110599","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"title":["ADP-ribose is a competitive inhibitor of methanol dehydrogenases from Bacillus methanolicus"],"prefix":"10.1016","volume":"301","author":[{"given":"Bao-Di","family":"Ma","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jia-Yi","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jian-He","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tao","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xu-Dong","family":"Kong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2025.110599_bib1","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1038\/s41929-023-01063-7","article-title":"Metabolic engineering of yeast for the production of carbohydrate-derived foods and chemicals from C1\u20133 molecules","volume":"7","author":"Tang","year":"2024","journal-title":"Nat. Catal."},{"key":"10.1016\/j.jbc.2025.110599_bib2","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1038\/s42255-022-00601-0","article-title":"Rescuing yeast from cell death enables overproduction of fatty acids from sole methanol","volume":"4","author":"Gao","year":"2022","journal-title":"Nat. Metab."},{"key":"10.1016\/j.jbc.2025.110599_bib3","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/j.cell.2020.07.010","article-title":"Converting Escherichia coli to a synthetic methylotroph growing solely on methanol","volume":"182","author":"Chen","year":"2020","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2025.110599_bib4","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.synbio.2023.06.001","article-title":"Methanol-based biomanufacturing of fuels and chemicals using native and synthetic methylotrophs","volume":"8","author":"Sarwar","year":"2023","journal-title":"Synth. Syst. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib5","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.copbio.2019.10.002","article-title":"Renewable methanol and formate as microbial feedstocks","volume":"62","author":"Cotton","year":"2020","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib6","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1186\/s40643-021-00444-9","article-title":"Metabolic engineering of methylotrophic Pichia pastoris for the production of \u03b2-alanine","volume":"8","author":"Miao","year":"2021","journal-title":"Bioresour. Bioproc."},{"key":"10.1016\/j.jbc.2025.110599_bib7","doi-asserted-by":"crossref","DOI":"10.3389\/fbioe.2021.787791","article-title":"Methanol dehydrogenases as a key biocatalysts for synthetic methylotrophy","volume":"9","author":"Le","year":"2021","journal-title":"Front. Bioeng. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib8","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/j.greenca.2024.03.004","article-title":"Engineering of cofactor preference and catalytic activity of methanol dehydrogenase by growth-coupled directed evolution","volume":"2","author":"Yang","year":"2024","journal-title":"Green. Carbon"},{"key":"10.1016\/j.jbc.2025.110599_bib9","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1186\/s40643-022-00547-x","article-title":"Improved succinic acid production through the reconstruction of methanol dissimilation in Escherichia coli","volume":"9","author":"Guo","year":"2022","journal-title":"Bioresour. Bioproc."},{"key":"10.1016\/j.jbc.2025.110599_bib10","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.ymben.2014.12.008","article-title":"Engineering Escherichia coli for methanol conversion","volume":"28","author":"Muller","year":"2015","journal-title":"Metab. Eng."},{"key":"10.1016\/j.jbc.2025.110599_bib11","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0166851","article-title":"Diversity and evolutionary analysis of iron-containing (Type-III) alcohol dehydrogenases in eukaryotes","volume":"11","author":"Gaona-Lopez","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110599_bib12","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/S0168-6445(03)00068-8","article-title":"Alcohol dehydrogenases from thermophilic and hyperthermophilic archaea and bacteria","volume":"27","author":"Radianingtyas","year":"2003","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.jbc.2025.110599_bib13","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1002\/bab.2376","article-title":"Industrial light at the end of the iron-containing (group III) alcohol dehydrogenase tunnel","volume":"70","author":"Shanbha","year":"2003","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.jbc.2025.110599_bib14","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1007\/BF00409664","article-title":"Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme","volume":"152","author":"Arfman","year":"1989","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.jbc.2025.110599_bib15","doi-asserted-by":"crossref","first-page":"3955","DOI":"10.1016\/S0021-9258(19)67886-5","article-title":"Purification and characterization of an activator protein for methanol dehydrogenase from thermotolerant Bacillus spp","volume":"266","author":"Arfman","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib16","doi-asserted-by":"crossref","first-page":"34785","DOI":"10.1074\/jbc.M205617200","article-title":"Molecular, biochemical, and functional characterization of a Nudix hydrolase protein that stimulates the activity of a nicotinoprotein alcohol dehydrogenase","volume":"277","author":"Kloosterman","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib17","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1111\/j.1432-1033.1997.00426.x","article-title":"Properties of an NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus","volume":"244","author":"Arfman","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2025.110599_bib18","doi-asserted-by":"crossref","first-page":"46966","DOI":"10.1074\/jbc.M207547200","article-title":"Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus","volume":"277","author":"Hektor","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0059188","article-title":"Methylotrophic Bacillus methanolicus encodes two chromosomal and one plasmid born NAD+ dependent methanol dehydrogenase paralogs with different catalytic and biochemical properties","volume":"8","author":"Krog","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110599_bib20","doi-asserted-by":"crossref","first-page":"2993","DOI":"10.1016\/j.febslet.2014.06.008","article-title":"In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed","volume":"588","author":"Ochsner","year":"2014","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2025.110599_bib21","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2020.140376","article-title":"Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase","volume":"1868","author":"Taxon","year":"2020","journal-title":"BBA-Proteins Proteom"},{"key":"10.1016\/j.jbc.2025.110599_bib22","doi-asserted-by":"crossref","first-page":"3949","DOI":"10.1016\/S0021-9258(19)67885-3","article-title":"Electron microscopic analysis and biochemical characterization of a novel methanol dehydrogenase from the thermotolerant Bacillus sp. C1","volume":"266","author":"Vonck","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib23","doi-asserted-by":"crossref","first-page":"5346","DOI":"10.1128\/jb.174.16.5346-5353.1992","article-title":"Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene","volume":"174","author":"de Vries","year":"1992","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jbc.2025.110599_bib24","doi-asserted-by":"crossref","first-page":"4969","DOI":"10.1007\/s00253-016-7320-3","article-title":"Characterization and evolution of an activator-independent methanol dehydrogenase from Cupriavidus necator N-1","volume":"100","author":"Wu","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib25","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1021\/acssynbio.8b00481","article-title":"Phage-assisted evolution of Bacillus methanolicus methanol dehydrogenase 2","volume":"8","author":"Roth","year":"2019","journal-title":"ACS Synth. Biol."},{"key":"10.1016\/j.jbc.2025.110599_bib26","doi-asserted-by":"crossref","first-page":"1471","DOI":"10.3390\/ijms22031471","article-title":"Biosensor-based directed evolution of methanol dehydrogenase from Lysinibacillus xylanilyticus","volume":"22","author":"Le","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2025.110599_bib27","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/j.synbio.2023.05.004","article-title":"Directed evolution of a neutrophilic and mesophilic methanol dehydrogenase based on high-throughput and accurate measurement of formaldehyde","volume":"8","author":"Qian","year":"2023","journal-title":"Synth. Syst. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib28","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1016\/S0021-9258(18)81208-X","article-title":"The effect of buffers on nicotinamide adenine dinucleotide hydrolysis","volume":"238","author":"Anderson","year":"1963","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib29","doi-asserted-by":"crossref","first-page":"2257","DOI":"10.1021\/ja00215a041","article-title":"Pyridine nucleotide chemistry. A new mechanism for the hydroxide-catalyzed hydrolysis of the nicotinamide-glycosyl bond","volume":"110","author":"Johnson","year":"1988","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2025.110599_bib30","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0141716","article-title":"Structural and enzymatic characterization of a nucleoside diphosphate sugar hydrolase from Bdellovibrio bacteriovorus","volume":"10","author":"de la Pena","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2025.110599_bib31","doi-asserted-by":"crossref","first-page":"37163","DOI":"10.1074\/jbc.M403817200","article-title":"Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal","volume":"279","author":"Yoshiba","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib32","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.abb.2004.08.017","article-title":"Structures and mechanisms of Nudix hydrolases","volume":"433","author":"Mildvan","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2025.110599_bib33","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/s41392-020-00311-7","article-title":"NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential","volume":"5","author":"Xie","year":"2020","journal-title":"Signal. Transduct. Target. Ther."},{"key":"10.1016\/j.jbc.2025.110599_bib34","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/s41580-020-00313-x","article-title":"NAD+ metabolism and its roles in cellular processes during ageing","volume":"22","author":"Covarrubias","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2025.110599_bib35","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.jchromb.2005.05.002","article-title":"Determination of intracellular concentrations of the TRPM2 agonist ADP-ribose by reversed-phase HPLC","volume":"821","author":"Gasser","year":"2005","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"10.1016\/j.jbc.2025.110599_bib36","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1042\/BJ20060183","article-title":"Endogenous ADP-ribose enables calcium-regulated cation currents through TRPM2 channels in neutrophil granulocytes","volume":"398","author":"Heiner","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2025.110599_bib37","doi-asserted-by":"crossref","first-page":"11256","DOI":"10.1074\/jbc.M809790200","article-title":"Hydrolase regulates NAD+ metabolites and modulates cellular redox","volume":"284","author":"Tong","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2025.110599_bib38","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/j.str.2009.05.012","article-title":"Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism","volume":"17","author":"Huang","year":"2009","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2025.110599_bib39","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1002\/prot.25223","article-title":"The evolution of function within the Nudix homology clan","volume":"85","author":"Srouji","year":"2017","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2025.110599_bib40","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s00018-005-5386-7","article-title":"The Nudix hydrolase superfamily","volume":"63","author":"McLennan","year":"2006","journal-title":"Cell Mol. Life Sci."},{"key":"10.1016\/j.jbc.2025.110599_bib41","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1038\/s41586-024-07986-w","article-title":"Phages reconstitute NAD+ to counter bacterial immunity","volume":"634","author":"Osterman","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2025.110599_bib42","doi-asserted-by":"crossref","DOI":"10.1128\/aem.00341-22","article-title":"Engineering isopropanol dehydrogenase for efficient regeneration of nicotinamide cofactors","volume":"88","author":"Jia","year":"2022","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jbc.2025.110599_bib43","doi-asserted-by":"crossref","first-page":"1280","DOI":"10.1046\/j.1432-1327.2000.01123.x","article-title":"Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues","volume":"267","author":"Slusarczyk","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2025.110599_bib44","doi-asserted-by":"crossref","first-page":"2680","DOI":"10.1002\/cbic.202000196","article-title":"Evolution of glucose dehydrogenase for cofactor regeneration in bioredox processes with denaturing agents","volume":"21","author":"Qian","year":"2020","journal-title":"ChemBioChem"},{"key":"10.1016\/j.jbc.2025.110599_bib45","doi-asserted-by":"crossref","first-page":"3802","DOI":"10.1002\/cctc.201900492","article-title":"One pot asymmetric synthesis of (R)-phenylglycinol from racemic styrene oxide via cascade biocatalysis","volume":"11","author":"Sun","year":"2019","journal-title":"ChemCatChem"},{"key":"10.1016\/j.jbc.2025.110599_bib46","article-title":"Development of a thermodynamically favorable multi-enzyme cascade reaction for efficient sustainable production of \u03c9-amino fatty acids and \u03b1,\u03c9-diamines","volume":"17","author":"Li","year":"2024","journal-title":"ChemSusChem"},{"key":"10.1016\/j.jbc.2025.110599_bib47","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jbc.2025.110599_bib48","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2025.110599_bib49","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jbc.2025.110599_bib50","doi-asserted-by":"crossref","first-page":"8963","DOI":"10.1007\/s00253-013-4725-0","article-title":"Structural and biochemical characterisation of a NAD+-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications","volume":"97","author":"Elleuche","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2025.110599_bib51","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. Sect. D"},{"key":"10.1016\/j.jbc.2025.110599_bib52","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. Sect. D"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825024500?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925825024500?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T21:38:13Z","timestamp":1772833093000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925825024500"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9]]},"references-count":52,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2025,9]]}},"alternative-id":["S0021925825024500"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110599","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2025,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"ADP-ribose is a competitive inhibitor of methanol dehydrogenases from Bacillus methanolicus","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2025.110599","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":"110599"}}