{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T11:29:30Z","timestamp":1774438170780,"version":"3.50.1"},"reference-count":24,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[1994,6,1]],"date-time":"1994-06-01T00:00:00Z","timestamp":770428800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[1994,6,1]],"date-time":"1994-06-01T00:00:00Z","timestamp":770428800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Genet"],"published-print":{"date-parts":[[1994,6,1]]},"DOI":"10.1038\/ng0694-195","type":"journal-article","created":{"date-parts":[[2004,8,18]],"date-time":"2004-08-18T21:07:44Z","timestamp":1092863264000},"page":"195-200","source":"Crossref","is-referenced-by-count":620,"title":["Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification"],"prefix":"10.1038","volume":"7","author":[{"given":"Philippe","family":"Goyette","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James S.","family":"Sumner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renate","family":"Milos","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alessandra M.V.","family":"Duncan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David S.","family":"Rosenblatt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rowena G.","family":"Matthews","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rima","family":"Rozen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","reference":[{"key":"BFng0694195_CR1","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/S0021-9258(19)68337-7","volume":"257","author":"SC Daubner","year":"1982","unstructured":"Daubner, S.C. & Matthews, R.G. Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. biol. Chem. 257, 140\u2013145 (1982).","journal-title":"J. biol. Chem."},{"key":"BFng0694195_CR2","doi-asserted-by":"crossref","first-page":"11647","DOI":"10.1016\/S0021-9258(20)71253-6","volume":"259","author":"RG Matthews","year":"1984","unstructured":"Matthews, R.G., Vanoni, M.A., Hainfeld, J.F. & Wall, J. Methylenetetrahydrofolate reductase. Evidence for spatially distinct subunit domains obtained by scanning transmission electron microscopy and limited proteolysis. J. biol. Chem. 259, 11647\u201311650 (1984).","journal-title":"J. biol. Chem."},{"key":"BFng0694195_CR3","doi-asserted-by":"crossref","first-page":"7697","DOI":"10.1016\/S0021-9258(19)57456-7","volume":"261","author":"J Sumner","year":"1986","unstructured":"Sumner, J., Jencks, D.A., Khani, S. & Matthews, R.G. Photoaffinity labeling of methylenetetrahydrofolate reductase with 8-azido-S-adenosylmethionine. J. biol. Chem. 261, 7697\u20137700 (1986).","journal-title":"J. biol. Chem."},{"key":"BFng0694195_CR4","first-page":"2049","volume-title":"The Metabolic Basis of Inherited Disease","author":"DS Rosenblatt","year":"1989","unstructured":"Rosenblatt, D.S. Inherited disorders of folate transport and metabolism. in The Metabolic Basis of Inherited Disease (eds Scriver, C.R., Beaudet, A.L., Sly, W.S. & Valle, D.) 2049\u20132064 (McGraw-Hill, New York, 1989)."},{"key":"BFng0694195_CR5","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/0885-4505(92)90029-X","volume":"47","author":"DS Rosenblatt","year":"1992","unstructured":"Rosenblatt, D.S., Lue-Shing, H., Arzoumanian, A., Low-Nang, L. & Matiaszuk, N. Methylenetetrahydrofolate reductase (MR) deficiency: Thermolability of residual MR activity, methionine synthase activity, and methylcobalamin levels in cultured fibroblasts. Biochem. Med. metab. Biol. 47, 221\u2013225 (1992).","journal-title":"Biochem. Med. metab. Biol."},{"key":"BFng0694195_CR6","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1002\/ajmg.1320450510","volume":"45","author":"JC Haworth","year":"1993","unstructured":"Haworth, J.C. et al. Symptomatic and asymptomatic methylenetetrahydrofolate reductase deficiency in two adult brothers. Am. J. med. Genet. 45, 572\u2013576 (1993).","journal-title":"Am. J. med. Genet."},{"key":"BFng0694195_CR7","first-page":"536","volume":"48","author":"S-S Kang","year":"1991","unstructured":"Kang, S.-S. et al. Thermolabile methylenetetrahydrofolate reductase: An inherited risk factor for coronary artery disease. Am. J. hum. Genet. 48, 536\u2013545 (1991).","journal-title":"Am. J. hum. Genet."},{"key":"BFng0694195_CR8","doi-asserted-by":"publisher","first-page":"6723","DOI":"10.1093\/nar\/11.19.6723","volume":"11","author":"I Saint-Girons","year":"1983","unstructured":"Saint-Girons, I. et al. Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylenetetrahydrofolate reductase and of its control region. Nucl. Acids Res. 11, 6723\u20136732 (1983).","journal-title":"Nucl. Acids Res."},{"key":"BFng0694195_CR9","doi-asserted-by":"publisher","first-page":"372","DOI":"10.1016\/0076-6879(86)22196-5","volume":"122","author":"RG Matthews","year":"1986","unstructured":"Matthews, R.G. Methylenetetrahydrofolate reductase from pig liver. Meth. Enzymol. 122, 372\u2013381 (1986).","journal-title":"Meth. Enzymol."},{"key":"BFng0694195_CR10","doi-asserted-by":"publisher","first-page":"246","DOI":"10.1007\/BF00334692","volume":"212","author":"GV Stauffer","year":"1988","unstructured":"Stauffer, G.V. & Stauffer, L.T. Cloning and nucleotide sequence of the Salmonella typhimurium LT2 metF gene and its homology with the corresponding sequence of Escherichia coli. Molec. Gen. Genet. 212, 246\u2013251 (1988).","journal-title":"Molec. Gen. Genet."},{"key":"BFng0694195_CR11","doi-asserted-by":"publisher","first-page":"2161","DOI":"10.1128\/MCB.4.10.2161","volume":"4","author":"E Yang","year":"1984","unstructured":"Yang, E. & Friedberg, E.G. Molecular cloning and nucleotide sequence analysis of the Saccaromyces cerevisiae RAD1 gene. Molec. Cell Biol. 4, 2161\u20132169 (1984).","journal-title":"Molec. Cell Biol."},{"key":"BFng0694195_CR12","doi-asserted-by":"publisher","first-page":"8874","DOI":"10.1016\/0888-7543(89)90129-8","volume":"5","author":"M Orita","year":"1989","unstructured":"Orita, M., Suzuki, Y., Sekiya, T. & Hayashi, K. Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 5, 8874\u20138879 (1989).","journal-title":"Genomics"},{"key":"BFng0694195_CR13","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/S0021-9258(17)45250-1","volume":"240","author":"HM Katzen","year":"1965","unstructured":"Katzen, H.M. & Buchanan, J.M. Enzymatic synthesis of the methyl group of methionine VIII. Repression-derepression, purification and properties of 5,10-methylenetetrahydrofolate reductase from Escherichia coli. J. biol. Chem. 240, 825\u2013835 (1965).","journal-title":"J. biol. Chem."},{"key":"BFng0694195_CR14","doi-asserted-by":"publisher","first-page":"459","DOI":"10.1016\/0005-2744(71)90247-6","volume":"250","author":"C Kutzbach","year":"1971","unstructured":"Kutzbach, C. & Stokstad, E.L.R. Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta 250, 459\u2013577 (1971).","journal-title":"Biochim. Biophys. Acta"},{"key":"BFng0694195_CR15","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1016\/0885-4505(90)90029-Z","volume":"43","author":"J Zhou","year":"1990","unstructured":"Zhou, J., Kang, S.-S., Wong, P.W.K., Fournier, B. & Rozen, R. Partial Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver. Biochem. Med. metab. Biol. 43, 234\u2013242 (1990).","journal-title":"Biochem. Med. metab. Biol."},{"key":"BFng0694195_CR16","volume-title":"Introduction to Protein Structure","author":"C Branden","year":"1991","unstructured":"Branden, C. & Tooze, J. in Introduction to Protein Structure (Garland Publishing, New York, 1991)."},{"key":"BFng0694195_CR17","first-page":"546","volume":"48","author":"S-S Kang","year":"1991","unstructured":"Kang, S.-S., Wong, P.W.K., Bock, H.-G., O., Horwitz, A. & Grix, A. Intermediate hyperhomocysteinemia resulting from compound heterozygosity of methylenetetrahydrofolate reductase mutations. Am. J. hum. Genet. 48, 546\u2013551 (1991).","journal-title":"Am. J. hum. Genet."},{"key":"BFng0694195_CR18","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1056\/NEJM198509193131201","volume":"313","author":"GHJ Boers","year":"1985","unstructured":"Boers, G.H.J. et al. Heterozygosity for homocystinuria in premature peripheral and cerebral occlusive arterial disease. New Engl. J. Med. 313, 709\u2013715 (1985).","journal-title":"New Engl. J. Med."},{"key":"BFng0694195_CR19","doi-asserted-by":"publisher","first-page":"1149","DOI":"10.1056\/NEJM199104253241701","volume":"324","author":"R Clarke","year":"1991","unstructured":"Clarke, R. et al. Homocysteinemia: an independent risk factor for vascular disease. New Engl. J. Med. 324, 1149\u20131155 (1991).","journal-title":"New Engl. J. Med."},{"key":"BFng0694195_CR20","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1016\/S0021-9258(19)39559-6","volume":"265","author":"S Som","year":"1990","unstructured":"Som, S. & Friedman, S. Direct photolabelling of the EcoRll methyltransferase with S-adenosyl-L-methionine. J. biol. Chem. 265, 4278\u20134283 (1990).","journal-title":"J. biol. Chem."},{"key":"BFng0694195_CR21","doi-asserted-by":"publisher","first-page":"431","DOI":"10.1007\/BF00327364","volume":"83","author":"ME Harper","year":"1981","unstructured":"Harper, M.E. & Saunders, G.F. Localization of single copy DNA sequences on G-banded human chromosomes by in situ hybridization. Chromosome 83, 431\u2013439 (1981).","journal-title":"Chromosome"},{"key":"BFng0694195_CR22","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1159\/000132156","volume":"39","author":"CC Lin","year":"1985","unstructured":"Lin, C.C., Draper, P.N. & De Braekeleer, M. High resolution chromosomal localization of the b gene of the human \u03b2 globin gene complex by in situ hybridization. Cytogenet. Cell Genet. 39, 269\u2013274 (1985).","journal-title":"Cytogenet. Cell Genet."},{"key":"BFng0694195_CR23","doi-asserted-by":"publisher","first-page":"2500","DOI":"10.1093\/nar\/19.9.2500","volume":"19","author":"B Dockhorn-Dworniczak","year":"1991","unstructured":"Dockhorn-Dworniczak, B. et al. Non-isotopic detection of single strand conformation polymorphism (PCR-SSCP): a rapid and sensitive technique in diagnosis of phenylketonuria. Nucl. Acids Res. 19, 2500 (1991).","journal-title":"Nucl. Acids Res."},{"key":"BFng0694195_CR24","doi-asserted-by":"publisher","first-page":"815","DOI":"10.1038\/313815a0","volume":"313","author":"R Rozen","year":"1985","unstructured":"Rozen, R., Fox, J., Fenton, W.A., Horwich, A.L. & Rosenberg, L.E. Gene deletion and restriction fragment length polymorphisms at the human ornithine transcarbamylase locus. Nature 313, 815\u2013817 (1985).","journal-title":"Nature"}],"updated-by":[{"DOI":"10.1038\/ng0894-551a","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[1994,8,1]],"date-time":"1994-08-01T00:00:00Z","timestamp":775699200000}}],"container-title":["Nature Genetics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/ng0694-195","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ng0694-195.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/ng0694-195.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T20:40:44Z","timestamp":1684442444000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/ng0694-195"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,6,1]]},"references-count":24,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1994,6,1]]}},"alternative-id":["BFng0694195"],"URL":"https:\/\/doi.org\/10.1038\/ng0694-195","relation":{},"ISSN":["1061-4036","1546-1718"],"issn-type":[{"value":"1061-4036","type":"print"},{"value":"1546-1718","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,6,1]]}}}