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Gene Review

MTHFR  -  methylenetetrahydrofolate reductase (NAD(P)H)

Sus scrofa

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Disease relevance of MTHFR


High impact information on MTHFR


Biological context of MTHFR


Associations of MTHFR with chemical compounds


Other interactions of MTHFR


Analytical, diagnostic and therapeutic context of MTHFR


  1. Multiple transcription start sites and alternative splicing in the methylenetetrahydrofolate reductase gene result in two enzyme isoforms. Tran, P., Leclerc, D., Chan, M., Pai, A., Hiou-Tim, F., Wu, Q., Goyette, P., Artigas, C., Milos, R., Rozen, R. Mamm. Genome (2002) [Pubmed]
  2. Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Goyette, P., Sumner, J.S., Milos, R., Duncan, A.M., Rosenblatt, D.S., Matthews, R.G., Rozen, R. Nat. Genet. (1994) [Pubmed]
  3. Folate-dependent 1-carbon transfer to biogenic amines mediated by methylenetetrahydrofolate reductase. Pearson, A.G., Turner, A.J. Nature (1975) [Pubmed]
  4. Photoaffinity labeling of methylenetetrahydrofolate reductase with 8-azido-S-adenosylmethionine. Sumner, J., Jencks, D.A., Khani, S., Matthews, R.G. J. Biol. Chem. (1986) [Pubmed]
  5. Characterization of the dihydropterin reductase activity of pig liver methylenetetrahydrofolate reductase. Matthews, R.G., Kaufman, S. J. Biol. Chem. (1980) [Pubmed]
  6. Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes. Matthews, R.G., Ghose, C., Green, J.M., Matthews, K.D., Dunlap, R.B. Adv. Enzyme Regul. (1987) [Pubmed]
  7. Inhibition of pig liver methylenetetrahydrofolate reductase by dihydrofolate: some mechanistic and regulatory implications. Matthews, R.G., Haywood, B.J. Biochemistry (1979) [Pubmed]
  8. Assays of methylenetetrahydrofolate reductase and methionine synthase activities by monitoring 5-methyltetrahydrofolate and tetrahydrofolate using high-performance liquid chromatography with fluorescence detection. Huang, L., Zhang, J., Hayakawa, T., Tsuge, H. Anal. Biochem. (2001) [Pubmed]
  9. Methylenetetrahydrofolate reductase. Evidence for spatially distinct subunit domains obtained by scanning transmission electron microscopy and limited proteolysis. Matthews, R.G., Vanoni, M.A., Hainfeld, J.F., Wall, J. J. Biol. Chem. (1984) [Pubmed]
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