{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T16:41:33Z","timestamp":1790786493242,"version":"4.1.0"},"reference-count":24,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2017,1,1]],"date-time":"2017-01-01T00:00:00Z","timestamp":1483228800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,1,1]],"date-time":"2018-01-01T00:00:00Z","timestamp":1514764800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001677","name":"Inserm","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001677","id-type":"DOI","asserted-by":"publisher"}]},{"name":"R\u00e9gion Lorraine"},{"name":"Nancy Hospital"},{"DOI":"10.13039\/501100001673","name":"Fondation J\u00e9r\u00f4me Lejeune","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001673","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Union","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2017,1]]},"DOI":"10.1016\/j.bbadis.2016.10.016","type":"journal-article","created":{"date-parts":[[2016,10,20]],"date-time":"2016-10-20T04:30:52Z","timestamp":1476937852000},"page":"103-112","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":42,"title":["Methionine synthase and methionine synthase reductase interact with MMACHC and with MMADHC"],"prefix":"10.1016","volume":"1863","author":[{"given":"Christine","family":"Bassila","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rose","family":"Ghemrawi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6376-517X","authenticated-orcid":false,"given":"Justine","family":"Flayac","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. Sean","family":"Froese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias R.","family":"Baumgartner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Louis","family":"Gu\u00e9ant","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7010-5789","authenticated-orcid":false,"given":"David","family":"Coelho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbadis.2016.10.016_bb0005","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.cbpa.2009.07.007","article-title":"The tinker, tailor, soldier in intracellular B12 trafficking","volume":"13","author":"Banerjee","year":"2009","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0010","doi-asserted-by":"crossref","first-page":"13186","DOI":"10.1074\/jbc.R113.458810","article-title":"Navigating the B(12) road: assimilation, delivery, and disorders of cobalamin","volume":"288","author":"Gherasim","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0015","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1016\/j.biochi.2013.01.013","article-title":"Lessons in biology from patients with inborn errors of vitamin B12 metabolism","volume":"95","author":"Watkins","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.bbadis.2016.10.016_bb0020","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1038\/ng.2386","article-title":"Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism","volume":"44","author":"Coelho","year":"2012","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0025","doi-asserted-by":"crossref","first-page":"4591","DOI":"10.1093\/hmg\/ddt308","article-title":"Interaction between methionine synthase isoforms and MMACHC: characterization in cblG-variant, cblG and cblC inherited causes of megaloblastic anaemia","volume":"22","author":"Fofou-Caillierez","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0030","doi-asserted-by":"crossref","first-page":"250","DOI":"10.3109\/09687688.2014.990998","article-title":"Purification and interaction analyses of two human lysosomal vitamin B12 transporters: LMBD1 and ABCD4","volume":"31","author":"Deme","year":"2014","journal-title":"Mol. Membr. Biol."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0035","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.ymgme.2010.10.011","article-title":"Interaction between MMACHC and MMADHC, two human proteins participating in intracellular vitamin B\u2081\u2082 metabolism","volume":"102","author":"Plesa","year":"2011","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0040","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.ymgme.2012.07.001","article-title":"Structural features of recombinant MMADHC isoforms and their interactions with MMACHC, proteins of mammalian vitamin B12 metabolism","volume":"107","author":"Deme","year":"2012","journal-title":"Mol. Genet. Metab."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0045","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1016\/j.biochi.2013.02.003","article-title":"The C-terminal domain of CblD interacts with CblC and influences intracellular cobalamin partitioning","volume":"95","author":"Gherasim","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.bbadis.2016.10.016_bb0050","doi-asserted-by":"crossref","first-page":"17838","DOI":"10.1074\/jbc.M600047200","article-title":"Energetics of interaction between the G-protein chaperone, MeaB, and B12-dependent methylmalonyl-CoA mutase","volume":"281","author":"Padovani","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0055","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1093\/hmg\/8.11.2009","article-title":"Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate\/cobalamin metabolism","volume":"8","author":"Wilson","year":"1999","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0060","doi-asserted-by":"crossref","first-page":"9476","DOI":"10.1073\/pnas.0603694103","article-title":"Human methionine synthase reductase is a molecular chaperone for human methionine synthase","volume":"103","author":"Yamada","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0065","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/0885-4505(92)90032-T","article-title":"Heterogeneity in cblG: differential retention of cobalamin on methionine synthase","volume":"47","author":"Sillaots","year":"2012","journal-title":"Biochem. Med. Metab. Biol."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0070","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1056\/NEJMoa072200","article-title":"Gene identification for the cblD defect of vitamin B12 metabolism","volume":"358","author":"Coelho","year":"2008","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0075","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1111\/j.1742-4658.2009.06919.x","article-title":"Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex","volume":"276","author":"Wolthers","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0080","doi-asserted-by":"crossref","first-page":"29167","DOI":"10.1074\/jbc.M115.683268","article-title":"Structural insights into the MMACHC-MMADHC protein complex involved in vitamin B12 trafficking","volume":"290","author":"Froese","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0085","doi-asserted-by":"crossref","first-page":"42742","DOI":"10.1074\/jbc.M407733200","article-title":"The cblD defect causes either isolated or combined deficiency of methylcobalamin and adenosylcobalamin synthesis","volume":"279","author":"Suormala","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0090","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1002\/wsbm.1209","article-title":"Modeling cellular compartmentation in one-carbon metabolism","volume":"5","author":"Scotti","year":"2013","journal-title":"Wiley Interdiscip. Rev. Syst. Biol. Med."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0095","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1126\/science.1152241","article-title":"Reversible compartmentalization of de novo purine biosynthetic complexes in living cells","volume":"320","author":"An","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.bbadis.2016.10.016_bb0100","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.ymben.2010.10.001","article-title":"Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon","volume":"13","author":"Meyer","year":"2011","journal-title":"Metab. Eng."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0105","doi-asserted-by":"crossref","first-page":"11893","DOI":"10.1074\/jbc.M700198200","article-title":"A novel branched-chain aminoa cid metabolon. Protein\u2013protein interactions in a supramolecular complex","volume":"282","author":"Islam","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0110","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/0303-2647(89)90038-5","article-title":"Supramolecular organization of tricarboxylic acid cycle enzymes","volume":"22","author":"Lyubarev","year":"1989","journal-title":"BioSystems"},{"key":"10.1016\/j.bbadis.2016.10.016_bb0115","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/1752-0509-2-27","article-title":"A stochastic automaton shows how enzyme assemblies may contribute to metabolic efficiency","volume":"2","author":"Amar","year":"2008","journal-title":"BMC Syst. Biol."},{"key":"10.1016\/j.bbadis.2016.10.016_bb0120","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1038\/nbt.3018","article-title":"Enzyme clustering accelerates processing of intermediates through metabolic channeling","volume":"32","author":"Castellana","year":"2014","journal-title":"Nat. Biotechnol."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443916302605?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443916302605?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,5,17]],"date-time":"2020-05-17T07:51:08Z","timestamp":1589701868000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443916302605"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,1]]},"references-count":24,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2017,1]]}},"alternative-id":["S0925443916302605"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2016.10.016","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2017,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Methionine synthase and methionine synthase reductase interact with MMACHC and with MMADHC","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbadis.2016.10.016","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}