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Volumn 426, Issue 6968, 2003, Pages 862-866

Evolutionary conservation of biogenesis of β-barrel membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELL MEMBRANES; COMPLEXATION; MORPHOLOGY; OLIGOMERS; PROTEINS; SYNTHESIS (CHEMICAL);

EID: 0346727130     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02208     Document Type: Article
Times cited : (361)

References (29)
  • 1
    • 0036535035 scopus 로고    scopus 로고
    • Biogenesis of the mitochondrial TOM complex
    • Rapaport, D. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 27, 191-197 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 191-197
    • Rapaport, D.1
  • 2
    • 0037379183 scopus 로고    scopus 로고
    • Predict ion of the plant β-barrel proteome: A case study of the chloroplast outer envelope
    • Schleiff, E. et al. Predict ion of the plant β-barrel proteome: A case study of the chloroplast outer envelope. Protein Sci. 12, 748-759 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 748-759
    • Schleiff, E.1
  • 3
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schutz, G. E. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta 1565, 308-317 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schutz, G.E.1
  • 5
    • 0032188847 scopus 로고    scopus 로고
    • Tom 40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill, K. et al. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395, 516-521 (1998).
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1
  • 6
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • Ahting, U. et al. Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria. J. Cell Biol. 153, 1151-1160 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1151-1160
    • Ahting, U.1
  • 7
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L. F. & Yaffe, M. P. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126, 1361-1373 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 8
    • 0037009087 scopus 로고    scopus 로고
    • Functions of outer membrane receptors in mitochondrial protein import
    • Endo, T. & Kohda, D. Functions of outer membrane receptors in mitochondrial protein import. Biochim. Biophys. Acta 1592, 3-14 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 3-14
    • Endo, T.1    Kohda, D.2
  • 9
    • 0035066642 scopus 로고    scopus 로고
    • Barreling through the outer membrane
    • Matouschek, A. & Glick, B. S. Barreling through the outer membrane. Nature Struct. Biol. 9, 284-286 (2001).
    • (2001) Nature Struct. Biol. , vol.9 , pp. 284-286
    • Matouschek, A.1    Glick, B.S.2
  • 10
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N. & Geissler, A. Versatility of the mitochondrial protein import machinery. Nature Rev. Mol. Cell Biol. 2, 339-349 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 11
    • 0036138945 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Paschen, S. A. & Neupert, W. Protein import into mitochondria. IUBMB Life 52, 101-112 (2001).
    • (2001) IUBMB Life , vol.52 , pp. 101-112
    • Paschen, S.A.1    Neupert, W.2
  • 12
    • 0035153316 scopus 로고    scopus 로고
    • The alpha and the beta: Protein translocation across mitochondrial and plastid outer membranes
    • Gabriel, K., Buchanan, S. K. & Lithgow, T. The alpha and the beta: protein translocation across mitochondrial and plastid outer membranes. Trends Biochem. Sci. 26, 36-40 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 36-40
    • Gabriel, K.1    Buchanan, S.K.2    Lithgow, T.3
  • 13
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray, M. W., Burger, G. & Lang, B. F. Mitochondrial evolution. Science 283, 1476-1481 (1999).
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 14
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M. & Tommassen, J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299, 262-265 (2003).
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 15
    • 0033962697 scopus 로고    scopus 로고
    • Analysis of deletion phenotypes and GFP fusions of 21 novel Saccharomyces cerevisiae open reading frames
    • Brachat, A. et al. Analysis of deletion phenotypes and GFP fusions of 21 novel Saccharomyces cerevisiae open reading frames. Yeast 16, 241-253 (2000).
    • (2000) Yeast , vol.16 , pp. 241-253
    • Brachat, A.1
  • 16
    • 0036427905 scopus 로고    scopus 로고
    • Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles
    • De Carlo, S., El-Bez, C., Alvarez-Rua, C., Borge, J. & Dubochet, J. Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. J. Struct. Biol. 138, 216-226 (2002).
    • (2002) J. Struct. Biol. , vol.138 , pp. 216-226
    • De Carlo, S.1    El-Bez, C.2    Alvarez-Rua, C.3    Borge, J.4    Dubochet, J.5
  • 17
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport, D. & Neupert, W. Biogenesis of Tom40, core component of the TOM complex of mitochondria. J. Cell Biol. 146, 321-331 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 18
    • 0035931764 scopus 로고    scopus 로고
    • Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex
    • Krimmer, T. et al. Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex. J. Cell Biol. 152, 289-300 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 289-300
    • Krimmer, T.1
  • 19
    • 0035066635 scopus 로고    scopus 로고
    • Multistep assembly of the protein import channel of the mitochondrial outer membrane
    • Model, K. et al. Multistep assembly of the protein import channel of the mitochondrial outer membrane. Nature Struct. Biol. 8, 361-370 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 361-370
    • Model, K.1
  • 20
    • 0042163218 scopus 로고    scopus 로고
    • Machinery for protein sorting and assembly in the mitochondrial outer membrane
    • Wiedemann, N. et al. Machinery for protein sorting and assembly in the mitochondrial outer membrane. Nature 424, 565-571 (2003).
    • (2003) Nature , vol.424 , pp. 565-571
    • Wiedemann, N.1
  • 21
    • 0028967994 scopus 로고
    • Mas37p, a novel receptor subunit for protein import into mitochondria
    • Gratzer, S. et al. Mas37p, a novel receptor subunit for protein import into mitochondria. J. Cell Biol. 129, 25-34 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 25-34
    • Gratzer, S.1
  • 23
    • 0344942599 scopus 로고    scopus 로고
    • The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane
    • Genevrois, S., Steeghs, L., Roholl, P., Letesson, J. J. & van der Ley, P. The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membrane. EMBO J. 22, 1780-1789 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1780-1789
    • Genevrois, S.1    Steeghs, L.2    Roholl, P.3    Letesson, J.J.4    Van Der Ley, P.5
  • 24
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the Anfinsen cage
    • Ellis, R. J. Revisiting the Anfinsen cage. Fold. Des. 1, R9-R15 (1996).
    • (1996) Fold. Des. , vol.1
    • Ellis, R.J.1
  • 25
    • 0035956426 scopus 로고    scopus 로고
    • A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast
    • Pavlov, E. V. et al. A novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeast. J. Cell Biol. 155, 725-731 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 725-731
    • Pavlov, E.V.1
  • 26
    • 0029814312 scopus 로고    scopus 로고
    • One-step PCR mediated strategy for the construction of conditionally expressed and epitope tagged yeast proteins
    • Lafontaine, D. & Tollervey, D. One-step PCR mediated strategy for the construction of conditionally expressed and epitope tagged yeast proteins. Nucleic Acids Res. 24, 3469-3471 (1996).
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3469-3471
    • Lafontaine, D.1    Tollervey, D.2
  • 27
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens, V., Ruysschaert, J. M. & Goormaghtigh, E. Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method. AnaL Biochem. 319, 114-121 (2003).
    • (2003) Anal. Biochem. , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 28
    • 0029879294 scopus 로고    scopus 로고
    • The EM Program Package: A platform for image processing in biological electron microscopy
    • Hegerl, R. The EM Program Package: A platform for image processing in biological electron microscopy. J. Struct Biol. 116, 30-34 (1996).
    • (1996) J. Struct Biol. , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 29
    • 0029920281 scopus 로고    scopus 로고
    • The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating
    • Popp, B., Court, D. A., Benz, R., Neupert, W. & Lill, R. The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating. J. Biol. Chem. 271, 13593-13599 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 13593-13599
    • Popp, B.1    Court, D.A.2    Benz, R.3    Neupert, W.4    Lill, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.