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Volumn 28, Issue 6, 2006, Pages 595-605

Mitochondrial one-carbon metabolism is adapted to the specific needs of yeast, plants and mammals

Author keywords

[No Author keywords available]

Indexed keywords

CELL DIFFERENTIATION; CELL LINE; CELL ORGANELLE; CELL TYPE; CYTOPLASM; EUKARYOTE; FOLATE METABOLISM; MAMMAL; METABOLISM; MITOCHONDRION; NONHUMAN; PHOTORESPIRATION; PHOTOSYNTHESIS; PLANT; PLASTID; REVIEW; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; SURVIVAL RATE; SURVIVAL TIME; SYNTHESIS; YEAST;

EID: 33745095012     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20420     Document Type: Review
Times cited : (112)

References (100)
  • 1
    • 0033808685 scopus 로고    scopus 로고
    • Folic acid: Nutritional biochemistry, molecular biology, and role in disease processes
    • Lucock M. 2000. Folic acid: nutritional biochemistry, molecular biology, and role in disease processes. Mol Genet Metab 71:121-138.
    • (2000) Mol Genet Metab , vol.71 , pp. 121-138
    • Lucock, M.1
  • 2
    • 21744454670 scopus 로고    scopus 로고
    • Homocysteine and folic acid: Implications for pregnancy
    • Daly S, Cotter A, Molloy A, Scott J. 2005. Homocysteine and folic acid: implications for pregnancy. Semin Vasc Med 5:190-200.
    • (2005) Semin Vasc Med , vol.5 , pp. 190-200
    • Daly, S.1    Cotter, A.2    Molloy, A.3    Scott, J.4
  • 4
    • 0242610825 scopus 로고    scopus 로고
    • Role of Folate in colon cancer development and progression
    • Kim Y-I. 2003. Role of Folate in colon cancer development and progression. J Nutr 133:3731S-3739S.
    • (2003) J Nutr , vol.133
    • Kim, Y.-I.1
  • 5
    • 0037364417 scopus 로고    scopus 로고
    • Folate and homocysteine metabolism in neural plasticity and neurodegenerative disorders
    • Mattson MP, Shea TB. 2003. Folate and homocysteine metabolism in neural plasticity and neurodegenerative disorders. Trends Neurosci 26: 137-146.
    • (2003) Trends Neurosci , vol.26 , pp. 137-146
    • Mattson, M.P.1    Shea, T.B.2
  • 6
    • 0024560579 scopus 로고
    • Effect of nitrous oxide inactivation of vitamin B12-dependent methionine synthetase on the subcellular distribution of folate coenzymes in rat liver
    • Horne DW, Patterson D, Cook RJ. 1989. Effect of nitrous oxide inactivation of vitamin B12-dependent methionine synthetase on the subcellular distribution of folate coenzymes in rat liver. Arch Biochem Biophys 270:729-733.
    • (1989) Arch Biochem Biophys , vol.270 , pp. 729-733
    • Horne, D.W.1    Patterson, D.2    Cook, R.J.3
  • 7
    • 0024511031 scopus 로고
    • Interaction of folylpolyglutamates with enzymes in one-carbon metabolism
    • Schirch V, Strong WB. 1989. Interaction of folylpolyglutamates with enzymes in one-carbon metabolism. Arch Biochem Biophys 269:371-380.
    • (1989) Arch Biochem Biophys , vol.269 , pp. 371-380
    • Schirch, V.1    Strong, W.B.2
  • 8
    • 0027501365 scopus 로고
    • Regulation of folate and one-carbon metabolism in mammalian cells. III. Role of mitochondrial folylpoly-gamma-glutamate synthetase
    • Lin BF, Huang RF, Shane B. 1993. Regulation of folate and one-carbon metabolism in mammalian cells. III. Role of mitochondrial folylpoly-gamma- glutamate synthetase. J Biol Chem 268:21674-21679.
    • (1993) J Biol Chem , vol.268 , pp. 21674-21679
    • Lin, B.F.1    Huang, R.F.2    Shane, B.3
  • 9
    • 0027952012 scopus 로고
    • The affinity of pea cotyledon 10-formyltetrahydrofolate synthetase for polyglutamate substrates
    • Kirk CD, Imeson HC, Zheng L-L, Cossins EA. 1994. The affinity of pea cotyledon 10-formyltetrahydrofolate synthetase for polyglutamate substrates. Phytochemistry 35:291-296.
    • (1994) Phytochemistry , vol.35 , pp. 291-296
    • Kirk, C.D.1    Imeson, H.C.2    Zheng, L.-L.3    Cossins, E.A.4
  • 10
    • 0019511740 scopus 로고
    • Uptake of oxidized folates by rat liver mitochondria
    • Cybulski RL, Fisher RR. 1981. Uptake of oxidized folates by rat liver mitochondria. Biochim Biophys Acta 646:329-333.
    • (1981) Biochim Biophys Acta , vol.646 , pp. 329-333
    • Cybulski, R.L.1    Fisher, R.R.2
  • 11
    • 0030044426 scopus 로고    scopus 로고
    • In vivo analysis of folate coenzymes and their compartmentation in Saccharomyces cerevisiae
    • McNeil JB, Bognar AL, Pearlman RE. 1996. In vivo analysis of folate coenzymes and their compartmentation in Saccharomyces cerevisiae. Genetics 142:371-381.
    • (1996) Genetics , vol.142 , pp. 371-381
    • McNeil, J.B.1    Bognar, A.L.2    Pearlman, R.E.3
  • 12
    • 0028177297 scopus 로고
    • 13C NMR analysis of intercompartmental flow of one-carbon units into choline and purines in Saccharomyces cerevisiae
    • 13C NMR analysis of intercompartmental flow of one-carbon units into choline and purines in Saccharomyces cerevisiae. Biochemistry 33:74-82.
    • (1994) Biochemistry , vol.33 , pp. 74-82
    • Pasternack, L.B.1    Laude Jr., D.A.2    Appling, D.R.3
  • 13
    • 0017070283 scopus 로고
    • Intramitochondrial localization and proposed metabolic significance of serine transhydroxymethylase
    • Cybulski RL, Fisher RR. 1976. Intramitochondrial localization and proposed metabolic significance of serine transhydroxymethylase. Biochemistry 15:3183-3187.
    • (1976) Biochemistry , vol.15 , pp. 3183-3187
    • Cybulski, R.L.1    Fisher, R.R.2
  • 14
    • 0014218163 scopus 로고
    • Folate coenzyme pattern, folate linked enzymes and methionine biosynthesis in rat liver mitochondria
    • Wang FK, Koch J, Stokstad EL. 1967. Folate coenzyme pattern, folate linked enzymes and methionine biosynthesis in rat liver mitochondria. Biochem Z 346:458-466.
    • (1967) Biochem Z , vol.346 , pp. 458-466
    • Wang, F.K.1    Koch, J.2    Stokstad, E.L.3
  • 15
    • 0022971275 scopus 로고
    • Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae
    • Shannon KW, Rabinowitz JC. 1986. Purification and characterization of a mitochondrial isozyme of C1-tetrahydrofolate synthase from Saccharomyces cerevisiae. J Biol Chem 261:12266-12271.
    • (1986) J Biol Chem , vol.261 , pp. 12266-12271
    • Shannon, K.W.1    Rabinowitz, J.C.2
  • 16
    • 0025954883 scopus 로고
    • Compartmentation of folate-mediated one-carbon metabolism in eukaryotes
    • Appling DR. 1991. Compartmentation of folate-mediated one-carbon metabolism in eukaryotes. FASEB J 5:2645-2651.
    • (1991) FASEB J , vol.5 , pp. 2645-2651
    • Appling, D.R.1
  • 18
    • 0028310829 scopus 로고
    • Thymidylate synthase is localized to the nuclear periphery in the yeast Saccharomyces cerevisiae
    • Poon PP, Storms RK. 1994. Thymidylate synthase is localized to the nuclear periphery in the yeast Saccharomyces cerevisiae. J Biol Chem 269:8341-8347.
    • (1994) J Biol Chem , vol.269 , pp. 8341-8347
    • Poon, P.P.1    Storms, R.K.2
  • 19
    • 0034617076 scopus 로고    scopus 로고
    • Characterization of two 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase isozymes from Saccharomyces cerevisiae
    • Tibbetts AS, Appling DR. 2000. Characterization of two 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine monophosphate cyclohydrolase isozymes from Saccharomyces cerevisiae. J Biol Chem 275:20920-20927.
    • (2000) J Biol Chem , vol.275 , pp. 20920-20927
    • Tibbetts, A.S.1    Appling, D.R.2
  • 20
    • 0023001574 scopus 로고
    • Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase
    • Staben C, Rabinowitz JC. 1986. Nucleotide sequence of the Saccharomyces cerevisiae ADE3 gene encoding C1-tetrahydrofolate synthase. J Biol Chem 261:4629-4637.
    • (1986) J Biol Chem , vol.261 , pp. 4629-4637
    • Staben, C.1    Rabinowitz, J.C.2
  • 21
    • 0027530611 scopus 로고
    • Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase
    • West MG, Barlowe CK, Appling DR. 1993. Cloning and characterization of the Saccharomyces cerevisiae gene encoding NAD-dependent 5,10- methylenetetrahydrofolate dehydrogenase. J Biol Chem 268:153-160.
    • (1993) J Biol Chem , vol.268 , pp. 153-160
    • West, M.G.1    Barlowe, C.K.2    Appling, D.R.3
  • 22
    • 0026611611 scopus 로고
    • 13C NMR detection of folate-mediated serine and glycine synthesis in vivo in Saccharomyces cerevisiae
    • 13C NMR detection of folate-mediated serine and glycine synthesis in vivo in Saccharomyces cerevisiae. Biochemistry 31:8713-8719.
    • (1992) Biochemistry , vol.31 , pp. 8713-8719
    • Pasternack, L.B.1    Laude Jr., D.A.2    Appling, D.R.3
  • 23
    • 0029929264 scopus 로고    scopus 로고
    • Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae
    • West MG, Horne DW, Appling DR. 1996. Metabolic role of cytoplasmic isozymes of 5,10-methylenetetrahydrofolate dehydrogenase in Saccharomyces cerevisiae. Biochemistry 35:3122-3132.
    • (1996) Biochemistry , vol.35 , pp. 3122-3132
    • West, M.G.1    Horne, D.W.2    Appling, D.R.3
  • 24
    • 0024278721 scopus 로고
    • Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase
    • Shannon KW, Rabinowitz JC. 1988. Isolation and characterization of the Saccharomyces cerevisiae MIS1 gene encoding mitochondrial C1-tetrahydrofolate synthase. J Biol Chem 263:7717-7725.
    • (1988) J Biol Chem , vol.263 , pp. 7717-7725
    • Shannon, K.W.1    Rabinowitz, J.C.2
  • 25
    • 0034655980 scopus 로고    scopus 로고
    • Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae
    • DeSouza L, Shen Y, Bognar AL. 2000. Disruption of cytoplasmic and mitochondrial folylpolyglutamate synthetase activity in Saccharomyces cerevisiae. Arch Biochem Biophys 376:299-312.
    • (2000) Arch Biochem Biophys , vol.376 , pp. 299-312
    • DeSouza, L.1    Shen, Y.2    Bognar, A.L.3
  • 26
    • 0029671069 scopus 로고    scopus 로고
    • 13C NMR analysis of the use of alternative donors to the tetrahydrofolate-dependent one-carbon pools in Saccharomyces cerevisiae
    • 13C NMR analysis of the use of alternative donors to the tetrahydrofolate-dependent one-carbon pools in Saccharomyces cerevisiae. Arch Biochem Biophys 326:158-165.
    • (1996) Arch Biochem Biophys , vol.326 , pp. 158-165
    • Pasternack, L.B.1    Littlepage, L.E.2    Laude Jr., D.A.3    Appling, D.R.4
  • 27
    • 0030862155 scopus 로고    scopus 로고
    • Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae
    • Kastanos EK, Woldman YY, Appling DR. 1997. Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae. Biochemistry 36: 14956-14964.
    • (1997) Biochemistry , vol.36 , pp. 14956-14964
    • Kastanos, E.K.1    Woldman, Y.Y.2    Appling, D.R.3
  • 28
    • 0034613194 scopus 로고    scopus 로고
    • Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae
    • Piper MD, Hong SP, Ball GE, Dawes IW. 2000. Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae. J Biol Chem 275:30987-30995.
    • (2000) J Biol Chem , vol.275 , pp. 30987-30995
    • Piper, M.D.1    Hong, S.P.2    Ball, G.E.3    Dawes, I.W.4
  • 29
    • 0036526578 scopus 로고    scopus 로고
    • A general method for determining the contribution of split pathways in metabolite production in the yeast Saccharomyces cerevisiae
    • Woldman Y, Appling DR. 2002. A general method for determining the contribution of split pathways in metabolite production in the yeast Saccharomyces cerevisiae. Metab Eng 4:170-181.
    • (2002) Metab Eng , vol.4 , pp. 170-181
    • Woldman, Y.1    Appling, D.R.2
  • 30
    • 0021994870 scopus 로고
    • Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism
    • Appling DR, Rabinowitz JC. 1985. Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism. J Biol Chem 260:1248-1256.
    • (1985) J Biol Chem , vol.260 , pp. 1248-1256
    • Appling, D.R.1    Rabinowitz, J.C.2
  • 31
    • 0034015357 scopus 로고    scopus 로고
    • Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA
    • Li Y, Holmes WB, Appling DR, RajBhandary UL. 2000. Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA. J Bacteriol 182:2886-2892.
    • (2000) J Bacteriol , vol.182 , pp. 2886-2892
    • Li, Y.1    Holmes, W.B.2    Appling, D.R.3    Rajbhandary, U.L.4
  • 33
    • 0031172735 scopus 로고    scopus 로고
    • Folates and one-carbon metabolism in plants and fungi
    • Cossins EA, Chen L. 1997. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45:437-452.
    • (1997) Phytochemistry , vol.45 , pp. 437-452
    • Cossins, E.A.1    Chen, L.2
  • 35
    • 0028858802 scopus 로고
    • A 5,10-methylenetetrahydrofolate dehydrogenase: 5,10- methenyltetrahydrofolate cyclohydrolase protein from Pisum sativum
    • Kirk CD, Chen L, Imeson HC, Cossins EA. 1995. A 5,10- methylenetetrahydrofolate dehydrogenase: 5,10-methenyltetrahydrofolate cyclohydrolase protein from Pisum sativum. Phytochemistry 39:1309-1317.
    • (1995) Phytochemistry , vol.39 , pp. 1309-1317
    • Kirk, C.D.1    Chen, L.2    Imeson, H.C.3    Cossins, E.A.4
  • 36
    • 0031400751 scopus 로고    scopus 로고
    • Distribution of folate derivatives and enzymes for synthesis of 10-formyltetrahydrofolate in cytosolic and mitochondrial fractions of pea leaves
    • Chen L, Chan SY, Cossins EA. 1997. Distribution of folate derivatives and enzymes for synthesis of 10-formyltetrahydrofolate in cytosolic and mitochondrial fractions of pea leaves. Plant Physiol 115:299-309.
    • (1997) Plant Physiol , vol.115 , pp. 299-309
    • Chen, L.1    Chan, S.Y.2    Cossins, E.A.3
  • 37
    • 0033151551 scopus 로고    scopus 로고
    • Biochemical dissection of photorespiration
    • Douce R, Neuburger M. 1999. Biochemical dissection of photorespiration. Curr Opin Plant Biol 2:214-222.
    • (1999) Curr Opin Plant Biol , vol.2 , pp. 214-222
    • Douce, R.1    Neuburger, M.2
  • 38
    • 0027966736 scopus 로고
    • A mutant of Arabidopsis thaliana that defines a new locus for glycine decarboxylation
    • Artus NN, Naito S, Somerville CR. 1994. A mutant of Arabidopsis thaliana that defines a new locus for glycine decarboxylation. Plant Cell Physiol 35:879-885.
    • (1994) Plant Cell Physiol , vol.35 , pp. 879-885
    • Artus, N.N.1    Naito, S.2    Somerville, C.R.3
  • 39
    • 0000641262 scopus 로고
    • Photorespiration deficient mutants of Arabidopsis thaliana lacking mitochondrial serine transhydroxymethylase activity
    • Somerville CR, Ogren WL. 1981. Photorespiration deficient mutants of Arabidopsis thaliana lacking mitochondrial serine transhydroxymethylase activity. Plant Physiol 67:666-671.
    • (1981) Plant Physiol , vol.67 , pp. 666-671
    • Somerville, C.R.1    Ogren, W.L.2
  • 40
    • 0037365133 scopus 로고    scopus 로고
    • Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana
    • Li R, Moore M, King J. 2003. Investigating the regulation of one-carbon metabolism in Arabidopsis thaliana. Plant Cell Physiol 44:233-241.
    • (2003) Plant Cell Physiol , vol.44 , pp. 233-241
    • Li, R.1    Moore, M.2    King, J.3
  • 41
    • 0029659032 scopus 로고    scopus 로고
    • 13C Nuclear magnetic resonance detection of interactions of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboxylase complex activities in Arabidopsis
    • 13C Nuclear magnetic resonance detection of interactions of serine hydroxymethyltransferase with C1-tetrahydrofolate synthase and glycine decarboxylase complex activities in Arabidopsis. Plant Physiol 112:207-216.
    • (1996) Plant Physiol , vol.112 , pp. 207-216
    • Prabhu, V.1    Chatson, K.B.2    Abrams, G.D.3    King, J.4
  • 42
    • 0032734088 scopus 로고    scopus 로고
    • Glycine and serine catabolism in non-photosynthetic higher plant cells: Their role in C1 metabolism
    • Mouillon J-M, Aubert S, Bourguignon J, Gout E, Douce R, et al. 1999. Glycine and serine catabolism in non-photosynthetic higher plant cells: their role in C1 metabolism. Plant J 20:197-205.
    • (1999) Plant J , vol.20 , pp. 197-205
    • Mouillon, J.-M.1    Aubert, S.2    Bourguignon, J.3    Gout, E.4    Douce, R.5
  • 44
    • 0029869004 scopus 로고    scopus 로고
    • Mitochondria are a major site for folate and thymidylate synthesis in plants
    • Neuburger M, Rébeillé F, Jourdain A, Nakamura S, Douce R. 1996. Mitochondria are a major site for folate and thymidylate synthesis in plants. J Biol Chem 271:9466-9472.
    • (1996) J Biol Chem , vol.271 , pp. 9466-9472
    • Neuburger, M.1    Rébeillé, F.2    Jourdain, A.3    Nakamura, S.4    Douce, R.5
  • 45
    • 0032989239 scopus 로고    scopus 로고
    • Photorespiratory metabolism of glyoxylate and formate in glycine-accumulating mutants of barley and Amaranthus edulis
    • Wingler A, Lea PJ, Leegood RC. 1999. Photorespiratory metabolism of glyoxylate and formate in glycine-accumulating mutants of barley and Amaranthus edulis. Planta 207:518-526.
    • (1999) Planta , vol.207 , pp. 518-526
    • Wingler, A.1    Lea, P.J.2    Leegood, R.C.3
  • 46
    • 0031105834 scopus 로고    scopus 로고
    • Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein
    • Luo M, Orsi R, Patrucco E, Pancaldi S, Cella R. 1997. Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein. Plant Mol Biol 33:709-722.
    • (1997) Plant Mol Biol , vol.33 , pp. 709-722
    • Luo, M.1    Orsi, R.2    Patrucco, E.3    Pancaldi, S.4    Cella, R.5
  • 47
    • 0031047734 scopus 로고    scopus 로고
    • Reexamination of the intracellular localization of de novo purine synthesis in cowpea nodules
    • Atkins CA, Smith PMC, Storer PJ. 1997. Reexamination of the intracellular localization of de novo purine synthesis in cowpea nodules. Plant Physiol 113:127-135.
    • (1997) Plant Physiol , vol.113 , pp. 127-135
    • Atkins, C.A.1    Smith, P.M.C.2    Storer, P.J.3
  • 48
    • 2542430082 scopus 로고    scopus 로고
    • Methionine Metabolism in Plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosoi
    • Ravanel S, Block MA, Rippert P, Jabrin S, Curien G, et al. 2004. Methionine Metabolism in Plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosoi. J Biol Chem 279:22548-22557.
    • (2004) J Biol Chem , vol.279 , pp. 22548-22557
    • Ravanel, S.1    Block, M.A.2    Rippert, P.3    Jabrin, S.4    Curien, G.5
  • 49
    • 0029200019 scopus 로고
    • Evidence for three serine hydroxymethyltransferases in green leaf cells. Purification and characterization of the mitochondrial and chloroplastic isoforms
    • Besson V, Neuburger M, Rebeille F, Douce R. 1995. Evidence for three serine hydroxymethyltransferases in green leaf cells. Purification and characterization of the mitochondrial and chloroplastic isoforms. Plant Physiol Biochem 33:665-673.
    • (1995) Plant Physiol Biochem , vol.33 , pp. 665-673
    • Besson, V.1    Neuburger, M.2    Rebeille, F.3    Douce, R.4
  • 50
    • 0000930367 scopus 로고
    • Effects of glycolate pathway intermediates on glycine decarboxylation and serine synthesis in pea (Pisum sativum L.)
    • Shingles R, Woodrow L, Grodzinski B. 1984. Effects of glycolate pathway intermediates on glycine decarboxylation and serine synthesis in pea (Pisum sativum L.). Plant Physiol 74:705-710.
    • (1984) Plant Physiol , vol.74 , pp. 705-710
    • Shingles, R.1    Woodrow, L.2    Grodzinski, B.3
  • 52
    • 0027223085 scopus 로고
    • Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization
    • Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, et al. 1993. Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem 268:11910-11916.
    • (1993) J Biol Chem , vol.268 , pp. 11910-11916
    • Garrow, T.A.1    Brenner, A.A.2    Whitehead, V.M.3    Chen, X.N.4    Duncan, R.G.5
  • 53
    • 0023787347 scopus 로고
    • Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase
    • Hum DW, Bell AW, Rozen R, MacKenzie RE. 1988. Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem 263:15946-15950.
    • (1988) J Biol Chem , vol.263 , pp. 15946-15950
    • Hum, D.W.1    Bell, A.W.2    Rozen, R.3    MacKenzie, R.E.4
  • 54
    • 0028783622 scopus 로고
    • Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
    • Pelletier JN, MacKenzie RE. 1995. Binding and interconversion of tetrahydrofolates at a single site in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry 34:12673-12680.
    • (1995) Biochemistry , vol.34 , pp. 12673-12680
    • Pelletier, J.N.1    MacKenzie, R.E.2
  • 55
    • 0016425473 scopus 로고
    • Methylenetetrahydrofolate reductase in the rat central nervous system: Intracellular and regional distribution
    • Burton EG, Sallach HJ. 1975. Methylenetetrahydrofolate reductase in the rat central nervous system: intracellular and regional distribution. Arch Biochem Biophys 166:483-494.
    • (1975) Arch Biochem Biophys , vol.166 , pp. 483-494
    • Burton, E.G.1    Sallach, H.J.2
  • 56
    • 0021769542 scopus 로고
    • Kinetic isotope effects on the oxidation of reduced nicotinamide adenine-dinucleotide phosphate by the flavoprotein methylenetetrahydrofolate reductase
    • Vanoni MA, Matthews RG. 1984. Kinetic isotope effects on the oxidation of reduced nicotinamide adenine-dinucleotide phosphate by the flavoprotein methylenetetrahydrofolate reductase. Biochemistry 23:5272-5279.
    • (1984) Biochemistry , vol.23 , pp. 5272-5279
    • Vanoni, M.A.1    Matthews, R.G.2
  • 58
    • 0026335113 scopus 로고
    • Production and characterization of monoclonal-antibodies that localize human thymidylate synthase in the cytoplasm of human cells and tissue
    • Johnston PG, Liang CM, Henry S, Chabner BA, Allegra CJ. 1991. Production and characterization of monoclonal-antibodies that localize human thymidylate synthase in the cytoplasm of human cells and tissue. Cancer Res 51:6668-6676.
    • (1991) Cancer Res , vol.51 , pp. 6668-6676
    • Johnston, P.G.1    Liang, C.M.2    Henry, S.3    Chabner, B.A.4    Allegra, C.J.5
  • 59
    • 0032515921 scopus 로고    scopus 로고
    • Molecular cloning, characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene
    • Girgis S, Nasrallah IM, Sun JR, Oppenheim E, Zanetti KA, et al. 1998. Molecular cloning, characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene. Gene 210:315-324.
    • (1998) Gene , vol.210 , pp. 315-324
    • Girgis, S.1    Nasrallah, I.M.2    Sun, J.R.3    Oppenheim, E.4    Zanetti, K.A.5
  • 60
    • 0023213610 scopus 로고
    • Activities of serine hydroxymethyltransferase in murine tissues and tumours
    • Tendler SJB, Threadgill MD, Tisdale MJ. 1987. Activities of serine hydroxymethyltransferase in murine tissues and tumours. Cancer Lett 36:65-69.
    • (1987) Cancer Lett , vol.36 , pp. 65-69
    • Tendler, S.J.B.1    Threadgill, M.D.2    Tisdale, M.J.3
  • 61
    • 4444261606 scopus 로고    scopus 로고
    • The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth
    • Di Pietro E, Wang XL, MacKenzie RE. 2004. The expression of mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase supports a role in rapid cell growth. Biochim Biophys Acta 1674:78-84.
    • (2004) Biochim Biophys Acta , vol.1674 , pp. 78-84
    • Di Pietro, E.1    Wang, X.L.2    MacKenzie, R.E.3
  • 62
    • 0025676019 scopus 로고
    • Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells
    • Smith GK, Banks SD, Monaco TJ, Rigual R, Duch DS, et al. 1990. Activity of an NAD-dependent 5,10-methylenetetrahydrofolate dehydrogenase in normal tissue, neoplastic cells, and oncogene-transformed cells. Arch Biochem Biophys 283:367-371.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 367-371
    • Smith, G.K.1    Banks, S.D.2    Monaco, T.J.3    Rigual, R.4    Duch, D.S.5
  • 63
    • 0022378021 scopus 로고
    • NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells
    • Mejia NR, MacKenzie RE. 1985. NAD-dependent methylenetetrahydrofolate dehydrogenase is expressed by immortal cells. J Biol Chem 260: 14616-14620.
    • (1985) J Biol Chem , vol.260 , pp. 14616-14620
    • Mejia, N.R.1    MacKenzie, R.E.2
  • 64
    • 0036707812 scopus 로고    scopus 로고
    • 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, et al. 2002. Multiple transcription start sites and alternative splicing in the methylenetetrahydrofolate reductase gene result in two enzyme isoforms. Mamm Genome 13:483-492.
    • (2002) Mamm Genome , vol.13 , pp. 483-492
    • Tran, P.1    Leclerc, D.2    Chan, M.3    Pai, A.4    Hiou-Tim, F.5
  • 65
    • 0018069563 scopus 로고
    • Methionine metabolism in mammals: Regulation of methylenetetrahydrofolate reductase content of rat tissues
    • Finkelstein JD, Martin JJ, Kyle WE, Harris BJ. 1978. Methionine metabolism in mammals: regulation of methylenetetrahydrofolate reductase content of rat tissues. Arch Biochem Biophys 191:153-160.
    • (1978) Arch Biochem Biophys , vol.191 , pp. 153-160
    • Finkelstein, J.D.1    Martin, J.J.2    Kyle, W.E.3    Harris, B.J.4
  • 66
    • 0035041597 scopus 로고    scopus 로고
    • Ontogeny of hepatic enzymes involved in serine- and folate-dependent one-carbon metabolism in rabbits
    • Thompson HR, Jones GM, Narkewicz MR. 2001. Ontogeny of hepatic enzymes involved In serine- and folate-dependent one-carbon metabolism in rabbits. Am J Physiol Gastrointest Liver Physiol 280:G873-G878.
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.280
    • Thompson, H.R.1    Jones, G.M.2    Narkewicz, M.R.3
  • 67
    • 0036316013 scopus 로고    scopus 로고
    • A functional screen for myc-responsive genes reveals serine hydroxymethyltransferase, a major source of the one-carbon unit for cell metabolism
    • Nikiforov MA, Chandriani S, O'Connell B, Petrenko O, Kotenko I, et al. 2002. A functional screen for myc-responsive genes reveals serine hydroxymethyltransferase, a major source of the one-carbon unit for cell metabolism. Mol Cell Biol 22:5793-5800.
    • (2002) Mol Cell Biol , vol.22 , pp. 5793-5800
    • Ma, N.1    Chandriani, S.2    O'Connell, B.3    Petrenko, O.4    Kotenko, I.5
  • 68
    • 0015136686 scopus 로고
    • Glycine metabolism in rat liver mitochondria: V. Intramitochondrial localization of the reversible glycine cleavage system and serine hydroxymethyltransferase
    • Motokawa Y, Kikuchi G. 1971. Glycine metabolism in rat liver mitochondria: V. Intramitochondrial localization of the reversible glycine cleavage system and serine hydroxymethyltransferase. Arch Biochem Biophys 146:461-466.
    • (1971) Arch Biochem Biophys , vol.146 , pp. 461-466
    • Motokawa, Y.1    Kikuchi, G.2
  • 69
    • 0019519311 scopus 로고
    • Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics
    • Wittwer AJ, Wagner C. 1981. Identification of the folate-binding proteins of rat liver mitochondria as dimethylglycine dehydrogenase and sarcosine dehydrogenase. Purification and folate-binding characteristics. J Biol Chem 256:4102-4108.
    • (1981) J Biol Chem , vol.256 , pp. 4102-4108
    • Wittwer, A.J.1    Wagner, C.2
  • 70
    • 0024422803 scopus 로고
    • Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase
    • Peri KG, Belanger C, Mackenzie RE. 1989. Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase. Nucleic Acids Res 17:8853.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8853
    • Peri, K.G.1    Belanger, C.2    Mackenzie, R.E.3
  • 71
    • 0023695662 scopus 로고
    • NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme
    • Mejia NR, MacKenzie RE. 1988. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase in transformed cells is a mitochondrial enzyme. Biochem Biophys Res Commun 155:1-6.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 1-6
    • Mejia, N.R.1    MacKenzie, R.E.2
  • 72
    • 14844297720 scopus 로고    scopus 로고
    • Disruption of the Mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria
    • Christensen KE, Patel H, Kuzmanov U, Mejia NR, MacKenzie RE. 2005. Disruption of the Mthfd1 gene reveals a monofunctional 10-formyltetrahydrofolate synthetase in mammalian mitochondria. J Biol Chem 280:7597-7602.
    • (2005) J Biol Chem , vol.280 , pp. 7597-7602
    • Christensen, K.E.1    Patel, H.2    Kuzmanov, U.3    Mejia, N.R.4    MacKenzie, R.E.5
  • 73
    • 26844566507 scopus 로고    scopus 로고
    • Enzymatic characterization of human mitochondrial C-1-tetrahydrofolate synthase
    • Walkup AS, Appling DR. 2005. Enzymatic characterization of human mitochondrial C-1-tetrahydrofolate synthase. Arch Biochem Biophys 442:196-205.
    • (2005) Arch Biochem Biophys , vol.442 , pp. 196-205
    • Walkup, A.S.1    Appling, D.R.2
  • 74
    • 0242353316 scopus 로고    scopus 로고
    • Human mitochondrial C1-tetrahydrofolate synthase: Gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary cells
    • Prasannan P, Pike S, Peng K, Shane B, Appling DR. 2003. Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary cells. J Biol Chem 278:43178-43187.
    • (2003) J Biol Chem , vol.278 , pp. 43178-43187
    • Prasannan, P.1    Pike, S.2    Peng, K.3    Shane, B.4    Appling, D.R.5
  • 75
    • 0842286542 scopus 로고    scopus 로고
    • A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma
    • Sugiura T, Nagano Y, Inoue T, Hirotani K. 2004. A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma. Biochem Biophys Res Commun 315:204-211.
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 204-211
    • Sugiura, T.1    Nagano, Y.2    Inoue, T.3    Hirotani, K.4
  • 76
    • 0027384199 scopus 로고
    • NAD-dependent methylenetetrahydrofolate dehydrogenase- methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene
    • Yang XM, MacKenzie RE. 1993. NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is the mammalian homolog of the mitochondrial enzyme encoded by the yeast MIS1 gene. Biochemistry 32:11118-11123.
    • (1993) Biochemistry , vol.32 , pp. 11118-11123
    • Yang, X.M.1    MacKenzie, R.E.2
  • 77
    • 10744224439 scopus 로고    scopus 로고
    • Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria
    • Mootha VK, Bunkenborg J, Olsen JV, Hjerrild M, Wisniewski JR, et al. 2003. Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115:629-640.
    • (2003) Cell , vol.115 , pp. 629-640
    • Mootha, V.K.1    Bunkenborg, J.2    Olsen, J.V.3    Hjerrild, M.4    Wisniewski, J.R.5
  • 78
    • 0038819954 scopus 로고    scopus 로고
    • Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase are glycine auxotrophs
    • Patel H, Di Pietro E, MacKenzie RE. 2003. Mammalian fibroblasts lacking mitochondrial NAD+-dependent methylenetetrahydrofolate dehydrogenase- cyclohydrolase are glycine auxotrophs. J Biol Chem 278:19436-19441.
    • (2003) J Biol Chem , vol.278 , pp. 19436-19441
    • Patel, H.1    Di Pietro, E.2    MacKenzie, R.E.3
  • 79
    • 26644472196 scopus 로고    scopus 로고
    • Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase
    • Christensen KE, Mirza IA, Berghuis AM, Mackenzie RE. 2005. Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase. J Biol Chem 280:34316-34323.
    • (2005) J Biol Chem , vol.280 , pp. 34316-34323
    • Christensen, K.E.1    Mirza, I.A.2    Berghuis, A.M.3    Mackenzie, R.E.4
  • 80
    • 0036647022 scopus 로고    scopus 로고
    • Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase- cyclohydrolase derived from a trifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase-synthetase
    • Patel H, Christensen KE, Mejia N, MacKenzie RE. 2002. Mammalian mitochondrial methylenetetrahydrofolate dehydrogenase-cyclohydrolase derived from a trifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase- synthetase. Arch Biochem Biophys 403:145-148.
    • (2002) Arch Biochem Biophys , vol.403 , pp. 145-148
    • Patel, H.1    Christensen, K.E.2    Mejia, N.3    MacKenzie, R.E.4
  • 81
    • 0031035739 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene
    • Stover PJ, Chen LH, Sun JR, Stover DM, Keyomarsi K, et al. 1997. Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem 272:1842-1848.
    • (1997) J Biol Chem , vol.272 , pp. 1842-1848
    • Stover, P.J.1    Chen, L.H.2    Sun, J.R.3    Stover, D.M.4    Keyomarsi, K.5
  • 82
    • 17844406376 scopus 로고    scopus 로고
    • Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia
    • Kure S, Kojima K, Kudo T, Kanno K, Aoki Y, et al. 2001. Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia. J Hum Genet 46:378-384.
    • (2001) J Hum Genet , vol.46 , pp. 378-384
    • Kure, S.1    Kojima, K.2    Kudo, T.3    Kanno, K.4    Aoki, Y.5
  • 83
    • 0027500390 scopus 로고
    • NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: Detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines
    • Peri KG, MacKenzie RE. 1993. NAD(+)-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase: detection of the mRNA in normal murine tissues and transcriptional regulation of the gene in cell lines. Biochim Biophys Acta 1171:281-287.
    • (1993) Biochim Biophys Acta , vol.1171 , pp. 281-287
    • Peri, K.G.1    MacKenzie, R.E.2
  • 84
    • 0034711259 scopus 로고    scopus 로고
    • Retrovirally mediated complementation of the glyB phenotype. Cloning of a human gene encoding the carrier for entry of folates into mitochondria
    • Titus SA, Moran RG. 2000. Retrovirally mediated complementation of the glyB phenotype. Cloning of a human gene encoding the carrier for entry of folates into mitochondria. J Biol Chem 275:36811-36817.
    • (2000) J Biol Chem , vol.275 , pp. 36811-36817
    • Titus, S.A.1    Moran, R.G.2
  • 85
    • 0026686811 scopus 로고
    • Expression cloning of a human cDNA encoding folylpoly({gamma}-glutamate) synthetase and determination of its primary structure
    • Garrow TA, Admon A, Shane B. 1992. Expression cloning of a human cDNA encoding folylpoly({gamma}-glutamate) synthetase and determination of its primary structure. Proc Natl Acad Sci USA 89:9151-9155.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9151-9155
    • Garrow, T.A.1    Admon, A.2    Shane, B.3
  • 86
    • 0030030729 scopus 로고    scopus 로고
    • Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells
    • Narkewicz MR, Sauls SD, Tjoa SS, Teng C, Fennessey PV. 1996. Evidence for intracellular partitioning of serine and glycine metabolism in Chinese hamster ovary cells. Biochem J 313:991-996.
    • (1996) Biochem J , vol.313 , pp. 991-996
    • Narkewicz, M.R.1    Sauls, S.D.2    Tjoa, S.S.3    Teng, C.4    Fennessey, P.V.5
  • 89
    • 0033523088 scopus 로고    scopus 로고
    • Flux of the L-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase
    • Xue HH, Sakaguchi T, Fujie M, Ogawa H, Ichiyama A. 1999. Flux of the L-serine metabolism in rabbit, human, and dog livers. Substantial contributions of both mitochondrial and peroxisomal serine:pyruvate/alanine:glyoxylate aminotransferase. J Biol Chem 274:16028-16033.
    • (1999) J Biol Chem , vol.274 , pp. 16028-16033
    • Xue, H.H.1    Sakaguchi, T.2    Fujie, M.3    Ogawa, H.4    Ichiyama, A.5
  • 90
    • 0036261663 scopus 로고    scopus 로고
    • Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development
    • Di Pietro E, Sirois J, Tremblay ML, MacKenzie RE. 2002. Mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase is essential for embryonic development. Mol Cell Biol 22:4158-4166.
    • (2002) Mol Cell Biol , vol.22 , pp. 4158-4166
    • Di Pietro, E.1    Sirois, J.2    Tremblay, M.L.3    MacKenzie, R.E.4
  • 91
    • 15644377868 scopus 로고    scopus 로고
    • 5-Formyltetrahydrofolate regulates homocysteine remethylation in human neuroblastoma
    • Girgis S, Suh JR, Jolivet J, Stover PJ. 1997. 5-Formyltetrahydrofolate regulates homocysteine remethylation in human neuroblastoma. J Biol Chem 272:4729-4734.
    • (1997) J Biol Chem , vol.272 , pp. 4729-4734
    • Girgis, S.1    Suh, J.R.2    Jolivet, J.3    Stover, P.J.4
  • 92
    • 0034659692 scopus 로고    scopus 로고
    • Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain: The effects of site-directed mutagenesis of NADP binding residues
    • Pawelek PD, Allaire M, Cygler M, MacKenzie RE. 2000. Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/ cyclohydrolase domain: the effects of site-directed mutagenesis of NADP binding residues. Biochim Biophys Acta 1479:59-68.
    • (2000) Biochim Biophys Acta , vol.1479 , pp. 59-68
    • Pawelek, P.D.1    Allaire, M.2    Cygler, M.3    MacKenzie, R.E.4
  • 93
    • 0023789244 scopus 로고
    • In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units
    • Barlowe CK, Appling DR. 1988. In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units. Biofactors 1:171-176.
    • (1988) Biofactors , vol.1 , pp. 171-176
    • Barlowe, C.K.1    Appling, D.R.2
  • 94
    • 0027160524 scopus 로고
    • Characterization of the folate-dependent mitochondrial oxidation of carbon 3 of serine
    • Garcia-Martinez LF, Appling DR. 1993. Characterization of the folate-dependent mitochondrial oxidation of carbon 3 of serine. Biochemistry 32:4671-4676.
    • (1993) Biochemistry , vol.32 , pp. 4671-4676
    • Garcia-Martinez, L.F.1    Appling, D.R.2
  • 95
    • 0034015564 scopus 로고    scopus 로고
    • Vitamin B-6 deficiency in rats reduces hepatic serine hydroxymethyltransferase and cystathionine beta-synthase activities and rates of in vivo protein turnover, homocysteine remethylation and transsulfuration
    • Martinez M, Cuskelly GJ, Williamson J, Toth JP, Gregory JF 3rd. 2000. Vitamin B-6 deficiency in rats reduces hepatic serine hydroxymethyltransferase and cystathionine beta-synthase activities and rates of in vivo protein turnover, homocysteine remethylation and transsulfuration. J Nutr 130:1115-1123.
    • (2000) J Nutr , vol.130 , pp. 1115-1123
    • Martinez, M.1    Cuskelly, G.J.2    Williamson, J.3    Toth, J.P.4    Gregory III, J.F.5
  • 96
    • 0033646360 scopus 로고    scopus 로고
    • 3]serine allows in vivo kinetic measurement of serine turnover, homocysteine remethylation, and transsulfuration processes in human one-carbon metabolism
    • 3]serine allows in vivo kinetic measurement of serine turnover, homocysteine remethylation, and transsulfuration processes in human one-carbon metabolism. Am J Clin Nutr 72:1535-1541.
    • (2000) Am J Clin Nutr , vol.72 , pp. 1535-1541
    • Gregory III, J.F.1    Cuskelly, G.J.2    Shane, B.3    Toth, J.P.4    Baumgartner, T.G.5
  • 97
    • 0037064008 scopus 로고    scopus 로고
    • Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses
    • Herbig K, Chiang EP, Lee LR, Hills J, Shane B, et al. 2002. Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses. J Biol Chem 277:38381-38389.
    • (2002) J Biol Chem , vol.277 , pp. 38381-38389
    • Herbig, K.1    Chiang, E.P.2    Lee, L.R.3    Hills, J.4    Shane, B.5
  • 98
    • 0942265677 scopus 로고    scopus 로고
    • Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor
    • Davis SR, Stacpoole PW, Williamson J, Kick LS, Quinlivan EP, et al. 2004. Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor. Am J Physiol Endocrinol Metab 286:E272-279.
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Davis, S.R.1    Stacpoole, P.W.2    Williamson, J.3    Kick, L.S.4    Quinlivan, E.P.5
  • 99
    • 0034748746 scopus 로고    scopus 로고
    • Metabolism of methionine derived from deuterated serine infused in a human
    • Baggott JE. 2001. Metabolism of methionine derived from deuterated serine infused in a human. Am J Clin Nutr 74:701-703.
    • (2001) Am J Clin Nutr , vol.74 , pp. 701-703
    • Baggott, J.E.1
  • 100
    • 84855252084 scopus 로고    scopus 로고
    • Bethesda (MD): National Center for Biotechnology Information, National Library of Medicine. (dbSNP Build ID: 125)
    • Database of Single Nucleotide Polymorphisms (dbSNP). Bethesda (MD): National Center for Biotechnology Information, National Library of Medicine. (dbSNP Build ID: 125). Available from: http://www.ncbi.nlm. nih.gov/SNP/.
    • Database of Single Nucleotide Polymorphisms (dbSNP)


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