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Volumn 36, Issue 2, 2004, Pages 279-299

Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism

Author keywords

Aldehyde dehydrogenases; Human; Lipid peroxidation; Metabolism; Polymorphisms

Indexed keywords

4 AMINOBUTYRIC ACID; ALCOHOL; ALDEHYDE; ALDEHYDE DEHYDROGENASE; AMINO ACID; CARBOHYDRATE; CYCLOPHOSPHAMIDE; DRUG; FOLIC ACID; LIPID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RETINOIC ACID;

EID: 3042551383     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-120034001     Document Type: Conference Paper
Times cited : (264)

References (117)
  • 1
    • 0041669529 scopus 로고    scopus 로고
    • Fate of 4-hydroxynonenal in vivo: Disposition and metabolic pathways
    • Alary, J., Gueraud, F., Cravedi, J. P. (2003a). Fate of 4-hydroxynonenal in vivo: disposition and metabolic pathways. Mol. Aspects Med. 24(4-5):177-187.
    • (2003) Mol. Aspects Med. , vol.24 , Issue.4-5 , pp. 177-187
    • Alary, J.1    Gueraud, F.2    Cravedi, J.P.3
  • 2
    • 0037347349 scopus 로고    scopus 로고
    • Identification of intermediate pathways of 4-hydroxynonenal metabolism in the rat
    • Alary, J., Fernandez, Y., Debrauwer, L., Perdu, E., Gueraud, F. (2003b). Identification of intermediate pathways of 4-hydroxynonenal metabolism in the rat. Chem. Res. Toxicol. 16(3):320-327.
    • (2003) Chem. Res. Toxicol. , vol.16 , Issue.3 , pp. 320-327
    • Alary, J.1    Fernandez, Y.2    Debrauwer, L.3    Perdu, E.4    Gueraud, F.5
  • 3
    • 0023604469 scopus 로고
    • Human aldehyde dehydrogenase: Metabolism of putrescine and histamine
    • Ambroziak, W., Pietruszko, R. (1987). Human aldehyde dehydrogenase: metabolism of putrescine and histamine. Alcohol., Clin. Exp. Res. 11(6):528-532.
    • (1987) Alcohol., Clin. Exp. Res. , vol.11 , Issue.6 , pp. 528-532
    • Ambroziak, W.1    Pietruszko, R.2
  • 4
    • 0025785329 scopus 로고
    • Human aldehyde dehydrogenase. Activity with aldehyde metabolites of monoamines, diamines, and polyamines
    • Ambroziak, W., Pietruszko, R. (1991). Human aldehyde dehydrogenase. Activity with aldehyde metabolites of monoamines, diamines, and polyamines. J. Biol. Chem. 266(20):13011-13018.
    • (1991) J. Biol. Chem. , vol.266 , Issue.20 , pp. 13011-13018
    • Ambroziak, W.1    Pietruszko, R.2
  • 5
    • 0033585012 scopus 로고    scopus 로고
    • Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney
    • Ambroziak, W., Izaguirre, G., Pietruszko, R. (1999). Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. J. Biol. Chem. 274 (47):33366-33373.
    • (1999) J. Biol. Chem. , vol.274 , Issue.47 , pp. 33366-33373
    • Ambroziak, W.1    Izaguirre, G.2    Pietruszko, R.3
  • 6
    • 0000090925 scopus 로고    scopus 로고
    • Retinoic acid biosynthetic enzyme ALDH1 localizes in a subset of retinoid-dependent tissues during xenopus development
    • Ang, H. L., Duester, G. (1999). Retinoic acid biosynthetic enzyme ALDH1 localizes in a subset of retinoid-dependent tissues during xenopus development. Dev. Dyn. 215 (3):264-272.
    • (1999) Dev. Dyn. , vol.215 , Issue.3 , pp. 264-272
    • Ang, H.L.1    Duester, G.2
  • 7
    • 0029909051 scopus 로고    scopus 로고
    • Curcumin protects against 4-hydroxy-2-trans-nonenal-induced cataract formation in rat lenses
    • Awasthi, S., Srivatava, S. K., Piper, J. T., Singhal, S. S., Chaubey, M., Awasthi, Y. C. (1996). Curcumin protects against 4-hydroxy-2-trans-nonenal- induced cataract formation in rat lenses. Am. J. Clin. Nutr. 64(5):761-766.
    • (1996) Am. J. Clin. Nutr. , vol.64 , Issue.5 , pp. 761-766
    • Awasthi, S.1    Srivatava, S.K.2    Piper, J.T.3    Singhal, S.S.4    Chaubey, M.5    Awasthi, Y.C.6
  • 8
    • 0034703867 scopus 로고    scopus 로고
    • Hyperammonemia with reduced omithine, citrulline, arginine and proline: A new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline- 5-carboxylate synthase
    • Baumgartner, M. R., Hu, C. A., Almashanu, S., Steel, G., Obie, C., Aral, B., Rabier, D., Kamoun, P., Saudubray, J. M., Valle, D. (2000). Hyperammonemia with reduced omithine, 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(19):2853-2858.
    • (2000) Hum. Mol. Genet. , vol.9 , Issue.19 , 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
  • 9
    • 0033564830 scopus 로고    scopus 로고
    • Differential distribution of retinoic acid synthesis in the chicken embryo as determined by immunolocalization of the retinoic acid synthetic enzyme, RALDH-2
    • Berggren, K., McCaffery, P., Drager, U., Forehand, C. J. (1999). Differential distribution of retinoic acid synthesis in the chicken embryo as determined by immunolocalization of the retinoic acid synthetic enzyme, RALDH-2. Dev. Biol. 210(2):288-304.
    • (1999) Dev. Biol. , vol.210 , Issue.2 , pp. 288-304
    • Berggren, K.1    McCaffery, P.2    Drager, U.3    Forehand, C.J.4
  • 10
    • 0024381856 scopus 로고
    • Nutritional folate deficiency in Chinese hamster ovary cells. I. Characterization of the pleiotropic response and its modulation by nucleic acid precursors
    • Borman, L. S., Branda, R. F. (1989). Nutritional folate deficiency in Chinese hamster ovary cells. I. Characterization of the pleiotropic response and its modulation by nucleic acid precursors. J. Cell. Physiol. 140(2):335-343.
    • (1989) J. Cell. Physiol. , vol.140 , Issue.2 , pp. 335-343
    • Borman, L.S.1    Branda, R.F.2
  • 11
    • 0029936167 scopus 로고    scopus 로고
    • Protection by transfected rat or human class 3 aldehyde dehydrogenase against the cytotoxic effects of oxazaphosphorine alkylating agents in hamster V79 cell lines. Demonstration of aldophosphamide metabolism by the human cytosolic class 3 isozyme
    • Bunting, K. D., Townsend, A. J. (1996). Protection by transfected rat or human class 3 aldehyde dehydrogenase against the cytotoxic effects of oxazaphosphorine alkylating agents in hamster V79 cell lines. Demonstration of aldophosphamide metabolism by the human cytosolic class 3 isozyme. J. Biol. Chem. 271 (20):11891-11896.
    • (1996) J. Biol. Chem. , vol.271 , Issue.20 , pp. 11891-11896
    • Bunting, K.D.1    Townsend, A.J.2
  • 12
    • 0027932138 scopus 로고
    • Oxazaphosphorine-specific resistance in human MCF-7 breast carcinoma cell lines expressing transfected rat class 3 aldehyde dehydrogenase
    • Bunting, K. D., Lindahl, R., Townsend, A. J. (1994). Oxazaphosphorine- specific resistance in human MCF-7 breast carcinoma cell lines expressing transfected rat class 3 aldehyde dehydrogenase. J. Biol. Chem. 269(37):23197-23203.
    • (1994) J. Biol. Chem. , vol.269 , Issue.37 , pp. 23197-23203
    • Bunting, K.D.1    Lindahl, R.2    Townsend, A.J.3
  • 13
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid beta-peptide
    • Butterfield, D. A., Drake, J., Pocernich, C., Castegna, A. (2001). Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide. Trends Mol. Med. 7(12):548-554.
    • (2001) Trends Mol. Med. , vol.7 , Issue.12 , pp. 548-554
    • Butterfield, D.A.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 14
    • 0026725305 scopus 로고
    • Succinic semialdehyde dehydrogenase from mammalian brain: Subunit analysis using polyclonal antiserum
    • Chambliss, K. L., Gibson, K. M. (1992). Succinic semialdehyde dehydrogenase from mammalian brain: subunit analysis using polyclonal antiserum. Int. J. Biochem. 24 (9):1493-1499.
    • (1992) Int. J. Biochem. , vol.24 , Issue.9 , pp. 1493-1499
    • Chambliss, K.L.1    Gibson, K.M.2
  • 15
    • 0033931899 scopus 로고    scopus 로고
    • Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency
    • Chambliss, K. L., Gray, R. G., Rylance, G., Pollitt, R. J., Gibson, K. M. (2000). Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency. J. Inherit. Metab. Dis. 23(5):497-504.
    • (2000) J. Inherit. Metab. Dis. , vol.23 , Issue.5 , pp. 497-504
    • Chambliss, K.L.1    Gray, R.G.2    Rylance, G.3    Pollitt, R.J.4    Gibson, K.M.5
  • 16
    • 0027987995 scopus 로고
    • Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice
    • Champion, K. M., Cook, R. J., Tollaksen, S. L., Giometti, C. S. (1994). Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice. Proc. Natl. Acad. Sci. U. S. A. 91(24):11338-11342.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , Issue.24 , pp. 11338-11342
    • Champion, K.M.1    Cook, R.J.2    Tollaksen, S.L.3    Giometti, C.S.4
  • 17
    • 0242365646 scopus 로고    scopus 로고
    • Purification, N-terminal sequence determination and enzymatic characterization of antiquitin from the liver of grass carp
    • Chan, W. M., Tang, W. K., Cheng, C. H., Fong, W. P. (2003). Purification, N-terminal sequence determination and enzymatic characterization of antiquitin from the liver of grass carp. Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 136(3):443-450.
    • (2003) Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. , vol.136 , Issue.3 , pp. 443-450
    • Chan, W.M.1    Tang, W.K.2    Cheng, C.H.3    Fong, W.P.4
  • 18
    • 0028177496 scopus 로고
    • Polymorphism of alcohol and aldehyde dehydrogenase genes and alcoholic cirrhosis in Chinese patients
    • Chao, Y. C., Liou, S. R., Chung, Y. Y., Tang, H. S., Hsu, C. T., Li, T. K., Yin, S. J. (1994). Polymorphism of alcohol and aldehyde dehydrogenase genes and alcoholic cirrhosis in Chinese patients. Hepatology 19(2):360-366.
    • (1994) Hepatology , vol.19 , Issue.2 , pp. 360-366
    • Chao, Y.C.1    Liou, S.R.2    Chung, Y.Y.3    Tang, H.S.4    Hsu, C.T.5    Li, T.K.6    Yin, S.J.7
  • 19
    • 0029161037 scopus 로고
    • Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase
    • Chern, M. K., Pietruszko, R. (1995). Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase. Biochem. Biophys. Res. Commun. 213(2):561-568.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , Issue.2 , pp. 561-568
    • Chern, M.K.1    Pietruszko, R.2
  • 20
    • 0025828320 scopus 로고
    • Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase
    • Cook, R. J., Lloyd, R. S., Wagner, C. (1991). Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. J. Biol. Chem. 266 (8):4965-4973.
    • (1991) J. Biol. Chem. , vol.266 , Issue.8 , pp. 4965-4973
    • Cook, R.J.1    Lloyd, R.S.2    Wagner, C.3
  • 22
    • 1342323614 scopus 로고    scopus 로고
    • Fatty aldehyde dehydrogenase: Potential role in oxidative stress protection and regulation of its gene expression by insulin
    • Demozay, D., Rocchi, S., Mas, J. C., Grillo, S., Pirola, L., Chavey, C., Van Obberghen, E. (2003). Fatty aldehyde dehydrogenase: potential role in oxidative stress protection and regulation of its gene expression by insulin. J. Biol. Chem. 279(8):6261-6270.
    • (2003) J. Biol. Chem. , vol.279 , Issue.8 , pp. 6261-6270
    • Demozay, D.1    Rocchi, S.2    Mas, J.C.3    Grillo, S.4    Pirola, L.5    Chavey, C.6    Van Obberghen, E.7
  • 23
    • 0036226623 scopus 로고    scopus 로고
    • Can malondialdehyde be used as a biological marker of progression in neurodegenerative disease?
    • Dib, M., Garrel, C., Favier, A., Robin, V., Desnuelle, C. (2002). Can malondialdehyde be used as a biological marker of progression in neurodegenerative disease? J. Neurol. 249(4):367-374.
    • (2002) J. Neurol. , vol.249 , Issue.4 , pp. 367-374
    • Dib, M.1    Garrel, C.2    Favier, A.3    Robin, V.4    Desnuelle, C.5
  • 24
    • 0026667068 scopus 로고
    • Identification of human liver aldehyde dehydrogenases that catalyze the oxidation of aldophosphamide and retinaldehyde
    • Dockham, P. A., Lee, M. O., Sladek, N. E. (1992). Identification of human liver aldehyde dehydrogenases that catalyze the oxidation of aldophosphamide and retinaldehyde. Biochem. Pharmacol. 43(11):2453-2469.
    • (1992) Biochem. Pharmacol. , vol.43 , Issue.11 , pp. 2453-2469
    • Dockham, P.A.1    Lee, M.O.2    Sladek, N.E.3
  • 25
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin A function: Production of visual pigment and retinoic acid
    • Duester, G. (2000). Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid. Eur. J. Biochem. 267(14):4315-4324.
    • (2000) Eur. J. Biochem. , vol.267 , Issue.14 , pp. 4315-4324
    • Duester, G.1
  • 26
    • 0344630320 scopus 로고    scopus 로고
    • A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment
    • Dupe, V., Matt, N., Garnier, J. M., Chambon, P., Mark, M., Ghyselinck, N. B. (2003). A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment. Proc. Natl. Acad. Sci. U. S. A. 100 (24):14036-14041.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.24 , pp. 14036-14041
    • Dupe, V.1    Matt, N.2    Garnier, J.M.3    Chambon, P.4    Mark, M.5    Ghyselinck, N.B.6
  • 27
    • 0028354233 scopus 로고
    • Rat liver cytosolic retinal dehydrogenase: Comparison of 13-cis-, 9-cis-, and all-trans-retinal as substrates and effects of cellular retinoid-binding proteins and retinoic acid on activity
    • el Akawi, Z., Napoli, J. L. (1994). Rat liver cytosolic retinal dehydrogenase: comparison of 13-cis-, 9-cis-, and all-trans-retinal as substrates and effects of cellular retinoid-binding proteins and retinoic acid on activity. Biochemistry 33(7):1938-1943.
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1938-1943
    • El Akawi, Z.1    Napoli, J.L.2
  • 28
    • 0025947090 scopus 로고
    • Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes
    • Enomoto, N., Takase, S., Takada, N., Takada, A. (1991). Alcoholic liver disease in heterozygotes of mutant and normal aldehyde dehydrogenase-2 genes. Hepatology 13(6):1071-1075.
    • (1991) Hepatology , vol.13 , Issue.6 , pp. 1071-1075
    • Enomoto, N.1    Takase, S.2    Takada, N.3    Takada, A.4
  • 29
    • 0034975104 scopus 로고    scopus 로고
    • The role of acetaldehyde in the actions of alcohol (update 2000)
    • Eriksson, C. J. (2001). The role of acetaldehyde in the actions of alcohol (update 2000). Alcohol., Clin. Exp. Res. 25(5 suppl. ISBRA):15S-32S.
    • (2001) Alcohol., Clin. Exp. Res. , vol.25 , Issue.5 SUPPL. ISBRA
    • Eriksson, C.J.1
  • 30
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal malondialdehyde and related aldehydes
    • Esterbauer, H., Schaur, R. J., Zollner, H. (1991). Chemistry and biochemistry of 4-hydroxynonenal malondialdehyde and related aldehydes. Free Radic. Biol. Med. 11:81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 32
    • 0035805636 scopus 로고    scopus 로고
    • Pyridoxal phosphate de-activation by pyrroline-5-carboxylic acid. Increased risk of vitamin B6 deficiency and seizures in hyperprolinemia type II
    • Farrant, R. D., Walker, V., Mills, G. A., Mellor, J. M., Langley, G. J. (2001). Pyridoxal phosphate de-activation by pyrroline-5-carboxylic acid. Increased risk of vitamin B6 deficiency and seizures in hyperprolinemia type II. J. Biol. Chem. 276(18): 15107-15116.
    • (2001) J. Biol. Chem. , vol.276 , Issue.18 , pp. 15107-15116
    • Farrant, R.D.1    Walker, V.2    Mills, G.A.3    Mellor, J.M.4    Langley, G.J.5
  • 33
    • 0031887260 scopus 로고    scopus 로고
    • 4-Hydroxybutyric acid and the clinical phenotype of succinic semialdehyde dehydrogenase deficiency, an inborn error of GABA metabolism
    • Gibson, K. M., Hoffmann, G. F., Hodson, A. K., Bottiglieri, T., Jakobs, C. (1998). 4-Hydroxybutyric acid and the clinical phenotype of succinic semialdehyde dehydrogenase deficiency, an inborn error of GABA metabolism. Neuropediatrics 29(1):14-22.
    • (1998) Neuropediatrics , vol.29 , Issue.1 , pp. 14-22
    • Gibson, K.M.1    Hoffmann, G.F.2    Hodson, A.K.3    Bottiglieri, T.4    Jakobs, C.5
  • 34
    • 0025019083 scopus 로고
    • Pharmacogenetics of aldehyde dehydrogenase (ALDH)
    • Goedde, H. W., Agarwal, D. P. (1990). Pharmacogenetics of aldehyde dehydrogenase (ALDH). Pharmacol. Ther. 45(3):345-371.
    • (1990) Pharmacol. Ther. , vol.45 , Issue.3 , pp. 345-371
    • Goedde, H.W.1    Agarwal, D.P.2
  • 36
    • 0034731510 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase prominently expressed in sensory neuroepithelia during development
    • Grun, F., Hirose, Y., Kawauchi, S., Ogura, T., Umesono, K. (2000). Aldehyde dehydrogenase 6, a cytosolic retinaldehyde dehydrogenase prominently expressed in sensory neuroepithelia during development. J. Biol. Chem. 275(52):41210-41218.
    • (2000) J. Biol. Chem. , vol.275 , Issue.52 , pp. 41210-41218
    • Grun, F.1    Hirose, Y.2    Kawauchi, S.3    Ogura, T.4    Umesono, K.5
  • 38
    • 0032713404 scopus 로고    scopus 로고
    • Distinct functions for Aldh1 and Raldh2 in the control of ligand production for embryonic retinoid signaling pathways
    • Haselbeck, R. J., Hoffmann, I., Duester, G. (1999). Distinct functions for Aldh1 and Raldh2 in the control of ligand production for embryonic retinoid signaling pathways. Dev. Genet. 25(4):353-364.
    • (1999) Dev. Genet. , vol.25 , Issue.4 , pp. 353-364
    • Haselbeck, R.J.1    Hoffmann, I.2    Duester, G.3
  • 39
    • 0036089837 scopus 로고    scopus 로고
    • Relationship between genetic polymorphisms of alcohol-metabolizing enzymes and changes in risk factors for coronary heart disease associated with alcohol consumption
    • Hashimoto, Y., Nakayama, T., Futamura, A., Omura, M., Nakarai, H., Nakahara, K. (2002). Relationship between genetic polymorphisms of alcohol-metabolizing enzymes and changes in risk factors for coronary heart disease associated with alcohol consumption. Clin. Chem. 48(7):1043-1048.
    • (2002) Clin. Chem. , vol.48 , Issue.7 , pp. 1043-1048
    • Hashimoto, Y.1    Nakayama, T.2    Futamura, A.3    Omura, M.4    Nakarai, H.5    Nakahara, K.6
  • 40
    • 0033799084 scopus 로고    scopus 로고
    • Structure-activity relationships for growth inhibition and induction of apoptosis by 4-hydroxy-2-nonenal in raw 264.7 cells
    • Haynes, R. L., Szweda, L., Pickin, K., Welker, M. E., Townsend, A. J. (2000). Structure-activity relationships for growth inhibition and induction of apoptosis by 4-hydroxy-2-nonenal in raw 264.7 cells. Mol. Pharmacol. 58(4):788-794.
    • (2000) Mol. Pharmacol. , vol.58 , Issue.4 , pp. 788-794
    • Haynes, R.L.1    Szweda, L.2    Pickin, K.3    Welker, M.E.4    Townsend, A.J.5
  • 41
    • 0020523577 scopus 로고
    • Metabolism of malondialdehyde by rat liver aldehyde dehydrogenase
    • Hjelle, J. J., Petersen, D. R. (1983). Metabolism of malondialdehyde by rat liver aldehyde dehydrogenase. Toxicol. Appl. Pharmacol. 70(1):57-66.
    • (1983) Toxicol. Appl. Pharmacol. , vol.70 , Issue.1 , pp. 57-66
    • Hjelle, J.J.1    Petersen, D.R.2
  • 43
    • 0030942117 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: Genomic organization and gene structure comparison
    • Hsu, L. C., Chang, W. C., Yoshida, A. (1997). Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene structure comparison. Gene 189(1):89-94.
    • (1997) Gene , vol.189 , Issue.1 , pp. 89-94
    • Hsu, L.C.1    Chang, W.C.2    Yoshida, A.3
  • 44
    • 0034092174 scopus 로고    scopus 로고
    • Human cytochrome P450 (CYP) genes: Recommendations for the nomenclature of alleles
    • Ingelman-Sundberg, M., Daly, A. K., Oscarson, M., Nebert, D. W. (2000). Human cytochrome P450 (CYP) genes: recommendations for the nomenclature of alleles. Pharmacogenetics 10(1):91-93.
    • (2000) Pharmacogenetics , vol.10 , Issue.1 , pp. 91-93
    • Ingelman-Sundberg, M.1    Daly, A.K.2    Oscarson, M.3    Nebert, D.W.4
  • 47
    • 0034940179 scopus 로고    scopus 로고
    • The potential mechanism for glutamine-induced collagen biosynthesis in cultured human skin fibroblasts
    • Kama, E., Miltyk, W., Wolczynski, S., Palka, J. A. (2001). The potential mechanism for glutamine-induced collagen biosynthesis in cultured human skin fibroblasts. Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 130(1):23-32.
    • (2001) Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. , vol.130 , Issue.1 , pp. 23-32
    • Kama, E.1    Miltyk, W.2    Wolczynski, S.3    Palka, J.A.4
  • 48
    • 0030936743 scopus 로고    scopus 로고
    • Human liver fatty aldehyde dehydrogenase: Microsomal localization, purification, and biochemical characterization
    • Kelson, T. L., Secor, M. Jr., Rizzo, W. B. (1997). Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization. Biochim. Biophys. Acta 1335(1-2):99-110.
    • (1997) Biochim. Biophys. Acta , vol.1335 , Issue.1-2 , pp. 99-110
    • Kelson, T.L.1    Secor Jr., M.2    Rizzo, W.B.3
  • 49
    • 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
    • Krupenko, S. A., Oleinik, N. V. (2002). 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(5):227-236.
    • (2002) Cell Growth Differ. , vol.13 , Issue.5 , pp. 227-236
    • Krupenko, S.A.1    Oleinik, N.V.2
  • 50
    • 0030942262 scopus 로고    scopus 로고
    • Domain structure of rat 10-formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase
    • Krupenko, S. A., Wagner, C., Cook, R. J. (1997). Domain structure of rat 10-formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase. J. Biol. Chem. 272(15):10273-10278.
    • (1997) J. Biol. Chem. , vol.272 , Issue.15 , pp. 10273-10278
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 51
    • 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
    • Lin, M., Napoli, J. L. (2000). 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(51):40106-40112.
    • (2000) J. Biol. Chem. , vol.275 , Issue.51 , pp. 40106-40112
    • Lin, M.1    Napoli, J.L.2
  • 52
    • 0037646508 scopus 로고    scopus 로고
    • Mouse retinal dehydrogenase 4 (RALDH4), molecular cloning, cellular expression, and activity in 9-cis-retinoic acid biosynthesis in intact cells
    • Lin, M., Zhang, M., Abraham, M., Smith, S. M., Napoli, J. L. (2003). Mouse retinal dehydrogenase 4 (RALDH4), molecular cloning, cellular expression, and activity in 9-cis-retinoic acid biosynthesis in intact cells. J. Biol. Chem. 278(11):9856-9861.
    • (2003) J. Biol. Chem. , vol.278 , Issue.11 , pp. 9856-9861
    • Lin, M.1    Zhang, M.2    Abraham, M.3    Smith, S.M.4    Napoli, J.L.5
  • 53
    • 0012869069 scopus 로고    scopus 로고
    • Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA
    • Manzer, R., Qamar, L., Estey, T., Pappa, A., Petersen, D. R., Vasiliou, V. (2003). Molecular cloning and baculovirus expression of the rabbit corneal aldehyde dehydrogenase (ALDH1A1) cDNA. DNA Cell Biol. 22(5):329-338.
    • (2003) DNA Cell Biol. , vol.22 , Issue.5 , pp. 329-338
    • Manzer, R.1    Qamar, L.2    Estey, T.3    Pappa, A.4    Petersen, D.R.5    Vasiliou, V.6
  • 54
    • 0034700139 scopus 로고    scopus 로고
    • Differential gene expression in p53-mediated apoptosis-resistant vs. apoptosis-sensitive tumor cell lines
    • Maxwell, S. A., Davis, G. E. (2000). Differential gene expression in p53-mediated apoptosis-resistant vs. apoptosis-sensitive tumor cell lines. Proc. Natl. Acad. Sci. U. S. A. 97(24):13009-13014.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.24 , pp. 13009-13014
    • Maxwell, S.A.1    Davis, G.E.2
  • 55
    • 0034019794 scopus 로고    scopus 로고
    • Potential role of pyrroline 5-carboxylate in regulation of collagen biosynthesis in cultured human skin fibroblasts
    • Miltyk, W., Palka, J. A. (2000). Potential role of pyrroline 5-carboxylate in regulation of collagen biosynthesis in cultured human skin fibroblasts. Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 125(2):265-271.
    • (2000) Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. , vol.125 , Issue.2 , pp. 265-271
    • Miltyk, W.1    Palka, J.A.2
  • 56
    • 0023090971 scopus 로고
    • The oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases
    • Mitchell, D. Y., Petersen, D. R. (1987). The oxidation of alpha-beta unsaturated aldehydic products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol. Appl. Pharmacol. 87(3):403-410.
    • (1987) Toxicol. Appl. Pharmacol. , vol.87 , Issue.3 , pp. 403-410
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 57
    • 0037627824 scopus 로고    scopus 로고
    • Oxidation of 4-hydroxy-2-nonenal by succinic semialdehyde dehydrogenase (ALDH5A)
    • Murphy, T. C., Amarnath, V., Gibson, K. M., Picklo, M. J. Sr. (2003). Oxidation of 4-hydroxy-2-nonenal by succinic semialdehyde dehydrogenase (ALDH5A). J. Neurochem. 86(2):298-305.
    • (2003) J. Neurochem. , vol.86 , Issue.2 , pp. 298-305
    • Murphy, T.C.1    Amarnath, V.2    Gibson, K.M.3    Picklo Sr., M.J.4
  • 58
    • 0033915067 scopus 로고    scopus 로고
    • Association of aldehyde dehydrogenase 2 gene polymorphism with multiple oesophageal dysplasia in head and neck cancer patients
    • Muto, M., Hitorni, Y., Ohtsu, A., Ebihara, S., Yoshida, S., Esumi, H. (2000). Association of aldehyde dehydrogenase 2 gene polymorphism with multiple oesophageal dysplasia in head and neck cancer patients. Gut 47(2):256-261.
    • (2000) Gut , vol.47 , Issue.2 , pp. 256-261
    • Muto, M.1    Hitorni, Y.2    Ohtsu, A.3    Ebihara, S.4    Yoshida, S.5    Esumi, H.6
  • 59
    • 0031080555 scopus 로고    scopus 로고
    • Restricted expression and retinoic acid-induced downregulation of the retinaldehyde dehydrogenase type 2 (RALDH-2) gene during mouse development
    • Niederreither, K., McCaffery, P., Drager, U. C., Chambon, P., Dolle, P. (1997). Restricted expression and retinoic acid-induced downregulation of the retinaldehyde dehydrogenase type 2 (RALDH-2) gene during mouse development. Mech. Dev. 62(1):67-78.
    • (1997) Mech. Dev. , vol.62 , Issue.1 , pp. 67-78
    • Niederreither, K.1    McCaffery, P.2    Drager, U.C.3    Chambon, P.4    Dolle, P.5
  • 60
    • 0032958632 scopus 로고    scopus 로고
    • Embryonic retinoic acid synthesis is essential for early mouse post-implantation development
    • Niederreither, K., Subbarayan, V., Dolle, P., Chambon, P. (1999). Embryonic retinoic acid synthesis is essential for early mouse post-implantation development. Nat. Genet. 21(4):444-448.
    • (1999) Nat. Genet. , vol.21 , Issue.4 , pp. 444-448
    • Niederreither, K.1    Subbarayan, V.2    Dolle, P.3    Chambon, P.4
  • 61
    • 0033963641 scopus 로고    scopus 로고
    • Retinoic acid synthesis and hindbrain patterning in the mouse embryo
    • Niederreither, K., Vermot, J., Schuhbaur, B., Chambon, P., Dolle, P. (2000). Retinoic acid synthesis and hindbrain patterning in the mouse embryo. Development 127 (1):75-85.
    • (2000) Development , vol.127 , Issue.1 , pp. 75-85
    • Niederreither, K.1    Vermot, J.2    Schuhbaur, B.3    Chambon, P.4    Dolle, P.5
  • 62
    • 0036182385 scopus 로고    scopus 로고
    • Different blood acetaldehyde concentration following ethanol administration in a newly developed high alcohol preference and low alcohol preference rat model system
    • Nishiguchi, M., Kinoshita, H., Mostofa, J., Taniguchi, T., Ouchi, H., Minami, T., Hatake, K., Utsumi, T., Motomura, H., Hishida, S. (2002). Different blood acetaldehyde concentration following ethanol administration in a newly developed high alcohol preference and low alcohol preference rat model system. Alcohol Alcohol. 37 (1):9-12.
    • (2002) Alcohol Alcohol. , vol.37 , Issue.1 , pp. 9-12
    • Nishiguchi, M.1    Kinoshita, H.2    Mostofa, J.3    Taniguchi, T.4    Ouchi, H.5    Minami, T.6    Hatake, K.7    Utsumi, T.8    Motomura, H.9    Hishida, S.10
  • 63
    • 0037342862 scopus 로고    scopus 로고
    • Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells
    • Ohsawa, I., Nishimaki, K., Yasuda, C., Kamino, K., Ohta, S. (2003). Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells. J. Neurochem. 84(5):1110-1117.
    • (2003) J. Neurochem. , vol.84 , Issue.5 , pp. 1110-1117
    • Ohsawa, I.1    Nishimaki, K.2    Yasuda, C.3    Kamino, K.4    Ohta, S.5
  • 64
    • 0034436476 scopus 로고    scopus 로고
    • Roles of mitochondrial dysfunctions in Alzheimer's disease-contribution of deficiency of ALDH 2
    • Ohta, S. (2000). Roles of mitochondrial dysfunctions in Alzheimer's disease-contribution of deficiency of ALDH 2. Rinsho Shinkeigaku 40(12):1231-1233.
    • (2000) Rinsho Shinkeigaku , vol.40 , Issue.12 , pp. 1231-1233
    • Ohta, S.1
  • 65
    • 0037795789 scopus 로고    scopus 로고
    • Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in a549 cells induces g(1) cell cycle arrest and apoptosis
    • Oleinik, N. V., Krupenko, S. A. (2003). Ectopic expression of 10-formyltetrahydrofolate dehydrogenase in a549 cells induces g(1) cell cycle arrest and apoptosis. Mol. Cancer Res. 1(8):577-588.
    • (2003) Mol. Cancer Res. , vol.1 , Issue.8 , pp. 577-588
    • Oleinik, N.V.1    Krupenko, S.A.2
  • 66
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): Biochemical characterization and immunohistochemical localization in the cornea
    • Pappa, A., Estey, T., Manzer, R., Brown, D., Vasiliou, V. (2003a). Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea. Biochem. J. 376(Pt. 3):615-623.
    • (2003) Biochem. J. , vol.376 , Issue.PART 3 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 67
    • 0037403026 scopus 로고    scopus 로고
    • Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage
    • Pappa, A., Chen, C., Koutalos, Y., Townsend, A. J., Vasiliou, V. (2003b). Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage. Free Radic. Biol. Med. 34(9):1178-1189.
    • (2003) Free Radic. Biol. Med. , vol.34 , Issue.9 , pp. 1178-1189
    • Pappa, A.1    Chen, C.2    Koutalos, Y.3    Townsend, A.J.4    Vasiliou, V.5
  • 68
    • 0027304401 scopus 로고
    • NADPH-dependent enzyme-catalyzed reduction of aldophosphamide, the pivotal metabolite of cyclophosphamide
    • Parekh, H. K., Sladek, N. E. (1993). NADPH-dependent enzyme-catalyzed reduction of aldophosphamide, the pivotal metabolite of cyclophosphamide. Biochem. Pharmacol. 46(6):1043-1052.
    • (1993) Biochem. Pharmacol. , vol.46 , Issue.6 , pp. 1043-1052
    • Parekh, H.K.1    Sladek, N.E.2
  • 70
    • 0034944147 scopus 로고    scopus 로고
    • Expression and activities of aldo-keto oxidoreductases in Alzheimer disease
    • Picklo, M. J., Olson, S. J., Markesbery, W. R., Montine, T. J. (2001). Expression and activities of aldo-keto oxidoreductases in Alzheimer disease. J. Neuropathol. Exp. Neurol. 60(7):686-695.
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , Issue.7 , pp. 686-695
    • Picklo, M.J.1    Olson, S.J.2    Markesbery, W.R.3    Montine, T.J.4
  • 71
    • 0034721584 scopus 로고    scopus 로고
    • Characterization of 4-hydroxy-2-nonenal metabolism in stellate cell lines derived from normal and cirrhotic rat liver
    • Reichard, J. F., Vasiliou, V., Petersen, D. R. (2000). Characterization of 4-hydroxy-2-nonenal metabolism in stellate cell lines derived from normal and cirrhotic rat liver. Biochim. Biophys. Acta 1487(2-3):222-232.
    • (2000) Biochim. Biophys. Acta , vol.1487 , Issue.2-3 , pp. 222-232
    • Reichard, J.F.1    Vasiliou, V.2    Petersen, D.R.3
  • 72
    • 0032519652 scopus 로고    scopus 로고
    • Inhibition of human class 3 aldehyde dehydrogenase, and sensitization of tumor cells that express significant amounts of this enzyme to oxazaphosphorines, by chlorpropamide analogues
    • Rekha, G. K., Devaraj, V. R., Sreerama, L., Lee, M. J., Nagasawa, H. T., Sladek, N. E. (1998). Inhibition of human class 3 aldehyde dehydrogenase, and sensitization of tumor cells that express significant amounts of this enzyme to oxazaphosphorines, by chlorpropamide analogues. Biochem. Pharmacol. 55(4):465-474.
    • (1998) Biochem. Pharmacol. , vol.55 , Issue.4 , pp. 465-474
    • Rekha, G.K.1    Devaraj, V.R.2    Sreerama, L.3    Lee, M.J.4    Nagasawa, H.T.5    Sladek, N.E.6
  • 73
    • 0030799414 scopus 로고    scopus 로고
    • Oxidation of cyclophosphamide to 4-hydroxycyclophosphamide and deschloroethylcyclophosphamide in human liver microsomes
    • Ren, S., Yang, J. S., Kalhorn, T. F., Slattery, J. T. (1997). Oxidation of cyclophosphamide to 4-hydroxycyclophosphamide and deschloroethylcyclophosphamide in human liver microsomes. Cancer Res. 57(19):4229-4235.
    • (1997) Cancer Res. , vol.57 , Issue.19 , pp. 4229-4235
    • Ren, S.1    Yang, J.S.2    Kalhorn, T.F.3    Slattery, J.T.4
  • 74
    • 0038265173 scopus 로고    scopus 로고
    • Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains
    • Reuland, S. N., Vlasov, A. P., Krupenko, S. A. (2003). Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains. J. Biol. Chem. 278 (25):22894-22900.
    • (2003) J. Biol. Chem. , vol.278 , Issue.25 , pp. 22894-22900
    • Reuland, S.N.1    Vlasov, A.P.2    Krupenko, S.A.3
  • 75
    • 0033233482 scopus 로고    scopus 로고
    • The molecular basis of Sjögren-Larsson syndrome: Mutation analysis of the fatty aldehyde dehydrogenase gene
    • Rizzo, W. B., Carney, G., Liu, Z. (1999). The molecular basis of Sjögren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Am. J. Hum. Genet. 65(6):1547-1560.
    • (1999) Am. J. Hum. Genet. , vol.65 , Issue.6 , pp. 1547-1560
    • Rizzo, W.B.1    Carney, G.2    Liu, Z.3
  • 76
    • 0031737815 scopus 로고    scopus 로고
    • Methylmalonic semialdehyde dehydrogenase deficiency: Psychomotor delay and methylmalonic aciduria without metabolic decompensation
    • Roe, C. R., Struys, E., Kok, R. M., Roe, D. S., Harris, R. A., Jakobs, C. (1998). Methylmalonic semialdehyde dehydrogenase deficiency: psychomotor delay and methylmalonic aciduria without metabolic decompensation. Mol. Genet. Metab. 65 (1):35-43.
    • (1998) Mol. Genet. Metab. , vol.65 , Issue.1 , pp. 35-43
    • Roe, C.R.1    Struys, E.2    Kok, R.M.3    Roe, D.S.4    Harris, R.A.5    Jakobs, C.6
  • 77
    • 0037865228 scopus 로고    scopus 로고
    • Do the ethanol metabolizing enzymes modify the relationship between alcohol consumption and blood pressure?
    • Saito, K., Yokoyama, T., Yoshiike, N., Date, C., Yamamoto, A., Muramatsu, M., Tanaka, H. (2003). Do the ethanol metabolizing enzymes modify the relationship between alcohol consumption and blood pressure? J. Hypertens. 21(6):1097-1105.
    • (2003) J. Hypertens. , vol.21 , Issue.6 , pp. 1097-1105
    • Saito, K.1    Yokoyama, T.2    Yoshiike, N.3    Date, C.4    Yamamoto, A.5    Muramatsu, M.6    Tanaka, H.7
  • 78
    • 0035003439 scopus 로고    scopus 로고
    • Chemistry and biochemistry of oxidative stress in neurodegenerative disease
    • Sayre, L. M., Smith, M. A., Perry, G. (2001). Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr. Med. Chem. 8(7):721-738.
    • (2001) Curr. Med. Chem. , vol.8 , Issue.7 , pp. 721-738
    • Sayre, L.M.1    Smith, M.A.2    Perry, G.3
  • 79
    • 0019920815 scopus 로고
    • Metabolism of malonaldehyde in vivo and in vitro
    • Siu, G. M., Draper, H. H. (1982). Metabolism of malonaldehyde in vivo and in vitro. Lipids 17(5):349-355.
    • (1982) Lipids , vol.17 , Issue.5 , pp. 349-355
    • Siu, G.M.1    Draper, H.H.2
  • 80
    • 0031467111 scopus 로고    scopus 로고
    • An ancient conserved gene expressed in the human inner ear: Identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1)
    • Skvorak, A. B., Robertson, N. G., Yin, Y., Weremowicz, S., Her, H., Bieber, F. R., Beisel, K. W., Lynch, E. D., Beier, D. R., Morton, C. C. (1997). An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics 46(2):191-199.
    • (1997) Genomics , vol.46 , Issue.2 , pp. 191-199
    • Skvorak, A.B.1    Robertson, N.G.2    Yin, Y.3    Weremowicz, S.4    Her, H.5    Bieber, F.R.6    Beisel, K.W.7    Lynch, E.D.8    Beier, D.R.9    Morton, C.C.10
  • 81
    • 0032873333 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines
    • Sladek, N. E. (1999). Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines. Curr. Pharm. Des. 5(8):607-625.
    • (1999) Curr. Pharm. Des. , vol.5 , Issue.8 , pp. 607-625
    • Sladek, N.E.1
  • 82
    • 17744419979 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily: The 2002 update
    • Sophos, N. A., Vasiliou, V. (2003). Aldehyde dehydrogenase gene superfamily: the 2002 update. Chem. Biol. Interact. 143-144:5-22.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 5-22
    • Sophos, N.A.1    Vasiliou, V.2
  • 83
    • 0035969855 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily: The 2000 update
    • Sophos, N. A., Pappa, A., Ziegler, T. L., Vasiliou, V. (2001). Aldehyde dehydrogenase gene superfamily: the 2000 update. Chem. Biol. Interact. 130-132(1-3):323-337.
    • (2001) Chem. Biol. Interact. , vol.130-132 , Issue.1-3 , pp. 323-337
    • Sophos, N.A.1    Pappa, A.2    Ziegler, T.L.3    Vasiliou, V.4
  • 85
    • 0028946528 scopus 로고
    • Phenolic antioxidant-induced overexpression of class-3 aldehyde dehydrogenase and oxazaphosphorine-specific resistance
    • Sreerama, L., Rekha, G. K., Sladek, N. E. (1995). Phenolic antioxidant-induced overexpression of class-3 aldehyde dehydrogenase and oxazaphosphorine-specific resistance. Biochem. Pharmacol. 49(5):669-675.
    • (1995) Biochem. Pharmacol. , vol.49 , Issue.5 , pp. 669-675
    • Sreerama, L.1    Rekha, G.K.2    Sladek, N.E.3
  • 86
    • 0029073223 scopus 로고
    • The novel aldehyde dehydrogenase gene, ALDH5, encodes an active aldehyde dehydrogenase enzyme
    • Stewart, M. J., Malek, K., Xiao, Q., Dipple, K. M., Crabb, D. W. (1995). The novel aldehyde dehydrogenase gene, ALDH5, encodes an active aldehyde dehydrogenase enzyme. Biochem. Biophys. Res. Commun. 211(1):144-151.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , Issue.1 , pp. 144-151
    • Stewart, M.J.1    Malek, K.2    Xiao, Q.3    Dipple, K.M.4    Crabb, D.W.5
  • 87
    • 0032714961 scopus 로고    scopus 로고
    • Complementary domains of retinoic acid production and degradation in the early chick embryol
    • Swindell, E. C., Thaller, C., Sockanathan, S., Petkovich, M., Jessell, T. M., Eichele, G. (1999). Complementary domains of retinoic acid production and degradation in the early chick embryol. Dev. Biol. 216(1):282-296.
    • (1999) Dev. Biol. , vol.216 , Issue.1 , pp. 282-296
    • Swindell, E.C.1    Thaller, C.2    Sockanathan, S.3    Petkovich, M.4    Jessell, T.M.5    Eichele, G.6
  • 88
    • 0037051878 scopus 로고    scopus 로고
    • First purification of the antiquitin protein and demonstration of its enzymatic activity
    • Tang, W. K., Cheng, C. H., Fong, W. P. (2002). First purification of the antiquitin protein and demonstration of its enzymatic activity. FEBS Lett. 516(1-3):183-186.
    • (2002) FEBS Lett. , vol.516 , Issue.1-3 , pp. 183-186
    • Tang, W.K.1    Cheng, C.H.2    Fong, W.P.3
  • 89
    • 0348049466 scopus 로고    scopus 로고
    • Identification of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions
    • Thukkani, A. K., McHowat, J., Hsu, F. F., Brennan, M. L., Hazen, S. L., Ford, D. A. (2003). Identification of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions. Circulation 108(25):3128-3133.
    • (2003) Circulation , vol.108 , Issue.25 , pp. 3128-3133
    • Thukkani, A.K.1    McHowat, J.2    Hsu, F.F.3    Brennan, M.L.4    Hazen, S.L.5    Ford, D.A.6
  • 90
    • 0035670811 scopus 로고    scopus 로고
    • Plasma malondialdehyde and nitric oxide levels in age related macular degeneration
    • Totan, Y., Cekic, O., Borazan, M., Uz, E., Sogut, S., Akyol, O. (2001). Plasma malondialdehyde and nitric oxide levels in age related macular degeneration. Br. J. Ophthalmol. 85(12):1426-1428.
    • (2001) Br. J. Ophthalmol. , vol.85 , Issue.12 , pp. 1426-1428
    • Totan, Y.1    Cekic, O.2    Borazan, M.3    Uz, E.4    Sogut, S.5    Akyol, O.6
  • 91
    • 0035969833 scopus 로고    scopus 로고
    • Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells
    • Townsend, A. J., Leone-Kabler, S., Haynes, R. L., Wu, Y., Szweda, L., Bunting, K. D. (2001). Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells. Chem. Biol. Interact. 130-132(1-3):261-273.
    • (2001) Chem. Biol. Interact. , vol.130-132 , Issue.1-3 , 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
  • 94
    • 0027828378 scopus 로고
    • Role of the aldehyde dehydrogenase-1 isozyme in the metabolism of acetaldehyde
    • Ueshima, Y., Matsuda, Y., Tsutsumi, M., Takada, A. (1993). Role of the aldehyde dehydrogenase-1 isozyme in the metabolism of acetaldehyde. Alcohol Alcohol., Suppl. 1B:15-19.
    • (1993) Alcohol Alcohol., Suppl. , vol.1 B , pp. 15-19
    • Ueshima, Y.1    Matsuda, Y.2    Tsutsumi, M.3    Takada, A.4
  • 95
    • 0017136450 scopus 로고
    • Type II hyperprolinemia. Delta1-pyrroline-5-carboxylic acid dehydrogenase deficiency in cultured skin fibroblasts and circulating lymphocytes
    • Valle, D., Goodman, S. I., Applegarth, D. A., Shih, V. E., Phang, J. M. (1976). Type II hyperprolinemia. Delta1-pyrroline-5-carboxylic acid dehydrogenase deficiency in cultured skin fibroblasts and circulating lymphocytes. J. Clin. Invest. 58(3):598-603.
    • (1976) J. Clin. Invest. , vol.58 , Issue.3 , pp. 598-603
    • Valle, D.1    Goodman, S.I.2    Applegarth, D.A.3    Shih, V.E.4    Phang, J.M.5
  • 96
    • 0033824324 scopus 로고    scopus 로고
    • Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease
    • Vasiliou, V., Pappa, A. (2000). Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease. Pharmacology 61(3):192-198.
    • (2000) Pharmacology , vol.61 , Issue.3 , pp. 192-198
    • Vasiliou, V.1    Pappa, A.2
  • 97
    • 0026783747 scopus 로고
    • Negative regulation of the murine cytosolic aldehyde dehydrogenase-3 (Aldh-3c) gene by functional CYP1A1 and CYP1A2 proteins
    • Vasiliou, V., Puga, A., Nebert, D. W. (1992). Negative regulation of the murine cytosolic aldehyde dehydrogenase-3 (Aldh-3c) gene by functional CYP1A1 and CYP1A2 proteins. Biochem. Biophys. Res. Commun. 187(1):413-419.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , Issue.1 , pp. 413-419
    • Vasiliou, V.1    Puga, A.2    Nebert, D.W.3
  • 98
    • 0029623125 scopus 로고
    • Response of [Ah] battery genes to compounds that protect against menadione toxicity
    • Vasiliou, V., Shertzer, H. G., Liu, R. M., Sainsbury, M., Nebert, D. W. (1995). Response of [Ah] battery genes to compounds that protect against menadione toxicity. Biochem. Pharmacol. 50(11):1885-1891.
    • (1995) Biochem. Pharmacol. , vol.50 , Issue.11 , pp. 1885-1891
    • Vasiliou, V.1    Shertzer, H.G.2    Liu, R.M.3    Sainsbury, M.4    Nebert, D.W.5
  • 99
    • 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, K. F., Nebert, D. W. (1999). Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping. Pharmacogenetics 9(4):421-434.
    • (1999) Pharmacogenetics , vol.9 , Issue.4 , pp. 421-434
    • Vasiliou, V.1    Bairoch, A.2    Tipton, K.F.3    Nebert, D.W.4
  • 100
    • 0034534311 scopus 로고    scopus 로고
    • Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism
    • Vasiliou, V., Pappa, A., Petersen, D. R. (2000). Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chem. Biol. Interact. 129(1-2):1-19.
    • (2000) Chem. Biol. Interact. , vol.129 , Issue.1-2 , pp. 1-19
    • Vasiliou, V.1    Pappa, A.2    Petersen, D.R.3
  • 101
    • 0034629439 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of rat gamma- trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in camitine biosynthesis
    • Vaz, F. M., Fouchier, S. W., Ofman, R., Sommer, M., Wanders, R. J. (2000). Molecular and biochemical characterization of rat gamma- trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in camitine biosynthesis. J. Biol. Chem. 275(10):7390-7394.
    • (2000) J. Biol. Chem. , vol.275 , Issue.10 , pp. 7390-7394
    • Vaz, F.M.1    Fouchier, S.W.2    Ofman, R.3    Sommer, M.4    Wanders, R.J.5
  • 102
    • 0037452691 scopus 로고    scopus 로고
    • Decreased embryonic retinoic acid synthesis results in a DiGeorge syndrome phenotype in newborn mice
    • Vermot, J., Niederreither, K., Garnier, J. M., Chambon, P., Dolle, P. (2003). Decreased embryonic retinoic acid synthesis results in a DiGeorge syndrome phenotype in newborn mice. Proc. Natl. Acad. Sci. U. S. A. 100(4):1763-1768.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , Issue.4 , pp. 1763-1768
    • Vermot, J.1    Niederreither, K.2    Garnier, J.M.3    Chambon, P.4    Dolle, P.5
  • 103
    • 0030062208 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate
    • Wang, X., Penzes, P., Napoli, J. L. (1996). Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate. J. Biol. Chem. 271(27):16288-16293.
    • (1996) J. Biol. Chem. , vol.271 , Issue.27 , pp. 16288-16293
    • Wang, X.1    Penzes, P.2    Napoli, J.L.3
  • 106
    • 0028128943 scopus 로고
    • The oxidation hypothesis of atherosclerosis
    • Witztum, J. L. (1994). The oxidation hypothesis of atherosclerosis. Lancet 344(8925): 793-795.
    • (1994) Lancet , vol.344 , Issue.8925 , pp. 793-795
    • Witztum, J.L.1
  • 107
    • 0033617797 scopus 로고    scopus 로고
    • A novel calmodulin-like protein gene in rice which has an unusual prolonged C-terminal sequence carrying a putative prenylation site
    • Xiao, C., Xin, H., Dong, A., Sun, C., Cao, K. (1999). A novel calmodulin-like protein gene in rice which has an unusual prolonged C-terminal sequence carrying a putative prenylation site. DNA Res. 6(3):179-181.
    • (1999) DNA Res. , vol.6 , Issue.3 , pp. 179-181
    • Xiao, C.1    Xin, H.2    Dong, A.3    Sun, C.4    Cao, K.5
  • 108
    • 0035985011 scopus 로고    scopus 로고
    • Genetic differences in ethanol metabolizing enzymes and blood pressure in Japanese alcohol consumers
    • Yamada, Y., Sun, F., Tsuritani, I., Honda, R. (2002). Genetic differences in ethanol metabolizing enzymes and blood pressure in Japanese alcohol consumers. J. Hum. Hypertens. 16(7):479-486.
    • (2002) J. Hum. Hypertens. , vol.16 , Issue.7 , pp. 479-486
    • Yamada, Y.1    Sun, F.2    Tsuritani, I.3    Honda, R.4
  • 109
    • 0021333231 scopus 로고
    • The effect of pyrroline-5-carboxylic acid on nucleotide metabolism in erythrocytes from normal and glucose-6-phosphate dehydrogenase-deficient subjects
    • Yeh, G. C., Roth, E. F. Jr., Phang, J. M., Harris, S. C., Nagel, R. L., Rinaldi, A. (1984). The effect of pyrroline-5-carboxylic acid on nucleotide metabolism in erythrocytes from normal and glucose-6-phosphate dehydrogenase-deficient subjects. J. Biol. Chem. 259(9):5454-5458.
    • (1984) J. Biol. Chem. , vol.259 , Issue.9 , pp. 5454-5458
    • Yeh, G.C.1    Roth Jr., E.F.2    Phang, J.M.3    Harris, S.C.4    Nagel, R.L.5    Rinaldi, A.6
  • 110
    • 0035757115 scopus 로고    scopus 로고
    • Alcohol and oropharyngolaryngeal and digestive tract cancer
    • Yokoyama, A., Omori, T. (2001). Alcohol and oropharyngolaryngeal and digestive tract cancer. Nihon Arukoru, Yakubutsu Igakkai Zasshi 36(6):551-566.
    • (2001) Nihon Arukoru, Yakubutsu Igakkai Zasshi , vol.36 , Issue.6 , pp. 551-566
    • Yokoyama, A.1    Omori, T.2
  • 114
    • 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., Maruyama, K., Ishii, H. (2001). Alcohol and aldehyde dehydrogenase gene polymorphisms and oropharyngolaryngeal, esophageal and stomach cancers in Japanese alcoholics. Carcinogenesis 22(3):433-439.
    • (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
  • 115
    • 0026907527 scopus 로고
    • Molecular genetics of human aldehyde dehydrogenase
    • Yoshida, A. (1992). Molecular genetics of human aldehyde dehydrogenase. Pharmacogenetics 2(4):139-147.
    • (1992) Pharmacogenetics , vol.2 , Issue.4 , pp. 139-147
    • Yoshida, A.1
  • 116
    • 0011830097 scopus 로고
    • Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals
    • Yoshida, A., Huang, I. Y., Ikawa, M. (1984). Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc. Natl. Acad. Sci. U. S. A. 81(1):258-261.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , Issue.1 , pp. 258-261
    • Yoshida, A.1    Huang, I.Y.2    Ikawa, M.3
  • 117
    • 0033282003 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily. The 1998 update
    • Ziegler, T. L., Vasiliou, V. (1999). Aldehyde dehydrogenase gene superfamily. The 1998 update. Adv. Exp. Med. Biol. 463:255-263.
    • (1999) Adv. Exp. Med. Biol. , vol.463 , pp. 255-263
    • Ziegler, T.L.1    Vasiliou, V.2


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