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Volumn , Issue , 2006, Pages 83-105

Toxin secretion systems

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EID: 79955877385     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012088445-2/50010-X     Document Type: Chapter
Times cited : (5)

References (222)
  • 1
    • 1842506700 scopus 로고    scopus 로고
    • Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
    • Akeda Y., Galan J.E. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J. Bacteriol. 2004, 186:2402-2412.
    • (2004) J. Bacteriol. , vol.186 , pp. 2402-2412
    • Akeda, Y.1    Galan, J.E.2
  • 2
    • 0027436744 scopus 로고
    • Xcp-mediated protein secretion in Pseudomonas aeruginosa: identification of two additional genes and evidence for regulation of xcp gene expression
    • Akrim M., Bally M., Ball G., Tommassen J., Teerink H., Filloux A., Lazdunski A. Xcp-mediated protein secretion in Pseudomonas aeruginosa: identification of two additional genes and evidence for regulation of xcp gene expression. Mol. Microbiol. 1993, 10:431-443.
    • (1993) Mol. Microbiol. , vol.10 , pp. 431-443
    • Akrim, M.1    Bally, M.2    Ball, G.3    Tommassen, J.4    Teerink, H.5    Filloux, A.6    Lazdunski, A.7
  • 3
    • 0026628961 scopus 로고
    • Polar localization of a bacterial chemoreceptor
    • Alley M.R., Maddock J.R., Shapiro L. Polar localization of a bacterial chemoreceptor. Genes Dev. 1992, 6:825-836.
    • (1992) Genes Dev. , vol.6 , pp. 825-836
    • Alley, M.R.1    Maddock, J.R.2    Shapiro, L.3
  • 4
    • 0642345085 scopus 로고    scopus 로고
    • Channel-tunnels: outer membrane components of type I secretion systems and multidrug efflux pumps of Gram-negative bacteria
    • Andersen C. Channel-tunnels: outer membrane components of type I secretion systems and multidrug efflux pumps of Gram-negative bacteria. Rev. Physiol Biochem. Pharmacol. 2003, 147:122-165.
    • (2003) Rev. Physiol Biochem. Pharmacol. , vol.147 , pp. 122-165
    • Andersen, C.1
  • 6
    • 0036015627 scopus 로고    scopus 로고
    • An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations
    • Andersen C., Koronakis E., Hughes C., Koronakis V. An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations. Mol. Microbiol. 2002, 44:1131-1139.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1131-1139
    • Andersen, C.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 7
    • 0033003131 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ
    • Anderson D.M., Schneewind O. Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ. Mol. Microbiol. 1999, 31:1139-1148.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 8
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson D.M., Schneewind O. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 1997, 278:1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 9
    • 0029840358 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex
    • Anderson L.B., Hertzel A.V., Das A. Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex. Proc. Natl. Acad. Sci. U. S. A 1996, 93:8889-8894.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 8889-8894
    • Anderson, L.B.1    Hertzel, A.V.2    Das, A.3
  • 10
    • 9644272811 scopus 로고    scopus 로고
    • Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion
    • Atmakuri K., Cascales E., Christie P.J. Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion. Mol. Microbiol. 2004, 54:1199-1211.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1199-1211
    • Atmakuri, K.1    Cascales, E.2    Christie, P.J.3
  • 11
    • 0141789692 scopus 로고    scopus 로고
    • VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens
    • Atmakuri K., Ding Z., Christie P.J. VirE2, a type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens. Mol. Microbiol. 2003, 49:1699-1713.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1699-1713
    • Atmakuri, K.1    Ding, Z.2    Christie, P.J.3
  • 12
    • 0034968828 scopus 로고    scopus 로고
    • RpoS co-operates with other factors to induce Legionella pneumophila virulence in the stationary phase
    • Bachman M.A., Swanson M.S. RpoS co-operates with other factors to induce Legionella pneumophila virulence in the stationary phase. Mol. Microbiol. 2001, 40:1201-1214.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1201-1214
    • Bachman, M.A.1    Swanson, M.S.2
  • 13
    • 0035955547 scopus 로고    scopus 로고
    • Substratetriggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli
    • Balakrishnan L., Hughes C., Koronakis V. Substratetriggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli. J. Mol. Biol. 2001, 313:501-510.
    • (2001) J. Mol. Biol. , vol.313 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3
  • 14
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball G., Chapon-Herve V., Bleves S., Michel G., Bally M. Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J. Bacteriol. 1999, 181:382-388.
    • (1999) J. Bacteriol. , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Herve, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 15
    • 0031050787 scopus 로고    scopus 로고
    • The lipoprotein VirB7 interacts with VirB9 in the membranes of Agrobacterium tumefaciens
    • Baron C., Thorstenson Y.R., Zambryski P.C. The lipoprotein VirB7 interacts with VirB9 in the membranes of Agrobacterium tumefaciens. J. Bacteriol. 1997, 179:1211-1218.
    • (1997) J. Bacteriol. , vol.179 , pp. 1211-1218
    • Baron, C.1    Thorstenson, Y.R.2    Zambryski, P.C.3
  • 16
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks B.C. A common export pathway for proteins binding complex redox cofactors?. Mol. Microbiol. 1996, 22:393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 19
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan S.C., Phillips R.M., Ghosh P. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol. Cell 2002, 9:971-980.
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 20
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • Bitter W., Koster M., Latijnhouwers M., de C.H., Tommassen J. Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol. Microbiol. 1998, 27:209-219.
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    de, C.H.4    Tommassen, J.5
  • 21
    • 0035150176 scopus 로고    scopus 로고
    • Specificity of signal peptide recognition in tat-dependent bacterial protein translocation
    • Blaudeck N., Sprenger G.A., Freudl R., Wiegert T. Specificity of signal peptide recognition in tat-dependent bacterial protein translocation. J. Bacteriol. 2001, 183:604-610.
    • (2001) J. Bacteriol. , vol.183 , pp. 604-610
    • Blaudeck, N.1    Sprenger, G.A.2    Freudl, R.3    Wiegert, T.4
  • 22
    • 0031983197 scopus 로고    scopus 로고
    • The secretion apparatus of Pseudomonas aeruginosa: identification of a fifth pseudopilin, XcpX (GspK family)
    • Bleves S., Voulhoux R., Michel G., Lazdunski A., Tommassen J., Filloux A. The secretion apparatus of Pseudomonas aeruginosa: identification of a fifth pseudopilin, XcpX (GspK family). Mol. Microbiol. 1998, 27:31-40.
    • (1998) Mol. Microbiol. , vol.27 , pp. 31-40
    • Bleves, S.1    Voulhoux, R.2    Michel, G.3    Lazdunski, A.4    Tommassen, J.5    Filloux, A.6
  • 24
    • 0032541133 scopus 로고    scopus 로고
    • An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria
    • Bogsch E.G., Sargent F., Stanley N.R., Berks B.C., Robinson C., Palmer T. An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. J. Biol. Chem. 1998, 273:18003-18006.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18003-18006
    • Bogsch, E.G.1    Sargent, F.2    Stanley, N.R.3    Berks, B.C.4    Robinson, C.5    Palmer, T.6
  • 25
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis A., Mathers J.E., Thomas J.D., Barrett C.M., Robinson C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 2001, 276:20213-20219.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
  • 26
    • 0028282814 scopus 로고
    • Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi
    • Bortoli-German I., Brun E., Py B., Chippaux M., Barras F. Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi. Mol. Microbiol. 1994, 11:545-553.
    • (1994) Mol. Microbiol. , vol.11 , pp. 545-553
    • Bortoli-German, I.1    Brun, E.2    Py, B.3    Chippaux, M.4    Barras, F.5
  • 27
    • 0030029288 scopus 로고    scopus 로고
    • Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa
    • Braun P., Tommassen J., Filloux A. Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. Mol. Microbiol. 1996, 19:297-306.
    • (1996) Mol. Microbiol. , vol.19 , pp. 297-306
    • Braun, P.1    Tommassen, J.2    Filloux, A.3
  • 29
    • 0036646473 scopus 로고    scopus 로고
    • Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
    • Buchwald G., Friebel A., Galan J.E., Hardt W.D., Wittinghofer A., Scheffzek K. Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE. EMBO J. 2002, 21:3286-3295.
    • (2002) EMBO J. , vol.21 , pp. 3286-3295
    • Buchwald, G.1    Friebel, A.2    Galan, J.E.3    Hardt, W.D.4    Wittinghofer, A.5    Scheffzek, K.6
  • 30
    • 0036900016 scopus 로고    scopus 로고
    • Assembly of cell division proteins at the E. coli cell center
    • Buddelmeijer N., Beckwith J. Assembly of cell division proteins at the E. coli cell center. Curr. Opin. Microbiol. 2002, 5:553-557.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 553-557
    • Buddelmeijer, N.1    Beckwith, J.2
  • 31
    • 0037327351 scopus 로고    scopus 로고
    • Type IV transporters of pathogenic bacteria
    • Burns D.L. Type IV transporters of pathogenic bacteria. Curr. Opin. Microbiol. 2003, 6:29-34.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 29-34
    • Burns, D.L.1
  • 32
    • 11144271157 scopus 로고    scopus 로고
    • Molecular Analysis of the Vibrio cholerae Type II Secretion ATPase EpsE
    • Camberg J.L., Sandkvist M. Molecular Analysis of the Vibrio cholerae Type II Secretion ATPase EpsE. J. Bacteriol. 2005, 187:249-256.
    • (2005) J. Bacteriol. , vol.187 , pp. 249-256
    • Camberg, J.L.1    Sandkvist, M.2
  • 33
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV secretion systems
    • Cascales E., Christie P.J. The versatile bacterial type IV secretion systems. Nat. Rev. Microbiol. 2003, 1:137-149.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 34
    • 2442682800 scopus 로고    scopus 로고
    • Definition of a bacterial type IV secretion pathway for a DNA substrate
    • Cascales E., Christie P.J. Definition of a bacterial type IV secretion pathway for a DNA substrate. Science 2004, 304:1170-1173.
    • (2004) Science , vol.304 , pp. 1170-1173
    • Cascales, E.1    Christie, P.J.2
  • 35
    • 0026698151 scopus 로고
    • Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
    • Chang C.H., Winans S.C. Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein. J. Bacteriol. 1992, 174:7033-7039.
    • (1992) J. Bacteriol. , vol.174 , pp. 7033-7039
    • Chang, C.H.1    Winans, S.C.2
  • 36
    • 0035958760 scopus 로고    scopus 로고
    • Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi
    • Chapon V., Czjzek M., El H.M., Py B., Juy M., Barras F. Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi. J. Mol. Biol. 2001, 310:1055-1066.
    • (2001) J. Mol. Biol. , vol.310 , pp. 1055-1066
    • Chapon, V.1    Czjzek, M.2    El, H.M.3    Py, B.4    Juy, M.5    Barras, F.6
  • 37
    • 8844259469 scopus 로고    scopus 로고
    • Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems
    • Christie P.J. Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems. Biochim. Biophys. Acta 2004, 1694:219-234.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 219-234
    • Christie, P.J.1
  • 39
    • 0035920363 scopus 로고    scopus 로고
    • Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport
    • Cline K., Mori H. Thylakoid DeltapH-dependent precursor proteins bind to a cpTatC-Hcf106 complex before Tha4-dependent transport. J. Cell Biol. 2001, 154:719-729.
    • (2001) J. Cell Biol. , vol.154 , pp. 719-729
    • Cline, K.1    Mori, H.2
  • 40
    • 0024294402 scopus 로고
    • The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
    • Collier D.N., Bankaitis V.A., Weiss J.B., Bassford P.J. The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Cell 1988, 53:273-283.
    • (1988) Cell , vol.53 , pp. 273-283
    • Collier, D.N.1    Bankaitis, V.A.2    Weiss, J.B.3    Bassford, P.J.4
  • 41
    • 0029089690 scopus 로고
    • Initial studies of the structural signal for extracellular transport of cholera toxin and other proteins recognized by Vibrio cholerae
    • Connell T.D., Metzger D.J., Wang M., Jobling M.G., Holmes R.K. Initial studies of the structural signal for extracellular transport of cholera toxin and other proteins recognized by Vibrio cholerae. Infect. Immun. 1995, 63:4091-4098.
    • (1995) Infect. Immun. , vol.63 , pp. 4091-4098
    • Connell, T.D.1    Metzger, D.J.2    Wang, M.3    Jobling, M.G.4    Holmes, R.K.5
  • 42
    • 0026816008 scopus 로고
    • Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria
    • Coote J.G. Structural and functional relationships among the RTX toxin determinants of gram-negative bacteria. FEMS Microbiol. Rev. 1992, 8:137-161.
    • (1992) FEMS Microbiol. Rev. , vol.8 , pp. 137-161
    • Coote, J.G.1
  • 43
    • 0023255341 scopus 로고
    • Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes
    • Cornelis G., Vanootegem J.C., Sluiters C. Transcription of the yop regulon from Y. enterocolitica requires trans acting pYV and chromosomal genes. Microb. Pathog. 1987, 2:367-379.
    • (1987) Microb. Pathog. , vol.2 , pp. 367-379
    • Cornelis, G.1    Vanootegem, J.C.2    Sluiters, C.3
  • 44
    • 0345257863 scopus 로고    scopus 로고
    • How Yops find their way out of Yersinia
    • Cornelis G.R. How Yops find their way out of Yersinia. Mol. Microbiol. 2003, 50:1091-1094.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1091-1094
    • Cornelis, G.R.1
  • 45
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis G.R., Van G.F. Assembly and function of type III secretory systems. Annu. Rev. Microbiol. 2000, 54:735-774.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van, G.F.2
  • 46
    • 0024384953 scopus 로고
    • Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion
    • d'Enfert C., Pugsley A.P. Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion. J. Bacteriol. 1989, 171:3673-3679.
    • (1989) J. Bacteriol. , vol.171 , pp. 3673-3679
    • d'Enfert, C.1    Pugsley, A.P.2
  • 47
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert C., Ryter A., Pugsley A.P. Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J. 1987, 6:3531-3538.
    • (1987) EMBO J. , vol.6 , pp. 3531-3538
    • d'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 48
    • 0034525943 scopus 로고    scopus 로고
    • Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins
    • Dalbey R.E., Kuhn A. Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins. Annu. Rev. Cell Dev. Biol. 2000, 16:51-87.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 51-87
    • Dalbey, R.E.1    Kuhn, A.2
  • 49
    • 0030998468 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type 1 signal peptidases
    • Dalbey R.E., Lively M.O., Bron S., van Dijl J.M. The chemistry and enzymology of the type 1 signal peptidases. Protein Sci. 1997, 6:1129-1138.
    • (1997) Protein Sci. , vol.6 , pp. 1129-1138
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    van Dijl, J.M.4
  • 50
    • 0031014646 scopus 로고    scopus 로고
    • The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface
    • Dang T.A., Christie P.J. The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface. J. Bacteriol. 1997, 179:453-462.
    • (1997) J. Bacteriol. , vol.179 , pp. 453-462
    • Dang, T.A.1    Christie, P.J.2
  • 52
    • 0035154988 scopus 로고    scopus 로고
    • The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced
    • Darwin A.J., Miller V.L. The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced. Mol. Microbiol. 2001, 39:429-444.
    • (2001) Mol. Microbiol. , vol.39 , pp. 429-444
    • Darwin, A.J.1    Miller, V.L.2
  • 53
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson A.L., Chen J. ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 2004, 73:241-268.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 54
    • 0242439351 scopus 로고    scopus 로고
    • The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins
    • de Gier J.W., Luirink J. The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins. EMBO Rep. 2003, 4:939-943.
    • (2003) EMBO Rep. , vol.4 , pp. 939-943
    • de Gier, J.W.1    Luirink, J.2
  • 55
    • 0026056071 scopus 로고
    • Conservation of xcp genes, involved in the two-step protein secretion process, in different Pseudomonas species and other gram-negative bacteria
    • de G.A., Filloux A., Tommassen J. Conservation of xcp genes, involved in the two-step protein secretion process, in different Pseudomonas species and other gram-negative bacteria. Mol. Gen. Genet. 1991, 229:278-284.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 278-284
    • de, G.A.1    Filloux, A.2    Tommassen, J.3
  • 56
    • 0035148762 scopus 로고    scopus 로고
    • Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognition
    • de G.A., Koster M., Gerard-Vincent M., Gerritse G., Lazdunski A., Tommassen J., Filloux A. Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognition. J. Bacteriol. 2001, 183:959-967.
    • (2001) J. Bacteriol. , vol.183 , pp. 959-967
    • de, G.A.1    Koster, M.2    Gerard-Vincent, M.3    Gerritse, G.4    Lazdunski, A.5    Tommassen, J.6    Filloux, A.7
  • 57
    • 0035812905 scopus 로고    scopus 로고
    • Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
    • De L.E., Porcelli I., Sargent F., Palmer T., Berks B.C. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 2001, 506:143-148.
    • (2001) FEBS Lett. , vol.506 , pp. 143-148
    • De, L.E.1    Porcelli, I.2    Sargent, F.3    Palmer, T.4    Berks, B.C.5
  • 58
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa M.P., Tullman D., Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc. Natl. Acad. Sci. U. S. A 2003, 100:6115-6120.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 61
    • 0034943923 scopus 로고    scopus 로고
    • A variable genetic island specific for Neisseria gonorrhoeae is involved in providing DNA for natural transformation and is found more often in disseminated infection isolates
    • Dillard J.P., Seifert H.S. A variable genetic island specific for Neisseria gonorrhoeae is involved in providing DNA for natural transformation and is found more often in disseminated infection isolates. Mol. Microbiol. 2001, 41:263-277.
    • (2001) Mol. Microbiol. , vol.41 , pp. 263-277
    • Dillard, J.P.1    Seifert, H.S.2
  • 62
    • 1342302802 scopus 로고    scopus 로고
    • Systematic analysis, by the yeast two-hybrid, of protein interaction between components of the type II secretory machinery of Erwinia chrysanthemi
    • Douet V., Loiseau L., Barras F., Py B. Systematic analysis, by the yeast two-hybrid, of protein interaction between components of the type II secretory machinery of Erwinia chrysanthemi. Res. Microbiol. 2004, 155:71-75.
    • (2004) Res. Microbiol. , vol.155 , pp. 71-75
    • Douet, V.1    Loiseau, L.2    Barras, F.3    Py, B.4
  • 63
    • 0342437484 scopus 로고    scopus 로고
    • Lack of copper insertion into unprocessed cytoplasmic nitrous oxide reductase generated by an R20D substitution in the arginine consensus motif of the signal peptide
    • Dreusch A., Burgisser D.M., Heizmann C.W., Zumft W.G. Lack of copper insertion into unprocessed cytoplasmic nitrous oxide reductase generated by an R20D substitution in the arginine consensus motif of the signal peptide. Biochim. Biophys. Acta 1997, 1319:311-318.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 311-318
    • Dreusch, A.1    Burgisser, D.M.2    Heizmann, C.W.3    Zumft, W.G.4
  • 65
    • 0030745847 scopus 로고    scopus 로고
    • The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
    • Duong F., Wickner W. The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling. EMBO J. 1997, 16:4871-4879.
    • (1997) EMBO J. , vol.16 , pp. 4871-4879
    • Duong, F.1    Wickner, W.2
  • 66
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure
    • Durand E., Bernadac A., Ball G., Lazdunski A., Sturgis J.N., Filloux A. Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J. Bacteriol. 2003, 185:2749-2758.
    • (2003) J. Bacteriol. , vol.185 , pp. 2749-2758
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 67
    • 0032996078 scopus 로고    scopus 로고
    • Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor
    • El K.M., Ockhuijsen C., Bitter W., Jaeger K.E., Tommassen J. Specificity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor. Mol. Gen. Genet. 1999, 261:770-776.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 770-776
    • El, K.M.1    Ockhuijsen, C.2    Bitter, W.3    Jaeger, K.E.4    Tommassen, J.5
  • 69
    • 0037459244 scopus 로고    scopus 로고
    • Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus
    • Eswaran J., Hughes C., Koronakis V. Locking TolC entrance helices to prevent protein translocation by the bacterial type I export apparatus. J. Mol. Biol. 2003, 327:309-315.
    • (2003) J. Mol. Biol. , vol.327 , pp. 309-315
    • Eswaran, J.1    Hughes, C.2    Koronakis, V.3
  • 70
    • 0037321748 scopus 로고    scopus 로고
    • Mucosal priming of simian immunodeficiency virus-specific cytotoxic T-lymphocyte responses in rhesus macaques by the Salmonella type III secretion antigen delivery system
    • Evans D.T., et al. Mucosal priming of simian immunodeficiency virus-specific cytotoxic T-lymphocyte responses in rhesus macaques by the Salmonella type III secretion antigen delivery system. J. Virol. 2003, 77:2400-2409.
    • (2003) J. Virol. , vol.77 , pp. 2400-2409
    • Evans, D.T.1
  • 71
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • Fekkes P., van der D.C., Driessen A.J. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J. 1997, 16:6105-6113.
    • (1997) EMBO J. , vol.16 , pp. 6105-6113
    • Fekkes, P.1    van der, D.C.2    Driessen, A.J.3
  • 72
    • 0025608578 scopus 로고
    • Protein secretion in gram-negative bacteria: transport across the outer membrane involves common mechanisms in different bacteria
    • Filloux A., Bally M., Ball G., Akrim M., Tommassen J., Lazdunski A. Protein secretion in gram-negative bacteria: transport across the outer membrane involves common mechanisms in different bacteria. EMBO J. 1990, 9:4323-4329.
    • (1990) EMBO J. , vol.9 , pp. 4323-4329
    • Filloux, A.1    Bally, M.2    Ball, G.3    Akrim, M.4    Tommassen, J.5    Lazdunski, A.6
  • 73
    • 0027310249 scopus 로고
    • Analysis of enterotoxin synthesis in a Vibrio cholerae strain lacking DsbA, a periplasmic enzyme involved in disulphide bond formation
    • Findlay G., Yu J., Hirst T.R. Analysis of enterotoxin synthesis in a Vibrio cholerae strain lacking DsbA, a periplasmic enzyme involved in disulphide bond formation. Biochem. Soc. Trans. 1993, 21:212S.
    • (1993) Biochem. Soc. Trans. , vol.21
    • Findlay, G.1    Yu, J.2    Hirst, T.R.3
  • 74
    • 0029796966 scopus 로고    scopus 로고
    • Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli
    • Fralick J.A. Evidence that TolC is required for functioning of the Mar/AcrAB efflux pump of Escherichia coli. J. Bacteriol. 1996, 178:5803-5805.
    • (1996) J. Bacteriol. , vol.178 , pp. 5803-5805
    • Fralick, J.A.1
  • 76
    • 0030922964 scopus 로고    scopus 로고
    • Intracellular targeting of exoenzyme S of Pseudomonas aeruginosa via type III-dependent translocation induces phagocytosis resistance, cytotoxicity and disruption of actin microfilaments
    • Frithz-Lindsten E., Du Y., Rosqvist R., Forsberg A. Intracellular targeting of exoenzyme S of Pseudomonas aeruginosa via type III-dependent translocation induces phagocytosis resistance, cytotoxicity and disruption of actin microfilaments. Mol. Microbiol. 1997, 25:1125-1139.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1125-1139
    • Frithz-Lindsten, E.1    Du, Y.2    Rosqvist, R.3    Forsberg, A.4
  • 77
    • 0035188434 scopus 로고    scopus 로고
    • Salmonella interactions with host cells: type III secretion at work
    • Galan J.E. Salmonella interactions with host cells: type III secretion at work. Annu. Rev. Cell Dev. Biol. 2001, 17:53-86.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 53-86
    • Galan, J.E.1
  • 78
    • 0027430730 scopus 로고
    • Shigella subversion of the cellular cytoskeleton: a strategy for epithelial colonization
    • Goldberg M.B., Sansonetti P.J. Shigella subversion of the cellular cytoskeleton: a strategy for epithelial colonization. Infect. Immun. 1993, 61:4941-4946.
    • (1993) Infect. Immun. , vol.61 , pp. 4941-4946
    • Goldberg, M.B.1    Sansonetti, P.J.2
  • 79
    • 0034923461 scopus 로고    scopus 로고
    • Structure of TrwB, a gatekeeper in bacterial conjugation
    • Gomis-Ruth F.X., Coll M. Structure of TrwB, a gatekeeper in bacterial conjugation. Int. J. Biochem. Cell Biol. 2001, 33:839-843.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 839-843
    • Gomis-Ruth, F.X.1    Coll, M.2
  • 80
    • 0036510408 scopus 로고    scopus 로고
    • Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein. Detailed structural features and mapping of the active site cleft
    • Gomis-Ruth F.X., Moncalian G., de la C.F., Coll M. Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein. Detailed structural features and mapping of the active site cleft. J. Biol. Chem. 2002, 277:7556-7566.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7556-7566
    • Gomis-Ruth, F.X.1    Moncalian, G.2    de la, C.F.3    Coll, M.4
  • 81
    • 0032885925 scopus 로고    scopus 로고
    • The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from wolinella succinogenes
    • Gross R., Simon J., Kroger A. The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from wolinella succinogenes. Arch. Microbiol. 1999, 172:227-232.
    • (1999) Arch. Microbiol. , vol.172 , pp. 227-232
    • Gross, R.1    Simon, J.2    Kroger, A.3
  • 82
    • 0033565687 scopus 로고    scopus 로고
    • The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
    • Halbig D., Wiegert T., Blaudeck N., Freudl R., Sprenger G.A. The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding. Eur. J. Biochem. 1999, 263:543-551.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 543-551
    • Halbig, D.1    Wiegert, T.2    Blaudeck, N.3    Freudl, R.4    Sprenger, G.A.5
  • 83
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions
    • Hardie K.R., Seydel A., Guilvout I., Pugsley A.P. The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol. Microbiol. 1996, 22:967-976.
    • (1996) Mol. Microbiol. , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsley, A.P.4
  • 84
    • 0002588630 scopus 로고
    • Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro
    • Hardy S.J., Holmgren J., Johansson S., Sanchez J., Hirst T.R. Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro. Proc. Natl. Acad. Sci. U. S. A 1988, 85:7109-7113.
    • (1988) Proc. Natl. Acad. Sci. U. S. A , vol.85 , pp. 7109-7113
    • Hardy, S.J.1    Holmgren, J.2    Johansson, S.3    Sanchez, J.4    Hirst, T.R.5
  • 85
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F.U., Lecker S., Schiebel E., Hendrick J.P., Wickner W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 1990, 63:269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 86
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson I.R., Nataro J.P. Virulence functions of autotransporter proteins. Infect. Immun. 2001, 69:1231-1243.
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 87
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: structure and function of the autotransporter proteins
    • Henderson I.R., Navarro-Garcia F., Nataro J.P. The great escape: structure and function of the autotransporter proteins. Trends Microbiol. 1998, 6:370-378.
    • (1998) Trends Microbiol. , vol.6 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 88
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae
    • Hirst T.R., Holmgren J. Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae. Proc. Natl. Acad. Sci. U. S. A 1987, 84:7418-7422.
    • (1987) Proc. Natl. Acad. Sci. U. S. A , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 89
    • 0023144553 scopus 로고
    • Transient entry of enterotoxin subunits into the periplasm occurs during their secretion from Vibrio cholerae
    • Hirst T.R., Holmgren J. Transient entry of enterotoxin subunits into the periplasm occurs during their secretion from Vibrio cholerae. J. Bacteriol. 1987, 169:1037-1045.
    • (1987) J. Bacteriol. , vol.169 , pp. 1037-1045
    • Hirst, T.R.1    Holmgren, J.2
  • 90
    • 0034903021 scopus 로고    scopus 로고
    • Natural transformation competence in Helicobacter pyrlori is mediated by the basic components of a type IV secretion system
    • Hofreuter D., Odenbreit S., Haas R. Natural transformation competence in Helicobacter pyrlori is mediated by the basic components of a type IV secretion system. Mol. Microbiol. 2001, 41:379-391.
    • (2001) Mol. Microbiol. , vol.41 , pp. 379-391
    • Hofreuter, D.1    Odenbreit, S.2    Haas, R.3
  • 91
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk E., Blobel G. Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc. Natl. Acad. Sci. U. S. A 2001, 98:4669-4674.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 4669-4674
    • Hoiczyk, E.1    Blobel, G.2
  • 92
    • 0029828324 scopus 로고    scopus 로고
    • A TonB-like protein and a novel membrane protein containing an ATP-binding cassette function together in exotoxin secretion
    • Howard S.P., Meiklejohn H.G., Shivak D., Jahagirdar R. A TonB-like protein and a novel membrane protein containing an ATP-binding cassette function together in exotoxin secretion. Mol. Microbiol. 1996, 22:595-604.
    • (1996) Mol. Microbiol. , vol.22 , pp. 595-604
    • Howard, S.P.1    Meiklejohn, H.G.2    Shivak, D.3    Jahagirdar, R.4
  • 93
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 1998, 62:379-433.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 94
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung L.W., Wang I.X., Nikaido K., Liu P.Q., Ames G.F., Kim S.H. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 1998, 396:703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 95
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 2002, 297:2018-2026.
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 96
    • 0030858697 scopus 로고    scopus 로고
    • Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion proteinfamily, interacts with CvaB and TolC
    • Hwang J., Zhong X., Tai P.C. Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion proteinfamily, interacts with CvaB and TolC. J. Bacteriol. 1997, 179:6264-6270.
    • (1997) J. Bacteriol. , vol.179 , pp. 6264-6270
    • Hwang, J.1    Zhong, X.2    Tai, P.C.3
  • 97
    • 0036088769 scopus 로고    scopus 로고
    • Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery
    • Ignatova Z., Hornle C., Nurk A., Kasche V. Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 2002, 291:146-149.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 146-149
    • Ignatova, Z.1    Hornle, C.2    Nurk, A.3    Kasche, V.4
  • 98
    • 0032929404 scopus 로고    scopus 로고
    • Identification of SycN, YscX, and YscY, three new elements of the Yersinia yop virulon
    • Iriarte M., Cornelis G.R. Identification of SycN, YscX, and YscY, three new elements of the Yersinia yop virulon. J. Bacteriol. 1999, 181:675-680.
    • (1999) J. Bacteriol. , vol.181 , pp. 675-680
    • Iriarte, M.1    Cornelis, G.R.2
  • 101
    • 0035118223 scopus 로고    scopus 로고
    • Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth
    • Jack R.L., Sargent F., Berks B.C., Sawers G., Palmer T. Constitutive expression of Escherichia coli tat genes indicates an important role for the twin-arginine translocase during aerobic and anaerobic growth. J. Bacteriol. 2001, 183:1801-1804.
    • (2001) J. Bacteriol. , vol.183 , pp. 1801-1804
    • Jack, R.L.1    Sargent, F.2    Berks, B.C.3    Sawers, G.4    Palmer, T.5
  • 102
    • 0031682153 scopus 로고    scopus 로고
    • YscB of Yersinia pestis functions as a specific chaperone for YopN
    • Jackson M.W., Day J.B., Plano G.V. YscB of Yersinia pestis functions as a specific chaperone for YopN. J. Bacteriol. 1998, 180:4912-4921.
    • (1998) J. Bacteriol. , vol.180 , pp. 4912-4921
    • Jackson, M.W.1    Day, J.B.2    Plano, G.V.3
  • 103
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson F., Locht C., Antoine R. Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol. Microbiol. 2001, 40:306-313.
    • (2001) Mol. Microbiol. , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 104
    • 0028151687 scopus 로고
    • Isolation and characterization of a second exe operon required for extracellular protein secretion in Aeromonas hydrophila
    • Jahagirdar R., Howard S.P. Isolation and characterization of a second exe operon required for extracellular protein secretion in Aeromonas hydrophila. J. Bacteriol. 1994, 176:6819-6826.
    • (1994) J. Bacteriol. , vol.176 , pp. 6819-6826
    • Jahagirdar, R.1    Howard, S.P.2
  • 105
    • 3843139431 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB6 domains direct the ordered export of a DNA substrate through a type IV secretion System
    • Jakubowski S.J., Krishnamoorthy V., Cascales E., Christie P.J. Agrobacterium tumefaciens VirB6 domains direct the ordered export of a DNA substrate through a type IV secretion System. J. Mol. Biol. 2004, 341:961-977.
    • (2004) J. Mol. Biol. , vol.341 , pp. 961-977
    • Jakubowski, S.J.1    Krishnamoorthy, V.2    Cascales, E.3    Christie, P.J.4
  • 106
    • 0037407708 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB6 protein participates in formation of VirB7 and VirB9 complexes required for type IV secretion
    • Jakubowski S.J., Krishnamoorthy V., Christie P.J. Agrobacterium tumefaciens VirB6 protein participates in formation of VirB7 and VirB9 complexes required for type IV secretion. J. Bacteriol. 2003, 185:2867-2878.
    • (2003) J. Bacteriol. , vol.185 , pp. 2867-2878
    • Jakubowski, S.J.1    Krishnamoorthy, V.2    Christie, P.J.3
  • 107
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: towards a functional architecture
    • Jones P.M., George A.M. Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol. Lett. 1999, 179:187-202.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 108
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L., Agrain C., Broz P., Cornelis G.R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 2003, 302:1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 109
    • 0031962224 scopus 로고    scopus 로고
    • Type II protein secretion by Pseudomonas aeruginosa: genetic suppression of a conditional mutation in the pilin-like component XcpT by the cytoplasmic component XcpR
    • Kagami Y., Ratliff M., Surber M., Martinez A., Nunn D.N. Type II protein secretion by Pseudomonas aeruginosa: genetic suppression of a conditional mutation in the pilin-like component XcpT by the cytoplasmic component XcpR. Mol. Microbiol. 1998, 27:221-233.
    • (1998) Mol. Microbiol. , vol.27 , pp. 221-233
    • Kagami, Y.1    Ratliff, M.2    Surber, M.3    Martinez, A.4    Nunn, D.N.5
  • 110
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • Kihara A., Akiyama Y., Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. U. S. A 1995, 92:4532-4536.
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 111
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: the bacterial exit duct for proteins and drugs
    • Koronakis V., Eswaran J., Hughes C. Structure and function of TolC: the bacterial exit duct for proteins and drugs. Annu. Rev. Biochem. 2004, 73:467-489.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 112
    • 0024386073 scopus 로고
    • Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes
    • Koronakis V., Koronakis E., Hughes C. Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes. EMBO J. 1989, 8:595-605.
    • (1989) EMBO J. , vol.8 , pp. 595-605
    • Koronakis, V.1    Koronakis, E.2    Hughes, C.3
  • 113
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 2000, 405:914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 114
    • 0037143720 scopus 로고    scopus 로고
    • Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens
    • Krall L., Wiedemann U., Unsin G., Weiss S., Domke N., Baron C. Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens. Proc. Natl. Acad. Sci. U. S. A 2002, 99:11405-11410.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 11405-11410
    • Krall, L.1    Wiedemann, U.2    Unsin, G.3    Weiss, S.4    Domke, N.5    Baron, C.6
  • 116
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
    • Kubori T., Sukhan A., Aizawa S.I., Galan J.E. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc. Natl. Acad. Sci. U. S. A 2000, 97:10225-10230.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 117
    • 0020536194 scopus 로고
    • Mutations in a new gene, secB, cause defective protein localization in Escherichia coli
    • Kumamoto C.A., Beckwith J. Mutations in a new gene, secB, cause defective protein localization in Escherichia coli. J. Bacteriol. 1983, 154:253-260.
    • (1983) J. Bacteriol. , vol.154 , pp. 253-260
    • Kumamoto, C.A.1    Beckwith, J.2
  • 118
    • 0036268202 scopus 로고    scopus 로고
    • Polar location and functional domains of the Agrobacterium tumefaciens DNA transfer protein VirD4
    • Kumar R.B., Das A. Polar location and functional domains of the Agrobacterium tumefaciens DNA transfer protein VirD4. Mol. Microbiol. 2002, 43:1523-1532.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1523-1532
    • Kumar, R.B.1    Das, A.2
  • 119
    • 0036136240 scopus 로고    scopus 로고
    • Biogenesis of T pili in Agrobacterium tumefaciens requires precise VirB2 propilin cleavage and cyclization
    • Lai E.M., Eisenbrandt R., Kalkum M., Lanka E., Kado C.I. Biogenesis of T pili in Agrobacterium tumefaciens requires precise VirB2 propilin cleavage and cyclization. J. Bacteriol. 2002, 184:327-330.
    • (2002) J. Bacteriol. , vol.184 , pp. 327-330
    • Lai, E.M.1    Eisenbrandt, R.2    Kalkum, M.3    Lanka, E.4    Kado, C.I.5
  • 120
    • 0026542646 scopus 로고
    • Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica
    • Lambert de R.C., Sluiters C., Cornelis G.R. Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol. Microbiol. 1992, 6:395-409.
    • (1992) Mol. Microbiol. , vol.6 , pp. 395-409
    • Lambert de, R.C.1    Sluiters, C.2    Cornelis, G.R.3
  • 122
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • Lee S.H., Galan J.E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 2004, 51:483-495.
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galan, J.E.2
  • 123
    • 0034889276 scopus 로고    scopus 로고
    • A program of Yersinia enterocolitica type III secretion reactions is activated by specific signals
    • Lee V.T., Mazmanian S.K., Schneewind O. A program of Yersinia enterocolitica type III secretion reactions is activated by specific signals. J. Bacteriol. 2001, 183:4970-4978.
    • (2001) J. Bacteriol. , vol.183 , pp. 4970-4978
    • Lee, V.T.1    Mazmanian, S.K.2    Schneewind, O.3
  • 124
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage pIV multimer visualized by scanning transmission electron microscopy
    • Linderoth N.A., Simon M.N., Russel M. The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 1997, 278:1635-1638.
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1    Simon, M.N.2    Russel, M.3
  • 126
    • 3142587123 scopus 로고    scopus 로고
    • Euroconference on the Biology of Type IV Secretion Processes: bacterial gates into the outer world
    • Llosa M., O'Callaghan D. Euroconference on the Biology of Type IV Secretion Processes: bacterial gates into the outer world. Mol. Microbiol. 2004, 53:1-8.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1-8
    • Llosa, M.1    O'Callaghan, D.2
  • 127
    • 0042838290 scopus 로고    scopus 로고
    • Conjugative coupling proteinsinteract with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes
    • Llosa M., Zunzunegui S., de la C.F. Conjugative coupling proteinsinteract with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes. Proc. Natl. Acad. Sci. U. S. A 2003, 100:10465-10470.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 10465-10470
    • Llosa, M.1    Zunzunegui, S.2    de la, C.F.3
  • 128
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd S.A., Norman M., Rosqvist R., Wolf-Watz H. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol. Microbiol. 2001, 39:520-531.
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 129
    • 0030065420 scopus 로고    scopus 로고
    • A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosa
    • Lu H.M., Lory S. A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosa. EMBO J. 1996, 15:429-436.
    • (1996) EMBO J. , vol.15 , pp. 429-436
    • Lu, H.M.1    Lory, S.2
  • 130
    • 8844239874 scopus 로고    scopus 로고
    • SRP-mediated protein targeting: structure and function revisited
    • Luirink J., Sinning I. SRP-mediated protein targeting: structure and function revisited. Biochim. Biophys. Acta 2004, 1694:17-35.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 17-35
    • Luirink, J.1    Sinning, I.2
  • 131
    • 1642514882 scopus 로고    scopus 로고
    • Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer
    • Luo Z.Q., Isberg R.R. Multiple substrates of the Legionella pneumophila Dot/Icm system identified by interbacterial protein transfer. Proc. Natl. Acad. Sci. U. S. A 2004, 101:841-846.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , pp. 841-846
    • Luo, Z.Q.1    Isberg, R.R.2
  • 133
    • 0029417210 scopus 로고
    • Toxin A secretion in Pseudomonas aeruginosa: the role of the first 30 amino acids of the mature toxin
    • McVay C.S., Hamood A.N. Toxin A secretion in Pseudomonas aeruginosa: the role of the first 30 amino acids of the mature toxin. Mol. Gen. Genet. 1995, 249:515-525.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 515-525
    • McVay, C.S.1    Hamood, A.N.2
  • 134
    • 0024458990 scopus 로고
    • Environmental regulation of expression of virulence determinants in Bordetella pertussis
    • Melton A.R., Weiss A.A. Environmental regulation of expression of virulence determinants in Bordetella pertussis. J. Bacteriol. 1989, 171:6206-6212.
    • (1989) J. Bacteriol. , vol.171 , pp. 6206-6212
    • Melton, A.R.1    Weiss, A.A.2
  • 135
    • 0032434689 scopus 로고    scopus 로고
    • Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa
    • (Pt 12)
    • Michel G., Bleves S., Ball G., Lazdunski A., Filloux A. Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa. Microbiology 1998, 144:3379-3386. (Pt 12).
    • (1998) Microbiology , vol.144 , pp. 3379-3386
    • Michel, G.1    Bleves, S.2    Ball, G.3    Lazdunski, A.4    Filloux, A.5
  • 137
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • Nishiyama K., Suzuki T., Tokuda H. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell 1996, 85:71-81.
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 138
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen N., Stahlberg H., Pugsley A.P., Engel A. Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 2000, 19:2229-2236.
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 139
    • 0027273016 scopus 로고
    • Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT,-U,-V, and -W
    • Nunn D.N., Lory S. Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT,-U,-V, and -W. J. Bacteriol. 1993, 175:4375-4382.
    • (1993) J. Bacteriol. , vol.175 , pp. 4375-4382
    • Nunn, D.N.1    Lory, S.2
  • 140
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner U.A., Snyder A., Vasil A.I., Vasil M.L. Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc. Natl. Acad. Sci. U. S. A 2002, 99:8312-8317.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 8312-8317
    • Ochsner, U.A.1    Snyder, A.2    Vasil, A.I.3    Vasil, M.L.4
  • 141
    • 0028670436 scopus 로고
    • Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme
    • Ohnishi Y., Nishiyama M., Horinouchi S., Beppu T. Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme. J. Biol. Chem. 1994, 269:32800-32806.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32800-32806
    • Ohnishi, Y.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 142
    • 0019413905 scopus 로고
    • E. coli mutant pleiotropically defective in the export of secreted proteins
    • Oliver D.B., Beckwith J. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 1981, 25:765-772.
    • (1981) Cell , vol.25 , pp. 765-772
    • Oliver, D.B.1    Beckwith, J.2
  • 143
    • 0037224652 scopus 로고    scopus 로고
    • Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter
    • Oliver D.C., Huang G., Fernandez R.C. Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter. J. Bacteriol. 2003, 185:489-495.
    • (2003) J. Bacteriol. , vol.185 , pp. 489-495
    • Oliver, D.C.1    Huang, G.2    Fernandez, R.C.3
  • 144
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver D.C., Huang G., Nodel E., Pleasance S., Fernandez R.C. A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol. Microbiol. 2003, 47:1367-1383.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleasance, S.4    Fernandez, R.C.5
  • 145
    • 1942471665 scopus 로고    scopus 로고
    • Structure of the translocator domain of a bacterial autotransporter
    • Oomen C.J., Van U.P., Van G.P., Feijen M., Tommassen J., Gros P. Structure of the translocator domain of a bacterial autotransporter. EMBO J. 2004, 23:1257-1266.
    • (2004) EMBO J. , vol.23 , pp. 1257-1266
    • Oomen, C.J.1    Van, U.P.2    Van, G.P.3    Feijen, M.4    Tommassen, J.5    Gros, P.6
  • 146
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik I.J., Ladner C.L., Turner R.J. Identification of a twin-arginine leader-binding protein. Mol. Microbiol. 2001, 40:323-331.
    • (2001) Mol. Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 147
    • 0042859766 scopus 로고    scopus 로고
    • The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase
    • Papish A.L., Ladner C.L., Turner R.J. The twin-arginine leader-binding protein, DmsD, interacts with the TatB and TatC subunits of the Escherichia coli twin-arginine translocase. J. Biol. Chem. 2003, 278:32501-32506.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32501-32506
    • Papish, A.L.1    Ladner, C.L.2    Turner, R.J.3
  • 148
  • 150
    • 0033020320 scopus 로고    scopus 로고
    • Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator
    • Pimenta A.L., Young J., Holland I.B., Blight M.A. Antibody analysis of the localisation, expression and stability of HlyD, the MFP component of the E. coli haemolysin translocator. Mol. Gen. Genet. 1999, 261:122-132.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 122-132
    • Pimenta, A.L.1    Young, J.2    Holland, I.B.3    Blight, M.A.4
  • 151
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner J., Halter R., Beyreuther K., Meyer T.F. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 1987, 325:458-462.
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 152
    • 0344915159 scopus 로고    scopus 로고
    • Membrane association and multimerization of secreton component pulC
    • Possot O.M., Gerard-Vincent M., Pugsley A.P. Membrane association and multimerization of secreton component pulC. J. Bacteriol. 1999, 181:4004-4011.
    • (1999) J. Bacteriol. , vol.181 , pp. 4004-4011
    • Possot, O.M.1    Gerard-Vincent, M.2    Pugsley, A.P.3
  • 153
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • Possot O.M., Vignon G., Bomchil N., Ebel F., Pugsley A.P. Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE. J. Bacteriol. 2000, 182:2142-2152.
    • (2000) J. Bacteriol. , vol.182 , pp. 2142-2152
    • Possot, O.M.1    Vignon, G.2    Bomchil, N.3    Ebel, F.4    Pugsley, A.P.5
  • 154
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 1993, 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 155
    • 0030976146 scopus 로고    scopus 로고
    • Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria-a review
    • Pugsley A.P., Francetic O., Possot O.M., Sauvonnet N., Hardie K.R. Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria-a review. Gene 1997, 192:13-19.
    • (1997) Gene , vol.192 , pp. 13-19
    • Pugsley, A.P.1    Francetic, O.2    Possot, O.M.3    Sauvonnet, N.4    Hardie, K.R.5
  • 156
    • 0027514147 scopus 로고
    • Mutagenesis of cellulase EGZ for studying the general protein secretory pathway in Erwinia chrysanthemi
    • Py B., Chippaux M., Barras F. Mutagenesis of cellulase EGZ for studying the general protein secretory pathway in Erwinia chrysanthemi. Mol. Microbiol. 1993, 7:785-793.
    • (1993) Mol. Microbiol. , vol.7 , pp. 785-793
    • Py, B.1    Chippaux, M.2    Barras, F.3
  • 157
    • 0033546401 scopus 로고    scopus 로고
    • Assembly of the type II secretion machinery of Erwinia chrysanthemi: direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL
    • Py B., Loiseau L., Barras F. Assembly of the type II secretion machinery of Erwinia chrysanthemi: direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL. J. Mol. Biol. 1999, 289:659-670.
    • (1999) J. Mol. Biol. , vol.289 , pp. 659-670
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 158
    • 0035065972 scopus 로고    scopus 로고
    • An inner membrane platform in the type II secretion machinery of Gram-negative bacteria
    • Py B., Loiseau L., Barras F. An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBO Rep. 2001, 2:244-248.
    • (2001) EMBO Rep. , vol.2 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 159
    • 0037307783 scopus 로고    scopus 로고
    • The VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorption
    • Rabel C., Grahn A.M., Lurz R., Lanka E. The VirB4 family of proposed traffic nucleoside triphosphatases: common motifs in plasmid RP4 TrbE are essential for conjugation and phage adsorption. J. Bacteriol. 2003, 185:1045-1058.
    • (2003) J. Bacteriol. , vol.185 , pp. 1045-1058
    • Rabel, C.1    Grahn, A.M.2    Lurz, R.3    Lanka, E.4
  • 160
    • 0037448423 scopus 로고    scopus 로고
    • DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
    • Ray N., Oates J., Turner R.J., Robinson C. DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus. FEBS Lett. 2003, 534:156-160.
    • (2003) FEBS Lett. , vol.534 , pp. 156-160
    • Ray, N.1    Oates, J.2    Turner, R.J.3    Robinson, C.4
  • 162
    • 0030012150 scopus 로고    scopus 로고
    • The pertussis toxin liberation genes of Bordetella pertussis are transcriptionally linked to the pertussis toxin operon
    • Ricci S., Rappuoli R., Scarlato V. The pertussis toxin liberation genes of Bordetella pertussis are transcriptionally linked to the pertussis toxin operon. Infect. Immun. 1996, 64:1458-1460.
    • (1996) Infect. Immun. , vol.64 , pp. 1458-1460
    • Ricci, S.1    Rappuoli, R.2    Scarlato, V.3
  • 163
    • 0141862137 scopus 로고    scopus 로고
    • Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae
    • Robien M.A., Krumm B.E., Sandkvist M., Hol W.G. Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae. J. Mol. Biol. 2003, 333:657-674.
    • (2003) J. Mol. Biol. , vol.333 , pp. 657-674
    • Robien, M.A.1    Krumm, B.E.2    Sandkvist, M.3    Hol, W.G.4
  • 164
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson C., Bolhuis A. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta 2004, 1694:135-147.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 165
    • 0032803976 scopus 로고    scopus 로고
    • The Yersinia enterocolitica pYV virulence plasmid contains multiple intrinsic DNA bends which melt at 37 degrees C
    • Rohde J.R., Luan X.S., Rohde H., Fox J.M., Minnich S.A. The Yersinia enterocolitica pYV virulence plasmid contains multiple intrinsic DNA bends which melt at 37 degrees C. J. Bacteriol. 1999, 181:4198-4204.
    • (1999) J. Bacteriol. , vol.181 , pp. 4198-4204
    • Rohde, J.R.1    Luan, X.S.2    Rohde, H.3    Fox, J.M.4    Minnich, S.A.5
  • 166
    • 0038046757 scopus 로고    scopus 로고
    • A novel sheathed surface organelle of the Helicobacter pylori cag type IV secretion system
    • Rohde M., Puls J., Buhrdorf R., Fischer W., Haas R. A novel sheathed surface organelle of the Helicobacter pylori cag type IV secretion system. Mol. Microbiol. 2003, 49:219-234.
    • (2003) Mol. Microbiol. , vol.49 , pp. 219-234
    • Rohde, M.1    Puls, J.2    Buhrdorf, R.3    Fischer, W.4    Haas, R.5
  • 167
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch J., Caparon M. A microdomain for protein secretion in Gram-positive bacteria. Science 2004, 304:1513-1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 168
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist R., Magnusson K.E., Wolf-Watz H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 1994, 13:964-972.
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 170
    • 0034944416 scopus 로고    scopus 로고
    • Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
    • Sanders C., Wethkamp N., Lill H. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system. Mol. Microbiol. 2001, 41:241-246.
    • (2001) Mol. Microbiol. , vol.41 , pp. 241-246
    • Sanders, C.1    Wethkamp, N.2    Lill, H.3
  • 171
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist M. Type II secretion and pathogenesis. Infect. Immun. 2001, 69:3523-3535.
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 172
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist M. Biology of type II secretion. Mol. Microbiol. 2001, 40:271-283.
    • (2001) Mol. Microbiol. , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 173
    • 0029060583 scopus 로고
    • Interaction between the autokinase EpsE and EpsL in the cytoplasmic membrane is required for extracellular secretion in Vibrio cholerae
    • Sandkvist M., Bagdasarian M., Howard S.P., DiRita V.J. Interaction between the autokinase EpsE and EpsL in the cytoplasmic membrane is required for extracellular secretion in Vibrio cholerae. EMBO J. 1995, 14:1664-1673.
    • (1995) EMBO J. , vol.14 , pp. 1664-1673
    • Sandkvist, M.1    Bagdasarian, M.2    Howard, S.P.3    DiRita, V.J.4
  • 174
    • 0032909439 scopus 로고    scopus 로고
    • Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae
    • Sandkvist M., Hough L.P., Bagdasarian M.M., Bagdasarian M. Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae. J. Bacteriol. 1999, 181:3129-3135.
    • (1999) J. Bacteriol. , vol.181 , pp. 3129-3135
    • Sandkvist, M.1    Hough, L.P.2    Bagdasarian, M.M.3    Bagdasarian, M.4
  • 175
    • 0036311769 scopus 로고    scopus 로고
    • Assembly of membrane-bound respiratory complexes by the Tat protein-transport system
    • Sargent F., Berks B.C., Palmer T. Assembly of membrane-bound respiratory complexes by the Tat protein-transport system. Arch. Microbiol. 2002, 178:77-84.
    • (2002) Arch. Microbiol. , vol.178 , pp. 77-84
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 177
    • 0034832014 scopus 로고    scopus 로고
    • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
    • Sargent F., Gohlke U., De L.E., Stanley N.R., Palmer T., Saibil H.R., Berks B.C. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 2001, 268:3361-3367.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3361-3367
    • Sargent, F.1    Gohlke, U.2    De, L.E.3    Stanley, N.R.4    Palmer, T.5    Saibil, H.R.6    Berks, B.C.7
  • 178
    • 0032951188 scopus 로고    scopus 로고
    • Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters
    • Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999, 48:22-41.
    • (1999) J. Mol. Evol. , vol.48 , pp. 22-41
    • Saurin, W.1    Hofnung, M.2    Dassa, E.3
  • 179
    • 0029816618 scopus 로고    scopus 로고
    • Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway
    • Sauvonnet N., Pugsley A.P. Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway. Mol. Microbiol. 1996, 22:1-7.
    • (1996) Mol. Microbiol. , vol.22 , pp. 1-7
    • Sauvonnet, N.1    Pugsley, A.P.2
  • 180
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet N., Vignon G., Pugsley A.P., Gounon P. Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J. 2000, 19:2221-2228.
    • (2000) EMBO J. , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 182
    • 0026073817 scopus 로고
    • Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase
    • Schiebel E., Driessen A.J., Hartl F.U., Wickner W. Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase. Cell 1991, 64:927-939.
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.2    Hartl, F.U.3    Wickner, W.4
  • 183
    • 0037327383 scopus 로고    scopus 로고
    • Analysis of Vir protein translocation from Agrobacterium tumefaciens using Saccharomyces cerevisiae as a model: evidence for transport of a novel effector protein VirE3
    • Schrammeijer B., den Dulk-Ras A., Vergunst A.C., Jurado J.E., Hooykaas P.J. Analysis of Vir protein translocation from Agrobacterium tumefaciens using Saccharomyces cerevisiae as a model: evidence for transport of a novel effector protein VirE3. Nucleic Acids Res. 2003, 31:860-868.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 860-868
    • Schrammeijer, B.1    den Dulk-Ras, A.2    Vergunst, A.C.3    Jurado, J.E.4    Hooykaas, P.J.5
  • 184
    • 0035923586 scopus 로고    scopus 로고
    • Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway
    • Scott M.E., Dossani Z.Y., Sandkvist M. Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway. Proc. Natl. Acad. Sci. U. S. A 2001, 98:13978-13983.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 13978-13983
    • Scott, M.E.1    Dossani, Z.Y.2    Sandkvist, M.3
  • 187
    • 0030875733 scopus 로고    scopus 로고
    • Disruption of IcsP, the major Shigella protease that cleaves IcsA, accelerates actin-based motility
    • Shere K.D., Sallustio S., Manessis A., D'Aversa T.G., Goldberg M.B. Disruption of IcsP, the major Shigella protease that cleaves IcsA, accelerates actin-based motility. Mol. Microbiol. 1997, 25:451-462.
    • (1997) Mol. Microbiol. , vol.25 , pp. 451-462
    • Shere, K.D.1    Sallustio, S.2    Manessis, A.3    D'Aversa, T.G.4    Goldberg, M.B.5
  • 188
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, and Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik V.E., Robert-Baudouy J., Condemine G. Specific interaction between OutD, and Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J. 1997, 16:3007-3016.
    • (1997) EMBO J. , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 189
    • 0028238717 scopus 로고
    • An inner-membrane-associated virulence protein essential for T-DNA transfer from Agrobacterium tumefaciens to plants exhibits ATPase activity and similarities to conjugative transfer genes
    • Shirasu K., Koukolikova-Nicola Z., Hohn B., Kado C.I. An inner-membrane-associated virulence protein essential for T-DNA transfer from Agrobacterium tumefaciens to plants exhibits ATPase activity and similarities to conjugative transfer genes. Mol. Microbiol. 1994, 11:581-588.
    • (1994) Mol. Microbiol. , vol.11 , pp. 581-588
    • Shirasu, K.1    Koukolikova-Nicola, Z.2    Hohn, B.3    Kado, C.I.4
  • 190
    • 0037799238 scopus 로고    scopus 로고
    • Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein
    • Sijbrandi R., Urbanus M.L., ten Hagen-Jongman C.M., Bernstein H.D., Oudega B., Otto B.R., Luirink J. Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein. J. Biol. Chem. 2003, 278:4654-4659.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4654-4659
    • Sijbrandi, R.1    Urbanus, M.L.2    ten Hagen-Jongman, C.M.3    Bernstein, H.D.4    Oudega, B.5    Otto, B.R.6    Luirink, J.7
  • 191
    • 2942544266 scopus 로고    scopus 로고
    • The type II protein secretion system of Legionella pneumophila promotes growth at low temperatures
    • Soderberg M.A., Rossier O., Cianciotto N.P. The type II protein secretion system of Legionella pneumophila promotes growth at low temperatures. J. Bacteriol. 2004, 186:3712-3720.
    • (2004) J. Bacteriol. , vol.186 , pp. 3712-3720
    • Soderberg, M.A.1    Rossier, O.2    Cianciotto, N.P.3
  • 192
    • 0029608720 scopus 로고
    • Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach
    • Sory M.P., Boland A., Lambermont I., Cornelis G.R. Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc. Natl. Acad. Sci. U. S. A 1995, 92:11998-12002.
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 193
    • 0029795239 scopus 로고    scopus 로고
    • Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus
    • Spudich G.M., Fernandez D., Zhou X.R., Christie P.J. Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus. Proc. Natl. Acad. Sci. U. S. A 1996, 93:7512-7517.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 7512-7517
    • Spudich, G.M.1    Fernandez, D.2    Zhou, X.R.3    Christie, P.J.4
  • 194
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley N.R., Palmer T., Berks B.C. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 2000, 275:11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 195
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley P., Koronakis V., Hughes C. Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 1991, 5:2391-2403.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 196
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins C.E., Galan J.E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 2001, 414:77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 198
    • 0027242120 scopus 로고
    • Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa
    • Strom M.S., Bergman P., Lory S. Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa. J. Biol. Chem. 1993, 268:15788-15794.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15788-15794
    • Strom, M.S.1    Bergman, P.2    Lory, S.3
  • 199
    • 0035086501 scopus 로고    scopus 로고
    • Antibiotic susceptibility profiles of Escherichia coli strains lacking multidrug efflux pump genes
    • Sulavik M.C., et al. Antibiotic susceptibility profiles of Escherichia coli strains lacking multidrug efflux pump genes. Antimicrob. Agents Chemother. 2001, 45:1126-1136.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1126-1136
    • Sulavik, M.C.1
  • 200
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E.coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • Thanabalu T., Koronakis E., Hughes C., Koronakis V. Substrate-induced assembly of a contiguous channel for protein export from E.coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore. EMBO J. 1998, 17:6487-6496.
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 201
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution
    • Thayer M.M., Flaherty K.M., McKay D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. J. Biol. Chem. 1991, 266:2864-2871.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 203
    • 0035980042 scopus 로고    scopus 로고
    • Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis
    • Veenendaal A.K., van der D.C., Driessen A.J. Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis. J. Biol. Chem. 2001, 276:32559-32566.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32559-32566
    • Veenendaal, A.K.1    van der, D.C.2    Driessen, A.J.3
  • 204
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga E., Sugawara E., Nikaido H., de L.V., Fernandez L.A. Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. EMBO J. 2002, 21:2122-2131.
    • (2002) EMBO J. , vol.21 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    de, L.V.4    Fernandez, L.A.5
  • 205
    • 3843078622 scopus 로고    scopus 로고
    • Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger
    • Velarde J.J., Nataro J.P. Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger. J. Biol. Chem. 2004, 279:31495-31504.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31495-31504
    • Velarde, J.J.1    Nataro, J.P.2
  • 207
    • 0344152245 scopus 로고    scopus 로고
    • Recognition of the Agrobacterium tumefaciens VirE2 translocation signal by the VirB/D4 transport system does not require VirE1
    • Vergunst A.C., van Lier M.C., den Dulk-Ras A., Hooykaas P.J. Recognition of the Agrobacterium tumefaciens VirE2 translocation signal by the VirB/D4 transport system does not require VirE1. Plant Physiol 2003, 133:978-988.
    • (2003) Plant Physiol , vol.133 , pp. 978-988
    • Vergunst, A.C.1    van Lier, M.C.2    den Dulk-Ras, A.3    Hooykaas, P.J.4
  • 208
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux R., Ball G., Ize B., Vasil M.L., Lazdunski A., Wu L.F., Filloux A. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 2001, 20:6735-6741.
    • (2001) EMBO J. , vol.20 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Filloux, A.7
  • 209
    • 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 2003, 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 210
    • 0033917666 scopus 로고    scopus 로고
    • Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa
    • Voulhoux R., Taupiac M.P., Czjzek M., Beaumelle B., Filloux A. Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa. J. Bacteriol. 2000, 182:4051-4058.
    • (2000) J. Bacteriol. , vol.182 , pp. 4051-4058
    • Voulhoux, R.1    Taupiac, M.P.2    Czjzek, M.3    Beaumelle, B.4    Filloux, A.5
  • 211
    • 4444290475 scopus 로고    scopus 로고
    • Structure and function of SecA, the preprotein translocase nanomotor
    • Vrontou E., Economou A. Structure and function of SecA, the preprotein translocase nanomotor. Biochim. Biophys. Acta 2004, 1694:67-80.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 67-80
    • Vrontou, E.1    Economou, A.2
  • 212
    • 5444259691 scopus 로고    scopus 로고
    • Demonstration of a specific Escherichia coli SecY-signal peptide interaction
    • Wang L., Miller A., Rusch S.L., Kendall D.A. Demonstration of a specific Escherichia coli SecY-signal peptide interaction. Biochemistry 2004, 43:13185-13192.
    • (2004) Biochemistry , vol.43 , pp. 13185-13192
    • Wang, L.1    Miller, A.2    Rusch, S.L.3    Kendall, D.A.4
  • 213
    • 0037143759 scopus 로고    scopus 로고
    • Peptide linkage mapping of the Agrobacterium tumefaciens virencoded type IV secretion system reveals protein subassemblies
    • Ward D.V., Draper O., Zupan J.R., Zambryski P.C. Peptide linkage mapping of the Agrobacterium tumefaciens virencoded type IV secretion system reveals protein subassemblies. Proc. Natl. Acad. Sci. U. S. A 2002, 99:11493-11500.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 11493-11500
    • Ward, D.V.1    Draper, O.2    Zupan, J.R.3    Zambryski, P.C.4
  • 214
    • 0035155060 scopus 로고    scopus 로고
    • Formation of a fibrous structure on the surface of Legionella pneumophila associated with exposure of DotH and DotO proteins after intracellular growth
    • Watarai M., Andrews H.L., Isberg R.R. Formation of a fibrous structure on the surface of Legionella pneumophila associated with exposure of DotH and DotO proteins after intracellular growth. Mol. Microbiol. 2001, 39:313-329.
    • (2001) Mol. Microbiol. , vol.39 , pp. 313-329
    • Watarai, M.1    Andrews, H.L.2    Isberg, R.R.3
  • 216
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau P., Woestyn S., Cornelis G.R. Customized secretion chaperones in pathogenic bacteria. Mol. Microbiol. 1996, 20:255-262.
    • (1996) Mol. Microbiol. , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 218
    • 0034509609 scopus 로고    scopus 로고
    • Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system
    • Yeo H.J., Savvides S.N., Herr A.B., Lanka E., Waksman G. Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system. Mol. Cell 2000, 6:1461-1472.
    • (2000) Mol. Cell , vol.6 , pp. 1461-1472
    • Yeo, H.J.1    Savvides, S.N.2    Herr, A.B.3    Lanka, E.4    Waksman, G.5
  • 219
    • 0032469732 scopus 로고    scopus 로고
    • Purification and characterization of thin pili of IncI1 plasmids ColIb-P9 and R64: formation of PilV-specific cell aggregates by type IV pili
    • Yoshida T., Furuya N., Ishikura M., Isobe T., Haino-Fukushima K., Ogawa T., Komano T. Purification and characterization of thin pili of IncI1 plasmids ColIb-P9 and R64: formation of PilV-specific cell aggregates by type IV pili. J. Bacteriol. 1998, 180:2842-2848.
    • (1998) J. Bacteriol. , vol.180 , pp. 2842-2848
    • Yoshida, T.1    Furuya, N.2    Ishikura, M.3    Isobe, T.4    Haino-Fukushima, K.5    Ogawa, T.6    Komano, T.7
  • 220
    • 0027151984 scopus 로고
    • Functional replacement of the hemolysin A transport signal by a different primary sequence
    • Zhang F., Greig D.I., Ling V. Functional replacement of the hemolysin A transport signal by a different primary sequence. Proc. Natl. Acad. Sci. U. S. A 1993, 90:4211-4215.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , pp. 4211-4215
    • Zhang, F.1    Greig, D.I.2    Ling, V.3
  • 221
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M., Aslund F., Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998, 279:1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 222
    • 0033907671 scopus 로고    scopus 로고
    • The transfer of DNA from agrobacterium tumefaciens into plants: a feast of fundamental insights
    • Zupan J., Muth T.R., Draper O., Zambryski P. The transfer of DNA from agrobacterium tumefaciens into plants: a feast of fundamental insights. Plant J. 2000, 23:11-28.
    • (2000) Plant J. , vol.23 , pp. 11-28
    • Zupan, J.1    Muth, T.R.2    Draper, O.3    Zambryski, P.4


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