메뉴 건너뛰기




Volumn 13, Issue 6, 2004, Pages 805-815

Respiratory complex III is required to maintain complex I in mammalian mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; MITOCHONDRIAL PROTEIN; RESPIRATORY COMPLEX I PROTEIN; RESPIRATORY COMPLEX III PROTEIN; UNCLASSIFIED DRUG;

EID: 12144291508     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00124-8     Document Type: Article
Times cited : (379)

References (36)
  • 4
    • 0242353332 scopus 로고    scopus 로고
    • Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency
    • Antonicka H., Ogilvie I., Taivassalo T., Anitori R.P., Haller R.G., Vissing J., Kennaway N.G., Shoubridge E.A. Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency. J. Biol. Chem. 278:2003;43081-43088.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43081-43088
    • Antonicka, H.1    Ogilvie, I.2    Taivassalo, T.3    Anitori, R.P.4    Haller, R.G.5    Vissing, J.6    Kennaway, N.G.7    Shoubridge, E.A.8
  • 6
    • 0032541401 scopus 로고    scopus 로고
    • The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme
    • Bai Y., Attardi G. The mtDNA-encoded ND6 subunit of mitochondrial NADH dehydrogenase is essential for the assembly of the membrane arm and the respiratory function of the enzyme. EMBO J. 17:1998;4848-4858.
    • (1998) EMBO J. , vol.17 , pp. 4848-4858
    • Bai, Y.1    Attardi, G.2
  • 8
    • 0035231595 scopus 로고    scopus 로고
    • Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues
    • Birch-Machin M.A., Turnbull D.M. Assaying mitochondrial respiratory complex activity in mitochondria isolated from human cells and tissues. Methods Cell Biol. 65:2001;97-117.
    • (2001) Methods Cell Biol. , vol.65 , pp. 97-117
    • Birch-Machin, M.A.1    Turnbull, D.M.2
  • 11
    • 0029876984 scopus 로고    scopus 로고
    • In vivo labeling and analysis of human mitochondrial translation products
    • Chomyn A. In vivo labeling and analysis of human mitochondrial translation products. Methods Enzymol. 264:1996;197-211.
    • (1996) Methods Enzymol. , vol.264 , pp. 197-211
    • Chomyn, A.1
  • 13
    • 0035794212 scopus 로고    scopus 로고
    • Reconstitution of mitochondrial processing peptidase from the core proteins (subunits I and II) of bovine heart mitochondrial cytochrome bc(1) complex
    • Deng K., Shenoy S.K., Tso S.C., Yu L., Yu C.A. Reconstitution of mitochondrial processing peptidase from the core proteins (subunits I and II) of bovine heart mitochondrial cytochrome bc(1) complex. J. Biol. Chem. 276:2001;6499-6505.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6499-6505
    • Deng, K.1    Shenoy, S.K.2    Tso, S.C.3    Yu, L.4    Yu, C.A.5
  • 14
    • 0027178848 scopus 로고
    • The C-terminal domain of yeast cytochrome b is essential for a correct assembly of the mitochondrial cytochrome bc1 complex
    • di Rago J.P., Macadre C., Lazowska J., Slonimski P.P. The C-terminal domain of yeast cytochrome b is essential for a correct assembly of the mitochondrial cytochrome bc1 complex. FEBS Lett. 328:1993;153-158.
    • (1993) FEBS Lett. , vol.328 , pp. 153-158
    • Di Rago, J.P.1    Macadre, C.2    Lazowska, J.3    Slonimski, P.P.4
  • 15
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S., Schon E.A. Mitochondrial respiratory-chain diseases. N. Engl. J. Med. 348:2003;2656-2668.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2656-2668
    • Dimauro, S.1    Schon, E.A.2
  • 17
    • 0029935370 scopus 로고    scopus 로고
    • Use of polarography to detect respiration defects in cell cultures
    • Hofhaus G., Shakeley R.M., Attardi G. Use of polarography to detect respiration defects in cell cultures. Methods Enzymol. 264:1996;476-483.
    • (1996) Methods Enzymol. , vol.264 , pp. 476-483
    • Hofhaus, G.1    Shakeley, R.M.2    Attardi, G.3
  • 19
    • 0033659683 scopus 로고    scopus 로고
    • Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene
    • Keightley J.A., Anitori R., Burton M.D., Quan F., Buist N.R., Kennaway N.G. Mitochondrial encephalomyopathy and complex III deficiency associated with a stop-codon mutation in the cytochrome b gene. Am. J. Hum. Genet. 67:2000;1400-1410.
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 1400-1410
    • Keightley, J.A.1    Anitori, R.2    Burton, M.D.3    Quan, F.4    Buist, N.R.5    Kennaway, N.G.6
  • 20
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King M.P., Attardi G. Human cells lacking mtDNA. repopulation with exogenous mitochondria by complementation Science. 246:1989;500-503.
    • (1989) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 21
    • 0036132671 scopus 로고    scopus 로고
    • A novel nonsense mutation (Q352X) in the mitochondrial cytochrome b gene associated with a combined deficiency of complexes I and III
    • Lamantea E., Carrara F., Mariotti C., Morandi L., Tiranti V., Zeviani M. A novel nonsense mutation (Q352X) in the mitochondrial cytochrome b gene associated with a combined deficiency of complexes I and III. Neuromuscul. Disord. 12:2002;49-52.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 49-52
    • Lamantea, E.1    Carrara, F.2    Mariotti, C.3    Morandi, L.4    Tiranti, V.5    Zeviani, M.6
  • 22
    • 0037723899 scopus 로고    scopus 로고
    • The 9.8 kDa subunit of complex I, related to bacterial Na(+)-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa
    • Marques I., Duarte M., Videira A. The 9.8 kDa subunit of complex I, related to bacterial Na(+)-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa. J. Mol. Biol. 329:2003;283-290.
    • (2003) J. Mol. Biol. , vol.329 , pp. 283-290
    • Marques, I.1    Duarte, M.2    Videira, A.3
  • 23
    • 0035379754 scopus 로고    scopus 로고
    • Ubiquinol:cytochrome c oxidoreductase (complex III). Effect of inhibitors on cytochrome b reduction in submitochondrial particles and the role of ubiquinone in complex III
    • Matsuno-Yagi A., Hatefi Y. Ubiquinol:cytochrome c oxidoreductase (complex III). Effect of inhibitors on cytochrome b reduction in submitochondrial particles and the role of ubiquinone in complex III. J. Biol. Chem. 276:2001;19006-19011.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19006-19011
    • Matsuno-Yagi, A.1    Hatefi, Y.2
  • 24
    • 0035229118 scopus 로고    scopus 로고
    • Transmitochondrial technology in animal cells
    • Moraes C.T., Dey R., Barrientos A. Transmitochondrial technology in animal cells. Methods Cell Biol. 65:2001;397-412.
    • (2001) Methods Cell Biol. , vol.65 , pp. 397-412
    • Moraes, C.T.1    Dey, R.2    Barrientos, A.3
  • 25
    • 0033767317 scopus 로고    scopus 로고
    • An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production
    • Rana M., de Coo I., Diaz F., Smeets H., Moraes C.T. An out-of-frame cytochrome b gene deletion from a patient with parkinsonism is associated with impaired complex III assembly and an increase in free radical production. Ann. Neurol. 48:2000;774-781.
    • (2000) Ann. Neurol. , vol.48 , pp. 774-781
    • Rana, M.1    De Coo, I.2    Diaz, F.3    Smeets, H.4    Moraes, C.T.5
  • 26
    • 0029924286 scopus 로고    scopus 로고
    • Electrophoretic techniques for isolation and quantification of oxidative phosphorylation complexes from human tissues
    • Schägger H. Electrophoretic techniques for isolation and quantification of oxidative phosphorylation complexes from human tissues. Methods Enzymol. 264:1996;555-566.
    • (1996) Methods Enzymol. , vol.264 , pp. 555-566
    • Schägger, H.1
  • 27
    • 0036139981 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes
    • Schägger H. Respiratory chain supercomplexes. IUBMB Life. 52:2001;119-128.
    • (2001) IUBMB Life , vol.52 , pp. 119-128
    • Schägger, H.1
  • 28
    • 0029980819 scopus 로고    scopus 로고
    • Electrophoretic separation of multiprotein complexes from blood platelets and cell lines: Technique for the analysis of diseases with defects in oxidative phosphorylation
    • Schägger H., Bentlage H., Ruitenbeek W., Pfeiffer K., Rotter S., Rother C., Bottcher-Purkl A., Lodemann E. Electrophoretic separation of multiprotein complexes from blood platelets and cell lines. technique for the analysis of diseases with defects in oxidative phosphorylation Electrophoresis. 17:1996;709-714.
    • (1996) Electrophoresis , vol.17 , pp. 709-714
    • Schägger, H.1    Bentlage, H.2    Ruitenbeek, W.3    Pfeiffer, K.4    Rotter, S.5    Rother, C.6    Bottcher-Purkl, A.7    Lodemann, E.8
  • 29
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H., Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19:2000;1777-1783.
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 30
    • 0021099992 scopus 로고
    • Kinetics of assembly of complex III into the yeast mitochondrial membrane. Evidence for a precursor to the iron-sulfur protein
    • Sidhu A., Beattie D.S. Kinetics of assembly of complex III into the yeast mitochondrial membrane. Evidence for a precursor to the iron-sulfur protein. J. Biol. Chem. 258:1983;10649-10656.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10649-10656
    • Sidhu, A.1    Beattie, D.S.2
  • 33
    • 0029893076 scopus 로고    scopus 로고
    • Production of transmitochondrial mouse cell lines by cybrid rescue of rhodamine-6G pre-treated L-cells
    • Trounce I., Wallace D.C. Production of transmitochondrial mouse cell lines by cybrid rescue of rhodamine-6G pre-treated L-cells. Somat. Cell Mol. Genet. 22:1996;81-85.
    • (1996) Somat. Cell Mol. Genet. , vol.22 , pp. 81-85
    • Trounce, I.1    Wallace, D.C.2
  • 35
    • 0031029962 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells
    • Villani G., Attardi G. In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells. Proc. Natl. Acad. Sci. USA. 94:1997;1166-1171.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1166-1171
    • Villani, G.1    Attardi, G.2
  • 36
    • 0019474322 scopus 로고
    • Elimination of mitochondrial elements and improved viability in hybrid cells
    • Ziegler M.L., Davidson R.L. Elimination of mitochondrial elements and improved viability in hybrid cells. Somatic Cell Genet. 7:1981;73-88.
    • (1981) Somatic Cell Genet. , vol.7 , pp. 73-88
    • Ziegler, M.L.1    Davidson, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.