메뉴 건너뛰기




Volumn 1777, Issue 10, 2008, Pages 1384-1391

Subunit mass fingerprinting of mitochondrial complex I

Author keywords

Complex I; LILBID; Mass spectrometry; Membrane protein; Mitochondria; Yarrowia lipolytica

Indexed keywords

MEMBRANE PROTEIN; MULTIPROTEIN COMPLEX; POLYACRYLAMIDE GEL; PROTEIN SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 52949098343     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.08.001     Document Type: Article
Times cited : (72)

References (28)
  • 3
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductases
    • Brandt U. Energy converting NADH:quinone oxidoreductases. Annu. Rev. Biochem. 75 (2006) 69-92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 4
    • 0027166358 scopus 로고
    • Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry
    • Schindler P.A., Van D.A., and Falick A.M. Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry. Anal. Biochem. 213 (1993) 256-263
    • (1993) Anal. Biochem. , vol.213 , pp. 256-263
    • Schindler, P.A.1    Van, D.A.2    Falick, A.M.3
  • 5
    • 0027989546 scopus 로고
    • 1 by reverse-phase HPLC and determination of the subunit molecular masses by electrospray ionization mass spectrometry
    • 1 by reverse-phase HPLC and determination of the subunit molecular masses by electrospray ionization mass spectrometry. Biochem. 33 (1994) 10561-10567
    • (1994) Biochem. , vol.33 , pp. 10561-10567
    • Musatov, A.1    Robinson, N.C.2
  • 7
    • 0042386232 scopus 로고    scopus 로고
    • Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage
    • Bodnar W.M., Blackburn R.K., Krise J.M., and Moseley M.A. Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage. J. Am. Soc. Mass Spectrom. 14 (2003) 971-979
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 971-979
    • Bodnar, W.M.1    Blackburn, R.K.2    Krise, J.M.3    Moseley, M.A.4
  • 8
    • 34249780156 scopus 로고    scopus 로고
    • Shotgun protein sequencing: assembly of peptide tandem mass spectra from mixtures of modified proteins
    • Bandeira N., Clauser K.R., and Pevzner P.A. Shotgun protein sequencing: assembly of peptide tandem mass spectra from mixtures of modified proteins. Mol. Cell. Proteomics 6 (2007) 1123-1134
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1123-1134
    • Bandeira, N.1    Clauser, K.R.2    Pevzner, P.A.3
  • 9
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., and Yates III J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19 (2001) 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 10
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu C.C., MacCoss M.J., Howell K.E., and Yates III J.R. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 21 (2003) 532-538
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 14
    • 1642382090 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., Vogel R., Huijbens R., Van den Heuvel L., Smeitink J., and Nijtmans L. Human mitochondrial complex I assembles through the combination of evolutionary conserved modules; a framework to interpret complex I deficiencies. Hum. Mol. Genet. 13 (2004) 659-667
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 659-667
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    Van den Heuvel, L.4    Smeitink, J.5    Nijtmans, L.6
  • 15
    • 33644777171 scopus 로고    scopus 로고
    • A new way to detect noncovalently bonded complexes of biomolecules from liquid micro-droplets by laser mass spectrometry
    • Morgner N., Barth H.D., and Brutschy B. A new way to detect noncovalently bonded complexes of biomolecules from liquid micro-droplets by laser mass spectrometry. Austral. J. Chem. 59 (2006) 109-114
    • (2006) Austral. J. Chem. , vol.59 , pp. 109-114
    • Morgner, N.1    Barth, H.D.2    Brutschy, B.3
  • 16
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: technology for structural genomics and proteomics
    • Benesch J.L., Ruotolo B.T., Simmons D.A., and Robinson C.V. Protein complexes in the gas phase: technology for structural genomics and proteomics. Chem. Rev. 107 (2007) 3544-3567
    • (2007) Chem. Rev. , vol.107 , pp. 3544-3567
    • Benesch, J.L.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 17
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex
    • Morgner N., Kleinschroth T., Barth H.D., Ludwig B., and Brutschy B. A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom. 18 (2007) 1429-1438
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.D.3    Ludwig, B.4    Brutschy, B.5
  • 18
    • 0032812743 scopus 로고    scopus 로고
    • A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • Kerscher S., Okun J.G., and Brandt U. A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell Sci. 112 (1999) 2347-2354
    • (1999) J. Cell Sci. , vol.112 , pp. 2347-2354
    • Kerscher, S.1    Okun, J.G.2    Brandt, U.3
  • 19
    • 0035795187 scopus 로고    scopus 로고
    • Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • Kashani-Poor N., Kerscher S., Zickermann V., and Brandt U. Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1504 (2001) 363-370
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 363-370
    • Kashani-Poor, N.1    Kerscher, S.2    Zickermann, V.3    Brandt, U.4
  • 21
    • 0015501042 scopus 로고
    • The binding of detergents to lipophilic and hydrophilic proteins
    • Helenius A., and Simons K. The binding of detergents to lipophilic and hydrophilic proteins. J. Biol. Chem. 247 (1972) 3656-3661
    • (1972) J. Biol. Chem. , vol.247 , pp. 3656-3661
    • Helenius, A.1    Simons, K.2
  • 22
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H., and von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199 (1991) 223-231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 23
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H. Tricine-SDS-PAGE. Nat. Protoc. 1 (2006) 16-22
    • (2006) Nat. Protoc. , vol.1 , pp. 16-22
    • Schägger, H.1
  • 24
    • 33751561773 scopus 로고    scopus 로고
    • Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex
    • Abdrakhmanova A., Zwicker K., Kerscher S., Zickermann V., and Brandt U. Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex. Biochim. Biophys. Acta 1757 (2006) 1676-1682
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1676-1682
    • Abdrakhmanova, A.1    Zwicker, K.2    Kerscher, S.3    Zickermann, V.4    Brandt, U.5
  • 25
    • 28844436044 scopus 로고    scopus 로고
    • Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters
    • Abdrakhmanova A., Dobrynin K., Zwicker K., Kerscher S., and Brandt U. Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters. FEBS Lett. 579 (2005) 6781-6785
    • (2005) FEBS Lett. , vol.579 , pp. 6781-6785
    • Abdrakhmanova, A.1    Dobrynin, K.2    Zwicker, K.3    Kerscher, S.4    Brandt, U.5
  • 26
    • 0020473231 scopus 로고
    • Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins
    • Ragan C.I., Galante Y.M., Hatefi Y., and Ohnishi T. Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins. Biochem. 21 (1982) 590-594
    • (1982) Biochem. , vol.21 , pp. 590-594
    • Ragan, C.I.1    Galante, Y.M.2    Hatefi, Y.3    Ohnishi, T.4
  • 27
    • 0026472383 scopus 로고
    • Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme
    • Finel M., Skehel J.M., Albracht S.P.J., Fearnley I.M., and Walker J.E. Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochem. 31 (1992) 11425-11434
    • (1992) Biochem. , vol.31 , pp. 11425-11434
    • Finel, M.1    Skehel, J.M.2    Albracht, S.P.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 28
    • 52949124541 scopus 로고    scopus 로고
    • Investigation of two accessory subunits of complex I from Yarrowia lipolytica
    • Dobrynin K., Abdrakhmanova A., Zwicker K., Kerscher S., and Brandt U. Investigation of two accessory subunits of complex I from Yarrowia lipolytica. Biochim. Biophys. Acta 1757 Supplement 1 (2006) 153
    • (2006) Biochim. Biophys. Acta , vol.1757 , Issue.SUPPL. 1 , pp. 153
    • Dobrynin, K.1    Abdrakhmanova, A.2    Zwicker, K.3    Kerscher, S.4    Brandt, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.