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References
Kutzbach, C.; Stokstad, E.L.R.: Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta, 250, 459–477 (1971)
Pearson, A.G.M.; Turner, A.J.: Folate-dependent 1-carbon transfer to biogenic amines mediated by methylenetetrahydrofolate reductase. Nature, 258, 173–174 (1975)
Daubner, S.C.; Matthews, R.G.: Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem., 257, 140–145 (1982)
Matthews, R.G.; Daubner, S.C.: Modulation of methylenetetrahydrofolate reductase activity by S-adenosylmethionine and by dihydrofolate and its polyglutamate analogues. Adv. Enzyme Regul., 20, 123–131 (1982)
Vanoni, M.A.; Ballou, D.P.; Matthews, R.G.: Methylenetetrahydrofolate reductase. Steady state and rapid reaction studies on the NADPH-methylenetetrahydrofolate, NADPH-menadione, and methyltetrahydrofolate-menadione oxidoreductase activities of the enzyme. J. Biol. Chem., 258, 11510–11514 (1983)
Varalakshmi, K.; Savithri, H.S.; Rao, N.A.: Identification of amino acid residues essential for enzyme activity of sheep liver 5,10-methylenetetrahydrofolate reductase. Biochem. J., 236, 295–298 (1986)
Matthews, R.G.: Methylenetetrahydrofolate reductase from pig liver. Methods Enzymol., 122, 372–381 (1986)
Jencks, D.A.; Matthews, R.G.: Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium. J. Biol. Chem., 262, 2485–2493 (1987)
Zhou, J.; Kang, S.S.; Wong, P.W.K.; Fournier, B.; Rozen, R.: Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver [published erratum appears in Biochem Med Metab Biol 1990 Oct;44(2):200]. Biochem. Med. Metab. Biol., 43, 234–242 (1990)
Green, J.M.; Ballou, D.P.; Matthews, R.G.: Examination of the role of methylenetetrahydrofolate reductase in incorporation of methyltetrahydrofolate into cellular metabolism. FASEB J., 2, 42–47 (1988)
Black, K.A.; Eells, J.T.; Noker, P.E.; Hawtrey C.A.; Tephly, T.R.: Role of hepatic tetrahydrofolate in the species difference in methanol toxicity. Proc. Natl. Acad. Sci. USA, 82, 3854–3858 (1985)
Matthews, R.G.; Ghose, C.; Green, J.M.; Matthews, K. D.; Dunlap, R.B.: Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes. Adv. Enzyme Regul, 26, 157–171 (1987)
Burton, E.G.; Sallach, H.J.: Methylenetetrahydrofolate reductase in the rat central nervous system: intracellular and regional distribution. Arch. Biochem. Biophys., 166, 483–494 (1975)
Matthews, R.G.; Kaufmann S.: Characterization of the dihydropterin reductase activity of pig liver methylenetetrahydrofolate reductase. J. Biol. Chem., 255, 6014–6017 (1980)
Guenther, B.D.; Sheppard, CA.; Tran, P.; Rozen, R.; Matthews, R.G.; Ludwig, M.L.: The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol., 6, 359–365 (1999)
Matthews, R.G.; Sheppard, C.; Goulding, C.: Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology. Eur. J. Pediatr., 157, 54–59 (1998)
Ravera, M.; Viazzi, F.; Berruti, V.; Leoncini, G.; Zagami, P.; Bezante, G.P.; Rosatto, N.; Ravazzolo, R.; Pontremoli, R.; Deferrari, G.: 5,10-Methylenetetrahydrofolate reductase polymorphism and early organ damage in primary hypertension. Am. J. Hypertens., 14, 371–376 (2001)
Shan, X.; Wang, L.; Hoffmaster, R.; Kruger, W.D.: Functional characterization of human methylenetetrahydrofolate reductase in Saccharomyces cerevisiae. J. Biol. Chem., 274, 32613–32618 (1999)
Suormala, T.; Gamse, G.; Fowler, B.: 5,10-Methylenetetrahydrofolate reductase (MTHFR) assay in the forward direction: residual activity in MTHFR deficiency. Clin. Chem., 48, 835–843 (2002)
Weisberg, L; Tran, P.; Christensen, B.; Sibani, S.; Rozen, R.: A second genetic polymorphism in methylenetetrahydrofolate reductase (MTHFR) associated with decreased enzyme activity. Mol. Genet. Metab., 64, 169–172 (1998)
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(2005). Methylenetetrahydrofolate reductase (NADPH). In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37648-8_20
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DOI: https://doi.org/10.1007/3-540-37648-8_20
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