메뉴 건너뛰기




Volumn 191, Issue 1-3, 2011, Pages 296-302

Drosophila lacking a homologue of mammalian ALDH2 have multiple fitness defects

Author keywords

Aldehyde dehydrogenase; Balancer equilibrium method; Drosophila; Protein carbonylation; Stress resistance

Indexed keywords

ALDEHYDE DEHYDROGENASE; CARBONYL DERIVATIVE;

EID: 79957566568     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.01.031     Document Type: Conference Paper
Times cited : (8)

References (30)
  • 1
    • 0017253860 scopus 로고
    • Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes
    • J. Eckfeldt, L. Mope, K. Takio, T. Yonetani, Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes, J. Biol. Chem. 251 (1976) 236-240.
    • (1976) J. Biol. Chem. , vol.251 , pp. 236-240
    • Eckfeldt, J.1    Mope, L.2    Takio, K.3    Yonetani, T.4
  • 2
    • 0017406798 scopus 로고
    • Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes
    • N.J. Greenfield, R. Pietruszko, Two aldehyde dehydrogenases from human liver. Isolation via affinity chromatography and characterization of the isozymes, Biochim. Biophys. Acta 483 (1977) 35-45. (Pubitemid 8118045)
    • (1977) Biochimica et Biophysica Acta , vol.483 , Issue.1 , pp. 35-45
    • Greenfield, N.J.1    Pietruszko, R.2
  • 4
    • 33646744136 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase is essential for both adult and larval ethanol resistance in Drosophila melanogaster
    • J.D. Fry, M. Saweikis, Aldehyde dehydrogenase is essential for both adult and larval ethanol resistance in Drosophila melanogaster, Genet. Res. 87 (2006) 87-92.
    • (2006) Genet. Res. , vol.87 , pp. 87-92
    • Fry, J.D.1    Saweikis, M.2
  • 6
    • 17744419979 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily: The 2002 update
    • DOI 10.1016/S0009-2797(02)00163-1, PII S0009279702001631
    • N.A. Sophos, V. Vasiliou, Aldehyde dehydrogenase gene superfamily: the 2002 update, Chem. Biol. Interact. 143-144 (2003) 5-22. (Pubitemid 36253575)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 5-22
    • Sophos, N.A.1    Vasiliou, V.2
  • 8
    • 0037342862 scopus 로고    scopus 로고
    • Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells
    • DOI 10.1046/j.1471-4159.2003.01619.x
    • I. Ohsawa, K. Nishimaki, C. Yasuda, K. Kamino, S. Ohta, Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells, J. Neurochem. 84 (2003) 1110-1117. (Pubitemid 36330663)
    • (2003) Journal of Neurochemistry , vol.84 , Issue.5 , pp. 1110-1117
    • Ohsawa, I.1    Nishimaki, K.2    Yasuda, C.3    Kamino, K.4    Ohta, S.5
  • 9
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • DOI 10.1074/jbc.272.33.20313
    • B.S. Berlett, E.R. Stadtman, Protein oxidation in aging, disease, and oxidative stress, J. Biol. Chem. 272 (1997) 20313-20316. (Pubitemid 27355575)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 10
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, 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
  • 11
    • 0032512411 scopus 로고    scopus 로고
    • Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2- Nonenal
    • DOI 10.1021/bi971958i
    • K.M. Humphries, Y. Yoo, L.I. Szweda, Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal, Biochemistry 37 (1998) 552-557. (Pubitemid 28123787)
    • (1998) Biochemistry , vol.37 , Issue.2 , pp. 552-557
    • Humphries, K.M.1    Yoo, Y.2    Szweda, L.I.3
  • 12
    • 0037172778 scopus 로고    scopus 로고
    • Identification of bovine heart cytochrome c oxidase subunits modified by the lipid peroxidation product 4-hydroxy-2-nonenal
    • DOI 10.1021/bi025896u
    • A. Musatov, C.A. Carroll, Y.C. Liu, G.I. Henderson, S.T. Weintraub, N.C. Robinson, Identification of bovine heart cytochrome c oxidase subunits modified by the lipid peroxidation product 4-hydroxy-2-nonenal, Biochemistry 41 (2002) 8212-8220. (Pubitemid 34655190)
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8212-8220
    • Musatov, A.1    Carroll, C.A.2    Liu, Y.-C.3    Henderson, G.I.4    Weintraub, S.T.5    Robinson, N.C.6
  • 13
    • 40849145511 scopus 로고    scopus 로고
    • The association of mitochondrial aldehyde dehydrogenase gene (ALDH2) polymorphism with susceptibility to late-onset Alzheimer's disease in Chinese
    • B. Wang, J. Wang, S. Zhou, S. Tan, X. He, Z. Yang, Y.C. Xie, S. Li, C. Zheng, X. Ma, The association of mitochondrial aldehyde dehydrogenase gene (ALDH2) polymorphism with susceptibility to late-onset Alzheimer's disease in Chinese, J. Neurol. Sci. 268 (2008) 172-175.
    • (2008) J. Neurol. Sci. , vol.268 , pp. 172-175
    • Wang, B.1    Wang, J.2    Zhou, S.3    Tan, S.4    He, X.5    Yang, Z.6    Xie, Y.C.7    Li, S.8    Zheng, C.9    Ma, X.10
  • 15
    • 0014846296 scopus 로고
    • A population cage test for heterosis in Drosophila pseudoobscura
    • J.A. Sved, F.J. Ayala, A population cage test for heterosis in Drosophila pseudoobscura, Genetics 66 (1970) 97-113.
    • (1970) Genetics , vol.66 , pp. 97-113
    • Sved, J.A.1    Ayala, F.J.2
  • 16
    • 0015101254 scopus 로고
    • An estimate of heterosis in Drosophila melanogaster
    • J.A. Sved, An estimate of heterosis in Drosophila melanogaster, Genet. Res. 18 (1971) 97-105.
    • (1971) Genet. Res. , vol.18 , pp. 97-105
    • Sved, J.A.1
  • 18
    • 0035055060 scopus 로고    scopus 로고
    • Direct and correlated responses to selection for larval ethanol tolerance in Drosophila melanogaster
    • J.D. Fry, Direct and correlated responses to selection for larval ethanol tolerance in Drosophila melanogaster, J. Evol. Biol. 14 (2001) 296-309.
    • (2001) J. Evol. Biol. , vol.14 , pp. 296-309
    • Fry, J.D.1
  • 19
    • 1442311568 scopus 로고    scopus 로고
    • Flying in the face of total disruption
    • P.R. Hiesinger, H.J. Bellen, Flying in the face of total disruption, Nat. Genet. 36 (2004) 211-212.
    • (2004) Nat. Genet. , vol.36 , pp. 211-212
    • Hiesinger, P.R.1    Bellen, H.J.2
  • 20
    • 0022374263 scopus 로고
    • Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase
    • A.J. Rivett, Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine proteinase, J. Biol. Chem. 260 (1985) 12600-12606. (Pubitemid 16233464)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.23 , pp. 12600-12606
    • Rivett, A.J.1
  • 21
    • 0023679752 scopus 로고
    • Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins
    • O. Marcillat, Y. Zhang, S.W. Lin, K.J. Davies, Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins, Biochem. J. 254 (1988) 677-683.
    • (1988) Biochem. J. , vol.254 , pp. 677-683
    • Marcillat, O.1    Zhang, Y.2    Lin, S.W.3    Davies, K.J.4
  • 22
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • DOI 10.1016/S0300-9084(01)01250-0
    • K.J. Davies, Degradation of oxidized proteins by the 20S proteasome, Biochimie 83 (2001) 301-310. (Pubitemid 32293650)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 301-310
    • Davies, K.J.A.1
  • 23
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome
    • T. Grune, T. Reinheckel, M. Joshi, K.J. Davies, Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome, J. Biol. Chem. 270 (1995) 2344-2351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.4
  • 25
    • 0034833919 scopus 로고    scopus 로고
    • Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products
    • S.P. Singh, J.A. Coronella, H. Benes, B.J. Cochrane, P. Zimniak, Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products, Eur. J. Biochem. 268 (2001) 2912-2923.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2912-2923
    • Singh, S.P.1    Coronella, J.A.2    Benes, H.3    Cochrane, B.J.4    Zimniak, P.5
  • 26
    • 77649339560 scopus 로고    scopus 로고
    • Retinoids regulate a developmental checkpoint for tissue regeneration in Drosophila
    • A. Halme, M. Cheng, I.K. Hariharan, Retinoids regulate a developmental checkpoint for tissue regeneration in Drosophila, Curr. Biol. 20 (2010) 458-463.
    • (2010) Curr. Biol. , vol.20 , pp. 458-463
    • Halme, A.1    Cheng, M.2    Hariharan, I.K.3
  • 28
    • 0029818644 scopus 로고    scopus 로고
    • Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase
    • D. Zhao, P. McCaffery, K.J. Ivins, R.L. Neve, P. Hogan, W.W. Chin, U.C. Drager, Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase, Eur. J. Biochem. 240 (1996) 15-22. (Pubitemid 26276748)
    • (1996) European Journal of Biochemistry , vol.240 , Issue.1 , pp. 15-22
    • Drager, U.C.1
  • 29
    • 38949113655 scopus 로고    scopus 로고
    • Functional characterization of a Drosophila melanogaster succinic semialdehyde dehydrogenase and a non-specific aldehyde dehydrogenase
    • B. Rothacker, T. Ilg, Functional characterization of a Drosophila melanogaster succinic semialdehyde dehydrogenase and a non-specific aldehyde dehydrogenase, Insect Biochem. Mol. Biol. 38 (2008) 354-366.
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 354-366
    • Rothacker, B.1    Ilg, T.2
  • 30
    • 37749035133 scopus 로고    scopus 로고
    • Aworldwide polymorphism in aldehyde dehydrogenase in Drosophila melanogaster: Evidence for selection mediated by dietary ethanol
    • J.D. Fry, K. Donlon, M. Saweikis, Aworldwide polymorphism in aldehyde dehydrogenase in Drosophila melanogaster: evidence for selection mediated by dietary ethanol, Evolution 62 (2008) 66-75.
    • (2008) Evolution , vol.62 , pp. 66-75
    • Fry, J.D.1    Donlon, K.2    Saweikis, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.