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Volumn 34, Issue 3, 1996, Pages 376-380

Human γ-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRALDEHYDE; ALDEHYDE DEHYDROGENASE; COMPLEMENTARY DNA; POLYADENYLATED RNA;

EID: 0030585739     PISSN: 08887543     EISSN: None     Source Type: Journal    
DOI: 10.1006/geno.1996.0300     Document Type: Article
Times cited : (49)

References (17)
  • 1
    • 0025785329 scopus 로고
    • Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines and polyamines
    • Ambroziak, W., and Pietruszko, R. (1991). Human aldehyde dehydrogenase: Activity with aldehyde metabolites of monoamines, diamines and polyamines. J. Biol. Chem. 266: 13011-13018.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13011-13018
    • Ambroziak, W.1    Pietruszko, R.2
  • 2
    • 0027401783 scopus 로고
    • Metabolic role of aldehyde dehydrogenase
    • Ambroziak, W., and Pietruszko, R. (1993). Metabolic role of aldehyde dehydrogenase. Adv. Exp. Med. Biol. 328: 5-15.
    • (1993) Adv. Exp. Med. Biol. , vol.328 , pp. 5-15
    • Ambroziak, W.1    Pietruszko, R.2
  • 3
    • 0027407394 scopus 로고
    • Excitatory amino acid receptors mediate the glutamate-induced release of GABA synthesized from putrescine in cultured cells of embryonic avian retina
    • DeMello, M. C. F., Guerra-Piexe, R., and DeMello, F. G. (1993). Excitatory amino acid receptors mediate the glutamate-induced release of GABA synthesized from putrescine in cultured cells of embryonic avian retina. Neurochem. Int. 22: 249-253.
    • (1993) Neurochem. Int. , vol.22 , pp. 249-253
    • DeMello, M.C.F.1    Guerra-Piexe, R.2    DeMello, F.G.3
  • 4
    • 0023064959 scopus 로고
    • The roles of human aldehyde dehydrogenase isozymes in ethanol metabolism
    • Harrington, M. C., Henehan, G. T. M., and Tipton, K. F. (1987). The roles of human aldehyde dehydrogenase isozymes in ethanol metabolism. Prog. Clin. Biol. Res. 232: 111-125.
    • (1987) Prog. Clin. Biol. Res. , vol.232 , pp. 111-125
    • Harrington, M.C.1    Henehan, G.T.M.2    Tipton, K.F.3
  • 5
    • 0029004449 scopus 로고
    • Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes
    • H. Weiner, Eds., 5th ed., Plenum, New York
    • Hsu, L. C., Chang, W-C., Lin, S., and Yoshida, A. (1995). Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes. In "Enzymology and Molecular Biology of Carbonyl Metabolism" (H. Weiner, Eds.), 5th ed., pp. 159-168, Plenum, New York.
    • (1995) Enzymology and Molecular Biology of Carbonyl Metabolism , pp. 159-168
    • Hsu, L.C.1    Chang, W.-C.2    Lin, S.3    Yoshida, A.4
  • 6
    • 0025611278 scopus 로고
    • The enzymes of detoxication
    • Jakoby, W. B., and Ziegler, D. M. (1990). The enzymes of detoxication. J. Biol. Chem. 265: 20715-20718.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20715-20718
    • Jakoby, W.B.1    Ziegler, D.M.2
  • 7
    • 0026099668 scopus 로고
    • Single nucleotide primer extension to detect diseases: Experimental application to hemo-philia B (factor IX) and cystic fibrosis gene
    • Kuppuswamy, M. N., Hoffman, J. W., Kasper, C. K., Spritzer, S. A., Groce, S. L., and Bajaj, S. P. (1991). Single nucleotide primer extension to detect diseases: Experimental application to hemo-philia B (Factor IX) and cystic fibrosis gene. Proc. Natl. Acad. Sci. USA 88: 1143-1147.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1143-1147
    • Kuppuswamy, M.N.1    Hoffman, J.W.2    Kasper, C.K.3    Spritzer, S.A.4    Groce, S.L.5    Bajaj, S.P.6
  • 8
    • 0027131429 scopus 로고
    • Human aldehyde dehydrogenase: CDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde
    • Kurys, G., Shah, P. C., Kikonyogo, A., Reed, D., Ambroziak, W., and Pietruszko, R. (1993). Human aldehyde dehydrogenase: cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur. J. Biochem. 218: 311-320.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 311-320
    • Kurys, G.1    Shah, P.C.2    Kikonyogo, A.3    Reed, D.4    Ambroziak, W.5    Pietruszko, R.6
  • 9
    • 84908823451 scopus 로고
    • Cloning and characterization of cDNA for human γaminobutyraldehyde dehydrogenase
    • Lin, S.W., Hsu, L. C., and Yoshida, A. (1993). Cloning and characterization of cDNA for human γaminobutyraldehyde dehydrogenase. FASEB J. 7(7): A 1427.
    • (1993) FASEB J. , vol.7 , Issue.7
    • Lin, S.W.1    Hsu, L.C.2    Yoshida, A.3
  • 10
    • 0028049336 scopus 로고
    • Human aldehyde dehydrogenase: Chromosomal assignment of the gene for the isozyme that metabolizes γ-aminobutyraldehyde
    • McPherson, J. D., Wasmuth, J. J., Kurys, G., and Pietruszko, R. (1994). Human aldehyde dehydrogenase: Chromosomal assignment of the gene for the isozyme that metabolizes γ-aminobutyraldehyde. Hum. Genet. 93: 211-212.
    • (1994) Hum. Genet. , vol.93 , pp. 211-212
    • McPherson, J.D.1    Wasmuth, J.J.2    Kurys, G.3    Pietruszko, R.4
  • 11
    • 0023090971 scopus 로고
    • The oxidation of α, β-unsaturated aldehyde products of lipid peroxidation by rat liver aldehyde dehydrogenases
    • Mitchell, D. Y., and Petersen, D. R. (1987). The oxidation of α, β-unsaturated aldehyde products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol. Appl. Pharmacol. 87: 403-410.
    • (1987) Toxicol. Appl. Pharmacol. , vol.87 , pp. 403-410
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 13
    • 0017885114 scopus 로고
    • Changes in concentrations of polyamines and γ-aminobutyric acid and their formation in chick embryo brain during development
    • Sobue, K., and Nakajima, T. (1978). Changes in concentrations of polyamines and γ-aminobutyric acid and their formation in chick embryo brain during development. J. Neurochem. 30: 277-279.
    • (1978) J. Neurochem. , vol.30 , pp. 277-279
    • Sobue, K.1    Nakajima, T.2
  • 14
    • 0026081677 scopus 로고
    • Homozygous tyrosinase gene mutation in an american black with tyrosinase-negative (type 1A) oculocutaneous albinasm
    • Spritz, R. A., Strunk, K. M., Hsieh, C-L., Sekhon, G. S., and Francke, U. (1991). Homozygous tyrosinase gene mutation in an american black with tyrosinase-negative (type 1A) oculocutaneous albinasm. Am. J. Hum. Genet. 48: 318-324.
    • (1991) Am. J. Hum. Genet. , vol.48 , pp. 318-324
    • Spritz, R.A.1    Strunk, K.M.2    Hsieh, C.-L.3    Sekhon, G.S.4    Francke, U.5
  • 15
    • 0025819890 scopus 로고
    • A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme
    • Yasunami, M., Chen, C. S., and Yoshida, A. (1991). A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. Proc. Natl. Acad. Sci. USA 88: 7610-7614.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7610-7614
    • Yasunami, M.1    Chen, C.S.2    Yoshida, A.3
  • 16
    • 0027058140 scopus 로고
    • Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase
    • Yoshida, A., Hsu, L. C., and Davé, V. (1992). Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase. Enzyme 46: 239-244.
    • (1992) Enzyme , vol.46 , pp. 239-244
    • Yoshida, A.1    Hsu, L.C.2    Davé, V.3
  • 17
    • 0027480124 scopus 로고
    • Biological role of human cytosolic aldehyde dehydrogenase. I. Hormonal response, retinal oxidation and implications in testicular feminization
    • Yoshida, A., Hsu, L. C., and Yanagawa, Y. (1993). Biological role of human cytosolic aldehyde dehydrogenase. I. Hormonal response, retinal oxidation and implications in testicular feminization. Adv. Exp. Med. Biol. 328: 37-44.
    • (1993) Adv. Exp. Med. Biol. , vol.328 , pp. 37-44
    • Yoshida, A.1    Hsu, L.C.2    Yanagawa, Y.3


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