메뉴 건너뛰기




Volumn 26, Issue 3, 2003, Pages 137-146

Folate and homocysteine metabolism in neural plasticity and neurodegenerative disorders

Author keywords

[No Author keywords available]

Indexed keywords

CYANOCOBALAMIN; FOLIC ACID; HOMOCYSTEINE; PYRIDOXINE;

EID: 0037364417     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-2236(03)00032-8     Document Type: Review
Times cited : (769)

References (104)
  • 1
    • 0032443019 scopus 로고    scopus 로고
    • Folic acid, homocysteine and one-carbon metabolism: A review of the essential biochemistry
    • Scott J.M., Weir D.G. Folic acid, homocysteine and one-carbon metabolism: a review of the essential biochemistry. J. Cardiovasc. Risk. 5:1998;223-227.
    • (1998) J. Cardiovasc. Risk , vol.5 , pp. 223-227
    • Scott, J.M.1    Weir, D.G.2
  • 2
    • 0026579875 scopus 로고
    • Methyl groups in carcinogenesis: Effects on DNA methylation and gene expression
    • Wainfan E., Poirier L.A. Methyl groups in carcinogenesis: effects on DNA methylation and gene expression. Cancer Res. 52:1992;S2071-S2077.
    • (1992) Cancer Res. , vol.52
    • Wainfan, E.1    Poirier, L.A.2
  • 3
    • 0028925741 scopus 로고
    • Breaks in genomic DNA and within the p53 gene are associated with hypomethylation in livers of folate/methyl-deficient rats
    • Pogribny I.P., et al. Breaks in genomic DNA and within the p53 gene are associated with hypomethylation in livers of folate/methyl-deficient rats. Cancer Res. 55:1995;1894-1901.
    • (1995) Cancer Res. , vol.55 , pp. 1894-1901
    • Pogribny, I.P.1
  • 4
    • 0003088670 scopus 로고
    • Biological transmethylation methyl-group neogenesis and other one carbon metabolic reactions dependent upon tetrahydrofolic acid
    • M. Florkin, Stot E.H. Elsevier
    • Mudd S.H., Cantoni G.L. Biological transmethylation methyl-group neogenesis and other one carbon metabolic reactions dependent upon tetrahydrofolic acid. Florkin M., Stot E.H. Comprehensive Biochemistry. Vol. 15:1964;147-148 Elsevier.
    • (1964) Comprehensive Biochemistry , vol.15 , pp. 147-148
    • Mudd, S.H.1    Cantoni, G.L.2
  • 5
    • 0026910943 scopus 로고
    • Folate-vitamin B12 interrelationships in the central nervous system
    • Scott J.M. Folate-vitamin B12 interrelationships in the central nervous system. Proc. Nutr. Soc. 51:1992;219-224.
    • (1992) Proc. Nutr. Soc. , vol.51 , pp. 219-224
    • Scott, J.M.1
  • 6
    • 0036892748 scopus 로고    scopus 로고
    • Multiple aspects of homocysteine neurotoxicity: Glutamate excitotoxicity, kinase hyperactivation and DNA damage
    • Ho P.I., et al. Multiple aspects of homocysteine neurotoxicity: glutamate excitotoxicity, kinase hyperactivation and DNA damage. J. Neurosci. Res. 70:2002;694-702.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 694-702
    • Ho, P.I.1
  • 7
    • 0034666267 scopus 로고    scopus 로고
    • Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity
    • Kruman I.I., et al. Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity. J. Neurosci. 20:2000;6920-6926.
    • (2000) J. Neurosci. , vol.20 , pp. 6920-6926
    • Kruman, I.I.1
  • 8
    • 0024532044 scopus 로고
    • Differential effects on growth, homocysteine, and related compounds of two inhibitors of S-adenosylhomocysteine catabolism, 3-deazaadenosine, and 3-deazaaristeromycin, in C3H/10T1/2 cells
    • Djurhuus R., et al. Differential effects on growth, homocysteine, and related compounds of two inhibitors of S-adenosylhomocysteine catabolism, 3-deazaadenosine, and 3-deazaaristeromycin, in C3H/10T1/2 cells. Cancer Res. 49:1989;324-330.
    • (1989) Cancer Res. , vol.49 , pp. 324-330
    • Djurhuus, R.1
  • 9
    • 0034711007 scopus 로고    scopus 로고
    • The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes
    • Mosharov E., et al. The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry. 39:2000;13005-13011.
    • (2000) Biochemistry , vol.39 , pp. 13005-13011
    • Mosharov, E.1
  • 10
    • 0031748093 scopus 로고    scopus 로고
    • The metabolism of homocysteine, pathways and regulation
    • Finkelstein J.D. The metabolism of homocysteine, pathways and regulation. Eur. J. Pediatr. 157:(Suppl. 2):1998;S40-S44.
    • (1998) Eur. J. Pediatr. , vol.157 , Issue.SUPPL. 2
    • Finkelstein, J.D.1
  • 11
    • 0037108213 scopus 로고    scopus 로고
    • Apolipoprotein E deficiency promotes increased oxidative stress and compensatory increases in antioxidants in brain tissue
    • Shea, T.B. et al. (2002) Apolipoprotein E deficiency promotes increased oxidative stress and compensatory increases in antioxidants in brain tissue. Free Radic Biol Med. 33, 1115-1120.
    • (2002) Free Radic Biol Med. , vol.33 , pp. 1115-1120
    • Shea, T.B.1
  • 12
    • 0032807982 scopus 로고    scopus 로고
    • Carrier-mediated membrane transport of folates in mammalian cells
    • Sirotnak F.M., Tolner B. Carrier-mediated membrane transport of folates in mammalian cells. Annu. Rev. Nutr. 19:1999;91-122.
    • (1999) Annu. Rev. Nutr. , vol.19 , pp. 91-122
    • Sirotnak, F.M.1    Tolner, B.2
  • 13
    • 0017097661 scopus 로고
    • Vitamin deficiencies and neural tube defects
    • Smithells R.W., et al. Vitamin deficiencies and neural tube defects. Arch. Dis. Child. 51:1976;944-950.
    • (1976) Arch. Dis. Child. , vol.51 , pp. 944-950
    • Smithells, R.W.1
  • 14
    • 0036523032 scopus 로고    scopus 로고
    • Folic acid deficiency and homocysteine impair DNA repair in hippocampal neurons and sensitize them to amyloid toxicity in experimental models of Alzheimer's disease
    • Kruman I.I., et al. Folic acid deficiency and homocysteine impair DNA repair in hippocampal neurons and sensitize them to amyloid toxicity in experimental models of Alzheimer's disease. J. Neurosci. 22:2002;1752-1762.
    • (2002) J. Neurosci. , vol.22 , pp. 1752-1762
    • Kruman, I.I.1
  • 15
    • 0036328028 scopus 로고    scopus 로고
    • Folate status: Effects on pathways of colorectal carcinogenesis
    • Choi S.W., Mason J.B. Folate status: effects on pathways of colorectal carcinogenesis. J. Nutr. 132:2002;S2413-S2418.
    • (2002) J. Nutr. , vol.132
    • Choi, S.W.1    Mason, J.B.2
  • 16
    • 0036637392 scopus 로고    scopus 로고
    • Relationship between total homocysteine and folate levels in pregnant women and their newborn babies according to maternal serum levels of vitamin B12
    • Guerr-Shinohar E.M., et al. Relationship between total homocysteine and folate levels in pregnant women and their newborn babies according to maternal serum levels of vitamin B12. Br. J. Obstet.Gynaecol. 109:2002;784-791.
    • (2002) Br. J. Obstet.Gynaecol. , vol.109 , pp. 784-791
    • Guerr-Shinohar, E.M.1
  • 17
    • 0025196051 scopus 로고
    • Function of vitamin B12 in the central nervous system as revealed by congenital defects
    • Hall C.A. Function of vitamin B12 in the central nervous system as revealed by congenital defects. Am. J. Hematol. 34:1990;121-127.
    • (1990) Am. J. Hematol. , vol.34 , pp. 121-127
    • Hall, C.A.1
  • 18
    • 1842368504 scopus 로고    scopus 로고
    • Retardation of myelination due to dietary vitamin B12 deficiency: Cranial MRI findings
    • Lovblad K., et al. Retardation of myelination due to dietary vitamin B12 deficiency: cranial MRI findings. Pediatr. Radiol. 27:1997;155-158.
    • (1997) Pediatr. Radiol. , vol.27 , pp. 155-158
    • Lovblad, K.1
  • 19
    • 0020044683 scopus 로고
    • Neurological involvement in hereditary transcobalamin II deficiency
    • Thomas P.K., et al. Neurological involvement in hereditary transcobalamin II deficiency. J. Neurol. Neurosurg. Psychiatry. 45:1982;74-77.
    • (1982) J. Neurol. Neurosurg. Psychiatry , vol.45 , pp. 74-77
    • Thomas, P.K.1
  • 20
    • 0029946542 scopus 로고    scopus 로고
    • Prenatal folic acid treatment suppresses acrania and meroanencephaly in mice mutant for the Cart1 homeobox gene
    • Zhao Q., et al. Prenatal folic acid treatment suppresses acrania and meroanencephaly in mice mutant for the Cart1 homeobox gene. Nat. Genet. 13:1996;275-283.
    • (1996) Nat. Genet. , vol.13 , pp. 275-283
    • Zhao, Q.1
  • 21
    • 0036844005 scopus 로고    scopus 로고
    • Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida
    • Doolin M.T., et al. Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am. J. Hum. Genet. 71:2002;1222-1226.
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 1222-1226
    • Doolin, M.T.1
  • 22
    • 0034703861 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II: A polymorphism associated with lower levels of serum folate and hyperhomocysteinemia
    • Devlin A.M., et al. Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. Hum. Mol. Genet. 9:2000;2837-2844.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2837-2844
    • Devlin, A.M.1
  • 23
    • 0035079052 scopus 로고    scopus 로고
    • Reduced vitamin B12 binding by transcobalamin II increases the risk of neural tube defects
    • Afman L.A., et al. Reduced vitamin B12 binding by transcobalamin II increases the risk of neural tube defects. Q. J. Med. 94:2001;159-166.
    • (2001) Q. J. Med. , vol.94 , pp. 159-166
    • Afman, L.A.1
  • 24
    • 0034029953 scopus 로고    scopus 로고
    • Apoptotic and anti-apoptotic synaptic signaling mechanisms
    • Mattson M.P. Apoptotic and anti-apoptotic synaptic signaling mechanisms. Brain Pathol. 10:2000;300-312.
    • (2000) Brain Pathol. , vol.10 , pp. 300-312
    • Mattson, M.P.1
  • 25
    • 0030915272 scopus 로고    scopus 로고
    • Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor
    • Lipton S.A., et al. Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor. Proc. Natl. Acad. Sci. U. S. A. 94:1997;5923-5928.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5923-5928
    • Lipton, S.A.1
  • 26
    • 0026683506 scopus 로고
    • Single-channel currents of NMDA type activated by L- and D-homocysteic acid in cerebellar granule cells in culture
    • Kilic G., et al. Single-channel currents of NMDA type activated by L- and D-homocysteic acid in cerebellar granule cells in culture. Neurosci. Lett. 141:1992;231-235.
    • (1992) Neurosci. Lett. , vol.141 , pp. 231-235
    • Kilic, G.1
  • 27
    • 0031746949 scopus 로고    scopus 로고
    • Homocysteic and homocysteine sulphinic acid exhibit excitotoxicity in organotypic cultures from rat brain
    • Flott-Rahmel B., et al. Homocysteic and homocysteine sulphinic acid exhibit excitotoxicity in organotypic cultures from rat brain. Eur. J. Pediatr. 157:1998;S112-S117.
    • (1998) Eur. J. Pediatr. , vol.157
    • Flott-Rahmel, B.1
  • 28
    • 0022394902 scopus 로고
    • Folic acid has a disinhibitory action in the rat hippocampal slice preparation
    • Otis L.C., et al. Folic acid has a disinhibitory action in the rat hippocampal slice preparation. Brain Res. 346:1985;281-286.
    • (1985) Brain Res. , vol.346 , pp. 281-286
    • Otis, L.C.1
  • 29
    • 0032884078 scopus 로고    scopus 로고
    • Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development
    • Piedrahita J.A., et al. Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development. Nat. Genet. 23:1999;228-232.
    • (1999) Nat. Genet. , vol.23 , pp. 228-232
    • Piedrahita, J.A.1
  • 30
    • 0033365197 scopus 로고    scopus 로고
    • The 'thermolabile' variant of methylenetetrahydrofolate reductase and neural tube defects: An evaluation of genetic risk and the relative importance of the genotypes of the embryo and the mother
    • Shields D.C., et al. The 'thermolabile' variant of methylenetetrahydrofolate reductase and neural tube defects: an evaluation of genetic risk and the relative importance of the genotypes of the embryo and the mother. Am. J. Hum. Genet. 64:1999;1045-1055.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1045-1055
    • Shields, D.C.1
  • 31
    • 0034190659 scopus 로고    scopus 로고
    • 5,10-Methylenetetrahydrofolate reductase gene variants and congenital anomalies, a HuGE review
    • Botto L.D., Yang Q. 5,10-Methylenetetrahydrofolate reductase gene variants and congenital anomalies, a HuGE review. Am. J. Epidemiol. 151:2000;862-867.
    • (2000) Am. J. Epidemiol. , vol.151 , pp. 862-867
    • Botto, L.D.1    Yang, Q.2
  • 32
    • 0028890671 scopus 로고
    • Thermolabile 5-10-methylenetetrahydrofolate reductase as a cause of mild hyperhomocysteinemia
    • Engbersen A.M., et al. Thermolabile 5-10-methylenetetrahydrofolate reductase as a cause of mild hyperhomocysteinemia. Am. J. Hum. Genet. 56:1995;142-150.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 142-150
    • Engbersen, A.M.1
  • 33
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease, a common mutation in methylenetetrahydrofolate reductase
    • Frosst P., et al. A candidate genetic risk factor for vascular disease, a common mutation in methylenetetrahydrofolate reductase. Nat. Genet. 10:1995;111-113.
    • (1995) Nat. Genet. , vol.10 , pp. 111-113
    • Frosst, P.1
  • 34
    • 0030610090 scopus 로고    scopus 로고
    • The mutation Ala677-Val in the methylene tetrahydrofolate reductase gene, a risk factor for arterial disease and venous thrombosis
    • Arruda V.R., et al. The mutation Ala677-Val in the methylene tetrahydrofolate reductase gene, a risk factor for arterial disease and venous thrombosis. Thromb. Haemost. 77:1997;818-821.
    • (1997) Thromb. Haemost. , vol.77 , pp. 818-821
    • Arruda, V.R.1
  • 35
    • 0033846460 scopus 로고    scopus 로고
    • Genomic DNA hypomethylation, a characteristic of most cancers, is present in peripheral leukocytes of individuals who are homozygous for the C677T polymorphism in the methylenetetrahydrofolate reductase gene
    • Stern L.L., et al. Genomic DNA hypomethylation, a characteristic of most cancers, is present in peripheral leukocytes of individuals who are homozygous for the C677T polymorphism in the methylenetetrahydrofolate reductase gene. Cancer Epidemiol. Biomarkers Prev. 9:2000;849-853.
    • (2000) Cancer Epidemiol. Biomarkers Prev. , vol.9 , pp. 849-853
    • Stern, L.L.1
  • 36
    • 0027536090 scopus 로고
    • Symptomatic and asymptomatic methylenetetrahydrofolate reductase deficiency in two adult brothers
    • Haworth J.C., et al. Symptomatic and asymptomatic methylenetetrahydrofolate reductase deficiency in two adult brothers. Am. J. Med. Genet. 45:1993;572-576.
    • (1993) Am. J. Med. Genet. , vol.45 , pp. 572-576
    • Haworth, J.C.1
  • 37
    • 0024831226 scopus 로고
    • Functional methionine synthase deficiency (cb1E and cb1G), clinical and biochemical heterogeneity
    • Watkins D., Rosenblatt D.S. Functional methionine synthase deficiency (cb1E and cb1G), clinical and biochemical heterogeneity. Am. J. Med. Genet. 34:1989;427-434.
    • (1989) Am. J. Med. Genet. , vol.34 , pp. 427-434
    • Watkins, D.1    Rosenblatt, D.S.2
  • 38
    • 0032878590 scopus 로고    scopus 로고
    • A polymorphism of the methionine synthase gene, Association with plasma folate, vitamin B12, homocystine, and Colorectal cancer risk
    • Ma J., et al. A polymorphism of the methionine synthase gene, Association with plasma folate, vitamin B12, homocystine, and Colorectal cancer risk. Cancer Epidemiol. Biomarkers Prev. 8:1999;825-829.
    • (1999) Cancer Epidemiol. Biomarkers Prev. , vol.8 , pp. 825-829
    • Ma, J.1
  • 39
    • 0021894152 scopus 로고
    • The natural history of homocystinuria due to cystathionine beta-synthase deficiency
    • Mudd S.H., et al. The natural history of homocystinuria due to cystathionine beta-synthase deficiency. Am. J. Hum. Genet. 37:1985;1-31.
    • (1985) Am. J. Hum. Genet. , vol.37 , pp. 1-31
    • Mudd, S.H.1
  • 40
    • 0024532044 scopus 로고
    • Differential effects on growth, homocysteine, and related compounds of two inhibitors of S-adenosylhomocysteine catabolism, 3-deazaadenosine, and 3-deazaaristeromycin, in C3H/10T1/2 cells
    • Djurhuus R., et al. Differential effects on growth, homocysteine, and related compounds of two inhibitors of S-adenosylhomocysteine catabolism, 3-deazaadenosine, and 3-deazaaristeromycin, in C3H/10T1/2 cells. Cancer Res. 49:1989;324-330.
    • (1989) Cancer Res. , vol.49 , pp. 324-330
    • Djurhuus, R.1
  • 41
    • 0034919112 scopus 로고    scopus 로고
    • Homocysteine potentiates beta-amyloid neurotoxicity, role of oxidative stress
    • Ho P.I., et al. Homocysteine potentiates beta-amyloid neurotoxicity, role of oxidative stress. J. Neurochem. 78:2001;249-253.
    • (2001) J. Neurochem. , vol.78 , pp. 249-253
    • Ho, P.I.1
  • 42
    • 0030825848 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma total homocysteine and related metabolites in children with cystathionine beta-synthase deficiency, the effect of treatment
    • Surtees R., et al. Cerebrospinal fluid and plasma total homocysteine and related metabolites in children with cystathionine beta-synthase deficiency, the effect of treatment. Pediatr. Res. 42:1997;577-582.
    • (1997) Pediatr. Res. , vol.42 , pp. 577-582
    • Surtees, R.1
  • 43
    • 0035479285 scopus 로고    scopus 로고
    • Abnormal folate metabolism and genetic polymorphism of the folate pathway in a child with Down syndrome and neural tube defect
    • Al-Gazali L.I., et al. Abnormal folate metabolism and genetic polymorphism of the folate pathway in a child with Down syndrome and neural tube defect. Am. J. Med. Genet. 103:2001;128-132.
    • (2001) Am. J. Med. Genet. , vol.103 , pp. 128-132
    • Al-Gazali, L.I.1
  • 44
    • 0032845227 scopus 로고    scopus 로고
    • Abnormal folate metabolism and mutation in the methylenetetrahydrofolate reductase gene may be maternal risk factors for Down syndrome
    • James S.J., et al. Abnormal folate metabolism and mutation in the methylenetetrahydrofolate reductase gene may be maternal risk factors for Down syndrome. Am. J. Clin. Nutr. 70:1999;495-501.
    • (1999) Am. J. Clin. Nutr. , vol.70 , pp. 495-501
    • James, S.J.1
  • 45
    • 0034969415 scopus 로고    scopus 로고
    • Homocysteine metabolism in children with Down syndrome, in vitro modulation
    • Pogribna M., et al. Homocysteine metabolism in children with Down syndrome, in vitro modulation. Am. J. Hum. Genet. 69:2001;88-95.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 88-95
    • Pogribna, M.1
  • 46
    • 0031798844 scopus 로고    scopus 로고
    • Strategies for the treatment of cystathionine beta-synthase deficiency, The experience of the Willink Biochemical Genetics Unit over the past 30 years
    • Walter J.H., et al. Strategies for the treatment of cystathionine beta-synthase deficiency, The experience of the Willink Biochemical Genetics Unit over the past 30 years. Eur. J. Pediatr. 157:(Suppl. 2):1998;S71-S76.
    • (1998) Eur. J. Pediatr. , vol.157 , Issue.SUPPL. 2
    • Walter, J.H.1
  • 47
    • 0029865546 scopus 로고    scopus 로고
    • Long term treatment with betaine in methylenetetrahydrofolate reductase deficiency
    • Ronge E., Kjellman B. Long term treatment with betaine in methylenetetrahydrofolate reductase deficiency. Arch. Dis. Child. 74:1996;239-241.
    • (1996) Arch. Dis. Child. , vol.74 , pp. 239-241
    • Ronge, E.1    Kjellman, B.2
  • 48
    • 0034861499 scopus 로고    scopus 로고
    • An open-label, 24-week pilot study of the methyl donor betaine in Alzheimer disease patients
    • Knopman D., Patterson M. An open-label, 24-week pilot study of the methyl donor betaine in Alzheimer disease patients. Alzheimer Dis. Assoc. Disord. 15:2001;162-165.
    • (2001) Alzheimer Dis. Assoc. Disord. , vol.15 , pp. 162-165
    • Knopman, D.1    Patterson, M.2
  • 49
    • 0026045338 scopus 로고
    • Betaine-homocysteine methyltransferase organ distribution in man, pig and rat and subcellular distribution in the rat
    • McKeever M.P., et al. Betaine-homocysteine methyltransferase organ distribution in man, pig and rat and subcellular distribution in the rat. Clin. Sci. 81:1991;551-556.
    • (1991) Clin. Sci. , vol.81 , pp. 551-556
    • McKeever, M.P.1
  • 50
    • 0018096036 scopus 로고
    • An ultrastructural study of subacute combined degeneration of the spinal cord in vitamin B12-deficient rhesus monkeys
    • Agamanolis D.P., et al. An ultrastructural study of subacute combined degeneration of the spinal cord in vitamin B12-deficient rhesus monkeys. J. Neuropathol. Exp. Neurol. 37:1978;273-299.
    • (1978) J. Neuropathol. Exp. Neurol. , vol.37 , pp. 273-299
    • Agamanolis, D.P.1
  • 51
    • 0019416248 scopus 로고
    • Pathogenesis of subacute combined degeneration: A result of methyl group deficiency
    • Scott J.M., et al. Pathogenesis of subacute combined degeneration: a result of methyl group deficiency. Lancet. 2:1981;334-337.
    • (1981) Lancet , vol.2 , pp. 334-337
    • Scott, J.M.1
  • 52
    • 0026533906 scopus 로고
    • The pathogenesis of homocysteinemia, interruption of the coordinate regulation by S-adenosylmethionine of theremethylation and transsulfuration of homocysteine
    • Selhub J., Miller J.W. The pathogenesis of homocysteinemia, interruption of the coordinate regulation by S-adenosylmethionine of theremethylation and transsulfuration of homocysteine. Am. J. Clin. Nutr. 55:1992;131-138.
    • (1992) Am. J. Clin. Nutr. , vol.55 , pp. 131-138
    • Selhub, J.1    Miller, J.W.2
  • 53
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration
    • Davey G.P., et al. Energy thresholds in brain mitochondria. Potential involvement in neurodegeneration. J. Biol. Chem. 273:1998;12753-12757.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1
  • 54
    • 0033396991 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms underlying perturbed energy metabolism and neuronal degeneration in Alzheimer's and Parkinson's diseases
    • Mattson M.P., et al. Cellular and molecular mechanisms underlying perturbed energy metabolism and neuronal degeneration in Alzheimer's and Parkinson's diseases. Ann. New York Acad. Sci. 893:1999;154-175.
    • (1999) Ann. New York Acad. Sci. , vol.893 , pp. 154-175
    • Mattson, M.P.1
  • 56
    • 0035182406 scopus 로고    scopus 로고
    • Folate depletion and elevated plasma homocysteine promote oxidative stress in rat livers
    • Huang R.F., et al. Folate depletion and elevated plasma homocysteine promote oxidative stress in rat livers. J. Nutr. 131:2001;33-88.
    • (2001) J. Nutr. , vol.131 , pp. 33-88
    • Huang, R.F.1
  • 57
    • 1842411860 scopus 로고    scopus 로고
    • Homocysteine decreases bioavailable nitric oxide by a mechanism involving glutathione peroxidase
    • Upchurch G.R., et al. Homocysteine decreases bioavailable nitric oxide by a mechanism involving glutathione peroxidase. J. Biol. Chem. 272:1997;17012-17017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17012-17017
    • Upchurch, G.R.1
  • 58
    • 0030856008 scopus 로고    scopus 로고
    • Vitamins C, E and A and heme oxygenase in rats fed methyl/folate-deficient diets
    • Henning S.M., et al. Vitamins C, E and A and heme oxygenase in rats fed methyl/folate-deficient diets. Free Radic. Biol. Med. 23:1997;936-942.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 936-942
    • Henning, S.M.1
  • 59
    • 0036721156 scopus 로고    scopus 로고
    • Effects of vitamin C and vitamin E on in vivo lipid peroxidation: Results of a randomized controlled trial
    • Huang H.Y., et al. Effects of vitamin C and vitamin E on in vivo lipid peroxidation: results of a randomized controlled trial. Am. J. Clin. Nutr. 76:2002;549-555.
    • (2002) Am. J. Clin. Nutr. , vol.76 , pp. 549-555
    • Huang, H.Y.1
  • 60
    • 0037121817 scopus 로고    scopus 로고
    • Folate quenches oxidative damage in brains of apolipoprotein E-deficient mice: Augmentation by vitamin E
    • Shea, T.B. and Rogers, E. (2002) Folate quenches oxidative damage in brains of apolipoprotein E-deficient mice: augmentation by vitamin E. Mol. Brain Res. 108, 1-6.
    • (2002) Mol. Brain Res. , vol.108 , pp. 1-6
    • Shea, T.B.1    Rogers, E.2
  • 61
    • 0035721992 scopus 로고    scopus 로고
    • Folate improves endothelial function in coronary artery disease: An effect mediated by reduction of intracellular superoxide
    • Doshi S.N., et al. Folate improves endothelial function in coronary artery disease: an effect mediated by reduction of intracellular superoxide. Arterioscler. Thromb. Vasc. Biol. 21:2001;1196-1202.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1196-1202
    • Doshi, S.N.1
  • 62
    • 0002304781 scopus 로고
    • The centrality of S-adenosylhomocysteine in the regulation of the biological utilization of S-adenosylmethionine
    • C. Borchardt, & P.M. Ueland. Humana Press
    • Cantoni G.L. The centrality of S-adenosylhomocysteine in the regulation of the biological utilization of S-adenosylmethionine. Borchardt C., Ueland P.M. Biological Methylation and Drug Design, Experimental and Clinical Roles of SAM. 1986;227-237 Humana Press.
    • (1986) Biological Methylation and Drug Design, Experimental and Clinical Roles of SAM , pp. 227-237
    • Cantoni, G.L.1
  • 64
    • 0037075257 scopus 로고    scopus 로고
    • Plasma homocysteine as a risk factor for dementia and Alzheimer's disease
    • Seshadri S., et al. Plasma homocysteine as a risk factor for dementia and Alzheimer's disease. New Engl. J. Med. 346:2002;476-483.
    • (2002) New Engl. J. Med. , vol.346 , pp. 476-483
    • Seshadri, S.1
  • 65
    • 0031597388 scopus 로고    scopus 로고
    • Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease
    • Clarke R., et al. Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease. Arch. Neurol. 55:1998;1449-1455.
    • (1998) Arch. Neurol. , vol.55 , pp. 1449-1455
    • Clarke, R.1
  • 66
    • 0033005334 scopus 로고    scopus 로고
    • Homocysteine and Alzheimer's disease
    • Miller J.W. Homocysteine and Alzheimer's disease. Nutr. Rev. 57:1999;126-129.
    • (1999) Nutr. Rev. , vol.57 , pp. 126-129
    • Miller, J.W.1
  • 67
    • 0031768722 scopus 로고    scopus 로고
    • Early diagnosis of cognitive impairment in the elderly with the focus on Alzheimer's disease
    • Gottfries C.G., et al. Early diagnosis of cognitive impairment in the elderly with the focus on Alzheimer's disease. J. Neural Transm. 105:1998;773-786.
    • (1998) J. Neural Transm. , vol.105 , pp. 773-786
    • Gottfries, C.G.1
  • 68
    • 0031902352 scopus 로고    scopus 로고
    • Total serum homocysteine in senile dementia of Alzheimer type
    • McCaddon A., et al. Total serum homocysteine in senile dementia of Alzheimer type. Int. J. Geriatr. Psychiatry. 13:1998;235-239.
    • (1998) Int. J. Geriatr. Psychiatry , vol.13 , pp. 235-239
    • McCaddon, A.1
  • 69
    • 0031003514 scopus 로고    scopus 로고
    • Is metabolic evidence for vitamin B-12 and folate deficiency more frequent in elderly patients with Alzheimer's disease?
    • Joosten E., et al. Is metabolic evidence for vitamin B-12 and folate deficiency more frequent in elderly patients with Alzheimer's disease? J. Gerontol. A Biol. Sci. Med. Sci. 52:1997;M76-M79.
    • (1997) J. Gerontol. A Biol. Sci. Med. Sci. , vol.52
    • Joosten, E.1
  • 70
    • 0032889343 scopus 로고    scopus 로고
    • Identification of cognitive impairment in the elderly, homocysteine is an early marker
    • Lehmann M., et al. Identification of cognitive impairment in the elderly, homocysteine is an early marker. Dement. Geriatr. Cogn. Disord. 10:1999;12-20.
    • (1999) Dement. Geriatr. Cogn. Disord. , vol.10 , pp. 12-20
    • Lehmann, M.1
  • 71
    • 0034068273 scopus 로고    scopus 로고
    • Serum folate and the severity of atrophy of the neocortex in Alzheimer disease, findings from the Nun Study
    • Snowdon D.A., et al. Serum folate and the severity of atrophy of the neocortex in Alzheimer disease, findings from the Nun Study. Am. J. Clin. Nutr. 71:2000;993-998.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 993-998
    • Snowdon, D.A.1
  • 72
    • 0034922510 scopus 로고    scopus 로고
    • CSF-folate levels are decreased in late-onset AD patients
    • Serot J.M., et al. CSF-folate levels are decreased in late-onset AD patients. J. Neural Transm. 108:2001;93-99.
    • (2001) J. Neural Transm. , vol.108 , pp. 93-99
    • Serot, J.M.1
  • 73
    • 0025606597 scopus 로고
    • Cerebrospinal fluid S-adenosylmethionine in depression and dementia, effects of treatment with parenteral and oral S-adenosylmethionine
    • Bottiglieri T., et al. Cerebrospinal fluid S-adenosylmethionine in depression and dementia, effects of treatment with parenteral and oral S-adenosylmethionine. J. Neurol. Neurosurg. Psychiatry. 53:1990;1096-1098.
    • (1990) J. Neurol. Neurosurg. Psychiatry , vol.53 , pp. 1096-1098
    • Bottiglieri, T.1
  • 74
    • 0032585818 scopus 로고    scopus 로고
    • Oxidative stress and neural dysfunction in Down syndrome
    • Iannello R.C., et al. Oxidative stress and neural dysfunction in Down syndrome. J. Neural Transm. Suppl. 57:1999;257-267.
    • (1999) J. Neural Transm. Suppl. , vol.57 , pp. 257-267
    • Iannello, R.C.1
  • 75
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M.P. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77:1997;1081-1132.
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 76
    • 0034972863 scopus 로고    scopus 로고
    • Incorporating biomarkers into clinical drug trials in Alzheimer's disease
    • Growdon J.H. Incorporating biomarkers into clinical drug trials in Alzheimer's disease. J. Alzheimers Dis. 3:2001;287-292.
    • (2001) J. Alzheimers Dis. , vol.3 , pp. 287-292
    • Growdon, J.H.1
  • 77
    • 0035093878 scopus 로고    scopus 로고
    • Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary cultures, possible risk factors in the Alzheimer's-type neurodegenerative pathways
    • White A.R., et al. Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary cultures, possible risk factors in the Alzheimer's-type neurodegenerative pathways. J. Neurochem. 76:2001;1509-1520.
    • (2001) J. Neurochem. , vol.76 , pp. 1509-1520
    • White, A.R.1
  • 78
    • 0034819473 scopus 로고    scopus 로고
    • Is hyperhomocysteinemia due to the oxidative depletion of folate rather than to insufficient dietary intake?
    • Fuchs D., et al. Is hyperhomocysteinemia due to the oxidative depletion of folate rather than to insufficient dietary intake? Clin. Chem. Lab. Med. 39:2001;691-694.
    • (2001) Clin. Chem. Lab. Med. , vol.39 , pp. 691-694
    • Fuchs, D.1
  • 79
    • 0037076486 scopus 로고    scopus 로고
    • 12 deficiency and Alzheimer disease
    • 12 deficiency and Alzheimer disease. Neurology. 58:2002;1395-1399.
    • (2002) Neurology , vol.58 , pp. 1395-1399
    • McCaddon, A.1
  • 80
    • 0031580615 scopus 로고    scopus 로고
    • Cerebral vascular complication of hyperhomocysteinemia. Controlling thromboembolic complications with folates
    • Candito M., et al. Cerebral vascular complication of hyperhomocysteinemia. Controlling thromboembolic complications with folates. Presse Med. 26:1997;1289-1291.
    • (1997) Presse Med. , vol.26 , pp. 1289-1291
    • Candito, M.1
  • 81
    • 0037066724 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid β-protein
    • Sai X., et al. Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid β-protein. J. Biol. Chem. 277:2002;12915-12920.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12915-12920
    • Sai, X.1
  • 82
    • 12244277786 scopus 로고    scopus 로고
    • Herp stabilizes neuronal calcium homeostasis and mitochondrial function during endoplasmic reticulum stress: Implications for neurodegenerative disorders
    • Chan S.L., et al. Herp stabilizes neuronal calcium homeostasis and mitochondrial function during endoplasmic reticulum stress: implications for neurodegenerative disorders. Soc. Neurosci. Abstr. 32:2002;19312.
    • (2002) Soc. Neurosci. Abstr. , vol.32 , pp. 19312
    • Chan, S.L.1
  • 83
    • 0036078424 scopus 로고    scopus 로고
    • Brain hydrogen sulfide is severely decreased in Alzheimer's disease
    • Eto K., et al. Brain hydrogen sulfide is severely decreased in Alzheimer's disease. Biochem. Biophys. Res. Commun. 293:2002;1485-1488.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1485-1488
    • Eto, K.1
  • 84
    • 0029799427 scopus 로고    scopus 로고
    • Brain S-adenosylmethionine levels are severely decreased in Alzheimer's disease
    • Morrison L.D., et al. Brain S-adenosylmethionine levels are severely decreased in Alzheimer's disease. J. Neurochem. 67:1996;1328-1331.
    • (1996) J. Neurochem. , vol.67 , pp. 1328-1331
    • Morrison, L.D.1
  • 85
    • 0032817968 scopus 로고    scopus 로고
    • Oxidative damage and by antioxidants in the frontal cortex of Alzheimer's disease is related to the apolipoprotein E genotype
    • Ramassamy C., et al. Oxidative damage and by antioxidants in the frontal cortex of Alzheimer's disease is related to the apolipoprotein E genotype. Free Radic. Biol. Med. 27:1999;544-553.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 544-553
    • Ramassamy, C.1
  • 86
    • 0034063728 scopus 로고    scopus 로고
    • A mechanism for the neuroprotective effect of apolipoprotein E: Isoform-specific modification by the lipid peroxidation product 4-hydroxynonenal
    • Pedersen W.A., et al. A mechanism for the neuroprotective effect of apolipoprotein E: isoform-specific modification by the lipid peroxidation product 4-hydroxynonenal. J. Neurochem. 74:2000;1426-1433.
    • (2000) J. Neurochem. , vol.74 , pp. 1426-1433
    • Pedersen, W.A.1
  • 87
    • 37849186628 scopus 로고    scopus 로고
    • Apolipoprotein E, methylenetetrahydrofolate reductase (MTHFR) mutation and the risk of senile dementia-an epidemiological study using the polymerase chain reaction (PCR) method
    • Nishiyama M. Apolipoprotein E, methylenetetrahydrofolate reductase (MTHFR) mutation and the risk of senile dementia-an epidemiological study using the polymerase chain reaction (PCR) method. J. Epidemiol. 10:2000;163-172.
    • (2000) J. Epidemiol. , vol.10 , pp. 163-172
    • Nishiyama, M.1
  • 88
    • 0035958729 scopus 로고    scopus 로고
    • Intracellular generation of free radicals and modifications of detoxifying enzymes in cultured neurons from the developing rat forebrain in response to transient hypoxia
    • Lievre V., et al. Intracellular generation of free radicals and modifications of detoxifying enzymes in cultured neurons from the developing rat forebrain in response to transient hypoxia. Neuroscience. 105:2001;287-297.
    • (2001) Neuroscience , vol.105 , pp. 287-297
    • Lievre, V.1
  • 89
    • 0035017801 scopus 로고    scopus 로고
    • Plasma homocysteine and l-dopa metabolism in patients with Parkinson disease
    • Blandini F., et al. Plasma homocysteine and l-dopa metabolism in patients with Parkinson disease. Clin. Chem. 47:2001;1102-1104.
    • (2001) Clin. Chem. , vol.47 , pp. 1102-1104
    • Blandini, F.1
  • 90
    • 0033845547 scopus 로고    scopus 로고
    • Plasma homocysteine and MTHFR C677T genotype in levodopa-treated patients with PD
    • Yasui K., et al. Plasma homocysteine and MTHFR C677T genotype in levodopa-treated patients with PD. Neurology. 55:2000;437-440.
    • (2000) Neurology , vol.55 , pp. 437-440
    • Yasui, K.1
  • 91
    • 0034725094 scopus 로고    scopus 로고
    • Effects of L-dopa treatment on methylation in mouse brain: Implications for the side effects of L-dopa
    • Liu X.X., et al. Effects of L-dopa treatment on methylation in mouse brain: implications for the side effects of L-dopa. Life Sci. 66:2000;2277-2288.
    • (2000) Life Sci. , vol.66 , pp. 2277-2288
    • Liu, X.X.1
  • 92
    • 0036270262 scopus 로고    scopus 로고
    • Dietary folate deficiency and elevated homocysteine levels endanger dopaminergic neurons in models of Parkinson's disease
    • Duan W., et al. Dietary folate deficiency and elevated homocysteine levels endanger dopaminergic neurons in models of Parkinson's disease. J. Neurochem. 80:2002;101-110.
    • (2002) J. Neurochem. , vol.80 , pp. 101-110
    • Duan, W.1
  • 93
    • 0014841318 scopus 로고
    • Folate deficiency in depressive illness
    • Reynolds E.H., et al. Folate deficiency in depressive illness. Br. J. Psychiatry. 117:1970;287-292.
    • (1970) Br. J. Psychiatry , vol.117 , pp. 287-292
    • Reynolds, E.H.1
  • 94
    • 0034235205 scopus 로고    scopus 로고
    • Nutrition and depression: Focus on folate
    • Alpert J.E., et al. Nutrition and depression: focus on folate. Nutrition. 16:2002;544-546.
    • (2002) Nutrition , vol.16 , pp. 544-546
    • Alpert, J.E.1
  • 95
    • 0024841191 scopus 로고
    • Nutrition and dementia
    • Gray G.E. Nutrition and dementia. J. Am. Diet. Assoc. 89:1989;1795-1802.
    • (1989) J. Am. Diet. Assoc. , vol.89 , pp. 1795-1802
    • Gray, G.E.1
  • 96
    • 0033925828 scopus 로고    scopus 로고
    • Homocysteine, folate, methylation, and monoamine metabolism in depression
    • Bottiglieri T., et al. Homocysteine, folate, methylation, and monoamine metabolism in depression. J. Neurol. Neurosurg. Psychiatry. 69:2000;228-232.
    • (2000) J. Neurol. Neurosurg. Psychiatry , vol.69 , pp. 228-232
    • Bottiglieri, T.1
  • 97
    • 0019981887 scopus 로고
    • Effect of folic acid and vitamin B12 deficiencies on 5-hydroxyindoleacetic acid in human cerebrospinal fluid
    • Botez M.I., et al. Effect of folic acid and vitamin B12 deficiencies on 5-hydroxyindoleacetic acid in human cerebrospinal fluid. Ann. Neurol. 12:1982;479-484.
    • (1982) Ann. Neurol. , vol.12 , pp. 479-484
    • Botez, M.I.1
  • 98
    • 0034924479 scopus 로고    scopus 로고
    • Antidepressive effect of pyridoxine (vitamin B6) in neuroleptic-treated schizophrenic patients with co-morbid minor depression-preliminary open-label trial
    • Shiloh R., et al. Antidepressive effect of pyridoxine (vitamin B6) in neuroleptic-treated schizophrenic patients with co-morbid minor depression-preliminary open-label trial. Harefuah. 140:2001;369-373.
    • (2001) Harefuah , vol.140 , pp. 369-373
    • Shiloh, R.1
  • 99
    • 0032527574 scopus 로고    scopus 로고
    • Schizophrenia and impaired homocysteine metabolism: A possible association
    • Susser E., et al. Schizophrenia and impaired homocysteine metabolism: a possible association. Biol. Psychiatry. 44:1998;141-143.
    • (1998) Biol. Psychiatry , vol.44 , pp. 141-143
    • Susser, E.1
  • 100
    • 0029042491 scopus 로고
    • Homocysteinemia is a common feature of schizophrenia
    • Regland B., et al. Homocysteinemia is a common feature of schizophrenia. J. Neural Transm. Gen. Sect. 100:1995;165-169.
    • (1995) J. Neural Transm. Gen. Sect. , vol.100 , pp. 165-169
    • Regland, B.1
  • 101
    • 0025113543 scopus 로고
    • Enhancement of recovery from psychiatric illness by methylfolate
    • Godfrey P.S., et al. Enhancement of recovery from psychiatric illness by methylfolate. Lancet. 336:1990;392-395.
    • (1990) Lancet , vol.336 , pp. 392-395
    • Godfrey, P.S.1
  • 102
    • 0030723892 scopus 로고    scopus 로고
    • Homozygous thermolabile methylenetetrahydrofolate reductase in schizophrenia-like psychosis
    • Regland B., et al. Homozygous thermolabile methylenetetrahydrofolate reductase in schizophrenia-like psychosis. J. Neural Transm. 104:1997;931-941.
    • (1997) J. Neural Transm. , vol.104 , pp. 931-941
    • Regland, B.1
  • 103
    • 0019394096 scopus 로고
    • Folic acid and B12 in autism and neuropsychiatric disturbances of childhood
    • Lowe T.L. Folic acid and B12 in autism and neuropsychiatric disturbances of childhood. J. Am. Acad. Child Psychiatry. 20:1981;104-111.
    • (1981) J. Am. Acad. Child Psychiatry , vol.20 , pp. 104-111
    • Lowe, T.L.1
  • 104
    • 2242477014 scopus 로고    scopus 로고
    • Lowering blood homocysteine with folic acid based supplements: Meta-analysis of randomized trials
    • Brattstrom L., et al. Lowering blood homocysteine with folic acid based supplements: meta-analysis of randomized trials. Br. Med. J. 316:1998;894-898.
    • (1998) Br. Med. J. , vol.316 , pp. 894-898
    • Brattstrom, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.