메뉴 건너뛰기




Volumn 19, Issue 11, 2009, Pages 893-902

Human aldehyde dehydrogenase genes: Alternatively spliced transcriptional variants and their suggested nomenclature

Author keywords

Aldehyde dehydrogenase; Alternatively spliced variants; Human; Nomenclature

Indexed keywords

ALDEHYDE DEHYDROGENASE; COMPLEMENTARY DNA;

EID: 74049098559     PISSN: 17446872     EISSN: 17446880     Source Type: Journal    
DOI: 10.1097/FPC.0b013e3283329023     Document Type: Article
Times cited : (57)

References (30)
  • 1
    • 0026655335 scopus 로고
    • Aldehyde dehydrogenases and their role in carcinogenesis
    • Lindahl R. Aldehyde dehydrogenases and their role in carcinogenesis. Crit Rev Biochem Mol Biol 1992; 27:283-335.
    • (1992) Crit Rev Biochem Mol Biol , vol.27 , pp. 283-335
    • Lindahl, R.1
  • 2
    • 0037259979 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenases: Potential pathological, pharmacological, and toxicologlcal impact
    • Sladek NE. Human aldehyde dehydrogenases: potential pathological, pharmacological, and toxicologlcal impact. J Biochem Mol Toxicol 2003; 17:7-23.
    • (2003) J Biochem Mol Toxicol , vol.17 , pp. 7-23
    • Sladek, N.E.1
  • 3
    • 0032859206 scopus 로고    scopus 로고
    • Eukaryotic aldehyde dehydrogenase (ALDH) genes: Human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping
    • Vasiliou V, Bairoch A, Tipton KF, Neberf DW Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evoluflon and chromosomal mapping. Pharmacogenetics 1999; 9:421-434. (Pubitemid 29419561)
    • (1999) Pharmacogenetics , vol.9 , Issue.4 , pp. 421-434
    • Vasiliou, V.1    Bairoch, A.2    Tipton, K.F.3    Nebert, D.W.4
  • 4
    • 0034534311 scopus 로고    scopus 로고
    • Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism
    • DOI 10.1016/S0009-2797(00)00211-8, PII S0009279700002118
    • Vasiliou V, Pappa A, Petersen DR. Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chem Biol Interact 2000; 129:1-19. (Pubitemid 32061051)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 1-19
    • Vasiliou, V.1    Pappa, A.2    Petersen, D.R.3
  • 5
    • 0032923555 scopus 로고    scopus 로고
    • Relationships within the aldehyde dehydrogenase extended family
    • Perozich J, Nicholas H, Wang BC, Lindahl R, Hempel J. Relationships within the aldehyde dehydrogenase extended family. Protein Sci 1999; 8:137-146. (Pubitemid 29035527)
    • (1999) Protein Science , vol.8 , Issue.1 , pp. 137-146
    • Perozich, J.1    Nicholas, H.2    Wang, B.-C.3    Lindahl, R.4    Hempel, J.5
  • 7
    • 33750024221 scopus 로고    scopus 로고
    • Bioactivation of nitroglycerin by the mitochondrial Aldehyde dehydrogenase
    • DOI 10.1016/j.tcm.2006.05.001, PII S1050173806000776
    • Chen Z, Stamler JS. Bioactivation of nitroglycerin by the mitochondrial aldehyde dehydrogenase. Trends Cardlovasc Med 2006; 16:259-265. (Pubitemid 44572801)
    • (2006) Trends in Cardiovascular Medicine , vol.16 , Issue.8 , pp. 259-265
    • Chen, Z.1    Stamler, J.S.2
  • 8
    • 3042551383 scopus 로고    scopus 로고
    • Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism
    • DOI 10.1081/DMR-120034001
    • Vasiliou V, Pappa A, Estey T. Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism. Drug Metab Rev 2004; 36:279-299. (Pubitemid 38807313)
    • (2004) Drug Metabolism Reviews , vol.36 , Issue.2 , pp. 279-299
    • Vasillou, V.1    Pappa, A.2    Estey, T.3
  • 9
    • 39249084265 scopus 로고    scopus 로고
    • The role of corneal crystallins in the cellular defense mechanisms against oxidative stress
    • Lassen N, Black WJ, Estey T, Vasiliou V. The role of corneal crystallins in the cellular defense mechanisms against oxidative stress. Semin Cell Dev Biol 2008; 19:100-112.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 100-112
    • Lassen, N.1    Black, W.J.2    Estey, T.3    Vasiliou, V.4
  • 11
    • 0029759226 scopus 로고    scopus 로고
    • Corneal aldehyde dehydrogenase displays antioxidant properties
    • DOI 10.1006/exer.1996.0098
    • Uma L, Hariharan J, Sharma Y, Balasubramanian D. Corneal aldehyde dehydrogenase displays antioxidant properties. Exp Eye Res 1996; 63:117-120. (Pubitemid 26258807)
    • (1996) Experimental Eye Research , vol.63 , Issue.1 , pp. 117-120
    • Uma, L.1    Hariharan, J.2    Sharma, Y.3    Balasubramanian, D.4
  • 12
    • 0033824324 scopus 로고    scopus 로고
    • Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease
    • Vasiliou V, Pappa A. Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease. Pharmacology 2000; 61:192-198.
    • (2000) Pharmacology , vol.61 , pp. 192-198
    • Vasiliou, V.1    Pappa, A.2
  • 13
    • 22144493352 scopus 로고    scopus 로고
    • Sjogren-Larsson syndrome: Diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2)
    • DOI 10.1002/humu.20181
    • Rizzo WB, Carney G. Sjogren-Larsson syndrome: diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2). Hum Mutat 2005; 26:1-10. (Pubitemid 40983989)
    • (2005) Human Mutation , vol.26 , Issue.1 , pp. 1-10
    • Rizzo, W.B.1    Carney, G.2
  • 15
    • 0346993682 scopus 로고    scopus 로고
    • Mutational Spectrum of the Succinate Semialdehyde Dehydrogenase (ALDH5A1) Gene and Functional Analysis of 27 Novel Disease-Causing Mutations in Patients with SSADH Deficiency
    • DOI 10.1002/humu.10288
    • Akaboshi S, Hogema BM, Novelletto A, Malaspina P, Salomons GS, Maropoulos GD, et al. Mutational spectrum of the succinate semlaldehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency. Hum Mutat 2003; 22:442-450. (Pubitemid 38009947)
    • (2003) Human Mutation , vol.22 , Issue.6 , pp. 442-450
    • Akaboshi, S.1    Hogema, B.M.2    Novelletto, A.3    Malaspina, P.4    Salomons, G.S.5    Maropoulos, G.D.6    Jakobs, C.7    Grompe, M.8    Gibson, K.M.9
  • 18
    • 0025947090 scopus 로고
    • Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes
    • Enomoto N, Takase S, Takada N, Takada A. Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes. Hepatology 1991; 13:1071-1075.
    • (1991) Hepatology , vol.13 , pp. 1071-1075
    • Enomoto, N.1    Takase, S.2    Takada, N.3    Takada, A.4
  • 19
    • 0035090650 scopus 로고    scopus 로고
    • Alcohol and aldehyde dehydrogenase gene polymorphisms and oropharyngolaryngeal, esophageal and stomach cancers in Japanese alcoholics
    • Yokoyama A, Muramatsu T, Omori T, Yokoyama T, Matsushita S, Higuchi S, et al. Alcohol and aldehyde dehydrogenase gene polymorphisms and oropharyngolaryngeal, esophageal and stomach cancers in Japanese alcoholics. Carcinogenesis 2001; 22:433-439. (Pubitemid 32203822)
    • (2001) Carcinogenesis , vol.22 , Issue.3 , pp. 433-439
    • Yokoyama, A.1    Muramatsu, T.2    Omori, T.3    Yokoyama, T.4    Matsushita, S.5    Higuchi, S.6    Maruyama, K.7    Ishii, H.8
  • 21
    • 0032958632 scopus 로고    scopus 로고
    • Embryonic retinoic acid synthesis is essential for early mouse post- Implantation development
    • DOI 10.1038/7788
    • Niederreither K, Subbarayan V, Dolle P, Chambon P. Embryonic retinoic acid synthesis is essential for early mouse post-Implantation development. Nat Genet 1999; 21:444-448. (Pubitemid 29159586)
    • (1999) Nature Genetics , vol.21 , Issue.4 , pp. 444-448
    • Niederreither, K.1    Subbarayan, V.2    Dolle, P.3    Chambon, P.4
  • 24
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences
    • Tatusova TA, Madden TL. BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 1999; 174:247-250.
    • (1999) FEMS Microbiol Lett , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 25
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • DOI 10.1006/jmbi.2000.4042
    • Notredame C, Higgins DG, Heringa J. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J Mol Biol 2000; 302:205-217. (Pubitemid 30694431)
    • (2000) Journal of Molecular Biology , vol.302 , Issue.1 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 27
    • 46649115430 scopus 로고    scopus 로고
    • Splign: Algorithms for computing spliced alignments with identification of paralogs
    • DOI 10.1186/1745-6150-3-20
    • Kapustin Y, Souvorov A, Tatusova T, Lipman D. Splign: algorithms for computing spliced alignments with identification of paralogs. Biol Direct 2008; 3:20. (Pubitemid 351943441)
    • (2008) Biology Direct , vol.3 , pp. 20
    • Kapustin, Y.1    Souvorov, A.2    Tatusova, T.3    Lipman, D.4
  • 29
    • 0031568268 scopus 로고    scopus 로고
    • Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH)
    • DOI 10.1006/geno.1996.4501
    • Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG. Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics 1997; 39:127-135. (Pubitemid 27069210)
    • (1997) Genomics , vol.39 , Issue.2 , pp. 127-135
    • Rogers, G.R.1    Markova, N.G.2    De Laurenzi, V.3    Rizzo, W.B.4    Compton, J.G.5
  • 30
    • 0033525863 scopus 로고    scopus 로고
    • 1-pyrroline-5- carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition
    • DOI 10.1074/jbc.274.10.6754
    • Hu CA, Lin WW, Obie C, Valle D. Molecular enzymology of mammalian Deitai -pyrrollne-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem 1999; 274:6754-6762. (Pubitemid 29111098)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6754-6762
    • Hu, C.-A.A.1    Lin, W.-W.2    Obie, C.3    Valle, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.