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Volumn 26, Issue 3, 2003, Pages 121-132

Hyperhomocysteinemia: Genetic determinants and selected mouse models

Author keywords

Animal; Cystathionine beta synthase; Folic acid; Genes; Homocysteine; Homocystinuria; Hyperhomocys teinemia; Mice; Models; Polymorphism (genetics); Review; Transcabolamins; Vitamin B 12

Indexed keywords

5 METHYLTETRAHYDROFOLIC ACID; 5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); ADENOSINE DEAMINASE; ADENOSYLHOMOCYSTEINASE; APOLIPOPROTEIN E; ARYLDIALKYLPHOSPHATASE; BINDING PROTEIN; CYSTATHIONINE BETA SYNTHASE; FOLIC ACID; GAMMA GLUTAMYL HYDROLASE; HOMOCYSTEINE; METHIONINE; METHIONINE SYNTHASE; METHIONINE SYNTHASE REDUCTASE; OXIDOREDUCTASE; REDUCED FOLATE CARRIER; THYMIDYLATE SYNTHASE; TRANSCOBALAMIN II; UNCLASSIFIED DRUG;

EID: 0041427757     PISSN: 0147958X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (8)

References (58)
  • 1
    • 0031821779 scopus 로고    scopus 로고
    • Homocysteine and vitamins in cardiovascular disease
    • Jacobsen DW. Homocysteine and vitamins in cardiovascular disease. Clin Chem 1998;44:1833-43.
    • (1998) Clin Chem , vol.44 , pp. 1833-1843
    • Jacobsen, D.W.1
  • 2
    • 0042250902 scopus 로고    scopus 로고
    • Cystathionine β-synthase and its deficiency
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Kraus JP, Kozich V. Cystathionine β-synthase and its deficiency. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 223-43.
    • (2001) Homocysteine in Health and Disease , pp. 223-243
    • Kraus, J.P.1    Kozich, V.2
  • 3
    • 0007475314 scopus 로고    scopus 로고
    • Inborn errors of folate and cobalamin metabolism
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Rosenblatt DS. Inborn errors of folate and cobalamin metabolism. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 244-58.
    • (2001) Homocysteine in Health and Disease , pp. 244-258
    • Rosenblatt, D.S.1
  • 5
    • 0003054506 scopus 로고    scopus 로고
    • Diseases and drugs associated with hyperhomocysteinemia
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Bloom HJ. Diseases and drugs associated with hyperhomocysteinemia. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 331-40.
    • (2001) Homocysteine in Health and Disease , pp. 331-340
    • Bloom, H.J.1
  • 6
    • 0030946890 scopus 로고    scopus 로고
    • Clinical chemistry and molecular biology of homocysteine metabolism: An update
    • Miner SE, Evrovski J, Cole DE. Clinical chemistry and molecular biology of homocysteine metabolism: an update. Clin Biochem 1997;30:189-201.
    • (1997) Clin Biochem , vol.30 , pp. 189-201
    • Miner, S.E.1    Evrovski, J.2    Cole, D.E.3
  • 7
    • 0032499024 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis
    • Welch GN, Loscalzo J. Homocysteine and atherothrombosis. N Engl J Med 1998;338:1042-50.
    • (1998) N Engl J Med , vol.338 , pp. 1042-1050
    • Welch, G.N.1    Loscalzo, J.2
  • 9
    • 0034703861 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II: A polymorphism associated with lower levels of serum folate and hyperhomocysteinemia
    • Devlin AM, Ling E, Peerson JM, Fernando S, Clarke R. Smith AD, et al. Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. Hum Mol Genet 2000;9:2837-44.
    • (2000) Hum Mol Genet , vol.9 , pp. 2837-2844
    • Devlin, A.M.1    Ling, E.2    Peerson, J.M.3    Fernando, S.4    Clarke, R.5    Smith, A.D.6
  • 11
    • 0036276029 scopus 로고    scopus 로고
    • The glutamate carboxypeptidase gene II (C>T) polymorphism does not affect folate status in the Framingham Offspring cohort
    • Vargas-Martinez C, Ordovas JM, Wilson PW, Selhub J. The glutamate carboxypeptidase gene II (C>T) polymorphism does not affect folate status in the Framingham Offspring cohort. J Nutr 2002;132:1176-9.
    • (2002) J Nutr , vol.132 , pp. 1176-1179
    • Vargas-Martinez, C.1    Ordovas, J.M.2    Wilson, P.W.3    Selhub, J.4
  • 12
    • 0345373993 scopus 로고    scopus 로고
    • Effect of glutamate carboxypepetidase II and the reduced folate carrier polymorphisms on folate and total homocysteine concentrations in dialysis patients
    • Födinger M, Dierkes J, Skoupy S, Röhrer C, Hagen W, Puttinger H, et al. Effect of glutamate carboxypepetidase II and the reduced folate carrier polymorphisms on folate and total homocysteine concentrations in dialysis patients. J Am Soc Nephrol 2003;14:1314-9.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 1314-1319
    • Födinger, M.1    Dierkes, J.2    Skoupy, S.3    Röhrer, C.4    Hagen, W.5    Puttinger, H.6
  • 13
    • 0005790727 scopus 로고    scopus 로고
    • Folate deficiency
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Carmel R. Folate deficiency. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 271-88.
    • (2001) Homocysteine in Health and Disease , pp. 271-288
    • Carmel, R.1
  • 14
    • 0033805360 scopus 로고    scopus 로고
    • A polymorphism (80G8 in a circle signA) in the reduced folate carrier gene and its association with folate status and hyperhomocysteinemia
    • Chango A, Emery-Fillon, de Courcy GP, Lambert D, Pfister M, Rosenblatt DS, et al. A polymorphism (80G8 in a circle signA) in the reduced folate carrier gene and its association with folate status and hyperhomocysteinemia. Mol Genet Metab 2000;70:310-5.
    • (2000) Mol Genet Metab , vol.70 , pp. 310-315
    • Chango, A.1    Emery-Fillon2    De Courcy, G.P.3    Lambert, D.4    Pfister, M.5    Rosenblatt, D.S.6
  • 15
    • 0037083014 scopus 로고    scopus 로고
    • Maternal periconceptional vitamin use, genetic variation of infant reduced folate carrier (A80G), and risk of spina bifida
    • Shaw GM, Lammer EJ, Zhu H, Baker MW, Neri E, Finnell RH. Maternal periconceptional vitamin use, genetic variation of infant reduced folate carrier (A80G), and risk of spina bifida. Am J Med Genet 2002;108:1-6.
    • (2002) Am J Med Genet , vol.108 , pp. 1-6
    • Shaw, G.M.1    Lammer, E.J.2    Zhu, H.3    Baker, M.W.4    Neri, E.5    Finnell, R.H.6
  • 16
    • 0037568152 scopus 로고    scopus 로고
    • Cobalamin deficiency
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Carmel R. Cobalamin deficiency. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 289-305.
    • (2001) Homocysteine in Health and Disease , pp. 289-305
    • Carmel, R.1
  • 17
    • 0036045429 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms in the cobalamin gene: Relationship with transcobalamin concentrations and the risk of neural tube defects
    • Afman LA, Lievers KJ, van der Put NM, Trijbels FJ, Blom HJ. Single nucleotide polymorphisms in the cobalamin gene: relationship with transcobalamin concentrations and the risk of neural tube defects. Eur J Hum Genet 2002;10:433-8.
    • (2002) Eur J Hum Genet , vol.10 , pp. 433-438
    • Afman, L.A.1    Lievers, K.J.2    Van Der Put, N.M.3    Trijbels, F.J.4    Blom, H.J.5
  • 19
    • 0036721305 scopus 로고    scopus 로고
    • Polymorphisms in the transcobalamin gene: Association with plasma homocysteine in healthy individuals and vascular disease patients
    • Lievers KJ, Afman LA, Kluijtmans LAJ, Boers GH, Verhoef P, den Heijer M, et al. Polymorphisms in the transcobalamin gene: association with plasma homocysteine in healthy individuals and vascular disease patients. Clin Chem 2002;48:1383-9.
    • (2002) Clin Chem , vol.48 , pp. 1383-1389
    • Lievers, K.J.1    Afman, L.A.2    Kluijtmans, L.A.J.3    Boers, G.H.4    Verhoef, P.5    Den Heijer, M.6
  • 20
    • 0000954081 scopus 로고    scopus 로고
    • Biosynthesis and reactions of homocysteine thiolactone
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Jakubowski H. Biosynthesis and reactions of homocysteine thiolactone. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 21-31.
    • (2001) Homocysteine in Health and Disease , pp. 21-31
    • Jakubowski, H.1
  • 21
    • 0035936847 scopus 로고    scopus 로고
    • Genetic determinants of homocysteine thiolactonase activity in humans: Implications for atherosclerosis
    • Jakubowski H, Ambrosius WT, Pratt JH. Genetic determinants of homocysteine thiolactonase activity in humans: implications for atherosclerosis. FEBS Lett 2001;491:35-9.
    • (2001) FEBS Lett , vol.491 , pp. 35-39
    • Jakubowski, H.1    Ambrosius, W.T.2    Pratt, J.H.3
  • 23
    • 0034904708 scopus 로고    scopus 로고
    • The methionine synthase reductase (MTRR) A66G polymorphism is a novel genetic determinant of plasma homocysteine concentrations
    • Gaughan DJ, Kluijtmans LA, Barbaux S, McMaster D, Young IS, Yarnell JW, et al. The methionine synthase reductase (MTRR) A66G polymorphism is a novel genetic determinant of plasma homocysteine concentrations. Atherosclerosis 2001;157:451-6.
    • (2001) Atherosclerosis , vol.157 , pp. 451-456
    • Gaughan, D.J.1    Kluijtmans, L.A.2    Barbaux, S.3    McMaster, D.4    Young, I.S.5    Yarnell, J.W.6
  • 24
    • 10544249877 scopus 로고    scopus 로고
    • Human methionine synthase: cDNA cloning and identification of mutations in patients of the cb1G complementation group of folate/cobalamin disorders
    • Leclerc D, Campeau, E, Goyette P, Adjalla CE, Christensen B, Ross M, et al. Human methionine synthase: cDNA cloning and identification of mutations in patients of the cb1G complementation group of folate/cobalamin disorders. Hum Mol Genet 1996;5:1867-74.
    • (1996) Hum Mol Genet , vol.5 , pp. 1867-1874
    • Leclerc, D.1    Campeau, E.2    Goyette, P.3    Adjalla, C.E.4    Christensen, B.5    Ross, M.6
  • 25
    • 0032713815 scopus 로고    scopus 로고
    • Methionine synthase D919G polymorphism is a significant but modest determinant of circulating homocysteine
    • Harmon DL, Shields DC, Woodside JV, McMaster D, Yarnell JW, Young IS, et al. Methionine synthase D919G polymorphism is a significant but modest determinant of circulating homocysteine. Genet Epidemiol 1999;17:298-309.
    • (1999) Genet Epidemiol , vol.17 , pp. 298-309
    • Harmon, D.L.1    Shields, D.C.2    Woodside, J.V.3    McMaster, D.4    Yarnell, J.W.5    Young, I.S.6
  • 26
    • 0002051637 scopus 로고    scopus 로고
    • Polymorphisms of folate and cobalamin metabolism
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Rozen R. Polymorphisms of folate and cobalamin metabolism. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 259-69.
    • (2001) Homocysteine in Health and Disease , pp. 259-269
    • Rozen, R.1
  • 27
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease: A common mutation in methylenetetrahydrofolate reductase
    • Frosst P, Blom HJ, Miols R, Goyette P, Sheppard CA, Matthews RG, et al. A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet 1995;10:111-3.
    • (1995) Nat Genet , vol.10 , pp. 111-113
    • Frosst, P.1    Blom, H.J.2    Miols, R.3    Goyette, P.4    Sheppard, C.A.5    Matthews, R.G.6
  • 28
    • 0030027668 scopus 로고    scopus 로고
    • Relation between folate status, a common mutation in methylenetetrahydrofolate reductase, and plasma homocysteine concentrations
    • Jacques PF, Bostom AG, Williams RR, Ellison RC, Eckfeldt JH, Rosenberg IH, et al. Relation between folate status, a common mutation in methylenetetrahydrofolate reductase, and plasma homocysteine concentrations. Circulation 1996;93:7-9.
    • (1996) Circulation , vol.93 , pp. 7-9
    • Jacques, P.F.1    Bostom, A.G.2    Williams, R.R.3    Ellison, R.C.4    Eckfeldt, J.H.5    Rosenberg, I.H.6
  • 29
    • 0036076711 scopus 로고    scopus 로고
    • Impaired functioning of thermolabile methylenetetrahydrofolate reductase is dependent on riboflavin status: Implications for riboflavin requirements
    • McNulty H, McKinley MC, Wilson B, McPartlin J, Strain JJ, Weir WG, et al. Impaired functioning of thermolabile methylenetetrahydrofolate reductase is dependent on riboflavin status: implications for riboflavin requirements. Am J Clin Nutr 2002;76:436-41.
    • (2002) Am J Clin Nutr , vol.76 , pp. 436-441
    • McNulty, H.1    McKinley, M.C.2    Wilson, B.3    McPartlin, J.4    Strain, J.J.5    Weir, W.G.6
  • 30
    • 0037163849 scopus 로고    scopus 로고
    • MTHFR 677C8 in a circle signT polymorphism and the risk of coronary heart disease
    • Klerk K, Verhoef P, Clarke R, Blom HJ, Kok FJ, Schouten EG, et al. MTHFR 677C8 in a circle signT polymorphism and the risk of coronary heart disease. JAMA 2002;288:2023-31.
    • (2002) JAMA , vol.288 , pp. 2023-2031
    • Klerk, K.1    Verhoef, P.2    Clarke, R.3    Blom, H.J.4    Kok, F.J.5    Schouten, E.G.6
  • 31
    • 0009877275 scopus 로고    scopus 로고
    • Methionine loading
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Silberberg J, Dudman N. Methionine loading. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 212-9.
    • (2001) Homocysteine in Health and Disease , pp. 212-219
    • Silberberg, J.1    Dudman, N.2
  • 32
    • 0032419374 scopus 로고    scopus 로고
    • Linkage disequilibrium at the cystathionine β synthase (CBS) locus and the association between genetic variation at the CBS locus and plasma levels of homocysteine
    • De Stefano V, Dekou V, Nicaud V, Chasse JF, London J, Stansbie D, et al. Linkage disequilibrium at the cystathionine β synthase (CBS) locus and the association between genetic variation at the CBS locus and plasma levels of homocysteine. Ann Hum Genet 1998;62:481-90.
    • (1998) Ann Hum Genet , vol.62 , pp. 481-490
    • De Stefano, V.1    Dekou, V.2    Nicaud, V.3    Chasse, J.F.4    London, J.5    Stansbie, D.6
  • 33
    • 0034882142 scopus 로고    scopus 로고
    • A 31 bp VNTR in the cystathionine beta-synthase (CBS) gene is associated with reduced CBS activity and elevated post-load homocysteine levels
    • Lievers KJ, Kluijtmans LA, Hell SG, Boers GH, Verhoef P, van Oppenraay-Emmerzaal D, et al. A 31 bp VNTR in the cystathionine beta-synthase (CBS) gene is associated with reduced CBS activity and elevated post-load homocysteine levels. Eur J Hum Genet 2001;9:583-9.
    • (2001) Eur J Hum Genet , vol.9 , pp. 583-589
    • Lievers, K.J.1    Kluijtmans, L.A.2    Hell, S.G.3    Boers, G.H.4    Verhoef, P.5    Van Oppenraay-Emmerzaal, D.6
  • 34
    • 0036705558 scopus 로고    scopus 로고
    • Major gene evidence after MTHFR-segregation analysis of serum homocysteine infamilies of patients undergoing coronary angioplasty
    • Jee SH, Song KS, Shim WH, Kim HK, Suh I, Park JY, et al. Major gene evidence after MTHFR-segregation analysis of serum homocysteine infamilies of patients undergoing coronary angioplasty. Hum Genet 2002;111:128-35.
    • (2002) Hum Genet , vol.111 , pp. 128-135
    • Jee, S.H.1    Song, K.S.2    Shim, W.H.3    Kim, H.K.4    Suh, I.5    Park, J.Y.6
  • 35
    • 0036765747 scopus 로고    scopus 로고
    • Thymidylate synthase: A novel genetic determinant of plasma homocysteine and folate levels
    • Trinh BN, Ong C, Coetzee GA, Yu MC, Laird P. Thymidylate synthase: a novel genetic determinant of plasma homocysteine and folate levels. Hum Genet 2002;111:299-302.
    • (2002) Hum Genet , vol.111 , pp. 299-302
    • Trinh, B.N.1    Ong, C.2    Coetzee, G.A.3    Yu, M.C.4    Laird, P.5
  • 37
    • 0032884078 scopus 로고    scopus 로고
    • Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development
    • Piedrahita JA, Oetama B, Bennett GD, van Waes J, Kamen BA, Richardson J, et al. Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development. Nat Genet 1999;23:228-32.
    • (1999) Nat Genet , vol.23 , pp. 228-232
    • Piedrahita, J.A.1    Oetama, B.2    Bennett, G.D.3    Van Waes, J.4    Kamen, B.A.5    Richardson, J.6
  • 38
    • 0002705479 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent methyltransferases
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Clarke S, Banfield K. S-adenosylmethionine-dependent methyltransferases. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 63-78.
    • (2001) Homocysteine in Health and Disease , pp. 63-78
    • Clarke, S.1    Banfield, K.2
  • 40
    • 0035191990 scopus 로고    scopus 로고
    • E1 mice epilepsy show genetic polymorphism for S-adenosyl-L-homocysteine hydrolase
    • Mira T, Kawazu I, Hirano H, Ohmori O, Janjua N, Shibata K. E1 mice epilepsy show genetic polymorphism for S-adenosyl-L-homocysteine hydrolase. Neurochem Int 2001;38:349-57.
    • (2001) Neurochem Int , vol.38 , pp. 349-357
    • Mira, T.1    Kawazu, I.2    Hirano, H.3    Ohmori, O.4    Janjua, N.5    Shibata, K.6
  • 41
    • 0032570814 scopus 로고    scopus 로고
    • Adenosine deaminase-deficient mice generated using a two-stage genetic engineering strategy exhibit a combined immunodeficiency
    • Blackburn MR, Datta SK, Kellems RE. Adenosine deaminase-deficient mice generated using a two-stage genetic engineering strategy exhibit a combined immunodeficiency. J Biol Chem 1998;273:5093-100.
    • (1998) J Biol Chem , vol.273 , pp. 5093-5100
    • Blackburn, M.R.1    Datta, S.K.2    Kellems, R.E.3
  • 42
    • 0018765904 scopus 로고
    • In vivo inactivation of erythrocyte S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine in adenosine deaminase-deficient patients
    • Hershfield MS, Kredich NM, Owenby DR, Owenby H, Buckley R. In vivo inactivation of erythrocyte S-adenosylhomocysteine hydrolase by 2′-deoxyadenosine in adenosine deaminase-deficient patients. J Clin Invest 1979;63:807-11.
    • (1979) J Clin Invest , vol.63 , pp. 807-811
    • Hershfield, M.S.1    Kredich, N.M.2    Owenby, D.R.3    Owenby, H.4    Buckley, R.5
  • 44
    • 0026592806 scopus 로고
    • Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E
    • Zang SH, Reddick RL, Piedrahita JA, Maeda N. Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E. Science 1992;258:468-71.
    • (1992) Science , vol.258 , pp. 468-471
    • Zang, S.H.1    Reddick, R.L.2    Piedrahita, J.A.3    Maeda, N.4
  • 45
    • 17944371852 scopus 로고    scopus 로고
    • Pathophysiology of apolipoprotein E deficiency in mice: Relevance to apoE-related disorders in humans
    • Moghadasian MH, McManus BM, Hguyen LB, Shefer S, Nadji M, Godin DV, et al. Pathophysiology of apolipoprotein E deficiency in mice: relevance to apoE-related disorders in humans. FASEB J 2001;15;2623-30.
    • (2001) FASEB J , vol.15 , pp. 2623-2630
    • Moghadasian, M.H.1    McManus, B.M.2    Hguyen, L.B.3    Shefer, S.4    Nadji, M.5    Godin, D.V.6
  • 46
    • 0035282903 scopus 로고    scopus 로고
    • Mice deficient in methylenetetrahydrofolate reductase exhibit hyperhomocysteinemia and decreased methylation capacity, with neuropathology and aortic lipid deposition
    • Chen Z, Karaplis AC, Ackerman SL, Pogribny IP, Melnyk S, Lussier-Cacan S, et al. Mice deficient in methylenetetrahydrofolate reductase exhibit hyperhomocysteinemia and decreased methylation capacity, with neuropathology and aortic lipid deposition. Hum Mol Genet 2001;10:433-43.
    • (2001) Hum Mol Genet , vol.10 , pp. 433-443
    • Chen, Z.1    Karaplis, A.C.2    Ackerman, S.L.3    Pogribny, I.P.4    Melnyk, S.5    Lussier-Cacan, S.6
  • 50
    • 0028917268 scopus 로고
    • Hyperhomocysteinemia in premature arterial disease: Examination of cystathionine β-synthase alleles at the molecular level
    • Kozich V, Kraus E, de Franchis R, Fowler B, Boers GH, Graham I, et al. Hyperhomocysteinemia in premature arterial disease: examination of cystathionine β-synthase alleles at the molecular level. Hum Mol Genet 1995;4;623-9.
    • (1995) Hum Mol Genet , vol.4 , pp. 623-629
    • Kozich, V.1    Kraus, E.2    De Franchis, R.3    Fowler, B.4    Boers, G.H.5    Graham, I.6
  • 52
    • 0035172715 scopus 로고    scopus 로고
    • Intracellular S-adeosylhomocystine concentrations predict global DNA hypomethylation in tissues of methyl-deficient cystathionine beta-synthase heterozygous mice
    • Caudill MA, Wang JC, Melnyk S, Pogribny IP, Jernigan S, Collins MD, et al. Intracellular S-adeosylhomocystine concentrations predict global DNA hypomethylation in tissues of methyl-deficient cystathionine beta-synthase heterozygous mice. J Nutr 2001;131:2811-8.
    • (2001) J Nutr , vol.131 , pp. 2811-2818
    • Caudill, M.A.1    Wang, J.C.2    Melnyk, S.3    Pogribny, I.P.4    Jernigan, S.5    Collins, M.D.6
  • 53
    • 0043253373 scopus 로고    scopus 로고
    • Homocysteine and human reproduction
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Eskes TK. Homocysteine and human reproduction. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 451-65.
    • (2001) Homocysteine in Health and Disease , pp. 451-465
    • Eskes, T.K.1
  • 54
    • 0005790055 scopus 로고    scopus 로고
    • Homocysteine and the nervous system
    • Carmel R, Jacobsen DW, editors. Cambridge (UK): Cambridge University Press
    • Molloy AM, Weir DG. Homocysteine and the nervous system. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge (UK): Cambridge University Press; 2001. p. 183-97.
    • (2001) Homocysteine in Health and Disease , pp. 183-197
    • Molloy, A.M.1    Weir, D.G.2
  • 55
    • 0034640007 scopus 로고    scopus 로고
    • Mouse models for neural tube closure defects
    • Juriloff DM, Harris MJ. Mouse models for neural tube closure defects. Hum Mol Genet 2000;9:993-1000.
    • (2000) Hum Mol Genet , vol.9 , pp. 993-1000
    • Juriloff, D.M.1    Harris, M.J.2
  • 56
  • 58
    • 0034425606 scopus 로고    scopus 로고
    • The roads from phenotypic variation to gene discovery: Mutagensis versus QTLs
    • Nadeau JH, Frankel WN. The roads from phenotypic variation to gene discovery: mutagensis versus QTLs. Nat Genet 2000;25:381-4.
    • (2000) Nat Genet , vol.25 , pp. 381-384
    • Nadeau, J.H.1    Frankel, W.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.