{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T03:07:03Z","timestamp":1761102423065,"version":"3.40.5"},"reference-count":54,"publisher":"Elsevier BV","issue":"23","license":[{"start":{"date-parts":[[2020,6,1]],"date-time":"2020-06-01T00:00:00Z","timestamp":1590969600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,15]],"date-time":"2020-11-15T00:00:00Z","timestamp":1605398400000},"content-version":"vor","delay-in-days":167,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["9R15GM116077-01","R21HD088775","R03HD092878"],"award-info":[{"award-number":["9R15GM116077-01","R21HD088775","R03HD092878"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["CHE-1402675","CHE-1213550"],"award-info":[{"award-number":["CHE-1402675","CHE-1213550"]}],"id":[{"id":"10.13039\/100000001","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":[[2020,6]]},"DOI":"10.1074\/jbc.ra120.012761","type":"journal-article","created":{"date-parts":[[2020,4,18]],"date-time":"2020-04-18T01:41:01Z","timestamp":1587174061000},"page":"8078-8095","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"title":["Structure\u2013function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine metabolism"],"prefix":"10.1016","volume":"295","author":[{"given":"Xu","family":"Zhang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natalia S.","family":"Nemeria","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u00e3o","family":"Leandro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6167-9147","authenticated-orcid":false,"given":"Sander","family":"Houten","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6738-2563","authenticated-orcid":false,"given":"Michael","family":"Lazarus","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gary","family":"Gerfen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Oliver","family":"Ozohanics","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6014-3175","authenticated-orcid":false,"given":"Attila","family":"Ambrus","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3669-7041","authenticated-orcid":false,"given":"Balint","family":"Nagy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roman","family":"Brukh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1354-718X","authenticated-orcid":false,"given":"Frank","family":"Jordan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.012761_bib1","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1016\/j.ajhg.2012.10.006","article-title":"DHTKD1 mutations cause 2-aminoadipic and 2-oxoadipic aciduria","volume":"91","author":"Danhauser","year":"2012","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.RA120.012761_bib2","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/8904_2015_462","article-title":"New cases of DHTKD1 mutations in patients with 2-ketoadipic aciduria","volume":"25","author":"Stiles","year":"2016","journal-title":"JIMD Rep"},{"key":"10.1074\/jbc.RA120.012761_bib3","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1007\/s10545-015-9841-9","article-title":"Genetic basis of \u03b1-aminoadipic and \u03b1-ketoadipic aciduria","volume":"38","author":"Hagen","year":"2015","journal-title":"J. Inherit. Metab. Dis"},{"key":"10.1074\/jbc.RA120.012761_bib4","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1016\/j.ajhg.2012.09.018","article-title":"A nonsense mutation in DHTKD1 causes Charcot-Marie-Tooth type 2 in a large Chinese pedigree","volume":"91","author":"Xu","year":"2012","journal-title":"Am. J. Hum. Genet"},{"key":"10.1074\/jbc.RA120.012761_bib5","doi-asserted-by":"crossref","first-page":"3587","DOI":"10.1016\/j.febslet.2013.08.047","article-title":"DHTKD1 is essential for mitochondrial biogenesis and function maintenance","volume":"587","author":"Xu","year":"2013","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA120.012761_bib6","doi-asserted-by":"crossref","first-page":"e00085","DOI":"10.1128\/MCB.00085-18","article-title":"DHTKD1 deficiency causes Charcot-Marie-Tooth disease in mice","volume":"38","author":"Xu","year":"2018","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib7","doi-asserted-by":"crossref","first-page":"e99922","DOI":"10.1172\/jci.insight.99922","article-title":"Whole-exome sequencing uncovers oxidoreductases DHTKD1 and OGDHc as linkers between mitochondrial dysfunction and eosinophilic esophagitis","volume":"3","author":"Sherrill","year":"2018","journal-title":"JCI Insight"},{"key":"10.1074\/jbc.RA120.012761_bib8","doi-asserted-by":"crossref","first-page":"2220","DOI":"10.1016\/j.bbadis.2017.05.018","article-title":"Elevated glutaric acid levels in Dhtkd1-\/Gcdh- double knockout mice challenge our current understanding of lysine metabolism","volume":"1863","author":"Biagosch","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis"},{"key":"10.1074\/jbc.RA120.012761_bib9","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1093\/hmg\/ddaa037","article-title":"DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo","volume":"29","author":"Leandro","year":"2020","journal-title":"Human Mol. Gen"},{"key":"10.1074\/jbc.RA120.012761_bib10","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1016\/j.bbabio.2018.05.001","article-title":"Evidence for functional and regulatory cross-talk between the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex and 2-oxoadipate dehydrogenase on the l-lysine, l- hydroxylysine and l-tryptophan degradation pathways from studies in vitro","volume":"1859","author":"Nemeria","year":"2018","journal-title":"Biochim. Biophys. Acta Bioenerg"},{"key":"10.1074\/jbc.RA120.012761_bib11","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.freeradbiomed.2017.11.018","article-title":"The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species","volume":"115","author":"Nemeria","year":"2018","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA120.012761_bib12","doi-asserted-by":"crossref","first-page":"2325","DOI":"10.1007\/s11064-019-02765-w","article-title":"Human 2-oxoglutarate dehydrogenase and 2-oxoadipate dehydrogenase both generate superoxide\/H2O2 in a side-reaction and each could contribute to oxidative stress in mitochondria","volume":"44","author":"Jordan","year":"2019","journal-title":"Neurochem. Res"},{"key":"10.1074\/jbc.RA120.012761_bib13","doi-asserted-by":"crossref","first-page":"21688","DOI":"10.1074\/jbc.M113.465419","article-title":"Influence of allosteric regulators on individual steps in the reaction catalyzed by Mycobacterium tuberculosis 2-hydroxy-3-oxoadipate synthase","volume":"288","author":"Balakrishnan","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib14","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1016\/j.freeradbiomed.2017.04.017","article-title":"The human Krebs cycle 2-oxoglutarate dehydrogenase complex creates an additional source of superoxide\/hydrogen peroxide from 2-oxoadipate as alternative source","volume":"108","author":"Nemeria","year":"2017","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA120.012761_bib15","doi-asserted-by":"crossref","first-page":"29859","DOI":"10.1074\/jbc.M114.591073","article-title":"Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate","volume":"289","author":"Nemeria","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib16","doi-asserted-by":"crossref","first-page":"19213","DOI":"10.1074\/jbc.RA118.005432","article-title":"A multipronged approach unravels unprecedented protein\u2013protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complex","volume":"293","author":"Zhou","year":"2018","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib17","doi-asserted-by":"crossref","first-page":"15215","DOI":"10.1074\/jbc.M113.544080","article-title":"Structure and function of the catalytic domain of the dihydrolipoylacetyltransferase component in the Escherichia coli pyruvate dehydrogenase complex","volume":"289","author":"Wang","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib18","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1002\/2211-5463.12431","article-title":"Catalysis of transthiolacylation in the active centers of dihydrolipoamide acyltransferase components of 2-oxo acid dehydrogenase complexes","volume":"8","author":"Chakraborty","year":"2018","journal-title":"FEBS Open Bio"},{"key":"10.1074\/jbc.RA120.012761_bib19","doi-asserted-by":"crossref","first-page":"18644","DOI":"10.1021\/ja3062375","article-title":"Determination of pre-steady-state rate constants on the Escherichia coli pyruvate dehydrogenase complex reveals that loop movement controls the rate-limiting step","volume":"134","author":"Balakrishnan","year":"2012","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA120.012761_bib20","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1021\/bi201614n","article-title":"Inter-chain acetyl transfer in the E2 component of bacterial pyruvate dehydrogenase suggests a model with different roles for each chain in a trimer of the homooligomeric component","volume":"51","author":"Song","year":"2012","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.012761_bib21","doi-asserted-by":"crossref","first-page":"3540","DOI":"10.1021\/bi1020056","article-title":"Substrate specificity of 2-hydroxyglutaryl-CoA dehydratase from Clostridium symbiosum: toward a bio-based production of adipic acid","volume":"50","author":"Parthasarathy","year":"2011","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.012761_bib22","doi-asserted-by":"crossref","first-page":"1224","DOI":"10.1039\/C0CS00113A","article-title":"Hydrogen exchange mass spectrometry for studying protein structure and dynamics","volume":"40","author":"Konermann","year":"2011","journal-title":"Chem. Soc. Rev"},{"key":"10.1074\/jbc.RA120.012761_bib23","doi-asserted-by":"crossref","first-page":"9355","DOI":"10.1073\/pnas.1619981114","article-title":"Conformational dynamics of 1-deoxy-d-xylulose 5-phosphate synthase on ligand binding revealed by H\/D exchange MS","volume":"114","author":"Zhou","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.012761_bib24","doi-asserted-by":"crossref","first-page":"4970","DOI":"10.1021\/acs.biochem.9b00878","article-title":"Active site histidines link conformational dynamics with catalysis on the anti-infective target 1-deoxy-d-xylulose 5-phosphate synthase","volume":"58","author":"DeColli","year":"2019","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.012761_bib25","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1016\/j.chembiol.2011.06.004","article-title":"Functional plasticity and allosteric regulation of \u03b1-ketoglutarate decarboxylase in central mycobacterial metabolism","volume":"18","author":"Wagner","year":"2011","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib26","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1042\/BJ20131142","article-title":"A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (\u03b1-ketoglutarate decarboxylase)","volume":"457","author":"Wagner","year":"2014","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.012761_bib27","article-title":"Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine metabolism","author":"Bezerra","year":"2020","journal-title":"bioRxiv"},{"key":"10.1074\/jbc.RA120.012761_bib28","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1073\/pnas.68.6.1135","article-title":"Crystallization and preliminary structural analysis of dihydrolipoyltranssuccinylase, the core of the 2-oxoglutarate dehydrogenase complex","volume":"68","author":"Derosier","year":"1971","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.012761_bib29","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1006\/jmbi.1998.1924","article-title":"Crystal structure of the truncated cubic core component of the Escherichia coli 2 oxoglutarate dehydrogenase multienzyme complex","volume":"280","author":"Knapp","year":"1998","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib30","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1110\/ps.9.1.37","article-title":"Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase","volume":"9","author":"Knapp","year":"2000","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.RA120.012761_bib31","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1107\/S0907444902005048","article-title":"Crystallization and preliminary X-ray analysis of the full-size cubic core of pig 2-oxoglutarate dehydrogenase complex","volume":"58","author":"Suzuki","year":"2002","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.012761_bib32","doi-asserted-by":"crossref","first-page":"22402","DOI":"10.1016\/S0021-9258(18)45719-5","article-title":"Cryoelectron microscopy of frozen-hydrated \u03b1-ketoacid dehydrogenase complexes from Escherichia coli","volume":"265","author":"Wagenknecht","year":"1990","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib33","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/1047-8477(92)90069-M","article-title":"Configuration of interdomain linkers in pyruvate dehydrogenase complex of Escherichia coli as determined by cryoelectron microscopy","volume":"109","author":"Wagenknecht","year":"1992","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib34","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1016\/j.str.2005.08.016","article-title":"Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes","volume":"13","author":"Murphy","year":"2005","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.012761_bib35","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1007\/978-3-319-46503-6_19","article-title":"The pyruvate dehydrogenase complex and related assemblies in health and disease","volume":"83","author":"Byron","year":"2017","journal-title":"Subcell. Biochem"},{"key":"10.1074\/jbc.RA120.012761_bib36","doi-asserted-by":"crossref","first-page":"14551","DOI":"10.1002\/anie.201708273","article-title":"The first zero-length mass spectrometry-cleavable cross-linker for protein structure analysis","volume":"56","author":"Hage","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.RA120.012761_bib37","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/j.jsb.2010.10.014","article-title":"The beginning of a beautiful friendship: cross-linking\/mass spectrometry and modelling of proteins and multi-protein complexes","volume":"173","author":"Rappsilber","year":"2011","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib38","article-title":"Engineering 2-oxoglutarate dehydrogenase to a 2-oxo aliphatic dehydrogenase complex by optimizing consecutive components","volume":"66","author":"Chakraborty","year":"2019","journal-title":"AIChE J"},{"key":"10.1074\/jbc.RA120.012761_bib39","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.jmb.2007.01.080","article-title":"Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex","volume":"368","author":"Frank","year":"2007","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.012761_bib40","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1021\/bi5013113","article-title":"Elucidation of the interaction loci of the human pyruvate dehydrogenase complex E2\u00b7E3BP core with pyruvate dehydrogenase kinase 1 and kinase 2 by H\/D exchange mass spectrometry and nuclear magnetic resonance","volume":"54","author":"Wang","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.012761_bib41","doi-asserted-by":"crossref","first-page":"30161","DOI":"10.1074\/jbc.M114.592915","article-title":"Novel binding motif and new flexibility revealed by structural analyses of a pyruvate dehydrogenase-dihydrolipoyl acetyltransferase subcomplex from the Escherichia coli pyruvate dehydrogenase multienzyme complex","volume":"289","author":"Arjunan","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.012761_bib42","doi-asserted-by":"crossref","first-page":"2098","DOI":"10.1016\/j.bbadis.2016.08.013","article-title":"Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen\/deuterium-exchange mass spectrometry: implications for structural basis of E3 deficiency","volume":"1862","author":"Ambrus","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.012761_bib43","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1002\/rcm.3467","article-title":"Specificity of immobilized porcine pepsin in H\/D exchange compatible conditions","volume":"22","author":"Hamuro","year":"2008","journal-title":"Rapid Commun. Mass Spectrom"},{"key":"10.1074\/jbc.RA120.012761_bib44","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1186\/s12859-014-0403-1","article-title":"QUDeX-MS: hydrogen\/deuterium exchange calculation for mass spectra with resolved isotopic fine structure","volume":"15","author":"Salisbury","year":"2014","journal-title":"BMC Bioinformatics"},{"key":"10.1074\/jbc.RA120.012761_bib45","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1016\/j.jasms.2006.07.025","article-title":"Semi-automated data processing of hydrogen exchange mass spectra using HX-Express","volume":"17","author":"Weis","year":"2006","journal-title":"J. Am. Soc. Mass Spectrom"},{"key":"10.1074\/jbc.RA120.012761_bib46","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1007\/s13361-014-1001-1","article-title":"Automated assignment of MS\/MS cleavable cross-links in protein 3D-structure analysis","volume":"26","author":"G\u00f6tze","year":"2015","journal-title":"J. Am. Soc. Mass. Spectrom"},{"key":"10.1074\/jbc.RA120.012761_bib47","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/nprot.2010.5","article-title":"I-TASSER: a unified platform for automated protein structure and function prediction","volume":"5","author":"Roy","year":"2010","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.RA120.012761_bib48","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1038\/nbt.2377","article-title":"A cross-platform toolkit for mass spectrometry and proteomics","volume":"30","author":"Chambers","year":"2012","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/jbc.RA120.012761_bib49","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1021\/acs.jproteome.8b00175","article-title":"SearchGUI: a highly adaptable common interface for proteomics search and de novo engines","volume":"17","author":"Barsnes","year":"2018","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.RA120.012761_bib50","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1038\/nbt.3109","article-title":"PeptideShaker enables reanalysis of MS-derived proteomics data sets","volume":"33","author":"Vaudel","year":"2015","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/jbc.RA120.012761_bib51","doi-asserted-by":"crossref","first-page":"W362","DOI":"10.1093\/nar\/gkv463","article-title":"xVis: a web server for the schematic visualization and interpretation of crosslink-derived spatial restraints","volume":"43","author":"Grimm","year":"2015","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.012761_bib52","doi-asserted-by":"crossref","first-page":"D1100","DOI":"10.1093\/nar\/gkw936","article-title":"The ProteomeXchange Consortium in 2017: supporting the cultural change in proteomics public data deposition","volume":"45","author":"Deutsch","year":"2017","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.012761_bib53","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.012761_bib54","article-title":"Inhibition and crystal structure of the human DHTKD1-thiamin diphosphate complex","author":"Leandro","year":"2020","journal-title":"bioRxiv"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494440?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817494440?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.012761","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,31]],"date-time":"2021-12-31T16:17:00Z","timestamp":1640967420000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817494440"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,6]]},"references-count":54,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2020,6]]}},"alternative-id":["S0021925817494440"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.012761","relation":{},"ISSN":["0021-9258"],"issn-type":[{"type":"print","value":"0021-9258"}],"subject":[],"published":{"date-parts":[[2020,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure\u2013function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine metabolism","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.012761","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Zhang et al.","name":"copyright","label":"Copyright"}]}}