메뉴 건너뛰기




Volumn 265, Issue 3, 1999, Pages 1056-1060

Cloning and expression of succinic semialdehyde reductase from human brain. Identity with aflatoxin B1 aldehyde reductase

Author keywords

hydroxybutyrate; Aldo keto reductase; Detoxification; Neurotransmitter

Indexed keywords

4 HYDROXYBUTYRIC ACID; AFLATOXIN B1; ALDEHYDE REDUCTASE; BENZALDEHYDE; BRAIN ENZYME; CARBONYL DERIVATIVE; COMPLEMENTARY DNA; PHENANTHRENE DERIVATIVE; PHENYLGLYOXAL; QUINONE DERIVATIVE; RECOMBINANT PROTEIN; SUCCINATE SEMIALDEHYDE DEHYDROGENASE; XENOBIOTIC AGENT;

EID: 0033231456     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00826.x     Document Type: Article
Times cited : (45)

References (22)
  • 1
    • 0028182864 scopus 로고
    • Gamma-hydroxybutyrate: An overview of the pros and cons for it being a neurotransmitter and/or useful therapeutic agent
    • 1. Cash, C.D. (1994) Gamma-hydroxybutyrate: an overview of the pros and cons for it being a neurotransmitter and/or useful therapeutic agent. Neurosci. Biobehav. Rev. 18, 291-304.
    • (1994) Neurosci. Biobehav. Rev. , vol.18 , pp. 291-304
    • Cash, C.D.1
  • 2
    • 0030856829 scopus 로고    scopus 로고
    • Sites of action of gamma-hydroxybutyrate (GBH): A neuroaetive drug with abuse potential
    • 2. Tunnicliff, G. (1997) Sites of action of gamma-hydroxybutyrate (GHB): a neuroaetive drug with abuse potential. Clin. Toxicol. 35, 581-590.
    • (1997) Clin. Toxicol. , vol.35 , pp. 581-590
    • Tunnicliff, G.1
  • 4
    • 0018596221 scopus 로고
    • Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate
    • 4. Cash, C.D., Maitre, M. & Mandel, P. (1979) Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate. J. Neurochem. 33, 1169-1175.
    • (1979) J. Neurochem. , vol.33 , pp. 1169-1175
    • Cash, C.D.1    Maitre, M.2    Mandel, P.3
  • 5
    • 0018956583 scopus 로고
    • Human brain aldehyde reductases: Relationship to succinic semialdehyde reductase and aldose reductase
    • 5. Hoffman, P.L., von Wermuth, B. & Wartburg, J.-P. (1980) Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase. J. Neurochem. 35, 354-366.
    • (1980) J. Neurochem. , vol.35 , pp. 354-366
    • Hoffman, P.L.1    Von Wermuth, B.2    Wartburg, J.-P.3
  • 6
    • 0024333867 scopus 로고
    • The aldo-keto reductase superfamily: cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • 6. Bohren, K.M., Bullock, B., Wermuth, B. & Gabbay, K.H. (1989) The aldo-keto reductase superfamily: cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 264, 9547-9551.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wermuth, B.3    Gabbay, K.H.4
  • 8
    • 0000829121 scopus 로고
    • A convenient synthesis of γ-ethoxy-γ-butyrolactone and of succinic semialdehyde
    • 8. Wermuth, C.G. (1979) A convenient synthesis of γ-ethoxy-γ-butyrolactone and of succinic semialdehyde. J. Org. Chem. 44, 2406-2408.
    • (1979) J. Org. Chem. , vol.44 , pp. 2406-2408
    • Wermuth, C.G.1
  • 9
    • 0020392283 scopus 로고
    • Aldose reductase from human tissues
    • 9. Wermuth, B. & Wartburg, J.-P. (1982) Aldose reductase from human tissues. Methods Enzymol. 89, 181-186.
    • (1982) Methods Enzymol. , vol.89 , pp. 181-186
    • Wermuth, B.1    Wartburg, J.-P.2
  • 10
    • 0018867123 scopus 로고
    • Production of reagent antibodies
    • 10. Hurn, B.A.L. & Chantler, S.M. (1980) Production of reagent antibodies. Methods Enzymol. 70, 125-126.
    • (1980) Methods Enzymol. , vol.70 , pp. 125-126
    • Hurn, B.A.L.1    Chantler, S.M.2
  • 15
    • 0032533855 scopus 로고    scopus 로고
    • Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-36.1 in a region frequently altered in human tumor cells
    • 15. Praml, C., Savelyeva, L., Perri, P. & Schwab, M. (1998) Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-36.1 in a region frequently altered in human tumor cells. Cancer Res. 58, 5014-5018.
    • (1998) Cancer Res. , vol.58 , pp. 5014-5018
    • Praml, C.1    Savelyeva, L.2    Perri, P.3    Schwab, M.4
  • 16
    • 0016698931 scopus 로고
    • Separation of aldehyde reductases and alcohol dehydrogenase from brain by affinity chromatography: Metabolism of succinic semialdehyde and ethanol
    • 16. Tabakoff, B. & Wartburg, J.-P. (1975) Separation of aldehyde reductases and alcohol dehydrogenase from brain by affinity chromatography: metabolism of succinic semialdehyde and ethanol. Biochem. Biophys. Res. Commun. 63, 957-966.
    • (1975) Biochem. Biophys. Res. Commun. , vol.63 , pp. 957-966
    • Tabakoff, B.1    Wartburg, J.-P.2
  • 17
    • 0021878724 scopus 로고
    • m aldehyde reductase and aldose reductase, carbonyl reductase, and succinic semialdehyde reductase
    • m aldehyde reductase and aldose reductase, carbonyl reductase, and succinic semialdehyde reductase. J. Neurochem. 44, 1485-1493.
    • (1985) J. Neurochem. , vol.44 , pp. 1485-1493
    • Cromlish, J.A.1    Flynn, T.G.2
  • 18
    • 0025944441 scopus 로고
    • +-dependent oxidoreductase EC 1.1.1.19 and of a mitochondrial hydroxyacid-oxoacid transhydrogenase in the initial, rate limiting step in this pathway
    • +-dependent oxidoreductase EC 1.1.1.19 and of a mitochondrial hydroxyacid-oxoacid transhydrogenase in the initial, rate limiting step in this pathway. Neurochem. Res. 16, 965-974.
    • (1991) Neurochem. Res. , vol.16 , pp. 965-974
    • Kaufman, E.E.1    Nelson, T.2
  • 19
    • 0028650735 scopus 로고
    • Developmental time course in the brain and kidney of two enzymes that oxidize γ-hydroxybutyrate
    • 19. Nelson, T. & Kaufman, E.E. (1994) Developmental time course in the brain and kidney of two enzymes that oxidize γ-hydroxybutyrate. Dev. Neurosci. 16, 352-358.
    • (1994) Dev. Neurosci. , vol.16 , pp. 352-358
    • Nelson, T.1    Kaufman, E.E.2
  • 22
    • 0027337582 scopus 로고
    • 1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytosolic aldehyde-containing metabolite of the toxin
    • 1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytosolic aldehyde-containing metabolite of the toxin. Cancer Res. 53, 3887-3894.
    • (1993) Cancer Res. , vol.53 , pp. 3887-3894
    • Hayes, J.D.1    Judah, D.J.2    Neal, G.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.