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Volumn 22, Issue 12, 2003, Pages 2913-2923

Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain

Author keywords

Alzheimer's disease; Cytochrome c oxidase; Dihydrolipoamide succinyltransferase; Mitochondria; Oxidative stress

Indexed keywords

DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE; GENE PRODUCT; MAXIZYME; MESSENGER RNA; OXOGLUTARATE DEHYDROGENASE; PROTEIN MIRTD; RIBOZYME; UNCLASSIFIED DRUG;

EID: 0038714406     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg299     Document Type: Article
Times cited : (27)

References (41)
  • 2
    • 0037080769 scopus 로고    scopus 로고
    • Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome
    • Barrientos, A., Korr, D. and Tzagoloff, A. (2002b) Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome. EMBO J., 21, 43-52.
    • (2002) EMBO J. , vol.21 , pp. 43-52
    • Barrientos, A.1    Korr, D.2    Tzagoloff, A.3
  • 3
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., Davis, J.B., Lesley, R. and Schubert, D. (1994) Hydrogen peroxide mediates amyloid β protein toxicity. Cell, 77, 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 4
    • 0035231595 scopus 로고    scopus 로고
    • Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues
    • Birch-Machin, M.A. and Turnbull, D.M. (2001) Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues. Methods Cell Biol., 65, 97-117.
    • (2001) Methods Cell Biol. , vol.65 , pp. 97-117
    • Birch-Machin, M.A.1    Turnbull, D.M.2
  • 6
    • 0036272650 scopus 로고    scopus 로고
    • β-amyloid inhibits integrated mitochondrial respiration and key enzyme activity
    • Caseley, C.S., Canevari, L., Land, J.M., Clark, J.B. and Sharpe, M.A. (2002) β-amyloid inhibits integrated mitochondrial respiration and key enzyme activity. J. Neurochem., 80, 91-100.
    • (2002) J. Neurochem. , vol.80 , pp. 91-100
    • Caseley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 7
    • 0035943058 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficient hippocampal neurons and choroids epithelial cells are increased in Alzheimer's disease
    • Cottrell, D.A., Borthwick, G.M., Johnson, M.A., Ince, P.G. and Tumbull, D.M. (2001) Cytochrome c oxidase deficient hippocampal neurons and choroids epithelial cells are increased in Alzheimer's disease. Neurology, 57, 260-264.
    • (2001) Neurology , vol.57 , pp. 260-264
    • Cottrell, D.A.1    Borthwick, G.M.2    Johnson, M.A.3    Ince, P.G.4    Tumbull, D.M.5
  • 8
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons
    • Harris, M.E., Hensley, K., Butterfield, D.A., Leedle, R.A. and Carney, J.M. (1995) Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol., 131, 193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.A.4    Carney, J.M.5
  • 9
    • 0025836655 scopus 로고
    • Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction
    • Hayashi, J., Ohta, S., Kikuchi, A., Takemitsu, M., Goto, Y. and Nonaka, I. (1991) Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction. Proc. Natl Acad. Sci. USA, 88, 10614-10618.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10614-10618
    • Hayashi, J.1    Ohta, S.2    Kikuchi, A.3    Takemitsu, M.4    Goto, Y.5    Nonaka, I.6
  • 11
    • 0025861818 scopus 로고
    • Detection of specific polymerase chain reaction product by utilizing the 5′-3′ exonuclease activity of Thermus aquaticus DNA polymerase
    • Holland, P.M., Abramson, R.D., Watson, R. and Gelfand, D.H. (1991) Detection of specific polymerase chain reaction product by utilizing the 5′-3′ exonuclease activity of Thermus aquaticus DNA polymerase. Proc. Natl. Acad. Sci. USA, 88, 7276-7280.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7276-7280
    • Holland, P.M.1    Abramson, R.D.2    Watson, R.3    Gelfand, D.H.4
  • 12
    • 0030056765 scopus 로고    scopus 로고
    • Selection of the best target site for ribozyme-mediated cleavage within a fusion gene for adenovirus E1A-associated 300 kDa protein (p300) and luciferase
    • Kawasaki, H., Ohkawa, J., Tanishige, N., Yoshinari, K., Murata, K., Yokoyama, K.K. and Taira, K. (1996) Selection of the best target site for ribozyme-mediated cleavage within a fusion gene for adenovirus E1A-associated 300 kDa protein (p300) and luciferase. Nucleic Acids Res., 24, 3010-3016.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3010-3016
    • Kawasaki, H.1    Ohkawa, J.2    Tanishige, N.3    Yoshinari, K.4    Murata, K.5    Yokoyama, K.K.6    Taira, K.7
  • 13
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King, MP. and Attardi, G. (1989) Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation. Science, 246, 500-503.
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 17
    • 0032214088 scopus 로고    scopus 로고
    • A novel allosterically trans-activated ribozyme, the maxizyme, with exceptional specificity in vitro and in vivo
    • Kuwabara, T., Warashina, M., Tanabe, T., Tani, K., Asano, S. and Taira, K. (1998) A novel allosterically trans-activated ribozyme, the maxizyme, with exceptional specificity in vitro and in vivo. Mol. Cell, 2, 617-627.
    • (1998) Mol. Cell , vol.2 , pp. 617-627
    • Kuwabara, T.1    Warashina, M.2    Tanabe, T.3    Tani, K.4    Asano, S.5    Taira, K.6
  • 18
    • 0033514517 scopus 로고    scopus 로고
    • Val-heterodimeric maxizymes with high potential as gene-inactivating agents: Simultaneous cleavage at two sites in HIV-1 tat mRNA in cultured cells
    • Val-heterodimeric maxizymes with high potential as gene-inactivating agents: Simultaneous cleavage at two sites in HIV-1 tat mRNA in cultured cells. Proc. Natl Acad. Sci. USA, 96, 1886-1891.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1886-1891
    • Kuwabara, T.1    Warashina, M.2    Nakayama, A.3    Ohkawa, J.4    Taira, K.5
  • 19
    • 0028834086 scopus 로고
    • Oligonucleotides with fluorescent dyes at opposite ends provide a quenched probe system useful for detecting PCR product and nucleic acid hybridization
    • Livak, K.J., Flood, S.J., Marmaro, J., Giusti, W. and Deetz, K. (1995) Oligonucleotides with fluorescent dyes at opposite ends provide a quenched probe system useful for detecting PCR product and nucleic acid hybridization. PCR Methods Appl., 4, 357-362.
    • (1995) PCR Methods Appl. , vol.4 , pp. 357-362
    • Livak, K.J.1    Flood, S.J.2    Marmaro, J.3    Giusti, W.4    Deetz, K.5
  • 21
    • 0031560445 scopus 로고    scopus 로고
    • A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle
    • Matuda, S., Kodama, J., Goshi, N., Takase, C., Nakano, K., Nakagawa, S. and Ohta, S. (1997) A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle. Biochem. Biophys. Res. Commun., 241, 151-156.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 151-156
    • Matuda, S.1    Kodama, J.2    Goshi, N.3    Takase, C.4    Nakano, K.5    Nakagawa, S.6    Ohta, S.7
  • 22
    • 0027759516 scopus 로고
    • Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3
    • Nakano, K. et al. (1993) Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. Biochim. Biophys. Acta, 1216, 360-368.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 360-368
    • Nakano, K.1
  • 23
    • 0027935643 scopus 로고
    • Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex
    • Nakano, K., Takase, C., Sakamoto, T., Nakagawa, S., Inazawa, J., Ohta, S. and Matuda, S. (1994) Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur. J. Biochem., 224, 179-189.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 179-189
    • Nakano, K.1    Takase, C.2    Sakamoto, T.3    Nakagawa, S.4    Inazawa, J.5    Ohta, S.6    Matuda, S.7
  • 26
    • 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. and Ohta, S. (2003) Deficiency in a mitochondrial aldehyde dehydrogenase increases vulnerability to oxidative stress in PC12 cells. J. Neurochem., 84, 1110-1117.
    • (2003) J. Neurochem. , vol.84 , pp. 1110-1117
    • Ohsawa, I.1    Nishimaki, K.2    Yasuda, C.3    Kamino, K.4    Ohta, S.5
  • 27
    • 0021398312 scopus 로고
    • A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria
    • Ohta, S. and Schatz, G. (1984) A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria. EMBO J., 3, 651-657.
    • (1984) EMBO J. , vol.3 , pp. 651-657
    • Ohta, S.1    Schatz, G.2
  • 28
    • 0029055772 scopus 로고
    • Cytochrome c oxidase in Alzheimer's disease brain: Purification and characterization
    • Parker, W.D. and Parks, J.K. (1995) Cytochrome c oxidase in Alzheimer's disease brain: Purification and characterization. Neurology, 45, 482-486.
    • (1995) Neurology , vol.45 , pp. 482-486
    • Parker, W.D.1    Parks, J.K.2
  • 29
    • 0030629511 scopus 로고    scopus 로고
    • tRNA-delivery systems for ribozymes
    • Turner, P.C. (ed.). Humana Press, Totowa, NJ
    • Perriman, R. and de Feyter, R. (1997) tRNA-delivery systems for ribozymes. In Turner, P.C. (ed.), Methods in Molecular Biology, Ribozyme Protocols. Humana Press, Totowa, NJ, pp. 393-402.
    • (1997) Methods in Molecular Biology, Ribozyme Protocols , pp. 393-402
    • Perriman, R.1    De Feyter, R.2
  • 30
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N. and Geissler, A. (2001) Versatility of the mitochondrial protein import machinery. Nat. Rev. Mol. Cell Biol., 2, 339-349.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 31
    • 0037314215 scopus 로고    scopus 로고
    • Neuronal degeneration and mitochondrial dysfunction
    • Schon, E.A. and Manfredi, G. (2003) Neuronal degeneration and mitochondrial dysfunction. J. Clin. Invest, 111, 303-312.
    • (2003) J. Clin. Invest. , vol.111 , pp. 303-312
    • Schon, E.A.1    Manfredi, G.2
  • 33
    • 0037601033 scopus 로고    scopus 로고
    • Polymorphisms of the DLST gene associate with late-onset and with familial Alzheimer's disease
    • Sheu, K.F. et al. (1998) Polymorphisms of the DLST gene associate with late-onset and with familial Alzheimer's disease. Neurobiol. Aging, 19, S293.
    • (1998) Neurobiol. Aging , vol.19
    • Sheu, K.F.1
  • 34
    • 0032932396 scopus 로고    scopus 로고
    • Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population
    • Sheu, K.F. et al. (1999a) Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population. Ann. Neurol., 45, 48-53.
    • (1999) Ann. Neurol. , vol.45 , pp. 48-53
    • Sheu, K.F.1
  • 38
    • 0032712588 scopus 로고    scopus 로고
    • Characterization of SURF-1 expression and Surf-1p function in normal and disease conditions
    • Tiranti, V., Galimberti, C., Hijtmans, L., Bovolenta, S., Perini, M.P. and Zeviani, M. (1999) Characterization of SURF-1 expression and Surf-1p function in normal and disease conditions. Hum. Mol. Genet., 8, 2533-2540.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2533-2540
    • Tiranti, V.1    Galimberti, C.2    Hijtmans, L.3    Bovolenta, S.4    Perini, M.P.5    Zeviani, M.6
  • 39
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts and transmitochondrial cell lines
    • Trounce, I.A., Kim, Y.L., Jun, A.S. and Wallace, D.C. (1996) Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts and transmitochondrial cell lines. Methods Enzymol., 264, 484-509.
    • (1996) Methods Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 40
    • 0031792774 scopus 로고    scopus 로고
    • Sp1-mediated transcription of the Werner helicase gene is modulated by Rb and p53
    • Yamabe, Y., Shimamoto, A., Goto, M., Yokota, J., Sugawara, M. and Furuichi, Y. (1998) Sp1-mediated transcription of the Werner helicase gene is modulated by Rb and p53. Mol. Cell. Biol., 18, 6191-6200.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6191-6200
    • Yamabe, Y.1    Shimamoto, A.2    Goto, M.3    Yokota, J.4    Sugawara, M.5    Furuichi, Y.6
  • 41
    • 17344362021 scopus 로고    scopus 로고
    • SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome
    • Zhu, Z. et al. (1998) SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome. Nat. Genet., 20, 337-343.
    • (1998) Nat. Genet. , vol.20 , pp. 337-343
    • Zhu, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.