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Volumn 11, Issue 12, 2012, Pages 5720-5735

High-throughput isolation and characterization of untagged membrane protein complexes: Outer membrane complexes of Desulfovibrio vulgaris

Author keywords

Gram negative bacteria; interaction networks; mass spectrometry; membrane proteins; protein complexes; protein protein interactions

Indexed keywords

OUTER MEMBRANE PROTEIN;

EID: 84870909278     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300548d     Document Type: Article
Times cited : (21)

References (61)
  • 1
    • 50049135906 scopus 로고    scopus 로고
    • Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
    • Weiner, J. H.; Li, L. Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis Biochim. Biophys. Acta 2008, 1778 (9) 1698-1713
    • (2008) Biochim. Biophys. Acta , vol.1778 , Issue.9 , pp. 1698-1713
    • Weiner, J.H.1    Li, L.2
  • 2
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins - Theory and application
    • Speers, A. E.; Wu, C. C. Proteomics of integral membrane proteins - theory and application Chem. Rev. 2007, 107 (8) 3687-3714
    • (2007) Chem. Rev. , vol.107 , Issue.8 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 3
    • 55749112976 scopus 로고    scopus 로고
    • Membrane proteins and membrane proteomics
    • Tan, S.; Tan, H. T.; Chung, M. C. M. Membrane proteins and membrane proteomics Proteomics 2008, 8 (19) 3924-3932
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3924-3932
    • Tan, S.1    Tan, H.T.2    Chung, M.C.M.3
  • 4
    • 2442619448 scopus 로고    scopus 로고
    • Structural genomics of membrane proteins
    • Walian, P.; Cross, T. A.; Jap, B. K. Structural genomics of membrane proteins Genome Biol. 2004, 5 (4) 215
    • (2004) Genome Biol. , vol.5 , Issue.4 , pp. 215
    • Walian, P.1    Cross, T.A.2    Jap, B.K.3
  • 5
    • 73649093112 scopus 로고    scopus 로고
    • Identification of Neisseria meningitidis outer membrane vesicle complexes using 2-D high resolution clear native/SDS-PAGE
    • Marzoa, J.; Sánchez, S.; Ferreirós, C. M.; Criado, M. T. Identification of Neisseria meningitidis outer membrane vesicle complexes using 2-D high resolution clear native/SDS-PAGE J. Proteome Res. 2010, 9 (1) 611-619
    • (2010) J. Proteome Res. , vol.9 , Issue.1 , pp. 611-619
    • Marzoa, J.1    Sánchez, S.2    Ferreirós, C.M.3    Criado, M.T.4
  • 6
    • 77954381798 scopus 로고    scopus 로고
    • Complexome of Escherichia coli envelope proteins under normal physiological conditions
    • Pan, J.-Y.; Li, H.; Ma, Y.; Chen, P.; Zhao, P.; Wang, S.-Y.; Peng, X.-X. Complexome of Escherichia coli envelope proteins under normal physiological conditions J. Proteome Res. 2010, 9 (7) 3730-3740
    • (2010) J. Proteome Res. , vol.9 , Issue.7 , pp. 3730-3740
    • Pan, J.-Y.1    Li, H.2    Ma, Y.3    Chen, P.4    Zhao, P.5    Wang, S.-Y.6    Peng, X.-X.7
  • 7
    • 80053895756 scopus 로고    scopus 로고
    • Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles
    • Yang, X.; Promnares, K.; Qin, J.; He, M.; Shroder, D. Y.; Kariu, T.; Wang, Y.; Pal, U. Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles J. Proteome Res. 2011, 10 (10) 4556-4566
    • (2011) J. Proteome Res. , vol.10 , Issue.10 , pp. 4556-4566
    • Yang, X.1    Promnares, K.2    Qin, J.3    He, M.4    Shroder, D.Y.5    Kariu, T.6    Wang, Y.7    Pal, U.8
  • 8
    • 78651431723 scopus 로고    scopus 로고
    • Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guérin
    • Zheng, J.; Wei, C.; Zhao, L.; Liu, L.; Leng, W.; Li, W.; Jin, Q. Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guérin BMC Genomics 2011, 12, 40
    • (2011) BMC Genomics , vol.12 , pp. 40
    • Zheng, J.1    Wei, C.2    Zhao, L.3    Liu, L.4    Leng, W.5    Li, W.6    Jin, Q.7
  • 11
    • 0035106653 scopus 로고    scopus 로고
    • Enzymatic reduction of chromate: Comparative studies using sulfate-reducing bacteria
    • Michel, C.; Brugna, M.; Aubert, C.; Bernadac, A.; Bruschi, M. Enzymatic reduction of chromate: comparative studies using sulfate-reducing bacteria Appl. Microbiol. Biotechnol. 2001, 55 (1) 95-100
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , Issue.1 , pp. 95-100
    • Michel, C.1    Brugna, M.2    Aubert, C.3    Bernadac, A.4    Bruschi, M.5
  • 12
    • 0036272165 scopus 로고    scopus 로고
    • Uranium reduction by Desulfovibrio desulfuricans Strain G20 and a Cytochrome c3 mutant
    • Payne, R. B.; Gentry, D. M.; Rapp-Giles, B. J.; Casalot, L.; Wall, J. D. Uranium reduction by Desulfovibrio desulfuricans Strain G20 and a Cytochrome c3 mutant Appl. Environ. Microbiol. 2002, 68 (6) 3129-3132
    • (2002) Appl. Environ. Microbiol. , vol.68 , Issue.6 , pp. 3129-3132
    • Payne, R.B.1    Gentry, D.M.2    Rapp-Giles, B.J.3    Casalot, L.4    Wall, J.D.5
  • 13
    • 43849095105 scopus 로고    scopus 로고
    • The ecology and biotechnology of sulphate-reducing bacteria
    • Muyzer, G.; Stams, A. J. M. The ecology and biotechnology of sulphate-reducing bacteria Nat. Rev. Microbiol. 2008, 6 (6) 441-454
    • (2008) Nat. Rev. Microbiol. , vol.6 , Issue.6 , pp. 441-454
    • Muyzer, G.1    Stams, A.J.M.2
  • 16
    • 80053612533 scopus 로고    scopus 로고
    • Evidence-based annotation of transcripts and proteins in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Price, M. N.; Deutschbauer, A. M.; Kuehl, J. V.; Liu, H.; Witkowska, H. E.; Arkin, A. P. Evidence-based annotation of transcripts and proteins in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough J. Bacteriol. 2011, 193 (20) 5716-5727
    • (2011) J. Bacteriol. , vol.193 , Issue.20 , pp. 5716-5727
    • Price, M.N.1    Deutschbauer, A.M.2    Kuehl, J.V.3    Liu, H.4    Witkowska, H.E.5    Arkin, A.P.6
  • 18
    • 0019777576 scopus 로고
    • Growth of Desulfovibrio species on hydrogen and sulfate as sole energy source
    • Brandis, A.; Thauer, R. K. Growth of Desulfovibrio species on hydrogen and sulfate as sole energy source J. Gen. Microbiol. 1981, 126 (1) 249-252
    • (1981) J. Gen. Microbiol. , vol.126 , Issue.1 , pp. 249-252
    • Brandis, A.1    Thauer, R.K.2
  • 19
    • 0031831035 scopus 로고    scopus 로고
    • The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded beta-sheet proteins by its sequence and properties
    • Baldermann, C.; Lupas, A.; Lubieniecki, J.; Engelhardt, H. The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded beta-sheet proteins by its sequence and properties J. Bacteriol. 1998, 180 (15) 3741-3749
    • (1998) J. Bacteriol. , vol.180 , Issue.15 , pp. 3741-3749
    • Baldermann, C.1    Lupas, A.2    Lubieniecki, J.3    Engelhardt, H.4
  • 20
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H.; Cramer, W. A.; von Jagow, G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis Anal. Biochem. 1994, 217 (2) 220-230
    • (1994) Anal. Biochem. , vol.217 , Issue.2 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 21
    • 29344473941 scopus 로고    scopus 로고
    • Proteomic analysis of succinate dehydrogenase and ubiquinol-cytochrome c reductase (Complex II and III) isolated by immunoprecipitation from bovine and mouse heart mitochondria
    • Schilling, B.; Murray, J.; Yoo, C. B.; Row, R. H.; Cusack, M. P.; Capaldi, R. A.; Gibson, B. W. Proteomic analysis of succinate dehydrogenase and ubiquinol-cytochrome c reductase (Complex II and III) isolated by immunoprecipitation from bovine and mouse heart mitochondria Biochim. Biophys. Acta 2006, 1762 (2) 213-222
    • (2006) Biochim. Biophys. Acta , vol.1762 , Issue.2 , pp. 213-222
    • Schilling, B.1    Murray, J.2    Yoo, C.B.3    Row, R.H.4    Cusack, M.P.5    Capaldi, R.A.6    Gibson, B.W.7
  • 22
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V.; Seymour, S. L.; Patel, A. A.; Loboda, A.; Tang, W. H.; Keating, S. P.; Hunter, C. L.; Nuwaysir, L. M.; Schaeffer, D. A. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra Mol. Cell. Proteomics 2007, 6 (9) 1638-1655
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 23
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H.; Addona, T.; Burgess, M.; Kuhn, E.; Carr, S. A. Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution Mol. Cell. Proteomics 2007, 6 (12) 2212-2229
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 24
    • 26444539668 scopus 로고    scopus 로고
    • Orthogonality of separation in two-dimensional liquid chromatography
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Orthogonality of separation in two-dimensional liquid chromatography Anal. Chem. 2005, 77 (19) 6426-6434
    • (2005) Anal. Chem. , vol.77 , Issue.19 , pp. 6426-6434
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 25
    • 51549102028 scopus 로고    scopus 로고
    • Comparison of two-dimensional fractionation techniques for shotgun proteomics
    • Dowell, J. A.; Frost, D. C.; Zhang, J.; Li, L. Comparison of two-dimensional fractionation techniques for shotgun proteomics Anal. Chem. 2008, 80 (17) 6715-6723
    • (2008) Anal. Chem. , vol.80 , Issue.17 , pp. 6715-6723
    • Dowell, J.A.1    Frost, D.C.2    Zhang, J.3    Li, L.4
  • 32
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium
    • Osborn, M. J.; Gander, J. E.; Parisi, E; Carson, J. Mechanism of assembly of the outer membrane of Salmonella typhimurium J. Biol. Chem. 1972, 247 (12) 3962-3972
    • (1972) J. Biol. Chem. , vol.247 , Issue.12 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 33
    • 0023187089 scopus 로고
    • Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force
    • De Vrije, T.; Tommassen, J.; De Kruijff, B. Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force Biochim. Biophys. Acta 1987, 900 (1) 63-72
    • (1987) Biochim. Biophys. Acta , vol.900 , Issue.1 , pp. 63-72
    • De Vrije, T.1    Tommassen, J.2    De Kruijff, B.3
  • 35
    • 0036668515 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes
    • Brookes, P. S.; Pinner, A.; Ramachandran, A.; Coward, L.; Barnes, S.; Kim, H.; Darley-Usmar, V. M. High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes Proteomics 2002, 2 (8) 969-977
    • (2002) Proteomics , vol.2 , Issue.8 , pp. 969-977
    • Brookes, P.S.1    Pinner, A.2    Ramachandran, A.3    Coward, L.4    Barnes, S.5    Kim, H.6    Darley-Usmar, V.M.7
  • 36
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi, K.; Yu, F.; Inouye, M. A single amino acid determinant of the membrane localization of lipoproteins in E. coli Cell 1988, 53 (3) 423-432
    • (1988) Cell , vol.53 , Issue.3 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 37
    • 4544384204 scopus 로고    scopus 로고
    • Lipoprotein trafficking in Escherichia coli
    • Narita, S.; Matsuyama, S.; Tokuda, H. Lipoprotein trafficking in Escherichia coli Arch. Microbiol. 2004, 182 (1) 1-6
    • (2004) Arch. Microbiol. , vol.182 , Issue.1 , pp. 1-6
    • Narita, S.1    Matsuyama, S.2    Tokuda, H.3
  • 39
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch, G. L.; Lässle, M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions Bioessays 1999, 21 (11) 932-939
    • (1999) Bioessays , vol.21 , Issue.11 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 40
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea, L. D.; Regan, L. TPR proteins: the versatile helix Trends Biochem. Sci. 2003, 28 (12) 655-662
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.12 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 41
    • 0037569526 scopus 로고    scopus 로고
    • Fishing new proteins in the twilight zone of genomes: The test case of outer membrane proteins in Escherichia coli K12, Escherichia coli O157:H7, and outer Gram-negative bacteria
    • Casadio, R.; Fariselli, P.; Finocchiaro, G.; Martelli, P. L. Fishing new proteins in the twilight zone of genomes: the test case of outer membrane proteins in Escherichia coli K12, Escherichia coli O157:H7, and outer Gram-negative bacteria Protein Sci. 2003, 12 (6) 1158-1168
    • (2003) Protein Sci. , vol.12 , Issue.6 , pp. 1158-1168
    • Casadio, R.1    Fariselli, P.2    Finocchiaro, G.3    Martelli, P.L.4
  • 43
    • 78651335914 scopus 로고    scopus 로고
    • PSORTdb - An expanded, auto-updated, user-friendly protein subcellular localization database for Bacteria and Archaea
    • Yu, N. Y.; Laird, M. R.; Spencer, C.; Brinkman, F. S. L. PSORTdb - an expanded, auto-updated, user-friendly protein subcellular localization database for Bacteria and Archaea Nucleic Acids Res. 2011, 39 (suppl 1) D241-D244
    • (2011) Nucleic Acids Res. , vol.39 , Issue.SUPPL. 1
    • Yu, N.Y.1    Laird, M.R.2    Spencer, C.3    Brinkman, F.S.L.4
  • 45
    • 0031014882 scopus 로고    scopus 로고
    • Structure of TolC, the outer membrane component of the bacterial type i efflux system, derived from two-dimensional crystals
    • Koronakis, V.; Li, J.; Koronakis, E.; Stauffer, K. Structure of TolC, the outer membrane component of the bacterial type I efflux system, derived from two-dimensional crystals Mol. Microbiol. 1997, 23 (3) 617-626
    • (1997) Mol. Microbiol. , vol.23 , Issue.3 , pp. 617-626
    • Koronakis, V.1    Li, J.2    Koronakis, E.3    Stauffer, K.4
  • 46
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R.; Locher, K. P.; Van Gelder, P. Structure and function of bacterial outer membrane proteins: barrels in a nutshell Mol. Microbiol. 2000, 37 (2) 239-253
    • (2000) Mol. Microbiol. , vol.37 , Issue.2 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 47
    • 0029907916 scopus 로고    scopus 로고
    • Structure and functional mechanism of porins
    • Jap, B. K.; Walian, P. J. Structure and functional mechanism of porins Physiol. Rev. 1996, 76 (4) 1073-1088
    • (1996) Physiol. Rev. , vol.76 , Issue.4 , pp. 1073-1088
    • Jap, B.K.1    Walian, P.J.2
  • 48
    • 2642522855 scopus 로고    scopus 로고
    • Crystal structure of the long-chain fatty acid transporter FadL
    • van den Berg, B.; Black, P. N.; Clemons, W. M., Jr.; Rapoport, T. A. Crystal structure of the long-chain fatty acid transporter FadL Science 2004, 304 (5676) 1506-1509
    • (2004) Science , vol.304 , Issue.5676 , pp. 1506-1509
    • Van Den Berg, B.1    Black, P.N.2    Clemons, Jr.W.M.3    Rapoport, T.A.4
  • 49
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn, E. M.; Patel, D. R.; Lepore, B. W.; Indic, M.; van den Berg, B. Transmembrane passage of hydrophobic compounds through a protein channel wall Nature 2009, 458 (7236) 367-371
    • (2009) Nature , vol.458 , Issue.7236 , pp. 367-371
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    Van Den Berg, B.5
  • 50
    • 23044457742 scopus 로고    scopus 로고
    • TonB-dependent trans-envelope signaling: The exception or the rule?
    • Koebnik, R. TonB-dependent trans-envelope signaling: the exception or the rule? Trends Microbiol. 2005, 13 (8) 343-347
    • (2005) Trends Microbiol. , vol.13 , Issue.8 , pp. 343-347
    • Koebnik, R.1
  • 51
    • 0034724567 scopus 로고    scopus 로고
    • High-resolution structure of the OmpA membrane domain
    • Pautsch, A.; Schulz, G. E. High-resolution structure of the OmpA membrane domain J. Mol. Biol. 2000, 298 (2) 273-282
    • (2000) J. Mol. Biol. , vol.298 , Issue.2 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 53
    • 33144490288 scopus 로고    scopus 로고
    • Peptidoglycan recognition by Pal, an outer membrane lipoprotein
    • Parsons, L. M.; Lin, F.; Orban, J. Peptidoglycan recognition by Pal, an outer membrane lipoprotein Biochemistry 2006, 45 (7) 2122-2128
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2122-2128
    • Parsons, L.M.1    Lin, F.2    Orban, J.3
  • 54
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan, C. L.; Kim, S.; Kahne, D. Reconstitution of outer membrane protein assembly from purified components Science 2010, 328 (5980) 890-892
    • (2010) Science , vol.328 , Issue.5980 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 55
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo, P.; Lau, F. K.; Carpentieri, A.; De Castro, C.; Molinaro, A.; Deho, G.; Silhavy, T. J.; Polissi, A. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli J. Bacteriol. 2008, 190 (13) 4460-4469
    • (2008) J. Bacteriol. , vol.190 , Issue.13 , pp. 4460-4469
    • Sperandeo, P.1    Lau, F.K.2    Carpentieri, A.3    De Castro, C.4    Molinaro, A.5    Deho, G.6    Silhavy, T.J.7    Polissi, A.8
  • 56
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu, T.; McCandlish, A. C.; Gronenberg, L. S.; Chng, S.-S.; Silhavy, T. J.; Kahne, D. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (31) 11754-11759
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.31 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.-S.4    Silhavy, T.J.5    Kahne, D.6
  • 58
    • 34447267263 scopus 로고    scopus 로고
    • The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide
    • Valente, F. M. A.; Pereira, P. M.; Venceslau, S. S.; Regalla, M.; Coelho, A. V.; Pereira, I. A.C. The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide FEBS Lett. 2007, 581 (18) 3341-3344
    • (2007) FEBS Lett. , vol.581 , Issue.18 , pp. 3341-3344
    • Valente, F.M.A.1    Pereira, P.M.2    Venceslau, S.S.3    Regalla, M.4    Coelho, A.V.5    Pereira, I.A.C.6
  • 59
    • 34548513979 scopus 로고    scopus 로고
    • Function of periplasmic hydrogenases in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough
    • Caffrey, S. M.; Park, H.-S.; Voordouw, J. K.; He, Z.; Zhou, J.; Voordouw, G. Function of periplasmic hydrogenases in the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough J. Bacteriol. 2007, 189 (17) 6159-6167
    • (2007) J. Bacteriol. , vol.189 , Issue.17 , pp. 6159-6167
    • Caffrey, S.M.1    Park, H.-S.2    Voordouw, J.K.3    He, Z.4    Zhou, J.5    Voordouw, G.6
  • 60
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
    • Kihara, A.; Akiyama, Y.; Ito, K. A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY EMBO J. 1996, 15 (22) 6122-6131
    • (1996) EMBO J. , vol.15 , Issue.22 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 61
    • 77955964940 scopus 로고    scopus 로고
    • Effect of the deletion of qmoABC and the promoter-distal gene encoding a hypothetical protein on sulfate reduction in Desulfovibrio vulgaris Hildenborough
    • Zane, G. M.; Yen, H. B.; Wall, J. D. Effect of the deletion of qmoABC and the promoter-distal gene encoding a hypothetical protein on sulfate reduction in Desulfovibrio vulgaris Hildenborough Appl. Environ. Microbiol. 2010, 76 (16) 5500-5509
    • (2010) Appl. Environ. Microbiol. , vol.76 , Issue.16 , pp. 5500-5509
    • Zane, G.M.1    Yen, H.B.2    Wall, J.D.3


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