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Volumn 56, Issue , 2013, Pages 89-101

Aldehyde dehydrogenases in cellular responses to oxidative/ electrophilicstress

Author keywords

Aldehyde dehydrogenase; Cancer stem cells; Chemical stress; Dehydration; Electrophilic stress; Oxidative stress

Indexed keywords

ALCOHOL; ALDEHYDE; ALDEHYDE DEHYDROGENASE; ANTINEOPLASTIC METAL COMPLEX; MEMBRANE LIPID; OXAZAPHOSPHORINE; TAXANE DERIVATIVE;

EID: 84872117242     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.11.010     Document Type: Review
Times cited : (462)

References (218)
  • 1
    • 3042551383 scopus 로고    scopus 로고
    • Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism
    • V. Vasiliou, A. Pappa, and T. Estey Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism Drug Metab. Rev. 36 2004 279 299
    • (2004) Drug Metab. Rev. , vol.36 , pp. 279-299
    • Vasiliou, V.1    Pappa, A.2    Estey, T.3
  • 2
    • 77049120544 scopus 로고    scopus 로고
    • Antioxidant defenses in the ocular surface
    • Y. Chen, G. Mehta, and V. Vasiliou Antioxidant defenses in the ocular surface Ocul. Surf. 7 2009 176 185
    • (2009) Ocul. Surf. , vol.7 , pp. 176-185
    • Chen, Y.1    Mehta, G.2    Vasiliou, V.3
  • 3
    • 50849095474 scopus 로고    scopus 로고
    • -l. Molecular cloning and differential expression of an aldehyde dehydrogenase gene in rice leaves in response to infection by blast fungus
    • C.-x. Wu, S.-c. Su, and Y Peng -l. Molecular cloning and differential expression of an aldehyde dehydrogenase gene in rice leaves in response to infection by blast fungus Biologia 62 2007 523 528
    • (2007) Biologia , vol.62 , pp. 523-528
    • Wu, C.-X.1    Su, S.C.2    Peng, Y.3
  • 4
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • E. Cabiscol, J. Tamarit, and J. Ros Oxidative stress in bacteria and protein damage by reactive oxygen species Int. Microbiol. 3 2000 3 8
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 6
    • 0032784969 scopus 로고    scopus 로고
    • A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes
    • J.P. Navarro-Avino, R. Prasad, V.J. Miralles, R.M. Benito, and R. Serrano A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes Yeast 15 1999 829 842
    • (1999) Yeast , vol.15 , pp. 829-842
    • Navarro-Avino, J.P.1    Prasad, R.2    Miralles, V.J.3    Benito, R.M.4    Serrano, R.5
  • 7
    • 70349259208 scopus 로고    scopus 로고
    • Fat accumulation in Caenorhabditis elegans triggered by the electrophilic lipid peroxidation product 4-hydroxynonenal (4-HNE)
    • S.P. Singh, M. Niemczyk, L. Zimniak, and P. Zimniak Fat accumulation in Caenorhabditis elegans triggered by the electrophilic lipid peroxidation product 4-hydroxynonenal (4-HNE) Aging (Albany NY) 1 2009 68 80
    • (2009) Aging (Albany NY) , vol.1 , pp. 68-80
    • Singh, S.P.1    Niemczyk, M.2    Zimniak, L.3    Zimniak, P.4
  • 9
    • 77952650680 scopus 로고    scopus 로고
    • Systems analysis of protein modification and cellular responses induced by electrophile stress
    • A.T. Jacobs, and L.J. Marnett Systems analysis of protein modification and cellular responses induced by electrophile stress Acc. Chem. Res. 43 2010 673 683
    • (2010) Acc. Chem. Res. , vol.43 , pp. 673-683
    • Jacobs, A.T.1    Marnett, L.J.2
  • 10
    • 0028897831 scopus 로고
    • Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal
    • D.V. Nadkarni, and L.M. Sayre Structural definition of early lysine and histidine adduction chemistry of 4-hydroxynonenal Chem. Res. Toxicol. 8 1995 284 291
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 284-291
    • Nadkarni, D.V.1    Sayre, L.M.2
  • 11
    • 23144448354 scopus 로고    scopus 로고
    • DNA adducts from acetaldehyde: Implications for alcohol-related carcinogenesis
    • P.J. Brooks, and J.A. Theruvathu DNA adducts from acetaldehyde: implications for alcohol-related carcinogenesis Alcohol 35 2005 187 193
    • (2005) Alcohol , vol.35 , pp. 187-193
    • Brooks, P.J.1    Theruvathu, J.A.2
  • 12
    • 80054089650 scopus 로고    scopus 로고
    • Free radical lipid peroxidation: Mechanisms and analysis
    • H. Yin, L. Xu, and N.A. Porter Free radical lipid peroxidation: mechanisms and analysis Chem. Rev. 111 2011 5944 5972
    • (2011) Chem. Rev. , vol.111 , pp. 5944-5972
    • Yin, H.1    Xu, L.2    Porter, N.A.3
  • 15
    • 0037259979 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenases: Potential pathological, pharmacological, and toxicological impact
    • N.E. Sladek Human aldehyde dehydrogenases: potential pathological, pharmacological, and toxicological impact J. Biochem. Mol. Toxicol. 17 2003 7 23
    • (2003) J. Biochem. Mol. Toxicol. , vol.17 , pp. 7-23
    • Sladek, N.E.1
  • 17
    • 81055158018 scopus 로고    scopus 로고
    • Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications
    • B.J. Song, M.A. Abdelmegeed, S.H. Yoo, B.J. Kim, S.A. Jo, I. Jo, and K.H. Moon Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications J. Proteomics 74 2011 2691 2702
    • (2011) J. Proteomics , vol.74 , pp. 2691-2702
    • Song, B.J.1    Abdelmegeed, M.A.2    Yoo, S.H.3    Kim, B.J.4    Jo, S.A.5    Jo, I.6    Moon, K.H.7
  • 18
    • 0033824324 scopus 로고    scopus 로고
    • Polymorphisms of human aldehyde dehydrogenases: Consequences for drug metabolism and disease
    • V. Vasiliou, and A. Pappa Polymorphisms of human aldehyde dehydrogenases: consequences for drug metabolism and disease Pharmacology 61 2000 192 198
    • (2000) Pharmacology , vol.61 , pp. 192-198
    • Vasiliou, V.1    Pappa, A.2
  • 19
    • 22144493352 scopus 로고    scopus 로고
    • Sjogren-Larsson syndrome: Diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2)
    • W.B. Rizzo, and G. Carney Sjogren-Larsson syndrome: diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2) Hum. Mutat. 26 2005 1 10
    • (2005) Hum. Mutat. , vol.26 , pp. 1-10
    • Rizzo, W.B.1    Carney, G.2
  • 21
    • 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
    • S. Akaboshi, B.M. Hogema, A. Novelletto, P. Malaspina, G.S. Salomons, G.D. Maropoulos, C. Jakobs, M. Grompe, and K.M. Gibson Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency Hum. Mutat. 22 2003 442 450
    • (2003) Hum. Mutat. , vol.22 , 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
  • 23
    • 0034703867 scopus 로고    scopus 로고
    • Hyperammonemia with reduced ornithine, citrulline, arginine and proline: A new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase
    • M.R. Baumgartner, C.A. Hu, S. Almashanu, G. Steel, C. Obie, B. Aral, D. Rabier, P. Kamoun, J.M. Saudubray, and D. Valle Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase Hum. Mol. Genet. 9 2000 2853 2858
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2853-2858
    • Baumgartner, M.R.1    Hu, C.A.2    Almashanu, S.3    Steel, G.4    Obie, C.5    Aral, B.6    Rabier, D.7    Kamoun, P.8    Saudubray, J.M.9    Valle, D.10
  • 24
    • 0025947090 scopus 로고
    • Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes
    • N. Enomoto, S. Takase, N. Takada, and A. Takada Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes Hepatology 13 1991 1071 1075
    • (1991) Hepatology , vol.13 , pp. 1071-1075
    • Enomoto, N.1    Takase, S.2    Takada, N.3    Takada, A.4
  • 25
    • 0035090650 scopus 로고    scopus 로고
    • Alcohol and aldehyde dehydrogenase gene polymorphisms and oropharyngolaryngeal, esophageal and stomach cancers in Japanese alcoholics
    • A. Yokoyama, T. Muramatsu, T. Omori, T. Yokoyama, S. Matsushita, S. Higuchi, K. Maruyama, and H. Ishii Alcohol and aldehyde dehydrogenase gene polymorphisms and oropharyngolaryngeal, esophageal and stomach cancers in Japanese alcoholics Carcinogenesis 22 2001 433 439
    • (2001) Carcinogenesis , vol.22 , 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
  • 27
    • 0037403026 scopus 로고    scopus 로고
    • Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage
    • A. Pappa, C. Chen, Y. Koutalos, A.J. Townsend, and V. Vasiliou Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage Free Radic. Biol. Med. 34 2003 1178 1189
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1178-1189
    • Pappa, A.1    Chen, C.2    Koutalos, Y.3    Townsend, A.J.4    Vasiliou, V.5
  • 29
    • 33947535828 scopus 로고    scopus 로고
    • Mechanisms involved in the protection of UV-induced protein inactivation by the corneal crystallin ALDH3A1
    • T. Estey, M. Cantore, P.A. Weston, J.F. Carpenter, J.M. Petrash, and V. Vasiliou Mechanisms involved in the protection of UV-induced protein inactivation by the corneal crystallin ALDH3A1 J. Biol. Chem. 282 2007 4382 4392
    • (2007) J. Biol. Chem. , vol.282 , pp. 4382-4392
    • Estey, T.1    Cantore, M.2    Weston, P.A.3    Carpenter, J.F.4    Petrash, J.M.5    Vasiliou, V.6
  • 31
    • 0029759226 scopus 로고    scopus 로고
    • Corneal aldehyde dehydrogenase displays antioxidant properties
    • L. Uma, J. Hariharan, Y. Sharma, and D. Balasubramanian Corneal aldehyde dehydrogenase displays antioxidant properties Exp. Eye Res. 63 1996 117 120
    • (1996) Exp. Eye Res. , vol.63 , pp. 117-120
    • Uma, L.1    Hariharan, J.2    Sharma, Y.3    Balasubramanian, D.4
  • 32
    • 34249794888 scopus 로고    scopus 로고
    • Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: The role of aldehyde dehydrogenase
    • S.A. Marchitti, R.A. Deitrich, and V. Vasiliou Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase Pharmacol. Rev. 59 2007 125 150
    • (2007) Pharmacol. Rev. , vol.59 , pp. 125-150
    • Marchitti, S.A.1    Deitrich, R.A.2    Vasiliou, V.3
  • 34
    • 0017345903 scopus 로고
    • Elemental analyses of autoradiographic grains by X-ray microanalysis
    • R. Ishitani, A. Miyakawa, and T. Iwamoto Elemental analyses of autoradiographic grains by X-ray microanalysis Experientia 33 1977 440 441
    • (1977) Experientia , vol.33 , pp. 440-441
    • Ishitani, R.1    Miyakawa, A.2    Iwamoto, T.3
  • 35
    • 80051801444 scopus 로고    scopus 로고
    • Relationship of electrophilic stress to aging
    • P. Zimniak Relationship of electrophilic stress to aging Free Radic. Biol. Med. 51 2011 1087 1105
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1087-1105
    • Zimniak, P.1
  • 36
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin A function: Production of visual pigment and retinoic acid
    • G. Duester Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid Eur. J. Biochem 267 2000 4315 4324
    • (2000) Eur. J. Biochem , vol.267 , pp. 4315-4324
    • Duester, G.1
  • 37
    • 59049107134 scopus 로고    scopus 로고
    • FDH: An aldehyde dehydrogenase fusion enzyme in folate metabolism
    • S.A. Krupenko FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism Chem. Biol. Interact. 178 2009 84 93
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 84-93
    • Krupenko, S.A.1
  • 38
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 39
    • 4444314070 scopus 로고    scopus 로고
    • Reactions of 4-hydroxynonenal with proteins and cellular targets
    • D.R. Petersen, and J.A. Doorn Reactions of 4-hydroxynonenal with proteins and cellular targets Free Radic. Biol. Med. 37 2004 937 945
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 937-945
    • Petersen, D.R.1    Doorn, J.A.2
  • 40
    • 0026725305 scopus 로고
    • Succinic semialdehyde dehydrogenase from mammalian brain: Subunit analysis using polyclonal antiserum
    • K.L. Chambliss, and K.M. Gibson Succinic semialdehyde dehydrogenase from mammalian brain: subunit analysis using polyclonal antiserum Int. J. Biochem. 24 1992 1493 1499
    • (1992) Int. J. Biochem. , vol.24 , pp. 1493-1499
    • Chambliss, K.L.1    Gibson, K.M.2
  • 41
    • 0023604469 scopus 로고
    • Human aldehyde dehydrogenase: Metabolism of putrescine and histamine
    • W. Ambroziak, and R. Pietruszko Human aldehyde dehydrogenase: metabolism of putrescine and histamine Alcohol. Clin. Exp. Res. 11 1987 528 532
    • (1987) Alcohol. Clin. Exp. Res. , vol.11 , pp. 528-532
    • Ambroziak, W.1    Pietruszko, R.2
  • 42
    • 0036202207 scopus 로고    scopus 로고
    • Cellular levels of aldehyde dehydrogenases (ALDH1A1 and ALDH3A1) as predictors of therapeutic responses to cyclophosphamide-based chemotherapy of breast cancer: A retrospective study. Rational individualization of oxazaphosphorine-based cancer chemotherapeutic regimens
    • N.E. Sladek, R. Kollander, L. Sreerama, and D.T. Kiang Cellular levels of aldehyde dehydrogenases (ALDH1A1 and ALDH3A1) as predictors of therapeutic responses to cyclophosphamide-based chemotherapy of breast cancer: a retrospective study. Rational individualization of oxazaphosphorine-based cancer chemotherapeutic regimens Cancer Chemother. Pharmacol 49 2002 309 321
    • (2002) Cancer Chemother. Pharmacol , vol.49 , pp. 309-321
    • Sladek, N.E.1    Kollander, R.2    Sreerama, L.3    Kiang, D.T.4
  • 43
    • 0032873333 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines
    • N.E. Sladek Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines Curr. Pharm. Des 5 1999 607 625
    • (1999) Curr. Pharm. des , vol.5 , pp. 607-625
    • Sladek, N.E.1
  • 48
    • 79952343101 scopus 로고    scopus 로고
    • Characterization of proteome alterations in Phanerochaete chrysosporium in response to lead exposure
    • V. Yildirim, S. Ozcan, D. Becher, K. Buttner, M. Hecker, and G. Ozcengiz Characterization of proteome alterations in Phanerochaete chrysosporium in response to lead exposure Proteome Sci. 9 2011 12
    • (2011) Proteome Sci. , vol.9 , pp. 12
    • Yildirim, V.1    Ozcan, S.2    Becher, D.3    Buttner, K.4    Hecker, M.5    Ozcengiz, G.6
  • 49
    • 34548563918 scopus 로고    scopus 로고
    • Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens
    • R. Singh, R.J. Mailloux, S. Puiseux-Dao, and V.D. Appanna Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens J. Bacteriol. 189 2007 6665 6675
    • (2007) J. Bacteriol. , vol.189 , pp. 6665-6675
    • Singh, R.1    Mailloux, R.J.2    Puiseux-Dao, S.3    Appanna, V.D.4
  • 50
    • 78651301278 scopus 로고    scopus 로고
    • The disulfiram metabolites S-methyl-N,N-diethyldithiocarbamoyl sulfoxide and S-methyl-N,N-diethylthiocarbamoyl sulfone irreversibly inactivate betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, both in vitro and in situ, and arrest bacterial growth
    • V.J. Zaldivar-Machorro, M. Lopez-Ortiz, P. Demare, I. Regla, and R.A. Munoz-Clares The disulfiram metabolites S-methyl-N,N-diethyldithiocarbamoyl sulfoxide and S-methyl-N,N-diethylthiocarbamoyl sulfone irreversibly inactivate betaine aldehyde dehydrogenase from Pseudomonas aeruginosa, both in vitro and in situ, and arrest bacterial growth Biochimie 93 2011 286 295
    • (2011) Biochimie , vol.93 , pp. 286-295
    • Zaldivar-Machorro, V.J.1    Lopez-Ortiz, M.2    Demare, P.3    Regla, I.4    Munoz-Clares, R.A.5
  • 53
    • 84857079037 scopus 로고    scopus 로고
    • Genome-wide identification and analysis of grape aldehyde dehydrogenase (ALDH) gene superfamily
    • e32153 2012
    • Y. Zhang, L. Mao, H. Wang, C. Brocker, X. Yin, V. Vasiliou, Z. Fei, and X. Wang Genome-wide identification and analysis of grape aldehyde dehydrogenase (ALDH) gene superfamily PLoS One 7 2012 e32153 2012
    • (2012) PLoS One , vol.7
    • Zhang, Y.1    Mao, L.2    Wang, H.3    Brocker, C.4    Yin, X.5    Vasiliou, V.6    Fei, Z.7    Wang, X.8
  • 54
    • 17744381836 scopus 로고    scopus 로고
    • Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana
    • H.H. Kirch, S. Schlingensiepen, S. Kotchoni, R. Sunkar, and D. Bartels Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana Plant Mol. Biol. 57 2005 315 332
    • (2005) Plant Mol. Biol. , vol.57 , pp. 315-332
    • Kirch, H.H.1    Schlingensiepen, S.2    Kotchoni, S.3    Sunkar, R.4    Bartels, D.5
  • 55
    • 0034674015 scopus 로고    scopus 로고
    • Molecular and cellular characterizations of a cDNA clone encoding a novel isozyme of aldehyde dehydrogenase from rice
    • Y. Li, M. Nakazono, N. Tsutsumi, and A. Hirai Molecular and cellular characterizations of a cDNA clone encoding a novel isozyme of aldehyde dehydrogenase from rice Gene 249 2000 67 74
    • (2000) Gene , vol.249 , pp. 67-74
    • Li, Y.1    Nakazono, M.2    Tsutsumi, N.3    Hirai, A.4
  • 56
    • 79151481012 scopus 로고    scopus 로고
    • Betaine aldehyde dehydrogenase genes from Arabidopsis with different sub-cellular localization affect stress responses
    • T.D. Missihoun, J. Schmitz, R. Klug, H.H. Kirch, and D. Bartels Betaine aldehyde dehydrogenase genes from Arabidopsis with different sub-cellular localization affect stress responses Planta 233 2011 369 382
    • (2011) Planta , vol.233 , pp. 369-382
    • Missihoun, T.D.1    Schmitz, J.2    Klug, R.3    Kirch, H.H.4    Bartels, D.5
  • 57
    • 1042302352 scopus 로고    scopus 로고
    • The Arabidopsis thaliana reduced epidermal fluorescence1 gene encodes an aldehyde dehydrogenase involved in ferulic acid and sinapic acid biosynthesis
    • R.B. Nair, K.L. Bastress, M.O. Ruegger, J.W. Denault, and C. Chapple The Arabidopsis thaliana reduced epidermal fluorescence1 gene encodes an aldehyde dehydrogenase involved in ferulic acid and sinapic acid biosynthesis Plant Cell 16 2004 544 554
    • (2004) Plant Cell , vol.16 , pp. 544-554
    • Nair, R.B.1    Bastress, K.L.2    Ruegger, M.O.3    Denault, J.W.4    Chapple, C.5
  • 58
    • 0034524722 scopus 로고    scopus 로고
    • Cross-linking of maize walls by ferulate dimerization and incorporation into lignin
    • J.H. Grabber, J. Ralph, and R.D. Hatfield Cross-linking of maize walls by ferulate dimerization and incorporation into lignin J. Agric. Food Chem. 48 2000 6106 6113
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 6106-6113
    • Grabber, J.H.1    Ralph, J.2    Hatfield, R.D.3
  • 61
    • 33745593025 scopus 로고    scopus 로고
    • Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress
    • S.M. Rodrigues, M.O. Andrade, A.P. Gomes, F.M. Damatta, M.C. Baracat-Pereira, and E.P. Fontes Arabidopsis and tobacco plants ectopically expressing the soybean antiquitin-like ALDH7 gene display enhanced tolerance to drought, salinity, and oxidative stress J. Exp. Bot. 57 2006 1909 1918
    • (2006) J. Exp. Bot. , vol.57 , pp. 1909-1918
    • Rodrigues, S.M.1    Andrade, M.O.2    Gomes, A.P.3    Damatta, F.M.4    Baracat-Pereira, M.C.5    Fontes, E.P.6
  • 62
    • 0031005273 scopus 로고    scopus 로고
    • Betaine-aldehyde dehydrogenase from amaranth leaves efficiently catalyzes the NAD-dependent oxidation of dimethylsulfoniopropionaldehyde to dimethylsulfoniopropionate
    • M. Vojtechova, A.D. Hanson, and R.A. Munoz-Clares Betaine-aldehyde dehydrogenase from amaranth leaves efficiently catalyzes the NAD-dependent oxidation of dimethylsulfoniopropionaldehyde to dimethylsulfoniopropionate Arch. Biochem. Biophys. 337 1997 81 88
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 81-88
    • Vojtechova, M.1    Hanson, A.D.2    Munoz-Clares, R.A.3
  • 63
    • 45249125699 scopus 로고
    • Hydroxyl radical scavenging activity of compatible solutes
    • N. Smirnoff Hydroxyl radical scavenging activity of compatible solutes Phytochemistry 28 1989
    • (1989) Phytochemistry , vol.28
    • Smirnoff, N.1
  • 64
    • 0041762551 scopus 로고    scopus 로고
    • Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance
    • R. Sunkar, D. Bartels, and H.H. Kirch Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance Plant J. 35 2003 452 464
    • (2003) Plant J. , vol.35 , pp. 452-464
    • Sunkar, R.1    Bartels, D.2    Kirch, H.H.3
  • 65
    • 84863822564 scopus 로고    scopus 로고
    • Molecular cloning of a stress-responsive aldehyde dehydrogenase gene ScALDH21 from the desiccation-tolerant moss Syntrichia caninervis and its responses to different stresses
    • H. Yang, D. Zhang, J. Wang, A.J. Wood, and Y. Zhang Molecular cloning of a stress-responsive aldehyde dehydrogenase gene ScALDH21 from the desiccation-tolerant moss Syntrichia caninervis and its responses to different stresses Mol. Biol. Rep 39 2012 2645 2652
    • (2012) Mol. Biol. Rep , vol.39 , pp. 2645-2652
    • Yang, H.1    Zhang, D.2    Wang, J.3    Wood, A.J.4    Zhang, Y.5
  • 67
    • 42049115707 scopus 로고    scopus 로고
    • Aluminium induced oxidative stress and DNA damage in root cells of Allium cepa L
    • V.M. Achary, S. Jena, K.K. Panda, and B.B. Panda Aluminium induced oxidative stress and DNA damage in root cells of Allium cepa L Ecotoxicol. Environ. Saf 70 2008 300 310
    • (2008) Ecotoxicol. Environ. Saf , vol.70 , pp. 300-310
    • Achary, V.M.1    Jena, S.2    Panda, K.K.3    Panda, B.B.4
  • 68
    • 0031259854 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase in tobacco pollen
    • R.G. op den Camp, and C. Kuhlemeier Aldehyde dehydrogenase in tobacco pollen Plant Mol. Biol. 35 1997 355 365
    • (1997) Plant Mol. Biol. , vol.35 , pp. 355-365
    • Op Den Camp, R.G.1    Kuhlemeier, C.2
  • 69
    • 78650588015 scopus 로고    scopus 로고
    • The maize ALDH protein superfamily: Linking structural features to functional specificities
    • J.C. Jimenez-Lopez, E.W. Gachomo, M.J. Seufferheld, and S.O. Kotchoni The maize ALDH protein superfamily: linking structural features to functional specificities BMC Struct. Biol 10 2010 43
    • (2010) BMC Struct. Biol , vol.10 , pp. 43
    • Jimenez-Lopez, J.C.1    Gachomo, E.W.2    Seufferheld, M.J.3    Kotchoni, S.O.4
  • 70
    • 0033792187 scopus 로고    scopus 로고
    • Expression of a gene encoding mitochondrial aldehyde dehydrogenase in rice increases under submerged conditions
    • M. Nakazono, H. Tsuji, Y. Li, D. Saisho, S. Arimura, N. Tsutsumi, and A. Hirai Expression of a gene encoding mitochondrial aldehyde dehydrogenase in rice increases under submerged conditions Plant Physiol. 124 2000 587 598
    • (2000) Plant Physiol. , vol.124 , pp. 587-598
    • Nakazono, M.1    Tsuji, H.2    Li, Y.3    Saisho, D.4    Arimura, S.5    Tsutsumi, N.6    Hirai, A.7
  • 71
    • 0035007419 scopus 로고    scopus 로고
    • Mitochondrial aldehyde dehydrogenase activity is required for male fertility in maize
    • F. Liu, X. Cui, H.T. Horner, H. Weiner, and P.S. Schnable Mitochondrial aldehyde dehydrogenase activity is required for male fertility in maize Plant Cell 13 2001 1063 1078
    • (2001) Plant Cell , vol.13 , pp. 1063-1078
    • Liu, F.1    Cui, X.2    Horner, H.T.3    Weiner, H.4    Schnable, P.S.5
  • 72
    • 0033213346 scopus 로고    scopus 로고
    • Plant succinic semialdehyde dehydrogenase: Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides
    • K.B. Busch, and H. Fromm Plant succinic semialdehyde dehydrogenase: cloning, purification, localization in mitochondria, and regulation by adenine nucleotides Plant Physiol. 121 1999 589 597
    • (1999) Plant Physiol. , vol.121 , pp. 589-597
    • Busch, K.B.1    Fromm, H.2
  • 73
    • 0037636431 scopus 로고    scopus 로고
    • Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
    • N. Bouche, A. Fait, D. Bouchez, S.G. Moller, and H. Fromm Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants Proc. Natl. Acad. Sci. USA 100 2003 6843 6848
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6843-6848
    • Bouche, N.1    Fait, A.2    Bouchez, D.3    Moller, S.G.4    Fromm, H.5
  • 74
    • 60249100968 scopus 로고    scopus 로고
    • Rice aldehyde dehydrogenase7 is needed for seed maturation and viability
    • J.H. Shin, S.R. Kim, and G. An Rice aldehyde dehydrogenase7 is needed for seed maturation and viability Plant Physiol. 149 2009 905 915
    • (2009) Plant Physiol. , vol.149 , pp. 905-915
    • Shin, J.H.1    Kim, S.R.2    An, G.3
  • 75
    • 0025136856 scopus 로고
    • Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis
    • F.M. Hulett, C. Bookstein, and K. Jensen Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis J. Bacteriol. 172 1990 735 740
    • (1990) J. Bacteriol. , vol.172 , pp. 735-740
    • Hulett, F.M.1    Bookstein, C.2    Jensen, K.3
  • 76
    • 0030970522 scopus 로고    scopus 로고
    • Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning
    • B. Rathinasabapathi, M. Burnet, B.L. Russell, D.A. Gage, P.C. Liao, G.J. Nye, P. Scott, J.H. Golbeck, and A.D. Hanson Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning Proc. Natl. Acad. Sci. USA 94 1997 3454 3458
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3454-3458
    • Rathinasabapathi, B.1    Burnet, M.2    Russell, B.L.3    Gage, D.A.4    Liao, P.C.5    Nye, G.J.6    Scott, P.7    Golbeck, J.H.8    Hanson, A.D.9
  • 77
    • 72049132909 scopus 로고    scopus 로고
    • Kinetic and structural features of betaine aldehyde dehydrogenases: Mechanistic and regulatory implications
    • R.A. Munoz-Clares, A.G. Diaz-Sanchez, L. Gonzalez-Segura, and C. Montiel Kinetic and structural features of betaine aldehyde dehydrogenases: mechanistic and regulatory implications Arch. Biochem. Biophys. 493 2010 71 81
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 71-81
    • Munoz-Clares, R.A.1    Diaz-Sanchez, A.G.2    Gonzalez-Segura, L.3    Montiel, C.4
  • 78
    • 0031149153 scopus 로고    scopus 로고
    • Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes
    • T. Nakamura, S. Yokota, Y. Muramoto, K. Tsutsui, Y. Oguri, K. Fukui, and T. Takabe Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes Plant J. 11 1997 1115 1120
    • (1997) Plant J. , vol.11 , pp. 1115-1120
    • Nakamura, T.1    Yokota, S.2    Muramoto, Y.3    Tsutsui, K.4    Oguri, Y.5    Fukui, K.6    Takabe, T.7
  • 79
    • 0023126357 scopus 로고
    • Oxidized polyamines and the growth of human vascular endothelial cells: Prevention of cytotoxic effects by selective acetylation
    • D.M. Morgan Oxidized polyamines and the growth of human vascular endothelial cells: prevention of cytotoxic effects by selective acetylation Biochem. J. 242 1987 347 352
    • (1987) Biochem. J. , vol.242 , pp. 347-352
    • Morgan, D.M.1
  • 80
    • 0141853870 scopus 로고    scopus 로고
    • 3-Aminopropanal is a lysosomotropic aldehyde that causes oxidative stress and apoptosis by rupturing lysosomes
    • Z. Yu, W. Li, and U.T. Brunk 3-Aminopropanal is a lysosomotropic aldehyde that causes oxidative stress and apoptosis by rupturing lysosomes APMIS 111 2003 643 652
    • (2003) APMIS , vol.111 , pp. 643-652
    • Yu, Z.1    Li, W.2    Brunk, U.T.3
  • 81
    • 3042777753 scopus 로고    scopus 로고
    • Human neuroblastoma (SH-SY5Y) cells are highly sensitive to the lysosomotropic aldehyde 3-aminopropanal
    • Z. Yu, W. Li, J. Hillman, and U.T. Brunk Human neuroblastoma (SH-SY5Y) cells are highly sensitive to the lysosomotropic aldehyde 3-aminopropanal Brain Res. 1016 2004 163 169
    • (2004) Brain Res. , vol.1016 , pp. 163-169
    • Yu, Z.1    Li, W.2    Hillman, J.3    Brunk, U.T.4
  • 82
    • 0033830281 scopus 로고    scopus 로고
    • NADPH supply and mannitol biosynthesis: Characterization, cloning, and regulation of the non-reversible glyceraldehyde-3-phosphate dehydrogenase in celery leaves
    • Z. Gao, and W.H. Loescher NADPH supply and mannitol biosynthesis: characterization, cloning, and regulation of the non-reversible glyceraldehyde-3-phosphate dehydrogenase in celery leaves Plant Physiol 124 2000 321 330
    • (2000) Plant Physiol , vol.124 , pp. 321-330
    • Gao, Z.1    Loescher, W.H.2
  • 84
    • 85047685444 scopus 로고    scopus 로고
    • Desiccation tolerance in the resurrection plant Craterostigma plantagineum: A contribution to the study of drought tolerance at the molecular level
    • D. Bartels, and F. Salamini Desiccation tolerance in the resurrection plant Craterostigma plantagineum: a contribution to the study of drought tolerance at the molecular level Plant Physiol 127 2001 1346 1353
    • (2001) Plant Physiol , vol.127 , pp. 1346-1353
    • Bartels, D.1    Salamini, F.2
  • 85
    • 70350362955 scopus 로고    scopus 로고
    • Unraveling delta1-pyrroline-5-carboxylate-proline cycle in plants by uncoupled expression of proline oxidation enzymes
    • G. Miller, A. Honig, H. Stein, N. Suzuki, R. Mittler, and A. Zilberstein Unraveling delta1-pyrroline-5-carboxylate-proline cycle in plants by uncoupled expression of proline oxidation enzymes J. Biol. Chem. 284 2009 26482 26492
    • (2009) J. Biol. Chem. , vol.284 , pp. 26482-26492
    • Miller, G.1    Honig, A.2    Stein, H.3    Suzuki, N.4    Mittler, R.5    Zilberstein, A.6
  • 86
    • 1942520427 scopus 로고    scopus 로고
    • Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses
    • K.A. Yoon, Y. Nakamura, and H. Arakawa Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses J. Hum. Genet. 49 2004 134 140
    • (2004) J. Hum. Genet. , vol.49 , pp. 134-140
    • Yoon, K.A.1    Nakamura, Y.2    Arakawa, H.3
  • 87
    • 79961186675 scopus 로고    scopus 로고
    • Proline accumulation is inhibitory to Arabidopsis seedlings during heat stress
    • W.T. Lv, B. Lin, M. Zhang, and X.J. Hua Proline accumulation is inhibitory to Arabidopsis seedlings during heat stress Plant Physiol. 156 2011 1921 1933
    • (2011) Plant Physiol. , vol.156 , pp. 1921-1933
    • Lv, W.T.1    Lin, B.2    Zhang, M.3    Hua, X.J.4
  • 88
    • 0036068778 scopus 로고    scopus 로고
    • The stress-responsive Tortula ruralis gene ALDH21A1 describes a novel eukaryotic aldehyde dehydrogenase protein family
    • X. Chen, Q. Zeng i. n.; and A.J. Wood The stress-responsive Tortula ruralis gene ALDH21A1 describes a novel eukaryotic aldehyde dehydrogenase protein family J. Plant Physiol. 159 2002 677 684
    • (2002) J. Plant Physiol. , vol.159 , pp. 677-684
    • Chen, X.1    Zeng, I.N.Q.2    Wood, A.J.3
  • 89
    • 53249130670 scopus 로고    scopus 로고
    • Significant improvement of stress tolerance in tobacco plants by overexpressing a stress-responsive aldehyde dehydrogenase gene from maize (Zea mays)
    • W. Huang, X. Ma, Q. Wang, Y. Gao, Y. Xue, X. Niu, G. Yu, and Y. Liu Significant improvement of stress tolerance in tobacco plants by overexpressing a stress-responsive aldehyde dehydrogenase gene from maize (Zea mays) Plant Mol. Biol. 68 2008 451 463
    • (2008) Plant Mol. Biol. , vol.68 , pp. 451-463
    • Huang, W.1    Ma, X.2    Wang, Q.3    Gao, Y.4    Xue, Y.5    Niu, X.6    Yu, G.7    Liu, Y.8
  • 90
    • 0038818642 scopus 로고    scopus 로고
    • Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain-dependent regulation of several ALD genes and is mediated by the general stress response pathway
    • A. Aranda, and M.M. del Olmo Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae involves a strain-dependent regulation of several ALD genes and is mediated by the general stress response pathway Yeast 20 2003 747 759
    • (2003) Yeast , vol.20 , pp. 747-759
    • Aranda, A.1    Del Olmo, M.M.2
  • 91
    • 67649654054 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in yeast under ethanol stress
    • S. Izawa, and Y. Inoue Post-transcriptional regulation of gene expression in yeast under ethanol stress Biotechnol. Appl. Biochem. 53 2009 93 99
    • (2009) Biotechnol. Appl. Biochem. , vol.53 , pp. 93-99
    • Izawa, S.1    Inoue, Y.2
  • 92
    • 77958135565 scopus 로고    scopus 로고
    • Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid
    • N.P. Mira, M. Palma, J.F. Guerreiro, and I. Sa-Correia Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid Microb. Cell Fact. 9 2010 79
    • (2010) Microb. Cell Fact. , vol.9 , pp. 79
    • Mira, N.P.1    Palma, M.2    Guerreiro, J.F.3    Sa-Correia, I.4
  • 93
    • 84857802218 scopus 로고    scopus 로고
    • KlRox1p contributes to yeast resistance to metals and is necessary for KlYCF1 expression in the presence of cadmium
    • A.M. Torres, M.L. Maceiras, E.R. Belmonte, L.N. Naveira, M.B. Calvo, and M.E. Cerdan KlRox1p contributes to yeast resistance to metals and is necessary for KlYCF1 expression in the presence of cadmium Gene 497 2012 27 37
    • (2012) Gene , vol.497 , pp. 27-37
    • Torres, A.M.1    MacEiras, M.L.2    Belmonte, E.R.3    Naveira, L.N.4    Calvo, M.B.5    Cerdan, M.E.6
  • 94
    • 33645121842 scopus 로고    scopus 로고
    • Cell wall construction in Saccharomyces cerevisiae
    • F.M. Klis, A. Boorsma, and P.W. De Groot Cell wall construction in Saccharomyces cerevisiae Yeast 23 2006 185 202
    • (2006) Yeast , vol.23 , pp. 185-202
    • Klis, F.M.1    Boorsma, A.2    De Groot, P.W.3
  • 95
    • 67651065710 scopus 로고    scopus 로고
    • Protein amino acid composition of plasma membranes affects membrane fluidity and thereby ethanol tolerance in a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae
    • C.K. Hu, F.W. Bai, and L.J. An Protein amino acid composition of plasma membranes affects membrane fluidity and thereby ethanol tolerance in a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae Sheng Wu Gong Cheng Xue Bao 21 2005 809 813
    • (2005) Sheng Wu Gong Cheng Xue Bao , vol.21 , pp. 809-813
    • Hu, C.K.1    Bai, F.W.2    An, L.J.3
  • 96
    • 0036118388 scopus 로고    scopus 로고
    • Correlation between acetaldehyde and ethanol resistance and expression of HSP genes in yeast strains isolated during the biological aging of sherry wines
    • A. Aranda, A. Querol, and M. del Olmo Correlation between acetaldehyde and ethanol resistance and expression of HSP genes in yeast strains isolated during the biological aging of sherry wines Arch. Microbiol 177 2002 304 312
    • (2002) Arch. Microbiol , vol.177 , pp. 304-312
    • Aranda, A.1    Querol, A.2    Del Olmo, M.3
  • 98
    • 34249883824 scopus 로고    scopus 로고
    • Anaerobic glycerol production by Saccharomyces cerevisiae strains under hyperosmotic stress
    • T. Modig, K. Granath, L. Adler, and G. Liden Anaerobic glycerol production by Saccharomyces cerevisiae strains under hyperosmotic stress Appl. Microbiol. Biotechnol. 75 2007 289 296
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 289-296
    • Modig, T.1    Granath, K.2    Adler, L.3    Liden, G.4
  • 99
    • 0036051770 scopus 로고    scopus 로고
    • Novel insights into the osmotic stress response of yeast
    • W.H. Mager, and M. Siderius Novel insights into the osmotic stress response of yeast FEMS Yeast Res. 2 2002 251 257
    • (2002) FEMS Yeast Res. , vol.2 , pp. 251-257
    • Mager, W.H.1    Siderius, M.2
  • 100
    • 0042261992 scopus 로고    scopus 로고
    • Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae
    • D. Shenton, and C.M. Grant Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae Biochem. J. 374 2003 513 519
    • (2003) Biochem. J. , vol.374 , pp. 513-519
    • Shenton, D.1    Grant, C.M.2
  • 102
    • 79952692873 scopus 로고    scopus 로고
    • Characterization of the adaptive response and growth upon hyperosmotic shock in Saccharomyces cerevisiae
    • J.H. Parmar, S. Bhartiya, and K.V. Venkatesh Characterization of the adaptive response and growth upon hyperosmotic shock in Saccharomyces cerevisiae Mol. Biosyst. 7 2011 1138 1148
    • (2011) Mol. Biosyst. , vol.7 , pp. 1138-1148
    • Parmar, J.H.1    Bhartiya, S.2    Venkatesh, K.V.3
  • 103
    • 33746238073 scopus 로고    scopus 로고
    • Effects of GPD1 overexpression in Saccharomyces cerevisiae commercial wine yeast strains lacking ALD6 genes
    • B. Cambon, V. Monteil, F. Remize, C. Camarasa, and S. Dequin Effects of GPD1 overexpression in Saccharomyces cerevisiae commercial wine yeast strains lacking ALD6 genes Appl. Environ. Microbiol. 72 2006 4688 4694
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4688-4694
    • Cambon, B.1    Monteil, V.2    Remize, F.3    Camarasa, C.4    Dequin, S.5
  • 104
    • 0038529613 scopus 로고    scopus 로고
    • The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity
    • D. Grabowska, and A. Chelstowska The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity J. Biol. Chem 278 2003 13984 13988
    • (2003) J. Biol. Chem , vol.278 , pp. 13984-13988
    • Grabowska, D.1    Chelstowska, A.2
  • 105
    • 0021418719 scopus 로고
    • The Caenorhabditis elegans dauer larva: Developmental effects of pheromone, food, and temperature
    • J.W. Golden, and D.L. Riddle The Caenorhabditis elegans dauer larva: developmental effects of pheromone, food, and temperature Dev. Biol. 102 1984 368 378
    • (1984) Dev. Biol. , vol.102 , pp. 368-378
    • Golden, J.W.1    Riddle, D.L.2
  • 106
    • 77449158213 scopus 로고    scopus 로고
    • An overview of stress response and hypometabolic strategies in Caenorhabditis elegans: Conserved and contrasting signals with the mammalian system
    • B. Lant, and K.B. Storey An overview of stress response and hypometabolic strategies in Caenorhabditis elegans: conserved and contrasting signals with the mammalian system Int. J. Biol. Sci 6 2010 9 50
    • (2010) Int. J. Biol. Sci , vol.6 , pp. 9-50
    • Lant, B.1    Storey, K.B.2
  • 107
    • 54149083934 scopus 로고    scopus 로고
    • Mass spectrometric proteome analysis suggests anaerobic shift in metabolism of Dauer larvae of Caenorhabditis elegans
    • A. Madi, S. Mikkat, C. Koy, B. Ringel, H.J. Thiesen, and M.O. Glocker Mass spectrometric proteome analysis suggests anaerobic shift in metabolism of Dauer larvae of Caenorhabditis elegans Biochim. Biophys. Acta 1784 2008 1763 1770
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1763-1770
    • Madi, A.1    Mikkat, S.2    Koy, C.3    Ringel, B.4    Thiesen, H.J.5    Glocker, M.O.6
  • 108
    • 23044449799 scopus 로고    scopus 로고
    • Proteomic analysis of protein expression profiles during Caenorhabditis elegans development using two-dimensional difference gel electrophoresis
    • Y. Tabuse, T. Nabetani, and A. Tsugita Proteomic analysis of protein expression profiles during Caenorhabditis elegans development using two-dimensional difference gel electrophoresis Proteomics 5 2005 2876 2891
    • (2005) Proteomics , vol.5 , pp. 2876-2891
    • Tabuse, Y.1    Nabetani, T.2    Tsugita, A.3
  • 109
    • 1542509343 scopus 로고    scopus 로고
    • Ethanol-response genes and their regulation analyzed by a microarray and comparative genomic approach in the nematode Caenorhabditis elegans
    • J.Y. Kwon, M. Hong, M.S. Choi, S. Kang, K. Duke, S. Kim, S. Lee, and J. Lee Ethanol-response genes and their regulation analyzed by a microarray and comparative genomic approach in the nematode Caenorhabditis elegans Genomics 83 2004 600 614
    • (2004) Genomics , vol.83 , pp. 600-614
    • Kwon, J.Y.1    Hong, M.2    Choi, M.S.3    Kang, S.4    Duke, K.5    Kim, S.6    Lee, S.7    Lee, J.8
  • 111
    • 83555173305 scopus 로고    scopus 로고
    • Chronic alcohol intake-induced oxidative stress and apoptosis: Role of CYP2E1 and calpain-1 in alcoholic cardiomyopathy
    • L. Jing, C.M. Jin, S.S. Li, F.M. Zhang, L. Yuan, W.M. Li, Y. Sang, S. Li, and L.J. Zhou Chronic alcohol intake-induced oxidative stress and apoptosis: role of CYP2E1 and calpain-1 in alcoholic cardiomyopathy Mol. Cell. Biochem. 359 2012 283 292
    • (2012) Mol. Cell. Biochem. , vol.359 , pp. 283-292
    • Jing, L.1    Jin, C.M.2    Li, S.S.3    Zhang, F.M.4    Yuan, L.5    Li, W.M.6    Sang, Y.7    Li, S.8    Zhou, L.J.9
  • 112
  • 113
    • 0025312660 scopus 로고
    • The effects of chronic ethanol consumption on hepatic mitochondrial energy metabolism
    • C.C. Cunningham, W.B. Coleman, and P.I. Spach The effects of chronic ethanol consumption on hepatic mitochondrial energy metabolism Alcohol Alcohol. 25 1990 127 136
    • (1990) Alcohol Alcohol. , vol.25 , pp. 127-136
    • Cunningham, C.C.1    Coleman, W.B.2    Spach, P.I.3
  • 114
    • 2442685843 scopus 로고    scopus 로고
    • The role of oxidative damage in mitochondria during aging: A review
    • H. Huang, and K.G. Manton The role of oxidative damage in mitochondria during aging: a review Front. Biosci. 9 2004 1100 1117
    • (2004) Front. Biosci. , vol.9 , pp. 1100-1117
    • Huang, H.1    Manton, K.G.2
  • 115
    • 33747618005 scopus 로고    scopus 로고
    • Mitochondrial glutathione: Hepatocellular survival-death switch
    • C. Garcia-Ruiz, and J.C. Fernandez-Checa Mitochondrial glutathione: hepatocellular survival-death switch J. Gastroenterol. Hepatol. 21 Suppl. 3 2006 S3 6
    • (2006) J. Gastroenterol. Hepatol. , vol.21 , Issue.SUPPL. 3 , pp. 3-6
    • Garcia-Ruiz, C.1    Fernandez-Checa, J.C.2
  • 116
    • 0036322172 scopus 로고    scopus 로고
    • Selective mitochondrial glutathione depletion by ethanol enhances acetaminophen toxicity in rat liver
    • P. Zhao, T.F. Kalhorn, and J.T. Slattery Selective mitochondrial glutathione depletion by ethanol enhances acetaminophen toxicity in rat liver Hepatology (Baltimore, MD) 36 2002 326 335
    • (2002) Hepatology (Baltimore, MD) , vol.36 , pp. 326-335
    • Zhao, P.1    Kalhorn, T.F.2    Slattery, J.T.3
  • 118
    • 0030819482 scopus 로고    scopus 로고
    • Transport of reduced glutathione in hepatic mitochondria and mitoplasts from ethanol-treated rats: Effect of membrane physical properties and S-adenosyl-L-methionine
    • A. Colell, C. Garcia-Ruiz, A. Morales, A. Ballesta, M. Ookhtens, J. Rodes, N. Kaplowitz, and J.C. Fernandez-Checa Transport of reduced glutathione in hepatic mitochondria and mitoplasts from ethanol-treated rats: effect of membrane physical properties and S-adenosyl-L-methionine Hepatology (Baltimore, MD) 26 1997 699 708
    • (1997) Hepatology (Baltimore, MD) , vol.26 , pp. 699-708
    • Colell, A.1    Garcia-Ruiz, C.2    Morales, A.3    Ballesta, A.4    Ookhtens, M.5    Rodes, J.6    Kaplowitz, N.7    Fernandez-Checa, J.C.8
  • 119
    • 39149123560 scopus 로고    scopus 로고
    • CYP2E1 and oxidative liver injury by alcohol
    • Y. Lu, and A.I. Cederbaum CYP2E1 and oxidative liver injury by alcohol Free Radic. Biol. Med. 44 2008 723 738
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 723-738
    • Lu, Y.1    Cederbaum, A.I.2
  • 121
    • 0034954325 scopus 로고    scopus 로고
    • Effects of alcohol consumption on indices of iron stores and of iron stores on alcohol intake markers
    • J.B. Whitfield, G. Zhu, A.C. Heath, L.W. Powell, and N.G. Martin Effects of alcohol consumption on indices of iron stores and of iron stores on alcohol intake markers Alcohol. Clin. Exp. Res. 25 2001 1037 1045
    • (2001) Alcohol. Clin. Exp. Res. , vol.25 , pp. 1037-1045
    • Whitfield, J.B.1    Zhu, G.2    Heath, A.C.3    Powell, L.W.4    Martin, N.G.5
  • 122
    • 0023090971 scopus 로고
    • The oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol
    • D.Y. Mitchell, and D.R. Petersen The oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol Appl. Pharmacol 87 1987 403 410
    • (1987) Appl. Pharmacol , vol.87 , pp. 403-410
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 123
    • 0028842190 scopus 로고
    • The hepatocellular metabolism of 4-hydroxynonenal by alcohol dehydrogenase, aldehyde dehydrogenase, and glutathione S-transferase
    • D.P. Hartley, J.A. Ruth, and D.R. Petersen The hepatocellular metabolism of 4-hydroxynonenal by alcohol dehydrogenase, aldehyde dehydrogenase, and glutathione S-transferase Arch. Biochem. Biophys. 316 1995 197 205
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 197-205
    • Hartley, D.P.1    Ruth, J.A.2    Petersen, D.R.3
  • 124
    • 33746039656 scopus 로고    scopus 로고
    • Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: On defects in the cytochrome c oxidase complex and aldehyde detoxification
    • S. Ohta, and I. Ohsawa Dysfunction of mitochondria and oxidative stress in the pathogenesis of Alzheimer's disease: on defects in the cytochrome c oxidase complex and aldehyde detoxification J. Alzheimers Dis 9 2006 155 166
    • (2006) J. Alzheimers Dis , vol.9 , pp. 155-166
    • Ohta, S.1    Ohsawa, I.2
  • 125
    • 0012869069 scopus 로고    scopus 로고
    • Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
    • R. Manzer, L. Qamar, T. Estey, A. Pappa, D.R. Petersen, and V. Vasiliou Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA DNA Cell Biol 22 2003 329 338
    • (2003) DNA Cell Biol , vol.22 , pp. 329-338
    • Manzer, R.1    Qamar, L.2    Estey, T.3    Pappa, A.4    Petersen, D.R.5    Vasiliou, V.6
  • 126
    • 77949628274 scopus 로고    scopus 로고
    • Significantly increased levels of serum malonaldehyde in type 2diabetics with myocardial infarction
    • Mahreen, R.; Mohsin, M.; Nasreen, Z.; Siraj, M.; Ishaq, M. Significantly increased levels of serum malonaldehyde in type 2diabetics with myocardial infarction. Int. J. Diabetes Dev. Countries 30:49-51.
    • Int. J. Diabetes Dev. Countries , vol.30 , pp. 49-51
    • Mahreen, R.1    Mohsin, M.2    Nasreen, Z.3    Siraj, M.4    Ishaq, M.5
  • 127
    • 0019920815 scopus 로고
    • Metabolism of malonaldehyde in vivo and in vitro
    • G.M. Siu, and H.H. Draper Metabolism of malonaldehyde in vivo and in vitro Lipids 17 1982 349 355
    • (1982) Lipids , vol.17 , pp. 349-355
    • Siu, G.M.1    Draper, H.H.2
  • 128
    • 38649111641 scopus 로고    scopus 로고
    • Roles of the genetic variation of alcohol-metabolizing enzymes on biomarkers in trauma patients with excessive alcohol intake at emergency department
    • Y.M. Tseng, Y.R. Jin, I.J. Chen, F.D. Huang, S.H. Wu, H. Ma, S.Y. Chen, L.Y. Tsai, S.M. Tsai, and J.H. Lee Roles of the genetic variation of alcohol-metabolizing enzymes on biomarkers in trauma patients with excessive alcohol intake at emergency department Clin. Chim. Acta 389 2008 14 18
    • (2008) Clin. Chim. Acta , vol.389 , pp. 14-18
    • Tseng, Y.M.1    Jin, Y.R.2    Chen, I.J.3    Huang, F.D.4    Wu, S.H.5    Ma, H.6    Chen, S.Y.7    Tsai, L.Y.8    Tsai, S.M.9    Lee, J.H.10
  • 129
    • 77957134124 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 1B1: Molecular cloning and characterization of a novel mitochondrial acetaldehyde-metabolizing enzyme
    • D. Stagos, Y. Chen, C. Brocker, E. Donald, B.C. Jackson, D.J. Orlicky, D.C. Thompson, and V. Vasiliou Aldehyde dehydrogenase 1B1: molecular cloning and characterization of a novel mitochondrial acetaldehyde-metabolizing enzyme Drug Metab. Dispos. 38 2010 1679 1687
    • (2010) Drug Metab. Dispos. , vol.38 , pp. 1679-1687
    • Stagos, D.1    Chen, Y.2    Brocker, C.3    Donald, E.4    Jackson, B.C.5    Orlicky, D.J.6    Thompson, D.C.7    Vasiliou, V.8
  • 130
    • 0028945405 scopus 로고
    • The significance of ultraviolet radiation for eye diseases: A review with comments on the efficacy of UV-blocking contact lenses
    • J.P. Bergmanson, and P.G. Soderberg The significance of ultraviolet radiation for eye diseases: a review with comments on the efficacy of UV-blocking contact lenses Ophthalmic Physiol. Opt 15 1995 83 91
    • (1995) Ophthalmic Physiol. Opt , vol.15 , pp. 83-91
    • Bergmanson, J.P.1    Soderberg, P.G.2
  • 131
    • 0027319341 scopus 로고
    • Cytotoxicity and genotoxicity of lipid-oxidation products
    • 779S-785S discussion
    • H. Esterbauer Cytotoxicity and genotoxicity of lipid-oxidation products Am. J. Clin. Nutr. 57 779S-785S 1993 785S 786S discussion
    • (1993) Am. J. Clin. Nutr. , vol.57
    • Esterbauer, H.1
  • 132
    • 0031670727 scopus 로고    scopus 로고
    • Nuclear ferritin protects DNA from UV damage in corneal epithelial cells
    • C.X. Cai, D.E. Birk, and T.F. Linsenmayer Nuclear ferritin protects DNA from UV damage in corneal epithelial cells Mol. Biol. Cell 9 1998 1037 1051
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1037-1051
    • Cai, C.X.1    Birk, D.E.2    Linsenmayer, T.F.3
  • 133
  • 135
    • 73149104866 scopus 로고    scopus 로고
    • Corneal aldehyde dehydrogenases: Multiple functions and novel nuclear localization
    • D. Stagos, Y. Chen, M. Cantore, J.V. Jester, and V. Vasiliou Corneal aldehyde dehydrogenases: multiple functions and novel nuclear localization Brain Res. Bull. 81 2010 211 218
    • (2010) Brain Res. Bull. , vol.81 , pp. 211-218
    • Stagos, D.1    Chen, Y.2    Cantore, M.3    Jester, J.V.4    Vasiliou, V.5
  • 136
    • 0025885278 scopus 로고
    • Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase
    • C. Verhagen, R. Hoekzema, G.M. Verjans, and A. Kijlstra Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase Exp. Eye Res. 53 1991 283 284
    • (1991) Exp. Eye Res. , vol.53 , pp. 283-284
    • Verhagen, C.1    Hoekzema, R.2    Verjans, G.M.3    Kijlstra, A.4
  • 137
    • 23244450160 scopus 로고    scopus 로고
    • Corneal keratocytes: Phenotypic and species differences in abundant protein expression and in vitro light-scattering
    • J.V. Jester, A. Budge, S. Fisher, and J. Huang Corneal keratocytes: phenotypic and species differences in abundant protein expression and in vitro light-scattering Invest. Ophthalmol. Visual Sci. 46 2005 2369 2378
    • (2005) Invest. Ophthalmol. Visual Sci. , vol.46 , pp. 2369-2378
    • Jester, J.V.1    Budge, A.2    Fisher, S.3    Huang, J.4
  • 138
    • 4243490292 scopus 로고    scopus 로고
    • Corneal and stomach expression of aldehyde dehydrogenases: From fish to mammals
    • A. Pappa, N.A. Sophos, and V. Vasiliou Corneal and stomach expression of aldehyde dehydrogenases: from fish to mammals Chem. Biol. Interact. 130-132 2001 181 191
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 181-191
    • Pappa, A.1    Sophos, N.A.2    Vasiliou, V.3
  • 139
    • 0029984181 scopus 로고    scopus 로고
    • A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens: Gene recruitment of eta-crystallin
    • C. Graham, J. Hodin, and G. Wistow A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens: gene recruitment of eta-crystallin J. Biol. Chem. 271 1996 15623 15628
    • (1996) J. Biol. Chem. , vol.271 , pp. 15623-15628
    • Graham, C.1    Hodin, J.2    Wistow, G.3
  • 140
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • R.T. Dean, S. Fu, R. Stocker, and M.J. Davies Biochemistry and pathology of radical-mediated protein oxidation Biochem. J. 324 1997 1 18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 142
    • 78650975564 scopus 로고    scopus 로고
    • Structural and functional modifications of corneal crystallin ALDH3A1 by UVB light
    • T. Estey, Y. Chen, J.F. Carpenter, and V. Vasiliou Structural and functional modifications of corneal crystallin ALDH3A1 by UVB light PLoS One 5 2010 e15218
    • (2010) PLoS One , vol.5 , pp. 15218
    • Estey, T.1    Chen, Y.2    Carpenter, J.F.3    Vasiliou, V.4
  • 143
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): Biochemical characterization and immunohistochemical localization in the cornea
    • A. Pappa, T. Estey, R. Manzer, D. Brown, and V. Vasiliou Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea Biochem. J. 376 2003 615 623
    • (2003) Biochem. J. , vol.376 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 144
    • 0026588480 scopus 로고
    • Antioxidant and anticataractogenic effects of topical captopril in diquat-induced cataract in rabbits
    • K.C. Bhuyan, D.K. Bhuyan, O. Santos, and S.M. Podos Antioxidant and anticataractogenic effects of topical captopril in diquat-induced cataract in rabbits Free Radic. Biol. Med. 12 1992 251 261
    • (1992) Free Radic. Biol. Med. , vol.12 , pp. 251-261
    • Bhuyan, K.C.1    Bhuyan, D.K.2    Santos, O.3    Podos, S.M.4
  • 148
    • 0036960604 scopus 로고    scopus 로고
    • Glutathione in defense and signaling: Lessons from a small thiol
    • D.A. Dickinson, and H.J. Forman Glutathione in defense and signaling: lessons from a small thiol Ann. N. Y. Acad. Sci 973 2002 488 504
    • (2002) Ann. N. Y. Acad. Sci , vol.973 , pp. 488-504
    • Dickinson, D.A.1    Forman, H.J.2
  • 153
    • 67349191354 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase as a marker for stem cells
    • J.S. Moreb Aldehyde dehydrogenase as a marker for stem cells Curr. Stem Cell Res. Ther 3 2008 237 246
    • (2008) Curr. Stem Cell Res. Ther , vol.3 , pp. 237-246
    • Moreb, J.S.1
  • 156
    • 65949112714 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 1is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation during colon tumorigenesis
    • E.H. Huang, M.J. Hynes, T. Zhang, C. Ginestier, G. Dontu, H. Appelman, J.Z. Fields, M.S. Wicha, and B.M. Boman Aldehyde dehydrogenase 1is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation during colon tumorigenesis Cancer Res. 69 2009 3382 3389
    • (2009) Cancer Res. , vol.69 , pp. 3382-3389
    • Huang, E.H.1    Hynes, M.J.2    Zhang, T.3    Ginestier, C.4    Dontu, G.5    Appelman, H.6    Fields, J.Z.7    Wicha, M.S.8    Boman, B.M.9
  • 157
    • 0027828378 scopus 로고
    • Role of the aldehyde dehydrogenase-1 isozyme in the metabolism of acetaldehyde
    • Y. Ueshima, Y. Matsuda, M. Tsutsumi, and A. Takada Role of the aldehyde dehydrogenase-1 isozyme in the metabolism of acetaldehyde Alcohol Alcohol. Suppl. 1B 1993 15 19
    • (1993) Alcohol Alcohol. Suppl. , vol.1 B , pp. 15-19
    • Ueshima, Y.1    Matsuda, Y.2    Tsutsumi, M.3    Takada, A.4
  • 159
    • 0024495551 scopus 로고
    • Cytosolic aldehyde dehydrogenase (ALDH1) variants found in alcohol flushers
    • A. Yoshida, V. Dave, R.J. Ward, and T.J. Peters Cytosolic aldehyde dehydrogenase (ALDH1) variants found in alcohol flushers Ann. Hum. Genet. 53 1989 1 7
    • (1989) Ann. Hum. Genet. , vol.53 , pp. 1-7
    • Yoshida, A.1    Dave, V.2    Ward, R.J.3    Peters, T.J.4
  • 160
    • 0348109455 scopus 로고    scopus 로고
    • ALDH1 mRNA: Presence in human dopamine neurons and decreases in substantia nigra in Parkinson's disease and in the ventral tegmental area in schizophrenia
    • D. Galter, S. Buervenich, A. Carmine, M. Anvret, and L. Olson ALDH1 mRNA: presence in human dopamine neurons and decreases in substantia nigra in Parkinson's disease and in the ventral tegmental area in schizophrenia Neurobiol. Dis 14 2003 637 647
    • (2003) Neurobiol. Dis , vol.14 , pp. 637-647
    • Galter, D.1    Buervenich, S.2    Carmine, A.3    Anvret, M.4    Olson, L.5
  • 161
    • 0025880967 scopus 로고
    • Retinoids and their receptors in differentiation, embryogenesis, and neoplasia
    • L.M. De Luca Retinoids and their receptors in differentiation,
    • (1991) FASEB J. , vol.5 , pp. 2924-2933
    • De Luca, L.M.1
  • 163
    • 0032958632 scopus 로고    scopus 로고
    • Embryonic retinoic acid synthesis is essential for early mouse post-implantation development
    • K. Niederreither, V. Subbarayan, P. Dolle, and P. Chambon Embryonic retinoic acid synthesis is essential for early mouse post-implantation development Nat. Genet. 21 1999 444 448
    • (1999) Nat. Genet. , vol.21 , pp. 444-448
    • Niederreither, K.1    Subbarayan, V.2    Dolle, P.3    Chambon, P.4
  • 164
    • 0344630320 scopus 로고    scopus 로고
    • A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3is prevented by maternal retinoic acid treatment
    • V. Dupe, N. Matt, J.M. Garnier, P. Chambon, M. Mark, and N.B. Ghyselinck A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3is prevented by maternal retinoic acid treatment Proc. Natl. Acad. Sci. USA 100 2003 14036 14041
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14036-14041
    • Dupe, V.1    Matt, N.2    Garnier, J.M.3    Chambon, P.4    Mark, M.5    Ghyselinck, N.B.6
  • 165
    • 0035675295 scopus 로고    scopus 로고
    • External genitalia formation: Role of fibroblast growth factor, retinoic acid signaling, and distal urethral epithelium
    • Y. Ogino, K. Suzuki, R. Haraguchi, Y. Satoh, P. Dolle, and G. Yamada External genitalia formation: role of fibroblast growth factor, retinoic acid signaling, and distal urethral epithelium Ann. N. Y. Acad. Sci 948 2001 13 31
    • (2001) Ann. N. Y. Acad. Sci , vol.948 , pp. 13-31
    • Ogino, Y.1    Suzuki, K.2    Haraguchi, R.3    Satoh, Y.4    Dolle, P.5    Yamada, G.6
  • 166
    • 84860337266 scopus 로고    scopus 로고
    • Microarray analysis of differentially expressed background genes in rats following hemorrhagic shock
    • Y. Xiaojun, Q. Cheng, Z. Yuxing, and H. Zhiqian Microarray analysis of differentially expressed background genes in rats following hemorrhagic shock Mol. Biol. Rep. 39 2012 2045 2053
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 2045-2053
    • Xiaojun, Y.1    Cheng, Q.2    Yuxing, Z.3    Zhiqian, H.4
  • 167
    • 72949121455 scopus 로고    scopus 로고
    • Genetic determinants of both ethanol and acetaldehyde metabolism influence alcohol hypersensitivity and drinking behaviour among Scandinavians
    • A. Linneberg, A. Gonzalez-Quintela, C. Vidal, T. Jorgensen, M. Fenger, T. Hansen, O. Pedersen, and L.L. Husemoen Genetic determinants of both ethanol and acetaldehyde metabolism influence alcohol hypersensitivity and drinking behaviour among Scandinavians Clin. Exp. Allergy 40 2010 123 130
    • (2010) Clin. Exp. Allergy , vol.40 , pp. 123-130
    • Linneberg, A.1    Gonzalez-Quintela, A.2    Vidal, C.3    Jorgensen, T.4    Fenger, M.5    Hansen, T.6    Pedersen, O.7    Husemoen, L.L.8
  • 169
    • 0035998275 scopus 로고    scopus 로고
    • 10-Formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells
    • S.A. Krupenko, and N.V. Oleinik 10-Formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells Cell Growth Differ 13 2002 227 236
    • (2002) Cell Growth Differ , vol.13 , pp. 227-236
    • Krupenko, S.A.1    Oleinik, N.V.2
  • 170
    • 0037795789 scopus 로고    scopus 로고
    • Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis
    • N.V. Oleinik, and S.A. Krupenko Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in A549 cells induces G1 cell cycle arrest and apoptosis Mol. Cancer Res 1 2003 577 588
    • (2003) Mol. Cancer Res , vol.1 , pp. 577-588
    • Oleinik, N.V.1    Krupenko, S.A.2
  • 171
    • 0024315761 scopus 로고
    • Studies on the mechanism of methanol poisoning: Purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase
    • F.C. Johlin, E. Swain, C. Smith, and T.R. Tephly Studies on the mechanism of methanol poisoning: purification and comparison of rat and human liver 10-formyltetrahydrofolate dehydrogenase Mol. Pharmacol. 35 1989 745 750
    • (1989) Mol. Pharmacol. , vol.35 , pp. 745-750
    • Johlin, F.C.1    Swain, E.2    Smith, C.3    Tephly, T.R.4
  • 172
    • 33845595856 scopus 로고    scopus 로고
    • The folate metabolic enzyme ALDH1L1 is restricted to the midline of the early CNS, suggesting a role in human neural tube defects
    • T.E. Anthony, and N. Heintz The folate metabolic enzyme ALDH1L1 is restricted to the midline of the early CNS, suggesting a role in human neural tube defects J. Comp. Neurol 500 2007 368 383
    • (2007) J. Comp. Neurol , vol.500 , pp. 368-383
    • Anthony, T.E.1    Heintz, N.2
  • 173
    • 84859728526 scopus 로고    scopus 로고
    • Pericellular pH homeostasis is a primary function of the Warburg effect: Inversion of metabolic systems to control lactate steady state in tumor cells
    • E.A. Mazzio, N. Boukli, N. Rivera, and K.F. Soliman Pericellular pH homeostasis is a primary function of the Warburg effect: inversion of metabolic systems to control lactate steady state in tumor cells Cancer Sci 103 2012 422 432
    • (2012) Cancer Sci , vol.103 , pp. 422-432
    • Mazzio, E.A.1    Boukli, N.2    Rivera, N.3    Soliman, K.F.4
  • 175
    • 0029935028 scopus 로고    scopus 로고
    • Possible role of liver cytosolic and mitochondrial aldehyde dehydrogenases in acetaldehyde metabolism
    • A.A. Klyosov, L.G. Rashkovetsky, M.K. Tahir, and W.M. Keung Possible role of liver cytosolic and mitochondrial aldehyde dehydrogenases in acetaldehyde metabolism Biochemistry 35 1996 4445 4456
    • (1996) Biochemistry , vol.35 , pp. 4445-4456
    • Klyosov, A.A.1    Rashkovetsky, L.G.2    Tahir, M.K.3    Keung, W.M.4
  • 176
    • 0032721747 scopus 로고    scopus 로고
    • Evaluation of the self-rating of the effects of alcohol form in Asian Americans with aldehyde dehydrogenase polymorphisms
    • T.L. Wall, M.L. Johnson, S.M. Horn, L.G. Carr, T.L. Smith, and M.A. Schuckit Evaluation of the self-rating of the effects of alcohol form in Asian Americans with aldehyde dehydrogenase polymorphisms J. Stud. Alcohol 60 1999 784 789
    • (1999) J. Stud. Alcohol , vol.60 , pp. 784-789
    • Wall, T.L.1    Johnson, M.L.2    Horn, S.M.3    Carr, L.G.4    Smith, T.L.5    Schuckit, M.A.6
  • 177
    • 34748911671 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic basis for partial protection against alcoholism in Asians, heterozygous for the variant ALDH2*2 gene allele
    • G.S. Peng, Y.C. Chen, T.P. Tsao, M.F. Wang, and S.J. Yin Pharmacokinetic and pharmacodynamic basis for partial protection against alcoholism in Asians, heterozygous for the variant ALDH2*2 gene allele Pharmacogenet. Genomics 17 2007 845 855
    • (2007) Pharmacogenet. Genomics , vol.17 , pp. 845-855
    • Peng, G.S.1    Chen, Y.C.2    Tsao, T.P.3    Wang, M.F.4    Yin, S.J.5
  • 178
    • 0033915067 scopus 로고    scopus 로고
    • Association of aldehyde dehydrogenase 2gene polymorphism with multiple oesophageal dysplasia in head and neck cancer patients
    • M. Muto, Y. Hitomi, A. Ohtsu, S. Ebihara, S. Yoshida, and H. Esumi Association of aldehyde dehydrogenase 2gene polymorphism with multiple oesophageal dysplasia in head and neck cancer patients Gut 47 2000 256 261
    • (2000) Gut , vol.47 , pp. 256-261
    • Muto, M.1    Hitomi, Y.2    Ohtsu, A.3    Ebihara, S.4    Yoshida, S.5    Esumi, H.6
  • 180
    • 34249274973 scopus 로고    scopus 로고
    • Glu487Lys polymorphism in the gene for mitochondrial aldehyde dehydrogenase 2is associated with myocardial infarction in elderly Korean men
    • S.A. Jo, E.K. Kim, M.H. Park, C. Han, H.Y. Park, Y. Jang, B.J. Song, and I.A Jo Glu487Lys polymorphism in the gene for mitochondrial aldehyde dehydrogenase 2is associated with myocardial infarction in elderly Korean men Clin. Chim. Acta 382 2007 43 47
    • (2007) Clin. Chim. Acta , vol.382 , pp. 43-47
    • Jo, S.A.1    Kim, E.K.2    Park, M.H.3    Han, C.4    Park, H.Y.5    Jang, Y.6    Song, B.J.7    Jo, I.A.8
  • 182
    • 0027300380 scopus 로고
    • Identification and characterization of a novel class 3aldehyde dehydrogenase overexpressed in a human breast adenocarcinoma cell line exhibiting oxazaphosphorine-specific acquired resistance
    • L. Sreerama, and N.E. Sladek Identification and characterization of a novel class 3aldehyde dehydrogenase overexpressed in a human breast adenocarcinoma cell line exhibiting oxazaphosphorine-specific acquired resistance Biochem. Pharmacol 45 1993 2487 2505
    • (1993) Biochem. Pharmacol , vol.45 , pp. 2487-2505
    • Sreerama, L.1    Sladek, N.E.2
  • 183
    • 0025030409 scopus 로고
    • Identification of the mouse aldehyde dehydrogenases important in aldophosphamide detoxification
    • C.L. Manthey, G.J. Landkamer, and N.E. Sladek Identification of the mouse aldehyde dehydrogenases important in aldophosphamide detoxification Cancer Res. 50 1990 4991 5002
    • (1990) Cancer Res. , vol.50 , pp. 4991-5002
    • Manthey, C.L.1    Landkamer, G.J.2    Sladek, N.E.3
  • 184
    • 0034803769 scopus 로고    scopus 로고
    • Genetic modification of hematopoietic progenitor cells for combined resistance to 4-hydroperoxycyclophosphamide, vincristine, and daunorubicin
    • J.S. Wang, Q. Fang, D.J. Sun, J. Chen, X.L. Zhou, G.W. Lin, H.Z. Lu, and J. Fei Genetic modification of hematopoietic progenitor cells for combined resistance to 4-hydroperoxycyclophosphamide, vincristine, and daunorubicin Acta Pharmacol. Sin. 22 2001 949 955
    • (2001) Acta Pharmacol. Sin. , vol.22 , pp. 949-955
    • Wang, J.S.1    Fang, Q.2    Sun, D.J.3    Chen, J.4    Zhou, X.L.5    Lin, G.W.6    Lu, H.Z.7    Fei, J.8
  • 186
    • 24044542350 scopus 로고    scopus 로고
    • Multi-locus association study of schizophrenia susceptibility genes with a posterior probability method
    • X. Sun, Y. Jia, X. Zhang, Q. Xu, Y. Shen, and Y. Li Multi-locus association study of schizophrenia susceptibility genes with a posterior probability method Sci. China C Life Sci. 48 2005 263 269
    • (2005) Sci. China C Life Sci. , vol.48 , pp. 263-269
    • Sun, X.1    Jia, Y.2    Zhang, X.3    Xu, Q.4    Shen, Y.5    Li, Y.6
  • 187
    • 7744234003 scopus 로고    scopus 로고
    • Assay and subcellular localization of pyrroline-5-carboxylate dehydrogenase in rat liver
    • M.R. Haslett, D. Pink, B. Walters, and M.E. Brosnan Assay and subcellular localization of pyrroline-5-carboxylate dehydrogenase in rat liver Biochim. Biophys. Acta 1675 2004 81 86
    • (2004) Biochim. Biophys. Acta , vol.1675 , pp. 81-86
    • Haslett, M.R.1    Pink, D.2    Walters, B.3    Brosnan, M.E.4
  • 189
    • 26044443055 scopus 로고    scopus 로고
    • High-level expression and characterization of the recombinant enzyme, and tissue distribution of human succinic semialdehyde dehydrogenase
    • J.H. Kang, Y.B. Park, T.L. Huh, W.H. Lee, M.S. Choi, and O.S. Kwon High-level expression and characterization of the recombinant enzyme, and tissue distribution of human succinic semialdehyde dehydrogenase Protein Expression Purif 44 2005 16 22
    • (2005) Protein Expression Purif , vol.44 , pp. 16-22
    • Kang, J.H.1    Park, Y.B.2    Huh, T.L.3    Lee, W.H.4    Choi, M.S.5    Kwon, O.S.6
  • 190
    • 0024462212 scopus 로고
    • Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver: Identity to malonate-semialdehyde dehydrogenase
    • G.W. Goodwin, P.M. Rougraff, E.J. Davis, and R.A. Harris Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver: identity to malonate-semialdehyde dehydrogenase J. Biol. Chem. 264 1989 14965 14971
    • (1989) J. Biol. Chem. , vol.264 , pp. 14965-14971
    • Goodwin, G.W.1    Rougraff, P.M.2    Davis, E.J.3    Harris, R.A.4
  • 191
    • 79955599352 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity
    • C. Brocker, M. Cantore, P. Failli, and V. Vasiliou Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity Chem. Biol. Interact. 191 2011 269 277
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 269-277
    • Brocker, C.1    Cantore, M.2    Failli, P.3    Vasiliou, V.4
  • 193
    • 0025264451 scopus 로고
    • L-Pipecolic acid metabolism in human liver: L-alpha-aminoadipate delta-semialdehyde oxidoreductase
    • Y.F. Chang, P. Ghosh, and V.V. Rao L-Pipecolic acid metabolism in human liver: L-alpha-aminoadipate delta-semialdehyde oxidoreductase Biochim. Biophys. Acta 1038 1990 300 305
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 300-305
    • Chang, Y.F.1    Ghosh, P.2    Rao, V.V.3
  • 194
    • 0034704136 scopus 로고    scopus 로고
    • CDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog, ALDH12
    • M. Lin, and J.L. Napoli cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog, ALDH12 J. Biol. Chem 275 2000 40106 40112
    • (2000) J. Biol. Chem , vol.275 , pp. 40106-40112
    • Lin, M.1    Napoli, J.L.2
  • 195
    • 0024583015 scopus 로고
    • Human aldehyde dehydrogenase: Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde
    • G. Kurys, W. Ambroziak, and R. Pietruszko Human aldehyde dehydrogenase: purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde J. Biol. Chem. 264 1989 4715 4721
    • (1989) J. Biol. Chem. , vol.264 , pp. 4715-4721
    • Kurys, G.1    Ambroziak, W.2    Pietruszko, R.3
  • 198
    • 70249097395 scopus 로고    scopus 로고
    • Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1
    • M.C. Hanna, and C. Blackstone Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1 Neurogenetics 10 2009 217 228
    • (2009) Neurogenetics , vol.10 , pp. 217-228
    • Hanna, M.C.1    Blackstone, C.2
  • 199
    • 0031609943 scopus 로고    scopus 로고
    • [A new inherited metabolic disease: Delta1-pyrroline 5-carboxylate synthetase deficiency]
    • discussion
    • P. Kamoun, B. Aral, and J.M. Saudubray [A new inherited metabolic disease: delta1-pyrroline 5-carboxylate synthetase deficiency] Bull. Acad. Natl. Med. 182 131-137 1998 138 139 discussion
    • (1998) Bull. Acad. Natl. Med. , vol.182 , Issue.138-139 , pp. 131-137
    • Kamoun, P.1    Aral, B.2    Saudubray, J.M.3
  • 200
    • 12144266451 scopus 로고    scopus 로고
    • Delta1-pyrroline-5-carboxylate synthase deficiency: Neurodegeneration, cataracts and connective tissue manifestations combined with hyperammonaemia and reduced ornithine, citrulline, arginine and proline
    • M.R. Baumgartner, D. Rabier, M.C. Nassogne, J.L. Dufier, J.P. Padovani, P. Kamoun, D. Valle, and J.M. Saudubray Delta1-pyrroline-5-carboxylate synthase deficiency: neurodegeneration, cataracts and connective tissue manifestations combined with hyperammonaemia and reduced ornithine, citrulline, arginine and proline Eur. J. Pediatr. 164 2005 31 36
    • (2005) Eur. J. Pediatr. , vol.164 , pp. 31-36
    • Baumgartner, M.R.1    Rabier, D.2    Nassogne, M.C.3    Dufier, J.L.4    Padovani, J.P.5    Kamoun, P.6    Valle, D.7    Saudubray, J.M.8
  • 201
    • 0028134625 scopus 로고
    • Intrinsic cellular resistance to oxazaphosphorines exhibited by a human colon carcinoma cell line expressing relatively large amounts of a class-3 aldehyde dehydrogenase
    • G.K. Rekha, L. Sreerama, and N.E. Sladek Intrinsic cellular resistance to oxazaphosphorines exhibited by a human colon carcinoma cell line expressing relatively large amounts of a class-3 aldehyde dehydrogenase Biochem. Pharmacol 48 1994 1943 1952
    • (1994) Biochem. Pharmacol , vol.48 , pp. 1943-1952
    • Rekha, G.K.1    Sreerama, L.2    Sladek, N.E.3
  • 202
    • 0022220140 scopus 로고
    • Aldehyde dehydrogenase activity as the basis for the relative insensitivity of murine pluripotent hematopoietic stem cells to oxazaphosphorines
    • F.R. Kohn, and N.E. Sladek Aldehyde dehydrogenase activity as the basis for the relative insensitivity of murine pluripotent hematopoietic stem cells to oxazaphosphorines Biochem. Pharmacol 34 1985 3465 3471
    • (1985) Biochem. Pharmacol , vol.34 , pp. 3465-3471
    • Kohn, F.R.1    Sladek, N.E.2
  • 203
    • 0021922114 scopus 로고
    • Collateral sensitivity to cross-linking agents exhibited by cultured L1210 cells resistant to oxazaphosphorines
    • N.E. Sladek, J.E. Low, and G.J. Landkamer Collateral sensitivity to cross-linking agents exhibited by cultured L1210 cells resistant to oxazaphosphorines Cancer Res. 45 1985 625 629
    • (1985) Cancer Res. , vol.45 , pp. 625-629
    • Sladek, N.E.1    Low, J.E.2    Landkamer, G.J.3
  • 204
    • 0023952342 scopus 로고
    • Characterization of cytosolic aldehyde dehydrogenase from cyclophosphamide resistant L1210 cells
    • J.E. Russo, and J. Hilton Characterization of cytosolic aldehyde dehydrogenase from cyclophosphamide resistant L1210 cells Cancer Res. 48 1988 2963 2968
    • (1988) Cancer Res. , vol.48 , pp. 2963-2968
    • Russo, J.E.1    Hilton, J.2
  • 207
    • 0025004019 scopus 로고
    • Development and characterization of a cyclophosphamide-resistant subline of acute myeloid leukemia in the Lewis × Brown Norway hybrid rat
    • T.M. Koelling, A.M. Yeager, J. Hilton, D.T. Haynie, and J.M. Wiley Development and characterization of a cyclophosphamide-resistant subline of acute myeloid leukemia in the Lewis × Brown Norway hybrid rat Blood 76 1990 1209 1213
    • (1990) Blood , vol.76 , pp. 1209-1213
    • Koelling, T.M.1    Yeager, A.M.2    Hilton, J.3    Haynie, D.T.4    Wiley, J.M.5
  • 208
    • 0030024868 scopus 로고    scopus 로고
    • Induction of cyclophosphamide-resistance by aldehyde-dehydrogenase gene transfer
    • M. Magni, S. Shammah, R. Schiro, W. Mellado, R. Dalla-Favera, and A.M. Gianni Induction of cyclophosphamide-resistance by aldehyde-dehydrogenase gene transfer Blood 87 1996 1097 1103
    • (1996) Blood , vol.87 , pp. 1097-1103
    • Magni, M.1    Shammah, S.2    Schiro, R.3    Mellado, W.4    Dalla-Favera, R.5    Gianni, A.M.6
  • 209
    • 0032549486 scopus 로고    scopus 로고
    • In vitro selection for K562 cells with higher retrovirally mediated copy number of aldehyde dehydrogenase class-1 and higher resistance to 4-hydroperoxycyclophosphamide
    • J.S. Moreb, M. Schweder, B. Gray, J. Zucali, and R. Zori In vitro selection for K562 cells with higher retrovirally mediated copy number of aldehyde dehydrogenase class-1 and higher resistance to 4- hydroperoxycyclophosphamide Hum. Gene Ther 9 1998 611 619
    • (1998) Hum. Gene Ther , vol.9 , pp. 611-619
    • Moreb, J.S.1    Schweder, M.2    Gray, B.3    Zucali, J.4    Zori, R.5
  • 210
    • 0036627851 scopus 로고    scopus 로고
    • Aldehyde-dehydrogenase gene-transduced hematopoietic cell line K562 overcomes the cytotoxicity of cyclophosphamide in vitro
    • X.W. Yang, W. Wang, J.X. Fu, J.N. Cen, F. Guo, X.M. Xia, and Z.X. Chen Aldehyde-dehydrogenase gene-transduced hematopoietic cell line K562 overcomes the cytotoxicity of cyclophosphamide in vitro Zhongguo Shi Yan Xue Ye Xue Za Zhi 10 2002 205 208
    • (2002) Zhongguo Shi Yan Xue Ye Xue Za Zhi , vol.10 , pp. 205-208
    • Yang, X.W.1    Wang, W.2    Fu, J.X.3    Cen, J.N.4    Guo, F.5    Xia, X.M.6    Chen, Z.X.7
  • 211
    • 0029685930 scopus 로고    scopus 로고
    • Overexpression of the human aldehyde dehydrogenase class i results in increased resistance to 4-hydroperoxycyclophosphamide
    • J. Moreb, M. Schweder, A. Suresh, and J.R. Zucali Overexpression of the human aldehyde dehydrogenase class I results in increased resistance to 4-hydroperoxycyclophosphamide Cancer Gene Ther 3 1996 24 30
    • (1996) Cancer Gene Ther , vol.3 , pp. 24-30
    • Moreb, J.1    Schweder, M.2    Suresh, A.3    Zucali, J.R.4
  • 212
    • 0027932138 scopus 로고
    • Oxazaphosphorine-specific resistance in human MCF-7 breast carcinoma cell lines expressing transfected rat class 3aldehyde dehydrogenase
    • K.D. Bunting, R. Lindahl, and A.J. Townsend Oxazaphosphorine-specific resistance in human MCF-7 breast carcinoma cell lines expressing transfected rat class 3aldehyde dehydrogenase J. Biol. Chem 269 1994 23197 23203
    • (1994) J. Biol. Chem , vol.269 , pp. 23197-23203
    • Bunting, K.D.1    Lindahl, R.2    Townsend, A.J.3
  • 213
    • 0034099052 scopus 로고    scopus 로고
    • Expression of antisense RNA to aldehyde dehydrogenase class-1 sensitizes tumor cells to 4-hydroperoxycyclophosphamide in vitro
    • J.S. Moreb, C. Maccow, M. Schweder, and J. Hecomovich Expression of antisense RNA to aldehyde dehydrogenase class-1 sensitizes tumor cells to 4-hydroperoxycyclophosphamide in vitro J. Pharmacol. Exp. Ther. 293 2000 390 396
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , pp. 390-396
    • Moreb, J.S.1    MacCow, C.2    Schweder, M.3    Hecomovich, J.4
  • 214
    • 0029888371 scopus 로고    scopus 로고
    • De novo expression of transfected human class 1aldehyde dehydrogenase (ALDH) causes resistance to oxazaphosphorine anti-cancer alkylating agents in hamster V79 cell lines: Elevated class 1ALDH activity is closely correlated with reduction in DNA interstrand cross-linking and lethality
    • K.D. Bunting, and A.J. Townsend De novo expression of transfected human class 1aldehyde dehydrogenase (ALDH) causes resistance to oxazaphosphorine anti-cancer alkylating agents in hamster V79 cell lines: elevated class 1ALDH activity is closely correlated with reduction in DNA interstrand cross-linking and lethality J. Biol. Chem 271 1996 11884 11890
    • (1996) J. Biol. Chem , vol.271 , pp. 11884-11890
    • Bunting, K.D.1    Townsend, A.J.2
  • 215
    • 0029936167 scopus 로고    scopus 로고
    • Protection by transfected rat or human class 3aldehyde dehydrogenase against the cytotoxic effects of oxazaphosphorine alkylating agents in hamster V79 cell lines: Demonstration of aldophosphamide metabolism by the human cytosolic class 3isozyme
    • K.D. Bunting, and A.J. Townsend Protection by transfected rat or human class 3aldehyde dehydrogenase against the cytotoxic effects of oxazaphosphorine alkylating agents in hamster V79 cell lines: demonstration of aldophosphamide metabolism by the human cytosolic class 3isozyme J. Biol. Chem 271 1996 11891 11896
    • (1996) J. Biol. Chem , vol.271 , pp. 11891-11896
    • Bunting, K.D.1    Townsend, A.J.2
  • 216
    • 0035969833 scopus 로고    scopus 로고
    • Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells
    • A.J. Townsend, S. Leone-Kabler, R.L. Haynes, Y. Wu, L. Szweda, and K.D. Bunting Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells Chem. Biol. Interact. 130-132 2001 261 273
    • (2001) Chem. Biol. Interact. , vol.130-132 , pp. 261-273
    • Townsend, A.J.1    Leone-Kabler, S.2    Haynes, R.L.3    Wu, Y.4    Szweda, L.5    Bunting, K.D.6
  • 218
    • 0034985885 scopus 로고    scopus 로고
    • Generation of dual resistance to 4-hydroperoxycyclophosphamide and methotrexate by retroviral transfer of the human aldehyde dehydrogenase class 1gene and a mutated dihydrofolate reductase gene
    • N. Takebe, S.C. Zhao, D. Adhikari, S. Mineishi, M. Sadelain, J. Hilton, M. Colvin, D. Banerjee, and J.R. Bertino Generation of dual resistance to 4-hydroperoxycyclophosphamide and methotrexate by retroviral transfer of the human aldehyde dehydrogenase class 1gene and a mutated dihydrofolate reductase gene Mol. Ther. 3 2001 88 96
    • (2001) Mol. Ther. , vol.3 , pp. 88-96
    • Takebe, N.1    Zhao, S.C.2    Adhikari, D.3    Mineishi, S.4    Sadelain, M.5    Hilton, J.6    Colvin, M.7    Banerjee, D.8    Bertino, J.R.9


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