메뉴 건너뛰기




Volumn 27, Issue 12, 2007, Pages 4228-4237

Analysis of the assembly profiles for mitochondrial- and nuclear-DNA-encoded subunits into complex I

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS DNA; CHAPERONE; HOLOENZYME; MITOCHONDRIAL DNA; PROTEIN B17.2L; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

EID: 34250164233     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00074-07     Document Type: Article
Times cited : (220)

References (42)
  • 2
    • 0028856032 scopus 로고
    • Mitochondrial receptor complex from Neurospora crassa and Saccharomyecs cerevisiae
    • Alconada, A., F. Gartner, A. Honlinger, M. Kuhrich, and N. Pfanner. 1995. Mitochondrial receptor complex from Neurospora crassa and Saccharomyecs cerevisiae. Methods Enzymol. 260:263-286.
    • (1995) Methods Enzymol , vol.260 , pp. 263-286
    • Alconada, A.1    Gartner, F.2    Honlinger, A.3    Kuhrich, M.4    Pfanner, N.5
  • 3
    • 0242353332 scopus 로고    scopus 로고
    • Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiencv
    • Antonicka, H., I. Ogilvie, T. Taivassalo, R. P. Anitori, R. G. Haller, J. Vissing, N. G. Kennaway, and E. A. Shoubridge. 2003. Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiencv. J. Biol. Chem. 278:43081-43088.
    • (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
    • 0029876984 scopus 로고    scopus 로고
    • In vivo labeling and analysis of human mitochondrial translation products
    • Chomyn, A. 1996. In vivo labeling and analysis of human mitochondrial translation products. Methods Enzymol. 264:197-211.
    • (1996) Methods Enzymol , vol.264 , pp. 197-211
    • Chomyn, A.1
  • 7
    • 33745478725 scopus 로고    scopus 로고
    • Diaz, F., H. Fukui, S. Garcia, and C. T. Moraes. 2006. Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts. Mol. Cell. Biol. 26:48724881.
    • Diaz, F., H. Fukui, S. Garcia, and C. T. Moraes. 2006. Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts. Mol. Cell. Biol. 26:48724881.
  • 11
    • 0037009108 scopus 로고    scopus 로고
    • Import and assembly of proteins into mitochondria of mammalian cells
    • Hoogenraad, N. J., L. A. Ward, and M. T. Ryan. 2002. Import and assembly of proteins into mitochondria of mammalian cells. Biochim. Biophys. Acta 1592:97-105.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 97-105
    • Hoogenraad, N.J.1    Ward, L.A.2    Ryan, M.T.3
  • 13
  • 14
    • 33646948530 scopus 로고    scopus 로고
    • Keeney, P. M., J. Xie, R. A. Capaldi, and J. P. Bennett, Jr. 2006. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 26:5256-5264.
    • Keeney, P. M., J. Xie, R. A. Capaldi, and J. P. Bennett, Jr. 2006. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 26:5256-5264.
  • 16
    • 34147153222 scopus 로고    scopus 로고
    • Analysis of mitochondrial subunit assembly into respiratory chain complexes using blue native polyacrylamide gel electrophoresis
    • McKenzie, M., M. Lazarou, D. R. Thorburn, and M. T. Ryan. 2007. Analysis of mitochondrial subunit assembly into respiratory chain complexes using blue native polyacrylamide gel electrophoresis. Anal. Biochem. 364:2128-2137.
    • (2007) Anal. Biochem , vol.364 , pp. 2128-2137
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 17
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients
    • McKenzie, M., M. Lazarou, D. R. Thorburn, and M. T. Ryan. 2006. Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J. Mol. Biol. 361:462-469.
    • (2006) J. Mol. Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 19
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy
    • Ogilvie, I., N. G. Kennaway, and E. A. Shoubridge. 2005. A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy. J. Clin. Investig. 115:2784-2792.
    • (2005) J. Clin. Investig , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 22
    • 0034756937 scopus 로고    scopus 로고
    • Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria
    • Rapaport, D., R. D. Taylor, M. Kaser, T. Langer, W. Neupert, and F. E. Nargang. 2001. Structural requirements of Tom40 for assembly into preexisting TOM complexes of mitochondria. Mol. Biol. Cell 12:1189-1198.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1189-1198
    • Rapaport, D.1    Taylor, R.D.2    Kaser, M.3    Langer, T.4    Neupert, W.5    Nargang, F.E.6
  • 23
    • 0035229003 scopus 로고    scopus 로고
    • Assaying protein import into mitochondria
    • Ryan, M. T., W. Voos, and N. Pfanner. 2001. Assaying protein import into mitochondria. Methods Cell Biol. 65:189-215.
    • (2001) Methods Cell Biol , vol.65 , pp. 189-215
    • Ryan, M.T.1    Voos, W.2    Pfanner, N.3
  • 24
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov, L. A., and P. Hinchliffe. 2006. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311:1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 25
    • 0034691280 scopus 로고    scopus 로고
    • Resolution of the membrane domain of bovine complex I into subcomplexes: Implications for the structural organization of the enzyme
    • Sazanov, L. A., S. Y. Peak-Chew, I. M. Fearnley, and J. E. Walker. 2000. Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry 39:7229-7235.
    • (2000) Biochemistry , vol.39 , pp. 7229-7235
    • Sazanov, L.A.1    Peak-Chew, S.Y.2    Fearnley, I.M.3    Walker, J.E.4
  • 26
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • Sehagger, H. 2002. Respiratory chain supercomplexes of mitochondria and bacteria. Biochim. Biophys. Acta 1555:154-159.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 154-159
    • Sehagger, H.1
  • 27
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Sehagger, H., R. de Coo, M. F. Bauer, S. Hofmann, C. Godinot, and U. Brandt. 2004. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279:36349-36353.
    • (2004) J. Biol. Chem , vol.279 , pp. 36349-36353
    • Sehagger, H.1    de Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godinot, C.5    Brandt, U.6
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Sehagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Sehagger, H.1    von Jagow, G.2
  • 29
    • 0034951707 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency
    • Shoubridge, E. A. 2001. Cytochrome c oxidase deficiency. Am. J. Med. Genet. 106:46-52.
    • (2001) Am. J. Med. Genet , vol.106 , pp. 46-52
    • Shoubridge, E.A.1
  • 30
    • 33645052713 scopus 로고    scopus 로고
    • Mitochondrial medicine: A metabolic perspective on the pathology of oxidative phosphorylation disorders
    • Smeitink, J. A., M. Zeviani, D. M. Turnbull, and H. T. Jacobs. 2006. Mitochondrial medicine: a metabolic perspective on the pathology of oxidative phosphorylation disorders. Cell Metab. 3:9-13.
    • (2006) Cell Metab , vol.3 , pp. 9-13
    • Smeitink, J.A.1    Zeviani, M.2    Turnbull, D.M.3    Jacobs, H.T.4
  • 33
    • 0025295685 scopus 로고
    • Assembly of NADH: Ubiquinone reductase (complex I) in Neurospora mitochondria. Independent pathways of nuclear-encoded and mitochondrially encoded subunits
    • Tuschen, G., U. Sackmann, U. Nehls, H. Haiker, G. Buse, and H. Weiss. 1990. Assembly of NADH: ubiquinone reductase (complex I) in Neurospora mitochondria. Independent pathways of nuclear-encoded and mitochondrially encoded subunits. J. Mol. Biol. 213:845-857.
    • (1990) J. Mol. Biol , vol.213 , pp. 845-857
    • Tuschen, G.1    Sackmann, U.2    Nehls, U.3    Haiker, H.4    Buse, G.5    Weiss, H.6
  • 34
    • 1642382090 scopus 로고    scopus 로고
    • Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency
    • Ugalde, C., R. J. Janssen, L. P. van den Heuvel, J. A. Smeitink, and L. G. Nijtmans. 2004. Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. Hum. Mol. Genet. 13:659-667.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 659-667
    • Ugalde, C.1    Janssen, R.J.2    van den Heuvel, L.P.3    Smeitink, J.A.4    Nijtmans, L.G.5
  • 35
    • 19544369483 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: A framework to interpret complex I deficiencies
    • Ugalde, C., R. Vogel, R. Huijbens, B. Van Den Heuvel, J. Smeitink, and L. Nijtmans. 2004. Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies. Hum. Mol. Genet. 13:2461-2472.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2461-2472
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    Van Den Heuvel, B.4    Smeitink, J.5    Nijtmans, L.6
  • 38
    • 27144528747 scopus 로고    scopus 로고
    • Vogel, R. O., R. J. Janssen, C. Ugalde, M. Grovenstein, R. J. Huijbens, H. J. Visch, L. P. van den Heuvel, P. H. Willems, M. Zeviani, J. A. Smeitink, and L. G. Nijtmans. 2005. Human mitochondrial complex I assembly is mediated by NDUFAF1. FEES J. 272:5317-5326.
    • Vogel, R. O., R. J. Janssen, C. Ugalde, M. Grovenstein, R. J. Huijbens, H. J. Visch, L. P. van den Heuvel, P. H. Willems, M. Zeviani, J. A. Smeitink, and L. G. Nijtmans. 2005. Human mitochondrial complex I assembly is mediated by NDUFAF1. FEES J. 272:5317-5326.
  • 39
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: A dawn for evolutionary medicine
    • Wallace, D. C. 2005. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 39:359-407.
    • (2005) Annu. Rev. Genet , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 40
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • Wiedemann, N., A. E. Frazier, and N. Pfanner. 2004. The protein import machinery of mitochondria. J. Biol. Chem. 279:14473-14476.
    • (2004) J. Biol. Chem , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 42
    • 1842582613 scopus 로고    scopus 로고
    • Development and characterization of a conditional mitochondrial complex I assembly system
    • Yadava, N., T. Houchens, P. Potluri, and I. E. Scheffler. 2004. Development and characterization of a conditional mitochondrial complex I assembly system. J. Biol. Chem. 279:12406-12413.
    • (2004) J. Biol. Chem , vol.279 , pp. 12406-12413
    • Yadava, N.1    Houchens, T.2    Potluri, P.3    Scheffler, I.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.