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Volumn 1694, Issue 1-3 SPEC.ISS., 2004, Pages 181-206

Type III protein secretion mechanism in mammalian and plant pathogens

Author keywords

Disease resistance; Flagellum; Immunity; Protein secretion; Pseudomonas syringae; Yersinia

Indexed keywords

ADRENALIN; CHAPERONE; HORMONE; MEMBRANE PROTEIN;

EID: 8844275498     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.03.011     Document Type: Review
Times cited : (262)

References (273)
  • 1
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in Gram-negative bacteria
    • Salmond G.P.C., Reeves P.J. Membrane traffic wardens and protein secretion in Gram-negative bacteria. Trends Biochem. Sci. 18:1993;7-12
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 7-12
    • Salmond, G.P.C.1    Reeves, P.J.2
  • 2
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist R., Magnusson K., Wolf-Watz H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:1994;964-972
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.2    Wolf-Watz, H.3
  • 3
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory M.P., Cornelis G.R. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14:1994;583-594
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 4
    • 0023121521 scopus 로고
    • Molecular cloning and expression of calcium-regulated, plasmid-coded proteins of Y. pseudotuberculosis
    • Forsberg A., Bolin I., Norlander L., Wolf-Watz H. Molecular cloning and expression of calcium-regulated, plasmid-coded proteins of Y. pseudotuberculosis. Microb. Pathog. 2:1987;123-137
    • (1987) Microb. Pathog. , vol.2 , pp. 123-137
    • Forsberg, A.1    Bolin, I.2    Norlander, L.3    Wolf-Watz, H.4
  • 5
    • 0023013754 scopus 로고
    • Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media
    • Heesemann J., Gross U., Schmidt N., Laufs R. Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media. Infect. Immun. 54:1986;561-567
    • (1986) Infect. Immun. , vol.54 , pp. 561-567
    • Heesemann, J.1    Gross, U.2    Schmidt, N.3    Laufs, R.4
  • 6
    • 0022997655 scopus 로고
    • Gene cluster of Pseudomonas syringae pv. phaseolicola controls pathogenicity of bean plants and hypersensitivity on nonhost plants
    • Lindgren P.B., Peet R.C., Panopoulos N.J. Gene cluster of Pseudomonas syringae pv. phaseolicola controls pathogenicity of bean plants and hypersensitivity on nonhost plants. J. Bacteriol. 168:1986;512-522
    • (1986) J. Bacteriol. , vol.168 , pp. 512-522
    • Lindgren, P.B.1    Peet, R.C.2    Panopoulos, N.J.3
  • 7
    • 0027241625 scopus 로고
    • Pss: A protein that is secreted via the Hrp pathway and elicits the hypersensitive response in plants
    • Pss: a protein that is secreted via the Hrp pathway and elicits the hypersensitive response in plants. Cell. 73:1993;1255-1266
    • (1993) Cell , vol.73 , pp. 1255-1266
    • He, S.1    Huang, H.2    Collmer, A.3
  • 8
    • 0028144219 scopus 로고
    • PopA1, a protein which induces a hypersensitivity-like response on specific Petunia genotypes, is secreted via the Hrp pathway of Pseudomonas solanacearum
    • Arlat M., Gijsegem F.V., Huet J.C., Pernollet J.C., Boucher C.A. PopA1, a protein which induces a hypersensitivity-like response on specific Petunia genotypes, is secreted via the Hrp pathway of Pseudomonas solanacearum. EMBO J. 13:1994;543-553
    • (1994) EMBO J. , vol.13 , pp. 543-553
    • Arlat, M.1    Gijsegem, F.V.2    Huet, J.C.3    Pernollet, J.C.4    Boucher, C.A.5
  • 9
    • 0027146593 scopus 로고
    • HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new protein family
    • Wei Z.M., Beer S.V. HrpI of Erwinia amylovora functions in secretion of harpin and is a member of a new protein family. J. Bacteriol. 175:1993;7958-7967
    • (1993) J. Bacteriol. , vol.175 , pp. 7958-7967
    • Wei, Z.M.1    Beer, S.V.2
  • 10
    • 0030198512 scopus 로고    scopus 로고
    • Expression of the Pseudomonas syringae avirulence protein AvrB in plant cells alleviates its dependence on the hypersensitive response and pathogenicity (Hrp) secretion system in eliciting genotype-specific hypersensitive cell death
    • Gopalan S., Bauer D.W., Alfano J., Loniello A.O., He S.Y., Collmer A. Expression of the Pseudomonas syringae avirulence protein AvrB in plant cells alleviates its dependence on the hypersensitive response and pathogenicity (Hrp) secretion system in eliciting genotype-specific hypersensitive cell death. Plant Cell. 8:1996;1095-1105
    • (1996) Plant Cell , vol.8 , pp. 1095-1105
    • Gopalan, S.1    Bauer, D.W.2    Alfano, J.3    Loniello, A.O.4    He, S.Y.5    Collmer, A.6
  • 11
    • 0030448263 scopus 로고    scopus 로고
    • Initiation of plant disease resistance by physical interaction of AvrPto and Pto kinase
    • Tang X., Frederick R.D., Zhou J., Halterman D.A., Jia Y., Martin G.B. Initiation of plant disease resistance by physical interaction of AvrPto and Pto kinase. Science. 274:1996;2060-2062
    • (1996) Science , vol.274 , pp. 2060-2062
    • Tang, X.1    Frederick, R.D.2    Zhou, J.3    Halterman, D.A.4    Jia, Y.5    Martin, G.B.6
  • 13
    • 0030451446 scopus 로고    scopus 로고
    • Molecular recognition of pathogen attack occurs inside of plant cells in plant disease resistance specified by the Arabidopsis genes RPS2 and RPM1
    • Leister R.T., Ausubel F.M., Katagiri F. Molecular recognition of pathogen attack occurs inside of plant cells in plant disease resistance specified by the Arabidopsis genes RPS2 and RPM1. Proc. Natl. Acad. Sci. U. S. A. 93:1996;15497-15502
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 15497-15502
    • Leister, R.T.1    Ausubel, F.M.2    Katagiri, F.3
  • 14
    • 0030476711 scopus 로고    scopus 로고
    • Recognition of the bacterial avirulence protein AvrBs3 occurs inside the host plant cell
    • Van den Ackerveken G., Marois E., Bonas U. Recognition of the bacterial avirulence protein AvrBs3 occurs inside the host plant cell. Cell. 87:1996;1307-1316
    • (1996) Cell , vol.87 , pp. 1307-1316
    • Van Den Ackerveken, G.1    Marois, E.2    Bonas, U.3
  • 15
    • 0037062493 scopus 로고    scopus 로고
    • Direct biochemical evidence for type III secretion-dependent translocation of the AvrBs2 effector protein into plant cells
    • Casper-Lindley C., Dahlbeck D., Clark E.T., Staskawicz B.J. Direct biochemical evidence for type III secretion-dependent translocation of the AvrBs2 effector protein into plant cells. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8336-8341
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8336-8341
    • Casper-Lindley, C.1    Dahlbeck, D.2    Clark, E.T.3    Staskawicz, B.J.4
  • 16
    • 0036035474 scopus 로고    scopus 로고
    • Type III-dependent translocation of the Xanthomonas AvrBs3 protein into the plant cell
    • Szurek B., Rossier O., Hause G., Bonas U. Type III-dependent translocation of the Xanthomonas AvrBs3 protein into the plant cell. Mol. Microbiol. 46:2002;13-23
    • (2002) Mol. Microbiol. , vol.46 , pp. 13-23
    • Szurek, B.1    Rossier, O.2    Hause, G.3    Bonas, U.4
  • 17
  • 18
    • 0034932336 scopus 로고    scopus 로고
    • Rhizobium type III secretion systems: Legume charmers or alarmers?
    • Marie C., Broughton W.J., Deakin W.J. Rhizobium type III secretion systems: legume charmers or alarmers? Curr. Opin. Plant Biol. 4:2001;336-342
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 336-342
    • Marie, C.1    Broughton, W.J.2    Deakin, W.J.3
  • 19
    • 0035852690 scopus 로고    scopus 로고
    • The insect endosymbiont Sodalis glossinidius utilizes a type III secretion system for cell invasion
    • Dale C., Young S.A., Haydon D.T., Welburn S.C. The insect endosymbiont Sodalis glossinidius utilizes a type III secretion system for cell invasion. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1883-1888
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1883-1888
    • Dale, C.1    Young, S.A.2    Haydon, D.T.3    Welburn, S.C.4
  • 20
    • 0038323185 scopus 로고    scopus 로고
    • A chromosomally encoded type III secretion pathway in Yersinia enterocolitica is important in virulence
    • Haller J.C., Carlson S., Pederson K.J., Pierson D.E. A chromosomally encoded type III secretion pathway in Yersinia enterocolitica is important in virulence. Mol. Microbiol. 36:2000;1436-1446
    • (2000) Mol. Microbiol. , vol.36 , pp. 1436-1446
    • Haller, J.C.1    Carlson, S.2    Pederson, K.J.3    Pierson, D.E.4
  • 21
    • 0036017380 scopus 로고    scopus 로고
    • Characterization of the ysa pathogenicity locus in the chromosome of Yersinia enterocolitica and phylogeny analysis of type III secretion systems
    • Foultier B., Troisfontaines P., Müller S., Opperdoes F.R., Cornelis G.R. Characterization of the ysa pathogenicity locus in the chromosome of Yersinia enterocolitica and phylogeny analysis of type III secretion systems. J. Mol. Evol. 55:2002;37-51
    • (2002) J. Mol. Evol. , vol.55 , pp. 37-51
    • Foultier, B.1    Troisfontaines, P.2    Müller, S.3    Opperdoes, F.R.4    Cornelis, G.R.5
  • 22
    • 0038519642 scopus 로고    scopus 로고
    • Distribution of the secondary type III secretion system locus found in enterohemorrhagic Escherichia coli O157:H7 isolates among Shiga toxin-producing E. coli strains
    • Makino S., Tobe T., Asakura H., Watarai M., Ikeda T., Takeshi K., Sasakawa C. Distribution of the secondary type III secretion system locus found in enterohemorrhagic Escherichia coli O157:H7 isolates among Shiga toxin-producing E. coli strains. J. Clin. Microbiol. 41:2003;2341-2347
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 2341-2347
    • Makino, S.1    Tobe, T.2    Asakura, H.3    Watarai, M.4    Ikeda, T.5    Takeshi, K.6    Sasakawa, C.7
  • 23
    • 0033758756 scopus 로고    scopus 로고
    • Pathogenicity islands and the evolution of microbes
    • Hacker J., Kaper J.B. Pathogenicity islands and the evolution of microbes. Annu. Rev. Microbiol. 54:2000;641-679
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 641-679
    • Hacker, J.1    Kaper, J.B.2
  • 24
    • 0030726075 scopus 로고    scopus 로고
    • The exoenzyme S regulon of Pseudomonas aeruginosa
    • Frank D.W. The exoenzyme S regulon of Pseudomonas aeruginosa. Mol. Microbiol. 26:1997;621-629
    • (1997) Mol. Microbiol. , vol.26 , pp. 621-629
    • Frank, D.W.1
  • 25
    • 0024323292 scopus 로고
    • Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells
    • Galan J.E., Curtiss R.I. Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells. Proc. Natl. Acad. Sci. U. S. A. 86:1989;6383-6387
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 6383-6387
    • Galan, J.E.1    Curtiss, R.I.2
  • 26
    • 0021710132 scopus 로고
    • Genetic analysis of the low calcium response in Yersinia pestis Mu d1(Ap lac) insertion mutants
    • Goguen J.D., Yother J., Straley S.C. Genetic analysis of the low calcium response in Yersinia pestis Mu d1(Ap lac) insertion mutants. J. Bacteriol. 160:1984;842-848
    • (1984) J. Bacteriol. , vol.160 , pp. 842-848
    • Goguen, J.D.1    Yother, J.2    Straley, S.C.3
  • 27
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation
    • Jarvis K.G., Giron J.A., Jerse A.E., McDaniel T.K., Donnenberg M.S., Kaper J.B. Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc. Natl. Acad. Sci. U. S. A. 92:1995;7996-8000
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7996-8000
    • Jarvis, K.G.1    Giron, J.A.2    Jerse, A.E.3    McDaniel, T.K.4    Donnenberg, M.S.5    Kaper, J.B.6
  • 28
    • 0023908557 scopus 로고
    • Virulence-associated genetic regions comprising 31 kilobases of the 230-kilobase plasmid in Shigella flexneri 2a
    • Sasakawa C., Kamata K., Sakai T., Makino S., Yamada M., Okada N., Yoshikawa M. Virulence-associated genetic regions comprising 31 kilobases of the 230-kilobase plasmid in Shigella flexneri 2a. J. Bacteriol. 170:1988;2480-2484
    • (1988) J. Bacteriol. , vol.170 , pp. 2480-2484
    • Sasakawa, C.1    Kamata, K.2    Sakai, T.3    Makino, S.4    Yamada, M.5    Okada, N.6    Yoshikawa, M.7
  • 29
    • 0242500352 scopus 로고    scopus 로고
    • Use of the Galleria mellonella caterpillar as a model host to study the role of the type III secretion system in Pseudomonas aeruginosa pathogenesis
    • Miyata S., Casey M., Frank D.W., Ausubel F.M., Drenkard E. Use of the Galleria mellonella caterpillar as a model host to study the role of the type III secretion system in Pseudomonas aeruginosa pathogenesis. Infect. Immun. 71:2003;2404-2413
    • (2003) Infect. Immun. , vol.71 , pp. 2404-2413
    • Miyata, S.1    Casey, M.2    Frank, D.W.3    Ausubel, F.M.4    Drenkard, E.5
  • 31
    • 0001877136 scopus 로고
    • Isolation of a gene cluster from Xanthomonas campestris, pv. vesicatoria that determines pathogenicity and the hypersensitive response on pepper and tomato
    • Bonas U., Schulte R., Fenselau S., Minsavage G.V., Staskawicz B.J., Stall R.E. Isolation of a gene cluster from Xanthomonas campestris, pv. vesicatoria that determines pathogenicity and the hypersensitive response on pepper and tomato. Mol. Plant-Microb. Interact. 4:1991;81-88
    • (1991) Mol. Plant-Microb. Interact. , vol.4 , pp. 81-88
    • Bonas, U.1    Schulte, R.2    Fenselau, S.3    Minsavage, G.V.4    Staskawicz, B.J.5    Stall, R.E.6
  • 32
    • 0023462898 scopus 로고
    • Pseudomonas solanacearum genes controlling both pathogenicity on tomato and hypersensitivity on tobacco are clustered
    • Boucher C.A., Van Gijsegem F., Barberis P.A., Arlat M., Zischek C. Pseudomonas solanacearum genes controlling both pathogenicity on tomato and hypersensitivity on tobacco are clustered. J. Bacteriol. 169:1987;5626-5632
    • (1987) J. Bacteriol. , vol.169 , pp. 5626-5632
    • Boucher, C.A.1    Van Gijsegem, F.2    Barberis, P.A.3    Arlat, M.4    Zischek, C.5
  • 33
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan J.E., Collmer A. Type III secretion machines: bacterial devices for protein delivery into host cells. Science. 284:1999;1322-1328
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 34
    • 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. 17:2001;53-86
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 53-86
    • Galan, J.E.1
  • 35
    • 0030003139 scopus 로고    scopus 로고
    • Bacterial entry into epithelial cells: The paradigm of Shigella
    • Menard R., Dehio C., Sansonetti P.J. Bacterial entry into epithelial cells: the paradigm of Shigella. Trends Microbiol. 4:1996;220-226
    • (1996) Trends Microbiol. , vol.4 , pp. 220-226
    • Menard, R.1    Dehio, C.2    Sansonetti, P.J.3
  • 36
    • 0038011417 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion: Evidence for a functional apparatus during early-cycle development
    • Fields K.A., Mead D.J., Dooley C.A., Hackstadt T. Chlamydia trachomatis type III secretion: evidence for a functional apparatus during early-cycle development. Mol. Microbiol. 48:2003;671-683
    • (2003) Mol. Microbiol. , vol.48 , pp. 671-683
    • Fields, K.A.1    Mead, D.J.2    Dooley, C.A.3    Hackstadt, T.4
  • 37
    • 0344747136 scopus 로고
    • Electron microscopic evidence for in vivo extracellular localization of Yersinia pseudotuberculosis harboring the pYV plasmid
    • Simonet M., Richard S., Berch P. Electron microscopic evidence for in vivo extracellular localization of Yersinia pseudotuberculosis harboring the pYV plasmid. Infect. Immun. 60:1992;366-373
    • (1992) Infect. Immun. , vol.60 , pp. 366-373
    • Simonet, M.1    Richard, S.2    Berch, P.3
  • 38
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis G.R., Van Gijsegem F. Assembly and function of type III secretory systems. Annu. Rev. Microbiol. 54:2000;735-774
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 39
    • 0033031869 scopus 로고    scopus 로고
    • Macrophages and epithelial cells respond differently to the Pseudomonas aeruginosa type III secretion system
    • Coburn J., Frank D.W. Macrophages and epithelial cells respond differently to the Pseudomonas aeruginosa type III secretion system. Infect. Immun. 67:1999;3151-3154
    • (1999) Infect. Immun. , vol.67 , pp. 3151-3154
    • Coburn, J.1    Frank, D.W.2
  • 40
    • 0034003289 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: Exploiting the host cell cytoskeleton from the outside
    • Celli J., Deng W., Finlay B.B. Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outside. Cell. Microbiol. 2:2000;1-9
    • (2000) Cell. Microbiol. , vol.2 , pp. 1-9
    • Celli, J.1    Deng, W.2    Finlay, B.B.3
  • 41
    • 0013431036 scopus 로고    scopus 로고
    • The Arabidopsis thaliana-Pseudomonas syringae interaction
    • C.R. Somerville, & E.M. Meyerowitz. Rockville, MD: American Society of Plant Biologists.
    • Katagiri F., Thilmony R., He S.Y. The Arabidopsis thaliana-Pseudomonas syringae interaction. Somerville C.R., Meyerowitz E.M. The Arabidopsis Book. 2002;American Society of Plant Biologists, Rockville, MD. doi 10.1199-tab.0039
    • (2002) The Arabidopsis Book
    • Katagiri, F.1    Thilmony, R.2    He, S.Y.3
  • 42
    • 0004753911 scopus 로고    scopus 로고
    • Type III protein secretion systems in plant and animal pathogenic bacteria
    • He S.Y. Type III protein secretion systems in plant and animal pathogenic bacteria. Annu. Rev. Phytopathol. 36:1998;363-392
    • (1998) Annu. Rev. Phytopathol. , vol.36 , pp. 363-392
    • He, S.Y.1
  • 44
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: Insights into their function from structural similarities
    • Blocker A., Komoriya K., Aizawa S. Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc. Natl. Acad. Sci. U. S. A. 100:2003;3027-3030
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.3
  • 45
    • 0036008317 scopus 로고    scopus 로고
    • YplA is exported by the Ysc, Ysa, and flagellar type III secretion systems of Yersinia enterocolitica
    • Young B.M., Young G.M. YplA is exported by the Ysc, Ysa, and flagellar type III secretion systems of Yersinia enterocolitica. J. Bacteriol. 184:2002;1324-1334
    • (2002) J. Bacteriol. , vol.184 , pp. 1324-1334
    • Young, B.M.1    Young, G.M.2
  • 46
    • 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. 51:2004;483-495
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galan, J.E.2
  • 47
    • 0141430076 scopus 로고    scopus 로고
    • Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events
    • Gophna U., Ron E.Z., Graur D. Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events. Gene. 312:2003;151-163
    • (2003) Gene , vol.312 , pp. 151-163
    • Gophna, U.1    Ron, E.Z.2    Graur, D.3
  • 48
    • 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. 62:1998;379-433
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 51
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of the Salmonella typhimurium type III secretion components to needle complex formation
    • Kimbrough T.G., Miller S.I. Contribution of the Salmonella typhimurium type III secretion components to needle complex formation. Proc. Natl. Acad. Sci. U. S. A. 97:2000;11008-11013
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 53
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors
    • Tamano K., Aizawa S.-I., Katayama E., Nonaka T., Imajoh-Ohmi A., Kuwae A., Nagai S., Sasakawa C. Supramolecular structure of the Shigella type III secretion machinery: the needle part is changeable in length and essential for delivery of effectors. EMBO J. 19:2000;3876-3887
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.-I.2    Katayama, E.3    Nonaka, T.4    Imajoh-Ohmi, A.5    Kuwae, A.6    Nagai, S.7    Sasakawa, C.8
  • 54
    • 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. 98:2001;4669-4674
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4669-4674
    • Hoiczyk, E.1    Blobel, G.2
  • 56
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • Sekiya K., Ohishi M., Ogino T., Tamano K., Sasakawa C., Abe A. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. U. S. A. 98:2001;11638-11643
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 57
    • 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. 97:2000;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
  • 58
    • 0036282334 scopus 로고    scopus 로고
    • Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins
    • Magdalena J., Hachani A., Chamekh M., Jouihri N., Gounon P., Blocker A., Allaoui A. Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins. J. Bacteriol. 184:2002;3433-3441
    • (2002) J. Bacteriol. , vol.184 , pp. 3433-3441
    • Magdalena, J.1    Hachani, A.2    Chamekh, M.3    Jouihri, N.4    Gounon, P.5    Blocker, A.6    Allaoui, A.7
  • 59
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar typhimurium type III secretion-associated needle complex
    • Sukhan A., Kubori T., Wilson J., Galan J.E. Genetic analysis of assembly of the Salmonella enterica serovar typhimurium type III secretion-associated needle complex. J. Bacteriol. 183:2001;1159-1167
    • (2001) J. Bacteriol. , vol.183 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 60
    • 0036437055 scopus 로고    scopus 로고
    • Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein
    • Russmann H., Kubori T., Sauer J., Galan J.E. Molecular and functional analysis of the type III secretion signal of the Salmonella enterica InvJ protein. Mol. Microbiol. 46:2002;769-779
    • (2002) Mol. Microbiol. , vol.46 , pp. 769-779
    • Russmann, H.1    Kubori, T.2    Sauer, J.3    Galan, J.E.4
  • 61
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi K., Ohto Y., Aizawa S.-I., Macnab R.M., Iino T. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176:1994;2272-2281
    • (1994) J. Bacteriol. , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.-I.3    MacNab, R.M.4    Iino, T.5
  • 63
    • 0035868953 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling
    • Samatey F.A., Imada K., Nagashima S., Vonderviszt F., Kumasaka T., Yamamoto M., Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature. 410:2001;331-337
    • (2001) Nature , vol.410 , pp. 331-337
    • Samatey, F.A.1    Imada, K.2    Nagashima, S.3    Vonderviszt, F.4    Kumasaka, T.5    Yamamoto, M.6    Namba, K.7
  • 64
    • 0027402386 scopus 로고
    • Domain organization of the subunit of the Salmonella typhimurium flagellar hook
    • Morgan D.G., Macnab R.M., Francis N.R., DeRosier D.J. Domain organization of the subunit of the Salmonella typhimurium flagellar hook. J. Mol. Biol. 229:1993;79-84
    • (1993) J. Mol. Biol. , vol.229 , pp. 79-84
    • Morgan, D.G.1    MacNab, R.M.2    Francis, N.R.3    Derosier, D.J.4
  • 65
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature. 424:2003;643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 66
    • 0029039662 scopus 로고
    • The structure of the R-type straight flagellar filament of Salmonella at 9 a resolution by electron cryomicroscopy
    • Mimori Y., Yamashita I., Murata K., Fujiyoshi Y., Yonekura K., Toyoshima C., Namba K. The structure of the R-type straight flagellar filament of Salmonella at 9 A resolution by electron cryomicroscopy. J. Mol. Biol. 249:1995;69-87
    • (1995) J. Mol. Biol. , vol.249 , pp. 69-87
    • Mimori, Y.1    Yamashita, I.2    Murata, K.3    Fujiyoshi, Y.4    Yonekura, K.5    Toyoshima, C.6    Namba, K.7
  • 68
    • 0036041792 scopus 로고    scopus 로고
    • Coiled-coil proteins associated with type III secretion systems: A versatile domain revisited
    • Delahay R.M., Frankel G. Coiled-coil proteins associated with type III secretion systems: a versatile domain revisited. Mol. Microbiol. 45:2002;905-916
    • (2002) Mol. Microbiol. , vol.45 , pp. 905-916
    • Delahay, R.M.1    Frankel, G.2
  • 69
    • 0036165971 scopus 로고    scopus 로고
    • Assembly of the type III secretion needle complex of Salmonella typhimurium
    • Kimbrough T.G., Miller S.I. Assembly of the type III secretion needle complex of Salmonella typhimurium. Microbes Infect. 4:2002;75-82
    • (2002) Microbes Infect. , vol.4 , pp. 75-82
    • Kimbrough, T.G.1    Miller, S.I.2
  • 70
    • 0026792838 scopus 로고
    • M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF
    • Ueno T., Oosawa K., Aizawa S. M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF. J. Mol. Biol. 227:1992;672-677
    • (1992) J. Mol. Biol. , vol.227 , pp. 672-677
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.3
  • 71
    • 0030701512 scopus 로고    scopus 로고
    • The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body
    • Fan F., Ohnishi K., Francis N.R., Macnab R.M. The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body. Mol. Microbiol. 26:1997;1035-1046
    • (1997) Mol. Microbiol. , vol.26 , pp. 1035-1046
    • Fan, F.1    Ohnishi, K.2    Francis, N.R.3    MacNab, R.M.4
  • 72
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago A.M., Koronakis V. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30:1998;47-56
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 73
    • 0031777144 scopus 로고    scopus 로고
    • The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG
    • Daefler S., Russel M. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol. Microbiol. 28:1998;1367-1380
    • (1998) Mol. Microbiol. , vol.28 , pp. 1367-1380
    • Daefler, S.1    Russel, M.2
  • 74
    • 0038010148 scopus 로고    scopus 로고
    • Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system
    • Pucciarelli M.G., Garcia-Del Portillo F. Protein-peptidoglycan interactions modulate the assembly of the needle complex in the Salmonella invasion-associated type III secretion system. Mol. Microbiol. 48:2003;573-585
    • (2003) Mol. Microbiol. , vol.48 , pp. 573-585
    • Pucciarelli, M.G.1    Garcia-Del Portillo, F.2
  • 75
    • 0037219492 scopus 로고    scopus 로고
    • CesT is a bivalent enteropathogenic Escherichia coli chaperone required for translocation of both Tir and Map
    • Creasey E.A., Delahay R.M., Bishop A.A., Shaw R.K., Kenny B., Knutton S., Frankel G. CesT is a bivalent enteropathogenic Escherichia coli chaperone required for translocation of both Tir and Map. Mol. Microbiol. 47:2003;209-221
    • (2003) Mol. Microbiol. , vol.47 , pp. 209-221
    • Creasey, E.A.1    Delahay, R.M.2    Bishop, A.A.3    Shaw, R.K.4    Kenny, B.5    Knutton, S.6    Frankel, G.7
  • 76
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 370:1994;621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 78
    • 0035846895 scopus 로고    scopus 로고
    • Membrane traffic: What drives the AAA motor?
    • Dalal S., Hanson P.I. Membrane traffic: what drives the AAA motor? Cell. 104:2001;5-8
    • (2001) Cell , vol.104 , pp. 5-8
    • Dalal, S.1    Hanson, P.I.2
  • 79
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters J.M., Walsh M.J., Franke W.W. An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 9:1990;1757-1767
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 80
    • 0036178888 scopus 로고    scopus 로고
    • Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length
    • Tamano K., Katayama E., Toyotome T., Sasakawa C. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length. J. Bacteriol. 184:2002;1244-1252
    • (2002) J. Bacteriol. , vol.184 , pp. 1244-1252
    • Tamano, K.1    Katayama, E.2    Toyotome, T.3    Sasakawa, C.4
  • 81
    • 0029989240 scopus 로고    scopus 로고
    • Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium
    • Williams A.W., Yamaguchi S., Togashi F., Aizawa S.I., Kawagishi I., Macnab R.M. Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium. J. Bacteriol. 178:1996;2960-2970
    • (1996) J. Bacteriol. , vol.178 , pp. 2960-2970
    • Williams, A.W.1    Yamaguchi, S.2    Togashi, F.3    Aizawa, S.I.4    Kawagishi, I.5    MacNab, R.M.6
  • 82
    • 0035937441 scopus 로고    scopus 로고
    • Length of the flagellar hook and the capacity of the type III export apparatus
    • Makishima S., Komoriya K., Yamaguchi S., Aizawa S.I. Length of the flagellar hook and the capacity of the type III export apparatus. Science. 291:2001;2411-2413
    • (2001) Science , vol.291 , pp. 2411-2413
    • Makishima, S.1    Komoriya, K.2    Yamaguchi, S.3    Aizawa, S.I.4
  • 83
    • 0033900964 scopus 로고    scopus 로고
    • Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching
    • Minamino T., Macnab R.M. Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching. J. Bacteriol. 182:2000;4906-4914
    • (2000) J. Bacteriol. , vol.182 , pp. 4906-4914
    • Minamino, T.1    MacNab, R.M.2
  • 84
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino T., Macnab R.M. Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35:2000;1052-1064
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    MacNab, R.M.2
  • 86
    • 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. 302:2003;1757-1760
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 87
    • 0038190990 scopus 로고    scopus 로고
    • Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ
    • Sukhan A., Kubori T., Galan J.E. Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ. J. Bacteriol. 185:2003;3480-3483
    • (2003) J. Bacteriol. , vol.185 , pp. 3480-3483
    • Sukhan, A.1    Kubori, T.2    Galan, J.E.3
  • 88
    • 0032947339 scopus 로고    scopus 로고
    • YscP of Yersinia pestis is a secreted component of the Yop secretion system
    • Payne P.L., Straley S.C. YscP of Yersinia pestis is a secreted component of the Yop secretion system. J. Bacteriol. 181:1999;2852-2862
    • (1999) J. Bacteriol. , vol.181 , pp. 2852-2862
    • Payne, P.L.1    Straley, S.C.2
  • 89
    • 0032827183 scopus 로고    scopus 로고
    • FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly
    • Minamino T., Gonzalez-Pedrajo B., Yamaguchi K., Aizawa S.-I., Macnab R.M. FliK, the protein responsible for flagellar hook length control in Salmonella, is exported during hook assembly. Mol. Microbiol. 34:1999;295-304
    • (1999) Mol. Microbiol. , vol.34 , pp. 295-304
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Yamaguchi, K.3    Aizawa, S.-I.4    MacNab, R.M.5
  • 90
    • 0028288278 scopus 로고
    • Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium
    • Ginocchio C., Olmsted S.B., Wells C.L., Galan J.E. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell. 76:1994;717-724
    • (1994) Cell , vol.76 , pp. 717-724
    • Ginocchio, C.1    Olmsted, S.B.2    Wells, C.L.3    Galan, J.E.4
  • 91
    • 0029090966 scopus 로고
    • Contact with cultured epithelial cells stimulates secretion of Salmonella typhimurium invasion protein InvJ
    • Zierler M.K., Galán J.E. Contact with cultured epithelial cells stimulates secretion of Salmonella typhimurium invasion protein InvJ. Infect. Immun. 63:1995;4024-4028
    • (1995) Infect. Immun. , vol.63 , pp. 4024-4028
    • Zierler, M.K.1    Galán, J.E.2
  • 92
    • 0031923747 scopus 로고    scopus 로고
    • Cell-contact-stimulated formation of filamentous appendages by Salmonella typhimurium does not depend on the type III secretion system encoded by Salmonella pathogenicity island 1
    • Reed K.A., Clark M.A., Booth T.A., Hueck C.J., Miller S.I., Hirst B.H., Jepson M.A. Cell-contact-stimulated formation of filamentous appendages by Salmonella typhimurium does not depend on the type III secretion system encoded by Salmonella pathogenicity island 1. Infect. Immun. 66:1998;2007-2017
    • (1998) Infect. Immun. , vol.66 , pp. 2007-2017
    • Reed, K.A.1    Clark, M.A.2    Booth, T.A.3    Hueck, C.J.4    Miller, S.I.5    Hirst, B.H.6    Jepson, M.A.7
  • 93
    • 0032522344 scopus 로고    scopus 로고
    • A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells
    • Knutton S., Rosenshine I., Pallen M.J., Nisan I., Neves B.C., Bain C., Wolff C., Dougan G., Frankel G. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 17:1998;2166-2176
    • (1998) EMBO J. , vol.17 , pp. 2166-2176
    • Knutton, S.1    Rosenshine, I.2    Pallen, M.J.3    Nisan, I.4    Neves, B.C.5    Bain, C.6    Wolff, C.7    Dougan, G.8    Frankel, G.9
  • 94
    • 0031696843 scopus 로고    scopus 로고
    • Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages
    • Ebel F., Podzadel T., Rohde M., Kresse A.U., Kramer S., Deibel C., Guzman C.A., Chakraborty T. Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages. Mol. Microbiol. 30:1998;147-161
    • (1998) Mol. Microbiol. , vol.30 , pp. 147-161
    • Ebel, F.1    Podzadel, T.2    Rohde, M.3    Kresse, A.U.4    Kramer, S.5    Deibel, C.6    Guzman, C.A.7    Chakraborty, T.8
  • 95
    • 0035167256 scopus 로고    scopus 로고
    • Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli
    • Wilson R.K., Shaw R.K., Daniell S., Knutton S., Frankel G. Role of EscF, a putative needle complex protein, in the type III protein translocation system of enteropathogenic Escherichia coli. Cell. Microbiol. 3:2001;753-762
    • (2001) Cell. Microbiol. , vol.3 , pp. 753-762
    • Wilson, R.K.1    Shaw, R.K.2    Daniell, S.3    Knutton, S.4    Frankel, G.5
  • 97
    • 0037325044 scopus 로고    scopus 로고
    • The Hrp Pilus: Learning from flagella
    • He S.Y., Jin Q. The Hrp Pilus: learning from flagella. Curr. Opin. Microbiol. 6:2003;15-19
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 15-19
    • He, S.Y.1    Jin, Q.2
  • 99
    • 0034055715 scopus 로고    scopus 로고
    • Ralstonia solanacearum produces Hrp-dependent pili that are required for PopA secretion but not for attachment of bacteria to plant cells
    • Van Gijsegem F., Vasse J., Camus J., Marenda M., Boucher C. Ralstonia solanacearum produces Hrp-dependent pili that are required for PopA secretion but not for attachment of bacteria to plant cells. Mol. Microbiol. 36:2000;249-260
    • (2000) Mol. Microbiol. , vol.36 , pp. 249-260
    • Van Gijsegem, F.1    Vasse, J.2    Camus, J.3    Marenda, M.4    Boucher, C.5
  • 100
    • 0034973395 scopus 로고    scopus 로고
    • Visualization of secreted Hrp and Avr proteins along the Hrp pilus during type III secretion in Erwinia amylovora and Pseudomonas syringae
    • Jin Q., Hu W., Brown I., McGhee G., Hart P., Jones A., He S.Y. Visualization of secreted Hrp and Avr proteins along the Hrp pilus during type III secretion in Erwinia amylovora and Pseudomonas syringae. Mol. Microbiol. 40:2001;1129-1139
    • (2001) Mol. Microbiol. , vol.40 , pp. 1129-1139
    • Jin, Q.1    Hu, W.2    Brown, I.3    McGhee, G.4    Hart, P.5    Jones, A.6    He, S.Y.7
  • 101
    • 0035578330 scopus 로고    scopus 로고
    • The role of bacterial pili in protein and DNA translocation
    • Koebnik R. The role of bacterial pili in protein and DNA translocation. Trends Microbiol. 9:2001;586-590
    • (2001) Trends Microbiol. , vol.9 , pp. 586-590
    • Koebnik, R.1
  • 102
    • 0038545909 scopus 로고    scopus 로고
    • Extracellular proteins involved in soybean cultivar-specific nodulation are associated with pilus-like surface appendages and exported by a type III protein secretion system in Sinorhizobium fredii USDA257
    • Krishnan H.B., Lorio J., Kim W.S., Jiang G., Kim K.Y., DeBoer M., Pueppke S.G. Extracellular proteins involved in soybean cultivar-specific nodulation are associated with pilus-like surface appendages and exported by a type III protein secretion system in Sinorhizobium fredii USDA257. Mol. Plant-Microb. Interact. 16:2003;617-625
    • (2003) Mol. Plant-Microb. Interact. , vol.16 , pp. 617-625
    • Krishnan, H.B.1    Lorio, J.2    Kim, W.S.3    Jiang, G.4    Kim, K.Y.5    Deboer, M.6    Pueppke, S.G.7
  • 103
    • 0031783010 scopus 로고    scopus 로고
    • Characterization of the hrpC and hrpRS operons of Pseudomonas syringae pathovars syringae, tomato, and glycinea and analysis of the ability of hrpF, hrpG, hrcC, hrpT, and hrpV mutants to elicit the hypersensitive response and disease in plants
    • Deng W.L., Preston G., Collmer A., Chang C.J., Huang H.C. Characterization of the hrpC and hrpRS operons of Pseudomonas syringae pathovars syringae, tomato, and glycinea and analysis of the ability of hrpF, hrpG, hrcC, hrpT, and hrpV mutants to elicit the hypersensitive response and disease in plants. J. Bacteriol. 180:1998;4523-4531
    • (1998) J. Bacteriol. , vol.180 , pp. 4523-4531
    • Deng, W.L.1    Preston, G.2    Collmer, A.3    Chang, C.J.4    Huang, H.C.5
  • 105
    • 0030840106 scopus 로고    scopus 로고
    • Purified HrpA of Pseudomonas syringae pv. tomato DC3000 reassembles into pili
    • Roine E., Saarinen J., Kalkkinen N., Romantschuk M. Purified HrpA of Pseudomonas syringae pv. tomato DC3000 reassembles into pili. FEBS Lett. 417:1997;168-172
    • (1997) FEBS Lett. , vol.417 , pp. 168-172
    • Roine, E.1    Saarinen, J.2    Kalkkinen, N.3    Romantschuk, M.4
  • 107
    • 0036791896 scopus 로고    scopus 로고
    • Genomic mining type III secretion system effectors in Pseudomonas syringae yields new picks for all TTSS prospectors
    • Collmer A., Lindeberg M., Petnicki-Ocwieja T., Schneider D.J., Alfano J.R. Genomic mining type III secretion system effectors in Pseudomonas syringae yields new picks for all TTSS prospectors. Trends Microbiol. 10:2002;462-469
    • (2002) Trends Microbiol. , vol.10 , pp. 462-469
    • Collmer, A.1    Lindeberg, M.2    Petnicki-Ocwieja, T.3    Schneider, D.J.4    Alfano, J.R.5
  • 108
    • 0000233986 scopus 로고    scopus 로고
    • Hrp-controlled interkingdom protein transport: Learning from flagellar assembly?
    • He S.Y. Hrp-controlled interkingdom protein transport: learning from flagellar assembly? Trends Microbiol. 5:1997;489-495
    • (1997) Trends Microbiol. , vol.5 , pp. 489-495
    • He, S.Y.1
  • 109
  • 111
    • 0034090630 scopus 로고    scopus 로고
    • The structural protein of the Hrp pilus is required for coordinate regulation of the type III secretion system and secretion of Hrp and Avr proteins in Pseudomonas syringae pv. tomato
    • Wei W., Plovanich-Jones A., Deng W.-L., Collmer A., Huang H.-C., He S.Y. The structural protein of the Hrp pilus is required for coordinate regulation of the type III secretion system and secretion of Hrp and Avr proteins in Pseudomonas syringae pv. tomato. Proc. Natl. Acad. Sci. U. S. A. 97:2000;2247-2252
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2247-2252
    • Wei, W.1    Plovanich-Jones, A.2    Deng, W.-L.3    Collmer, A.4    Huang, H.-C.5    He, S.Y.6
  • 112
    • 0036091020 scopus 로고    scopus 로고
    • Genetic dissection of Ralstonia solanacearum hrp gene cluster reveals that the HrpV and HrpX proteins are required for Hrp pilus assembly
    • Van Gijsegem F., Vasse J., De Rycke R., Castello P., Boucher C. Genetic dissection of Ralstonia solanacearum hrp gene cluster reveals that the HrpV and HrpX proteins are required for Hrp pilus assembly. Mol. Microbiol. 44:2002;935-946
    • (2002) Mol. Microbiol. , vol.44 , pp. 935-946
    • Van Gijsegem, F.1    Vasse, J.2    De Rycke, R.3    Castello, P.4    Boucher, C.5
  • 113
    • 0035114376 scopus 로고    scopus 로고
    • Immunocytochemical localization of HrpA and HrpZ supports a role for the Hrp pilus in the transfer of effector proteins from Pseudomonas syringae pv. tomato across the host plant cell wall
    • Brown I.R., Mansfield J.W., Taira S., Roine E., Romantschuk M. Immunocytochemical localization of HrpA and HrpZ supports a role for the Hrp pilus in the transfer of effector proteins from Pseudomonas syringae pv. tomato across the host plant cell wall. Mol. Plant-Microb. Interact. 14:2001;394-404
    • (2001) Mol. Plant-Microb. Interact. , vol.14 , pp. 394-404
    • Brown, I.R.1    Mansfield, J.W.2    Taira, S.3    Roine, E.4    Romantschuk, M.5
  • 114
    • 0028318685 scopus 로고
    • A single promoter sequence recognized by a newly identified alternate sigma factor directs expression of pathogenicity and host range determinants in Pseudomonas syringae
    • Xiao Y., Hutcheson S. A single promoter sequence recognized by a newly identified alternate sigma factor directs expression of pathogenicity and host range determinants in Pseudomonas syringae. J. Bacteriol. 176:1994;3089-3091
    • (1994) J. Bacteriol. , vol.176 , pp. 3089-3091
    • Xiao, Y.1    Hutcheson, S.2
  • 115
    • 0035930715 scopus 로고    scopus 로고
    • Role of the Hrp pilus in type III secretion in Pseudomonas syringae
    • Jin Q.-L., He S.Y. Role of the Hrp pilus in type III secretion in Pseudomonas syringae. Science. 294:2001;2556-2558
    • (2001) Science , vol.294 , pp. 2556-2558
    • Jin, Q.-L.1    He, S.Y.2
  • 116
    • 0037090775 scopus 로고    scopus 로고
    • The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ
    • Li C.M., Brown I., Mansfield J., Stevens C., Boureau T., Romantschuk M., Taira S. The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ. EMBO J. 21:2002;1909-1915
    • (2002) EMBO J. , vol.21 , pp. 1909-1915
    • Li, C.M.1    Brown, I.2    Mansfield, J.3    Stevens, C.4    Boureau, T.5    Romantschuk, M.6    Taira, S.7
  • 117
    • 0014939798 scopus 로고
    • Bacterial flagella: Polarity of elongation
    • Emerson S.U., Tokuyasu K., Simon M. Bacterial flagella: Polarity of elongation. Science. 169:1970;190-192
    • (1970) Science , vol.169 , pp. 190-192
    • Emerson, S.U.1    Tokuyasu, K.2    Simon, M.3
  • 118
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels T., Cornelis G.R. Secretion of hybrid proteins by the Yersinia Yop export system. J. Bacteriol. 173:1991;1677-1685
    • (1991) J. Bacteriol. , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 119
    • 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. 92:1995;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
  • 120
    • 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. 278:1997;1140-1143
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 121
    • 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. 31:1999;1139-1148
    • (1999) Mol. Microbiol. , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 122
    • 0344826589 scopus 로고    scopus 로고
    • Substrate recognition by the Yersinia type III protein secretion machinery
    • Ramamurthi K.S., Schneewind O. Substrate recognition by the Yersinia type III protein secretion machinery. Mol. Microbiol. 50:2003;1189-1198
    • (2003) Mol. Microbiol. , vol.50 , pp. 1189-1198
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 123
    • 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. 50:2003;1091-1094
    • (2003) Mol. Microbiol. , vol.50 , pp. 1091-1094
    • Cornelis, G.R.1
  • 124
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd A., Norman M., Rosqvist R., Wolf-Watz H. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol. Microbiol. 39:2001;520-531
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 125
    • 0036197569 scopus 로고    scopus 로고
    • Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
    • Lloyd S.A., Sjostrom M., Andersson S., Wolf-Watz H. Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences. Mol. Microbiol. 43:2002;51-59
    • (2002) Mol. Microbiol. , vol.43 , pp. 51-59
    • Lloyd, S.A.1    Sjostrom, M.2    Andersson, S.3    Wolf-Watz, H.4
  • 127
    • 0035136805 scopus 로고    scopus 로고
    • Functional analysis of the type III effectors AvrRpt2 and AvrRpm1 of Pseudomonas syringae with the use of a single-copy genomic integration system
    • Guttman D.S., Greenberg J.T. Functional analysis of the type III effectors AvrRpt2 and AvrRpm1 of Pseudomonas syringae with the use of a single-copy genomic integration system. Mol. Plant-Microb. Interact. 14:2001;145-155
    • (2001) Mol. Plant-Microb. Interact. , vol.14 , pp. 145-155
    • Guttman, D.S.1    Greenberg, J.T.2
  • 128
    • 0036500995 scopus 로고    scopus 로고
    • A functional screen for the type III (Hrp) secretome of the plant pathogen Pseudomonas syringae
    • Guttman D.S., Vinatzer B.A., Sarkar S.F., Ranall M.V., Kettler G., Greenberg J.T. A functional screen for the type III (Hrp) secretome of the plant pathogen Pseudomonas syringae. Science. 295:2002;1722-1726
    • (2002) Science , vol.295 , pp. 1722-1726
    • Guttman, D.S.1    Vinatzer, B.A.2    Sarkar, S.F.3    Ranall, M.V.4    Kettler, G.5    Greenberg, J.T.6
  • 130
    • 0141789821 scopus 로고    scopus 로고
    • Pseudomonas syringae pv. tomato DC3000 HopPtoM (CEL ORF3) is important for lesion formation but not growth in tomato and is secreted and translocated by the Hrp type III secretion system in a chaperone-dependent manner
    • Badel J.L., Nomura K., Bandyopadhyay S., Shimizu R., Collmer A., He S.Y. Pseudomonas syringae pv. tomato DC3000 HopPtoM (CEL ORF3) is important for lesion formation but not growth in tomato and is secreted and translocated by the Hrp type III secretion system in a chaperone-dependent manner. Mol. Microbiol. 49:2003;1239-1251
    • (2003) Mol. Microbiol. , vol.49 , pp. 1239-1251
    • Badel, J.L.1    Nomura, K.2    Bandyopadhyay, S.3    Shimizu, R.4    Collmer, A.5    He, S.Y.6
  • 131
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot C., Hamiaux C., Page A.L. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6:2003;7-14
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 132
    • 0037469577 scopus 로고    scopus 로고
    • The multitalented type III chaperones: All you can do with 15 kDa
    • Feldman M.F., Cornelis G.R. The multitalented type III chaperones: all you can do with 15 kDa. FEMS Microbiol. Lett. 219:2003;151-158
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 151-158
    • Feldman, M.F.1    Cornelis, G.R.2
  • 133
    • 0036734864 scopus 로고    scopus 로고
    • The DspB/F protein of Erwinia amylovora is a type III secretion chaperone ensuring efficient intrabacterial production of the Hrp-secreted DspA/E pathogenicity factor
    • Gaudriault S., Paulin J.-P., Barny M.-A. The DspB/F protein of Erwinia amylovora is a type III secretion chaperone ensuring efficient intrabacterial production of the Hrp-secreted DspA/E pathogenicity factor. Mol. Plant Pathol. 3:2002;313-321
    • (2002) Mol. Plant Pathol. , vol.3 , pp. 313-321
    • Gaudriault, S.1    Paulin, J.-P.2    Barny, M.-A.3
  • 134
    • 0036016804 scopus 로고    scopus 로고
    • The ShcA protein is a molecular chaperone that assists in the secretion of the HopPsyA effector from the type III (Hrp) protein secretion system of Pseudomonas syringae
    • van Dijk K., Tam V.C., Records A.R., Petnicki-Ocwieja T., Alfano J.R. The ShcA protein is a molecular chaperone that assists in the secretion of the HopPsyA effector from the type III (Hrp) protein secretion system of Pseudomonas syringae. Mol. Microbiol. 44:2002;1469-1481
    • (2002) Mol. Microbiol. , vol.44 , pp. 1469-1481
    • Van Dijk, K.1    Tam, V.C.2    Records, A.R.3    Petnicki-Ocwieja, T.4    Alfano, J.R.5
  • 135
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau P., Cornelis G.R. SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol. Microbiol. 8:1993;123-131
    • (1993) Mol. Microbiol. , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 136
    • 0041335630 scopus 로고    scopus 로고
    • The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000
    • Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., et al. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc. Natl. Acad. Sci. U. S. A. 100:2003;10181-10186
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10181-10186
    • Buell, C.R.1    Joardar, V.2    Lindeberg, M.3    Selengut, J.4    Paulsen, I.T.5
  • 137
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • Auvray F., Thomas J., Fraser G.M., Hughes C. Flagellin polymerisation control by a cytosolic export chaperone. J. Mol. Biol. 308:2001;221-229
    • (2001) J. Mol. Biol. , vol.308 , pp. 221-229
    • Auvray, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 138
    • 0034753703 scopus 로고    scopus 로고
    • Structure of the Yersinia type III secretory system chaperone SycE
    • Birtalan S., Ghosh P. Structure of the Yersinia type III secretory system chaperone SycE. Nat. Struct. Biol. 8:2001;974-978
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 974-978
    • Birtalan, S.1    Ghosh, P.2
  • 139
    • 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. 9:2002;971-980
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 140
    • 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. 414:2001;77-81
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 143
    • 0030696362 scopus 로고    scopus 로고
    • DspA, an essential pathogenicity factor of Erwinia amylovora showing homology with AvrE of Pseudomonas syringae, is secreted via the Hrp secretion pathway in a DspB-dependent way
    • Gaudriault S., Malandrin L., Paulin J.-P., Barny M.A. DspA, an essential pathogenicity factor of Erwinia amylovora showing homology with AvrE of Pseudomonas syringae, is secreted via the Hrp secretion pathway in a DspB-dependent way. Mol. Microbiol. 26:1997;1057-1069
    • (1997) Mol. Microbiol. , vol.26 , pp. 1057-1069
    • Gaudriault, S.1    Malandrin, L.2    Paulin, J.-P.3    Barny, M.A.4
  • 144
    • 0031923066 scopus 로고    scopus 로고
    • Erwinia amylovora secretes DspE, a pathogenicity factor and functional AvrE homolog, through the Hrp (type III secretion) pathway
    • Bogdanove A.J., Bauer D.W., Beer S.V. Erwinia amylovora secretes DspE, a pathogenicity factor and functional AvrE homolog, through the Hrp (type III secretion) pathway. J. Bacteriol. 180:1998;2244-2247
    • (1998) J. Bacteriol. , vol.180 , pp. 2244-2247
    • Bogdanove, A.J.1    Bauer, D.W.2    Beer, S.V.3
  • 145
    • 0036436338 scopus 로고    scopus 로고
    • SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system
    • Feldman M.F., Muller S., Wuest E., Cornelis G.R. SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system. Mol. Microbiol. 46:2002;1183-1197
    • (2002) Mol. Microbiol. , vol.46 , pp. 1183-1197
    • Feldman, M.F.1    Muller, S.2    Wuest, E.3    Cornelis, G.R.4
  • 146
    • 0036283447 scopus 로고    scopus 로고
    • Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion
    • Lee V.T., Schneewind O. Yop fusions to tightly folded protein domains and their effects on Yersinia enterocolitica type III secretion. J. Bacteriol. 184:2002;3740-3745
    • (2002) J. Bacteriol. , vol.184 , pp. 3740-3745
    • Lee, V.T.1    Schneewind, O.2
  • 147
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD
    • Neyt C., Cornelis G.R. Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD. Mol. Microbiol. 31:1999;143-156
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 148
    • 0030967331 scopus 로고    scopus 로고
    • Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica
    • Cheng L.W., Anderson D.M., Schneewind O. Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica. Mol. Microbiol. 24:1997;757-765
    • (1997) Mol. Microbiol. , vol.24 , pp. 757-765
    • Cheng, L.W.1    Anderson, D.M.2    Schneewind, O.3
  • 149
    • 0033872740 scopus 로고    scopus 로고
    • Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE
    • Boyd A.P., Lambermont I., Cornelis G.R. Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE. J. Bacteriol. 182:2000;4811-4821
    • (2000) J. Bacteriol. , vol.182 , pp. 4811-4821
    • Boyd, A.P.1    Lambermont, I.2    Cornelis, G.R.3
  • 150
    • 0033618257 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells
    • Cheng L.W., Schneewind O. Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells. J. Biol. Chem. 274:1999;22102-22108
    • (1999) J. Biol. Chem. , vol.274 , pp. 22102-22108
    • Cheng, L.W.1    Schneewind, O.2
  • 151
    • 0029070827 scopus 로고
    • The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci
    • Frithz-Lindsten E., Rosqvist R., Johansson L., Forsberg A. The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci. Mol. Microbiol. 16:1995;635-647
    • (1995) Mol. Microbiol. , vol.16 , pp. 635-647
    • Frithz-Lindsten, E.1    Rosqvist, R.2    Johansson, L.3    Forsberg, A.4
  • 152
    • 0029944323 scopus 로고    scopus 로고
    • The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes
    • Woestyn S., Sory M.P., Boland A., Lequenne O., Cornelis G.R. The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes. Mol. Microbiol. 20:1996;1261-1271
    • (1996) Mol. Microbiol. , vol.20 , pp. 1261-1271
    • Woestyn, S.1    Sory, M.P.2    Boland, A.3    Lequenne, O.4    Cornelis, G.R.5
  • 153
    • 0028072943 scopus 로고
    • The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD
    • Ménard R., Sansonetti P., Parsot C. The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD. EMBO J. 13:1994;5293-5302
    • (1994) EMBO J. , vol.13 , pp. 5293-5302
    • Ménard, R.1    Sansonetti, P.2    Parsot, C.3
  • 154
    • 0032906245 scopus 로고    scopus 로고
    • Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly
    • Fraser G.M., Bennett J.C., Hughes C. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol. Microbiol. 32:1999;569-580
    • (1999) Mol. Microbiol. , vol.32 , pp. 569-580
    • Fraser, G.M.1    Bennett, J.C.2    Hughes, C.3
  • 155
    • 0035133472 scopus 로고    scopus 로고
    • Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT
    • Bennett J.C., Thomas J., Fraser G.M., Hughes C. Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT. Mol. Microbiol. 39:2001;781-791
    • (2001) Mol. Microbiol. , vol.39 , pp. 781-791
    • Bennett, J.C.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 156
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • Persson C., Nordfelth R., Holmstrom A., Hakansson S., Rosqvist R., Wolf-Watz H. Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol. Microbiol. 18:1995;135-150
    • (1995) Mol. Microbiol. , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmstrom, A.3    Hakansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 158
    • 0033485823 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion-translocation system: Channel formation by secreted Yops
    • Tardy F., Homble F., Neyt C., Wattiez R., Cornelis G.R., Ruysschaert J.M., Cabiaux V. Yersinia enterocolitica type III secretion-translocation system: channel formation by secreted Yops. EMBO J. 18:1999;6793-6799
    • (1999) EMBO J. , vol.18 , pp. 6793-6799
    • Tardy, F.1    Homble, F.2    Neyt, C.3    Wattiez, R.4    Cornelis, G.R.5    Ruysschaert, J.M.6    Cabiaux, V.7
  • 160
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for the
    • Håkansson S., Schesser K., Persson C., Galyov E.E., Rosqvist R., Homble F., Wolf-Watz H. The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact dependent membrane-disrupting activity. EMBO J. 15:1996;5812-5823
    • (1996) EMBO J. , vol.15 , pp. 5812-5823
    • Håkansson, S.1    Schesser, K.2    Persson, C.3    Galyov, E.E.4    Rosqvist, R.5    Homble, F.6    Wolf-Watz, H.7
  • 161
    • 0031885218 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD
    • Sarker M.R., Neyt C., Stainier I., Cornelis G.R. The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J. Bacteriol. 180:1998;1207-1214
    • (1998) J. Bacteriol. , vol.180 , pp. 1207-1214
    • Sarker, M.R.1    Neyt, C.2    Stainier, I.3    Cornelis, G.R.4
  • 162
    • 0031802098 scopus 로고    scopus 로고
    • The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG
    • Nilles M.L., Fields K.A., Straley S.C. The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG. J. Bacteriol. 180:1998;3410-3420
    • (1998) J. Bacteriol. , vol.180 , pp. 3410-3420
    • Nilles, M.L.1    Fields, K.A.2    Straley, S.C.3
  • 163
    • 0031928329 scopus 로고    scopus 로고
    • YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: Evidence of a structural domain necessary for translocation
    • Francis M.S., Wolf-Watz H. YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation. Mol. Microbiol. 29:1998;799-813
    • (1998) Mol. Microbiol. , vol.29 , pp. 799-813
    • Francis, M.S.1    Wolf-Watz, H.2
  • 165
    • 0031683634 scopus 로고    scopus 로고
    • Functional conservation of the effector protein translocators PopB/YopB and PopD/YopD of Pseudomonas aeruginosa and Yersinia pseudotuberculosis
    • Frithz-Lindsten E., Holmstrom A., Jacobsson L., Soltani M., Olsson J., Rosqvist R., Forsberg A. Functional conservation of the effector protein translocators PopB/YopB and PopD/YopD of Pseudomonas aeruginosa and Yersinia pseudotuberculosis. Mol. Microbiol. 29:1998;1155-1165
    • (1998) Mol. Microbiol. , vol.29 , pp. 1155-1165
    • Frithz-Lindsten, E.1    Holmstrom, A.2    Jacobsson, L.3    Soltani, M.4    Olsson, J.5    Rosqvist, R.6    Forsberg, A.7
  • 166
    • 0037380681 scopus 로고    scopus 로고
    • Protein binding between PcrG-PcrV and PcrH-PopB/PopD encoded by the pcrGVH-popBD operon of the Pseudomonas aeruginosa type III secretion system
    • Allmond L.R., Karaca T.J., Nguyen V.N., Nguyen T., Wiener-Kronish J.P., Sawa T. Protein binding between PcrG-PcrV and PcrH-PopB/PopD encoded by the pcrGVH-popBD operon of the Pseudomonas aeruginosa type III secretion system. Infect. Immun. 71:2003;2230-2233
    • (2003) Infect. Immun. , vol.71 , pp. 2230-2233
    • Allmond, L.R.1    Karaca, T.J.2    Nguyen, V.N.3    Nguyen, T.4    Wiener-Kronish, J.P.5    Sawa, T.6
  • 167
    • 0035047787 scopus 로고    scopus 로고
    • Pore-forming activity of type III system-secreted proteins leads to oncosis of Pseudomonas aeruginosa-infected macrophages
    • Dacheux D., Goure J., Chabert J., Usson Y., Attree I. Pore-forming activity of type III system-secreted proteins leads to oncosis of Pseudomonas aeruginosa-infected macrophages. Mol. Microbiol. 40:2001;76-85
    • (2001) Mol. Microbiol. , vol.40 , pp. 76-85
    • Dacheux, D.1    Goure, J.2    Chabert, J.3    Usson, Y.4    Attree, I.5
  • 168
    • 0032907634 scopus 로고    scopus 로고
    • Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury
    • Sawa T., Yahr T.L., Ohara M., Kurahashi K., Gropper M.A., Wiener-Kronish J.P., Frank D.W. Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury. Nat. Med. 5:1999;392-398
    • (1999) Nat. Med. , vol.5 , pp. 392-398
    • Sawa, T.1    Yahr, T.L.2    Ohara, M.3    Kurahashi, K.4    Gropper, M.A.5    Wiener-Kronish, J.P.6    Frank, D.W.7
  • 169
    • 0141642035 scopus 로고    scopus 로고
    • Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas
    • Schoehn G., Di Guilmi A.M., Lemaire D., Attree I., Weissenhorn W., Dessen A. Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22:2003;4957-4967
    • (2003) EMBO J. , vol.22 , pp. 4957-4967
    • Schoehn, G.1    Di Guilmi, A.M.2    Lemaire, D.3    Attree, I.4    Weissenhorn, W.5    Dessen, A.6
  • 170
    • 0031922691 scopus 로고    scopus 로고
    • Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli
    • Wolff C., Nisan I., Hanski E., Frankel G., Rosenshine I. Protein translocation into host epithelial cells by infecting enteropathogenic Escherichia coli. Mol. Microbiol. 1998;143-155
    • (1998) Mol. Microbiol. , pp. 143-155
    • Wolff, C.1    Nisan, I.2    Hanski, E.3    Frankel, G.4    Rosenshine, I.5
  • 171
    • 0032992390 scopus 로고    scopus 로고
    • Insertion of EspD into epithelial target cell membranes by infecting enteropathogenic Escherichia coli
    • Wachter C., Beinke C., Mattes M., Schmidt M.A. Insertion of EspD into epithelial target cell membranes by infecting enteropathogenic Escherichia coli. Mol. Microbiol. 31:1999;1695-1707
    • (1999) Mol. Microbiol. , vol.31 , pp. 1695-1707
    • Wachter, C.1    Beinke, C.2    Mattes, M.3    Schmidt, M.A.4
  • 172
    • 0032774771 scopus 로고    scopus 로고
    • The EspD protein of enterohemorrhagic Escherichia coli is required for the formation of bacterial surface appendages and is incorporated in the cytoplasmic membranes of target cells
    • Kresse A.U., Rohde M., Guzman C.A. The EspD protein of enterohemorrhagic Escherichia coli is required for the formation of bacterial surface appendages and is incorporated in the cytoplasmic membranes of target cells. Infect. Immun. 67:1999;4834-4842
    • (1999) Infect. Immun. , vol.67 , pp. 4834-4842
    • Kresse, A.U.1    Rohde, M.2    Guzman, C.A.3
  • 173
    • 0032868135 scopus 로고    scopus 로고
    • Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli
    • Warawa J., Finlay B.B., Kenny B. Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli. Infect. Immun. 67:1999;5538-5540
    • (1999) Infect. Immun. , vol.67 , pp. 5538-5540
    • Warawa, J.1    Finlay, B.B.2    Kenny, B.3
  • 174
    • 0034775390 scopus 로고    scopus 로고
    • Characterization of translocation pores inserted into plasma membranes by type III-secreted Esp proteins of enteropathogenic Escherichia coli
    • Ide T., Laarmann S., Greune L., Schillers H., Oberleithner H., Schmidt M.A. Characterization of translocation pores inserted into plasma membranes by type III-secreted Esp proteins of enteropathogenic Escherichia coli. Cell. Microbiol. 3:2001;669-679
    • (2001) Cell. Microbiol. , vol.3 , pp. 669-679
    • Ide, T.1    Laarmann, S.2    Greune, L.3    Schillers, H.4    Oberleithner, H.5    Schmidt, M.A.6
  • 176
    • 0028113512 scopus 로고
    • Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri
    • Menard R., Sansonetti P., Parsot C., Vasselon T. Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri. Cell. 79:1994;515-525
    • (1994) Cell , vol.79 , pp. 515-525
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3    Vasselon, T.4
  • 177
    • 0031007757 scopus 로고    scopus 로고
    • The invasion-associated type III secretion system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell
    • Collazo C.M., Galán J.E. The invasion-associated type III secretion system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell. Mol. Microbiol. 24:1997;747-756
    • (1997) Mol. Microbiol. , vol.24 , pp. 747-756
    • Collazo, C.M.1    Galán, J.E.2
  • 179
    • 0033825366 scopus 로고    scopus 로고
    • Characterisation of the interaction of IpaB and IpaD, proteins required for entry of Shigella flexneri into epithelial cells, with a lipid membrane
    • De Geyter C., Wattiez R., Sansonetti P., Falmagne P., Ruysschaert J.-M., Parsot C., Cabiaux V. Characterisation of the interaction of IpaB and IpaD, proteins required for entry of Shigella flexneri into epithelial cells, with a lipid membrane. Eur. J. Biochem. 267:2000;5769-5776
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5769-5776
    • De Geyter, C.1    Wattiez, R.2    Sansonetti, P.3    Falmagne, P.4    Ruysschaert, J.-M.5    Parsot, C.6    Cabiaux, V.7
  • 180
    • 0035943592 scopus 로고    scopus 로고
    • Shigella invasion of macrophage requires the insertion of IpaC into the host plasma membrane. Functional analysis of IpaC
    • Kuwae A., Yoshida S., Tamano K., Mimuro H., Suzuki T., Sasakawa C. Shigella invasion of macrophage requires the insertion of IpaC into the host plasma membrane. Functional analysis of IpaC. J. Bio. Chem. 276:2001;32230-32239
    • (2001) J. Bio. Chem. , vol.276 , pp. 32230-32239
    • Kuwae, A.1    Yoshida, S.2    Tamano, K.3    Mimuro, H.4    Suzuki, T.5    Sasakawa, C.6
  • 181
    • 0038501071 scopus 로고    scopus 로고
    • The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology
    • Hume P.J., McGhie E.J., Hayward R.D., Koronakis V. The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology. Mol. Microbiol. 49:2003;425-439
    • (2003) Mol. Microbiol. , vol.49 , pp. 425-439
    • Hume, P.J.1    McGhie, E.J.2    Hayward, R.D.3    Koronakis, V.4
  • 182
    • 0033852317 scopus 로고    scopus 로고
    • Membrane fusion activity of purified SipB, a Salmonella surface protein essential for mammalian cell invasion
    • Hayward R.D., McGhie E.J., Koronakis V. Membrane fusion activity of purified SipB, a Salmonella surface protein essential for mammalian cell invasion. Mol. Microbiol. 37:2000;727-739
    • (2000) Mol. Microbiol. , vol.37 , pp. 727-739
    • Hayward, R.D.1    McGhie, E.J.2    Koronakis, V.3
  • 184
    • 0033817265 scopus 로고    scopus 로고
    • The Salmonella type III secretion translocon protein SspC is inserted into the epithelial plasma membrane upon infection
    • Scherer C.A., Cooper E., Miller S.I. The Salmonella type III secretion translocon protein SspC is inserted into the epithelial plasma membrane upon infection. Mol. Microbiol. 37:2000;1133-1145
    • (2000) Mol. Microbiol. , vol.37 , pp. 1133-1145
    • Scherer, C.A.1    Cooper, E.2    Miller, S.I.3
  • 185
    • 0036032271 scopus 로고    scopus 로고
    • A Salmonella SipB-derived polypeptide blocks the 'trigger' mechanism of bacterial entry into eukaryotic cells
    • Hayward R.D., Hume P.J., McGhie E.J., Koronakis V. A Salmonella SipB-derived polypeptide blocks the 'trigger' mechanism of bacterial entry into eukaryotic cells. Mol. Microbiol. 45:2002;1715-1727
    • (2002) Mol. Microbiol. , vol.45 , pp. 1715-1727
    • Hayward, R.D.1    Hume, P.J.2    McGhie, E.J.3    Koronakis, V.4
  • 186
    • 0032422028 scopus 로고    scopus 로고
    • Protein-protein interactions in the assembly of Shigella flexneri invasion plasmid antigens IpaB and IpaC into protein complexes
    • Davis R., Marquart M.E., Lucius D., Picking W.D. Protein-protein interactions in the assembly of Shigella flexneri invasion plasmid antigens IpaB and IpaC into protein complexes. Biochim. Biophys. Acta. 1429:1998;45-56
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 45-56
    • Davis, R.1    Marquart, M.E.2    Lucius, D.3    Picking, W.D.4
  • 188
    • 0035162215 scopus 로고    scopus 로고
    • Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri
    • Page A.L., Fromont-Racine M., Sansonetti P., Legrain P., Parsot C. Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri. Mol. Microbiol. 42:2001;1133-1145
    • (2001) Mol. Microbiol. , vol.42 , pp. 1133-1145
    • Page, A.L.1    Fromont-Racine, M.2    Sansonetti, P.3    Legrain, P.4    Parsot, C.5
  • 190
    • 0036224026 scopus 로고    scopus 로고
    • Functional analysis of HrpF, a putative type III translocon protein from Xanthomonas campestris pv. vesicatoria
    • Buttner D., Nennstiel D., Klusener B., Bonas U. Functional analysis of HrpF, a putative type III translocon protein from Xanthomonas campestris pv. vesicatoria. J. Bacteriol. 184:2002;2389-2398
    • (2002) J. Bacteriol. , vol.184 , pp. 2389-2398
    • Buttner, D.1    Nennstiel, D.2    Klusener, B.3    Bonas, U.4
  • 191
    • 0033637353 scopus 로고    scopus 로고
    • HrpB2 and HrpF from Xanthomonas are type III-secreted proteins and essential for pathogenicity and recognition by the host plant
    • Rossier O., Van den Ackerveken G., Bonas U. HrpB2 and HrpF from Xanthomonas are type III-secreted proteins and essential for pathogenicity and recognition by the host plant. Mol. Microbiol. 38:2000;828-838
    • (2000) Mol. Microbiol. , vol.38 , pp. 828-838
    • Rossier, O.1    Van Den Ackerveken, G.2    Bonas, U.3
  • 192
    • 0036176974 scopus 로고    scopus 로고
    • NolX of Sinorhizobium fredii USDA257, a type III-secreted protein involved in host range determination, is localized in the infection threads of cowpea (Vigna unguiculata [L.] Walp) and soybean (Glycine max [L.] Merr.) nodules
    • Krishnan H.B. NolX of Sinorhizobium fredii USDA257, a type III-secreted protein involved in host range determination, is localized in the infection threads of cowpea (Vigna unguiculata [L.] Walp) and soybean (Glycine max [L.] Merr.) nodules. J. Bacteriol. 184:2002;831-839
    • (2002) J. Bacteriol. , vol.184 , pp. 831-839
    • Krishnan, H.B.1
  • 193
    • 0026724558 scopus 로고
    • Harpin, elicitor of the hypersensitive response produced by the plant pathogen Erwinia amylovora
    • Wei Z.M., Laby R.J., Zumoff C.H., Bauer D.W., He S.Y., Collmer A., Beer S.V. Harpin, elicitor of the hypersensitive response produced by the plant pathogen Erwinia amylovora. Science. 257:1992;85-88
    • (1992) Science , vol.257 , pp. 85-88
    • Wei, Z.M.1    Laby, R.J.2    Zumoff, C.H.3    Bauer, D.W.4    He, S.Y.5    Collmer, A.6    Beer, S.V.7
  • 194
    • 0035010868 scopus 로고    scopus 로고
    • A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity
    • Lee J., Klessig D.F., Nurnberger T. A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity. Plant Cell. 13:2001;1079-1093
    • (2001) Plant Cell , vol.13 , pp. 1079-1093
    • Lee, J.1    Klessig, D.F.2    Nurnberger, T.3
  • 196
    • 0030268188 scopus 로고    scopus 로고
    • Hrp gene-dependent induction of hin1: A plant gene activated rapidly by both harpins and the avrPto gene-mediated signal
    • Gopalan S., Wei W., He S.Y. hrp gene-dependent induction of hin1: a plant gene activated rapidly by both harpins and the avrPto gene-mediated signal. Plant J. 10:1996;591-600
    • (1996) Plant J. , vol.10 , pp. 591-600
    • Gopalan, S.1    Wei, W.2    He, S.Y.3
  • 197
    • 0034142162 scopus 로고    scopus 로고
    • Harpin-induced hypersensitive cell death is associated with altered mitochondrial functions in tobacco cells
    • Xie Z., Chen Z. Harpin-induced hypersensitive cell death is associated with altered mitochondrial functions in tobacco cells. Mol. Plant-Microb. Interact. 13:2000;183-190
    • (2000) Mol. Plant-Microb. Interact. , vol.13 , pp. 183-190
    • Xie, Z.1    Chen, Z.2
  • 198
    • 0033213626 scopus 로고    scopus 로고
    • Harpin induces disease resistance in Arabidopsis through the systemic acquired resistance pathway mediated by salicylic acid and the NIM1 gene
    • Dong H., Delaney T.P., Bauer D.W., Beer S.V. Harpin induces disease resistance in Arabidopsis through the systemic acquired resistance pathway mediated by salicylic acid and the NIM1 gene. Plant J. 20:1999;207-215
    • (1999) Plant J. , vol.20 , pp. 207-215
    • Dong, H.1    Delaney, T.P.2    Bauer, D.W.3    Beer, S.V.4
  • 199
    • 0035543414 scopus 로고    scopus 로고
    • A local accumulation of the Ralstonia solanacearum PopA protein in transgenic tobacco renders a compatible plant-pathogen interaction incompatible
    • Belbahri L., Boucher C., Candresse T., Nicole M., Ricci P., Keller H. A local accumulation of the Ralstonia solanacearum PopA protein in transgenic tobacco renders a compatible plant-pathogen interaction incompatible. Plant J. 28:2001;419-430
    • (2001) Plant J. , vol.28 , pp. 419-430
    • Belbahri, L.1    Boucher, C.2    Candresse, T.3    Nicole, M.4    Ricci, P.5    Keller, H.6
  • 200
    • 0037628742 scopus 로고    scopus 로고
    • Characterization of the Xanthomonas axonopodis pv. glycines Hrp pathogenicity island
    • Kim J.G., Park B.K., Yoo C.H., Jeon E., Oh J., Hwang I. Characterization of the Xanthomonas axonopodis pv. glycines Hrp pathogenicity island. J. Bacteriol. 185:2003;3155-3166
    • (2003) J. Bacteriol. , vol.185 , pp. 3155-3166
    • Kim, J.G.1    Park, B.K.2    Yoo, C.H.3    Jeon, E.4    Oh, J.5    Hwang, I.6
  • 201
    • 0034022602 scopus 로고    scopus 로고
    • Identification of two novel hrp-associated genes in the hrp gene cluster of Xanthomonas oryzae pv. oryzae
    • Zhu W., Magbanua M.M., White F.F. Identification of two novel hrp-associated genes in the hrp gene cluster of Xanthomonas oryzae pv. oryzae. J. Bacteriol. 182:2000;1844-1853
    • (2000) J. Bacteriol. , vol.182 , pp. 1844-1853
    • Zhu, W.1    Magbanua, M.M.2    White, F.F.3
  • 202
    • 0031714923 scopus 로고    scopus 로고
    • The Pseudomonas syringae pv. tomato HrpW protein has domains similar to harpins and pectate lyases and can elicit the plant hypersensitive response and bind to pectate
    • Charkowski A.O., Alfano J.R., Preston G., Yuan J., He S.Y., Collmer A. The Pseudomonas syringae pv. tomato HrpW protein has domains similar to harpins and pectate lyases and can elicit the plant hypersensitive response and bind to pectate. J. Bacteriol. 180:1998;5211-5217
    • (1998) J. Bacteriol. , vol.180 , pp. 5211-5217
    • Charkowski, A.O.1    Alfano, J.R.2    Preston, G.3    Yuan, J.4    He, S.Y.5    Collmer, A.6
  • 205
    • 0030029192 scopus 로고    scopus 로고
    • Analysis of the role of the Pseudomonas syringae pv. syringae HrpZ harpin in elicitation of the hypersensitive response in tobacco using functionally non-polar hrpZ deletion mutations, truncated HrpZ fragments, and hrmA mutations
    • Alfano J.R., Bauer D.W., Milos T.M., Collmer A. Analysis of the role of the Pseudomonas syringae pv. syringae HrpZ harpin in elicitation of the hypersensitive response in tobacco using functionally non-polar hrpZ deletion mutations, truncated HrpZ fragments, and hrmA mutations. Mol. Microbiol. 19:1996;715-728
    • (1996) Mol. Microbiol. , vol.19 , pp. 715-728
    • Alfano, J.R.1    Bauer, D.W.2    Milos, T.M.3    Collmer, A.4
  • 206
    • 0031684457 scopus 로고    scopus 로고
    • HrpW of Erwinia amylovora, a new harpin that contains a domain homologous to pectate lyases of a distinct class
    • Kim J.F., Beer S.V. HrpW of Erwinia amylovora, a new harpin that contains a domain homologous to pectate lyases of a distinct class. J. Bacteriol. 180:1998;5203-5210
    • (1998) J. Bacteriol. , vol.180 , pp. 5203-5210
    • Kim, J.F.1    Beer, S.V.2
  • 207
    • 0032577722 scopus 로고    scopus 로고
    • HrpW of Erwinia amylovora, a new Hrp-secreted protein
    • Gaudriault S., Brisset M.N., Barny M.A. HrpW of Erwinia amylovora, a new Hrp-secreted protein. FEBS Lett. 428:1998;224-228
    • (1998) FEBS Lett. , vol.428 , pp. 224-228
    • Gaudriault, S.1    Brisset, M.N.2    Barny, M.A.3
  • 209
    • 0036050978 scopus 로고    scopus 로고
    • Identification of novel hrp-regulated genes through functional genomic analysis of the Pseudomonas syringae pv. syringae DC3000 genome
    • Zwiesler-Vollick J., Plovanich-Jones A., Nomura K., Bandyopadhyay S., Joardar V., Kunkel B.N., He S.Y. Identification of novel hrp-regulated genes through functional genomic analysis of the Pseudomonas syringae pv. syringae DC3000 genome. Mol. Microbiol. 45:2002;1207-1218
    • (2002) Mol. Microbiol. , vol.45 , pp. 1207-1218
    • Zwiesler-Vollick, J.1    Plovanich-Jones, A.2    Nomura, K.3    Bandyopadhyay, S.4    Joardar, V.5    Kunkel, B.N.6    He, S.Y.7
  • 210
    • 0035423161 scopus 로고    scopus 로고
    • Targeting exported substrates to the Yersinia TTSS: Different functions for different signals?
    • Francis M.S., Lloyd S.A., Wolf-Watz H. Targeting exported substrates to the Yersinia TTSS: different functions for different signals? Trends Microbiol. 9:2001;367-371
    • (2001) Trends Microbiol. , vol.9 , pp. 367-371
    • Francis, M.S.1    Lloyd, S.A.2    Wolf-Watz, H.3
  • 211
    • 0037107426 scopus 로고    scopus 로고
    • Getting across-bacterial type III effector proteins on their way to the plant cell
    • Buttner D., Bonas U. Getting across-bacterial type III effector proteins on their way to the plant cell. EMBO J. 21:2002;5313-5322
    • (2002) EMBO J. , vol.21 , pp. 5313-5322
    • Buttner, D.1    Bonas, U.2
  • 212
    • 0036065408 scopus 로고    scopus 로고
    • Lon protease functions as a negative regulator of type III protein secretion in Pseudomonas syringae
    • Bretz J., Losada L., Lisboa K., Hutcheson S.W. Lon protease functions as a negative regulator of type III protein secretion in Pseudomonas syringae. Mol. Microbiol. 45:2002;397-409
    • (2002) Mol. Microbiol. , vol.45 , pp. 397-409
    • Bretz, J.1    Losada, L.2    Lisboa, K.3    Hutcheson, S.W.4
  • 213
    • 0029828325 scopus 로고    scopus 로고
    • Co-ordinate regulation of Salmonella typhimurium invasion genes by environmental and regulatory factors is mediated by control of hilA expression
    • Bajaj V., Lucas R.L., Hwang C., Lee C.A. Co-ordinate regulation of Salmonella typhimurium invasion genes by environmental and regulatory factors is mediated by control of hilA expression. Mol. Microbiol. 22:1996;703-714
    • (1996) Mol. Microbiol. , vol.22 , pp. 703-714
    • Bajaj, V.1    Lucas, R.L.2    Hwang, C.3    Lee, C.A.4
  • 214
    • 0036175124 scopus 로고    scopus 로고
    • Transcription of the SsrAB regulon is repressed by alkaline pH and is independent of PhoPQ and magnesium concentration
    • Miao E.A., Freeman J.A., Miller S.I. Transcription of the SsrAB regulon is repressed by alkaline pH and is independent of PhoPQ and magnesium concentration. J. Bacteriol. 184:2002;1493-1497
    • (2002) J. Bacteriol. , vol.184 , pp. 1493-1497
    • Miao, E.A.1    Freeman, J.A.2    Miller, S.I.3
  • 215
    • 0033954447 scopus 로고    scopus 로고
    • OmpR regulates the two-component system ssrA-ssrB in Salmonella pathogenicity island 2
    • Lee A.K., Detweiler C.S., Falkow S. OmpR regulates the two-component system ssrA-ssrB in Salmonella pathogenicity island 2. J. Bacteriol. 182:2000;771-781
    • (2000) J. Bacteriol. , vol.182 , pp. 771-781
    • Lee, A.K.1    Detweiler, C.S.2    Falkow, S.3
  • 216
    • 0141480261 scopus 로고    scopus 로고
    • The roles of SsrA-SsrB and OmpR-EnvZ in the regulation of genes encoding the Salmonella typhimurium SPI-2 type III secretion system
    • Garmendia J., Beuzon C.R., Ruiz-Albert J., Holden D.W. The roles of SsrA-SsrB and OmpR-EnvZ in the regulation of genes encoding the Salmonella typhimurium SPI-2 type III secretion system. Microbiology. 149:2003;2385-2396
    • (2003) Microbiology , vol.149 , pp. 2385-2396
    • Garmendia, J.1    Beuzon, C.R.2    Ruiz-Albert, J.3    Holden, D.W.4
  • 217
    • 0000737074 scopus 로고    scopus 로고
    • Induction of gene expression in Escherichia coli after pilus-mediated adherence
    • Zhang J.P., Normark S. Induction of gene expression in Escherichia coli after pilus-mediated adherence. Science. 273:1996;1234-1236
    • (1996) Science , vol.273 , pp. 1234-1236
    • Zhang, J.P.1    Normark, S.2
  • 218
    • 0031963191 scopus 로고    scopus 로고
    • PrhA controls a novel regulatory pathway required for the specific induction of Ralstonia solanacearum hrp genes in the presence of plant cells
    • Marenda M., Brito B., Callard D., Genin S., Barberis P., Boucher C., Arlat M. PrhA controls a novel regulatory pathway required for the specific induction of Ralstonia solanacearum hrp genes in the presence of plant cells. Mol. Microbiol. 27:1998;437-453
    • (1998) Mol. Microbiol. , vol.27 , pp. 437-453
    • Marenda, M.1    Brito, B.2    Callard, D.3    Genin, S.4    Barberis, P.5    Boucher, C.6    Arlat, M.7
  • 219
    • 0028224918 scopus 로고
    • Role of the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope
    • Koster M., van Klompenburg W., Bitter W., Leong J., Weisbeek P. Role of the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope. EMBO J. 13:1994;2805-2813
    • (1994) EMBO J. , vol.13 , pp. 2805-2813
    • Koster, M.1    Van Klompenburg, W.2    Bitter, W.3    Leong, J.4    Weisbeek, P.5
  • 220
    • 0028904880 scopus 로고
    • Signal transfer through three compartments: Transcription initiation of the Escherichia coli ferric citrate transport system from the cell surface
    • Härle C., Kim I., Angerer A., Braun V. Signal transfer through three compartments: transcription initiation of the Escherichia coli ferric citrate transport system from the cell surface. EMBO J. 14:1995;1430-1438
    • (1995) EMBO J. , vol.14 , pp. 1430-1438
    • Härle, C.1    Kim, I.2    Angerer, A.3    Braun, V.4
  • 221
    • 0036046297 scopus 로고    scopus 로고
    • Iron transport and regulation, cell signalling and genomics: Lessons from Escherichia coli and Pseudomonas
    • Visca P., Leoni L., Wilson M.J., Lamont I.L. Iron transport and regulation, cell signalling and genomics: lessons from Escherichia coli and Pseudomonas. Mol. Microbiol. 45:2002;1177-1190
    • (2002) Mol. Microbiol. , vol.45 , pp. 1177-1190
    • Visca, P.1    Leoni, L.2    Wilson, M.J.3    Lamont, I.L.4
  • 222
    • 0034657096 scopus 로고    scopus 로고
    • A bacterial sensor of plant cell contact controls the transcriptional induction of Ralstonia solanacearum pathogenicity genes
    • Aldon D., Brito B., Boucher C., Genin S. A bacterial sensor of plant cell contact controls the transcriptional induction of Ralstonia solanacearum pathogenicity genes. EMBO J. 19:2000;2304-2314
    • (2000) EMBO J. , vol.19 , pp. 2304-2314
    • Aldon, D.1    Brito, B.2    Boucher, C.3    Genin, S.4
  • 223
    • 0032925737 scopus 로고    scopus 로고
    • PrhJ and hrpG, two new components of the plant signal-dependent regulatory cascade controlled by PrhA in Ralstonia solanacearum
    • Brito B., Marenda M., Barberis P., Boucher C., Genin S. prhJ and hrpG, two new components of the plant signal-dependent regulatory cascade controlled by PrhA in Ralstonia solanacearum. Mol. Microbiol. 31:1999;237-251
    • (1999) Mol. Microbiol. , vol.31 , pp. 237-251
    • Brito, B.1    Marenda, M.2    Barberis, P.3    Boucher, C.4    Genin, S.5
  • 224
    • 0036190503 scopus 로고    scopus 로고
    • A signal transfer system through three compartments transduces the plant cell contact-dependent signal controlling Ralstonia solanacearum hrp genes
    • Brito B., Aldon D., Barberis P., Boucher C., Genin S. A signal transfer system through three compartments transduces the plant cell contact-dependent signal controlling Ralstonia solanacearum hrp genes. Mol. Plant-Microb. Interact. 15:2002;109-119
    • (2002) Mol. Plant-Microb. Interact. , vol.15 , pp. 109-119
    • Brito, B.1    Aldon, D.2    Barberis, P.3    Boucher, C.4    Genin, S.5
  • 225
    • 0028883418 scopus 로고
    • Mutational analysis of the Yersinia enterocolitica virC operon: Characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR
    • Allaoui A., Schulte R., Cornelis G.R. Mutational analysis of the Yersinia enterocolitica virC operon: characterization of yscE, F, G, I, J, K required for Yop secretion and yscH encoding YopR. Mol. Microbiol. 18:1995;343-355
    • (1995) Mol. Microbiol. , vol.18 , pp. 343-355
    • Allaoui, A.1    Schulte, R.2    Cornelis, G.R.3
  • 226
    • 0027724892 scopus 로고
    • Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator
    • Hughes K.T., Gillen K.L., Semon M.J., Karlinsey J.E. Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator. Science. 262:1993;1277-1280
    • (1993) Science , vol.262 , pp. 1277-1280
    • Hughes, K.T.1    Gillen, K.L.2    Semon, M.J.3    Karlinsey, J.E.4
  • 227
    • 0035170435 scopus 로고    scopus 로고
    • The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis
    • Francis M.S., Lloyd S.A., Wolf-Watz H. The type III secretion chaperone LcrH co-operates with YopD to establish a negative, regulatory loop for control of Yop synthesis in Yersinia pseudotuberculosis. Mol. Microbiol. 42:2001;1075-1093
    • (2001) Mol. Microbiol. , vol.42 , pp. 1075-1093
    • Francis, M.S.1    Lloyd, S.A.2    Wolf-Watz, H.3
  • 228
    • 0033943054 scopus 로고    scopus 로고
    • LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism
    • Cambronne E.D., Cheng L.W., Schneewind O. LcrQ/YscM1, regulators of the Yersinia yop virulon, are injected into host cells by a chaperone-dependent mechanism. Mol. Microbiol. 43:2000;263-273
    • (2000) Mol. Microbiol. , vol.43 , pp. 263-273
    • Cambronne, E.D.1    Cheng, L.W.2    Schneewind, O.3
  • 229
    • 0036170459 scopus 로고    scopus 로고
    • LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion
    • Wulff-Strobel C.R., Williams A.W., Straley S.C. LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion. Mol. Microbiol. 43:2002;411-423
    • (2002) Mol. Microbiol. , vol.43 , pp. 411-423
    • Wulff-Strobel, C.R.1    Williams, A.W.2    Straley, S.C.3
  • 230
    • 0026772670 scopus 로고
    • A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH
    • Rimpilainen M., Forsberg A., Wolf-Watz H. A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH. J. Bacteriol. 174:1992;3355-3363
    • (1992) J. Bacteriol. , vol.174 , pp. 3355-3363
    • Rimpilainen, M.1    Forsberg, A.2    Wolf-Watz, H.3
  • 231
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • Williams A.W., Straley S.C. YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J. Bacteriol. 180:1998;350-358
    • (1998) J. Bacteriol. , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2
  • 232
    • 0036182095 scopus 로고    scopus 로고
    • YopD and LcrH regulate expression of Yersinia enterocolitica YopQ by a posttranscriptional mechanism and bind to yopQ RNA
    • Anderson D.M., Ramamurthi K.S., Tam C., Schneewind O. YopD and LcrH regulate expression of Yersinia enterocolitica YopQ by a posttranscriptional mechanism and bind to yopQ RNA. J. Bacteriol. 184:2002;1287-1295
    • (2002) J. Bacteriol. , vol.184 , pp. 1287-1295
    • Anderson, D.M.1    Ramamurthi, K.S.2    Tam, C.3    Schneewind, O.4
  • 233
    • 0036838012 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: YscM1 and yscM2 regulate yop gene expression by a posttranscriptional mechanism that targets the 5′ untranslated region of yop mRNA
    • Cambronne E.D., Schneewind O. Yersinia enterocolitica type III secretion: yscM1 and yscM2 regulate yop gene expression by a posttranscriptional mechanism that targets the 5′ untranslated region of yop mRNA. J. Bacteriol. 184:2002;5880-5893
    • (2002) J. Bacteriol. , vol.184 , pp. 5880-5893
    • Cambronne, E.D.1    Schneewind, O.2
  • 234
    • 0029059332 scopus 로고
    • Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells
    • Kaniga K., Tucker S., Trollinger D., Galan J.E. Homologs of the Shigella IpaB and IpaC invasins are required for Salmonella typhimurium entry into cultured epithelial cells. J. Bacteriol. 177:1995;3965-3971
    • (1995) J. Bacteriol. , vol.177 , pp. 3965-3971
    • Kaniga, K.1    Tucker, S.2    Trollinger, D.3    Galan, J.E.4
  • 235
    • 0027982037 scopus 로고
    • The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins
    • Kaniga K., Bossio J.C., Galan J.E. The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins. Mol. Microbiol. 13:1994;555-568
    • (1994) Mol. Microbiol. , vol.13 , pp. 555-568
    • Kaniga, K.1    Bossio, J.C.2    Galan, J.E.3
  • 236
    • 0035901560 scopus 로고    scopus 로고
    • Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium
    • Darwin K.H., Miller V.L. Type III secretion chaperone-dependent regulation: activation of virulence genes by SicA and InvF in Salmonella typhimurium. EMBO J. 20:2001;1850-1862
    • (2001) EMBO J. , vol.20 , pp. 1850-1862
    • Darwin, K.H.1    Miller, V.L.2
  • 237
    • 0036276061 scopus 로고    scopus 로고
    • Regulation of transcription by the activity of the Shigella flexneri type III secretion apparatus
    • Mavris M., Page A.L., Tournebize R., Demers B., Sansonetti P., Parsot C. Regulation of transcription by the activity of the Shigella flexneri type III secretion apparatus. Mol. Microbiol. 43:2002;1543-1553
    • (2002) Mol. Microbiol. , vol.43 , pp. 1543-1553
    • Mavris, M.1    Page, A.L.2    Tournebize, R.3    Demers, B.4    Sansonetti, P.5    Parsot, C.6
  • 239
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defense responses to infection
    • Dangl J.L., Jones J.D.G. Plant pathogens and integrated defense responses to infection. Nature. 411:2001;826-833
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.G.2
  • 240
    • 0016331566 scopus 로고
    • Natural resistance to Salmonella infection, delayed hypersensitivity and Ir genes in different strains of mice
    • Plant J., Glynn A.A. Natural resistance to Salmonella infection, delayed hypersensitivity and Ir genes in different strains of mice. Nature. 248:1974;345-347
    • (1974) Nature , vol.248 , pp. 345-347
    • Plant, J.1    Glynn, A.A.2
  • 241
    • 0027262167 scopus 로고
    • Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg
    • Vidal S.M., Malo D., Vogan K., Skamene E., Gros P. Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg. Cell. 73:1993;469-485
    • (1993) Cell , vol.73 , pp. 469-485
    • Vidal, S.M.1    Malo, D.2    Vogan, K.3    Skamene, E.4    Gros, P.5
  • 242
    • 0031820381 scopus 로고    scopus 로고
    • Macrophage NRAMP1 and its role in resistance to microbial infections
    • Govoni G., Gros P. Macrophage NRAMP1 and its role in resistance to microbial infections. Inflamm. Res. 47:1998;277-284
    • (1998) Inflamm. Res. , vol.47 , pp. 277-284
    • Govoni, G.1    Gros, P.2
  • 244
    • 0036534742 scopus 로고    scopus 로고
    • Solute carrier 11a1 (Slc11a1; Formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake
    • Mulero V., Searle S., Blackwell J.M., Brock J.H. Solute carrier 11a1 (Slc11a1; formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake. Biochem. J. 363:2002;89-94
    • (2002) Biochem. J. , vol.363 , pp. 89-94
    • Mulero, V.1    Searle, S.2    Blackwell, J.M.3    Brock, J.H.4
  • 245
    • 0037180513 scopus 로고    scopus 로고
    • Host-pathogen interactions: Host resistance factor Nramp1 up-regulates the expression of Salmonella pathogenicity island-2 virulence genes
    • Zaharik M.L., Vallance B.A., Puente J.L., Gros P., Finlay B.B. Host-pathogen interactions: Host resistance factor Nramp1 up-regulates the expression of Salmonella pathogenicity island-2 virulence genes. Proc. Natl. Acad. Sci. U. S. A. 99:2002;15705-15710
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15705-15710
    • Zaharik, M.L.1    Vallance, B.A.2    Puente, J.L.3    Gros, P.4    Finlay, B.B.5
  • 246
    • 0033592919 scopus 로고    scopus 로고
    • Quorum sensing controls expression of the type III secretion gene transcription and protein secretion in enterohemorrhagic and enteropathogenic Escherichia coli
    • Sperandio V., Mellies J.L., Nguyen W., Shin S., Kaper J.B. Quorum sensing controls expression of the type III secretion gene transcription and protein secretion in enterohemorrhagic and enteropathogenic Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 96:1999;15196-15201
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 15196-15201
    • Sperandio, V.1    Mellies, J.L.2    Nguyen, W.3    Shin, S.4    Kaper, J.B.5
  • 247
    • 0033574064 scopus 로고    scopus 로고
    • Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: A new family of genes responsible for autoinducer production
    • Surette M.G., Miller M.B., Bassler B.L. Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: a new family of genes responsible for autoinducer production. Proc. Natl. Acad. Sci. U. S. A. 96:1999;1639-1644
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1639-1644
    • Surette, M.G.1    Miller, M.B.2    Bassler, B.L.3
  • 252
    • 0036532450 scopus 로고    scopus 로고
    • Port of entry-the type III secretion translocon
    • Buttner D., Bonas U. Port of entry-the type III secretion translocon. Trends Microbiol. 10:2002;186-192
    • (2002) Trends Microbiol. , vol.10 , pp. 186-192
    • Buttner, D.1    Bonas, U.2
  • 253
    • 0031931363 scopus 로고    scopus 로고
    • EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli
    • Wainwright L.A., Kaper J.B. EspB and EspD require a specific chaperone for proper secretion from enteropathogenic Escherichia coli. Mol. Microbiol. 27:1998;1247-1260
    • (1998) Mol. Microbiol. , vol.27 , pp. 1247-1260
    • Wainwright, L.A.1    Kaper, J.B.2
  • 254
    • 0036120245 scopus 로고    scopus 로고
    • A gene from the locus of enterocyte effacement that is required for enteropathogenic Escherichia coli to increase tight-junction permeability encodes a chaperone for EspF
    • Elliott S.J., O'Connell C.B., Koutsouris A., Brinkley C., Donnenberg M.S., Hecht G., Kaper J.B. A gene from the locus of enterocyte effacement that is required for enteropathogenic Escherichia coli to increase tight-junction permeability encodes a chaperone for EspF. Infect. Immun. 70:2002;2271-2277
    • (2002) Infect. Immun. , vol.70 , pp. 2271-2277
    • Elliott, S.J.1    O'Connell, C.B.2    Koutsouris, A.3    Brinkley, C.4    Donnenberg, M.S.5    Hecht, G.6    Kaper, J.B.7
  • 256
    • 0028944578 scopus 로고
    • Transcriptional analysis of the Pseudomonas aeruginosa exoenzyme S structural gene
    • Yahr T.L., Hovey A.K., Kulich S.M., Frank D.W. Transcriptional analysis of the Pseudomonas aeruginosa exoenzyme S structural gene. J. Bacteriol. 177:1995;1169-1178
    • (1995) J. Bacteriol. , vol.177 , pp. 1169-1178
    • Yahr, T.L.1    Hovey, A.K.2    Kulich, S.M.3    Frank, D.W.4
  • 257
    • 0141591619 scopus 로고    scopus 로고
    • Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis
    • Broms J.E., Forslund A.L., Forsberg A., Francis M.S. Dissection of homologous translocon operons reveals a distinct role for YopD in type III secretion by Yersinia pseudotuberculosis. Microbiology. 49:2003;2615-2626
    • (2003) Microbiology , vol.49 , pp. 2615-2626
    • Broms, J.E.1    Forslund, A.L.2    Forsberg, A.3    Francis, M.S.4
  • 258
    • 0031785949 scopus 로고    scopus 로고
    • Identification and characterization of SpcU, a chaperone required for efficient secretion of the ExoU cytotoxin
    • Finck-Barbancon V., Yahr T.L., Frank D.W. Identification and characterization of SpcU, a chaperone required for efficient secretion of the ExoU cytotoxin. J. Bacteriol. 180:1998;6224-6231
    • (1998) J. Bacteriol. , vol.180 , pp. 6224-6231
    • Finck-Barbancon, V.1    Yahr, T.L.2    Frank, D.W.3
  • 259
    • 0141789784 scopus 로고    scopus 로고
    • The type III secretion chaperone FlgN regulates flagellar assembly via a negative feedback loop containing its chaperone substrates FlgK and FlgL
    • Aldridge P., Karlinsey J., Hughes K.T. The type III secretion chaperone FlgN regulates flagellar assembly via a negative feedback loop containing its chaperone substrates FlgK and FlgL. Mol. Microbiol. 49:2003;1333-1345
    • (2003) Mol. Microbiol. , vol.49 , pp. 1333-1345
    • Aldridge, P.1    Karlinsey, J.2    Hughes, K.T.3
  • 260
    • 0034462757 scopus 로고    scopus 로고
    • InvB is a type III secretion chaperone specific for SspA
    • Bronstein P.A., Miao E.A., Miller S.I. InvB is a type III secretion chaperone specific for SspA. J. Bacteriol. 182:2000;6638-6644
    • (2000) J. Bacteriol. , vol.182 , pp. 6638-6644
    • Bronstein, P.A.1    Miao, E.A.2    Miller, S.I.3
  • 261
    • 0034079727 scopus 로고    scopus 로고
    • Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone
    • Tucker S.C., Galan J.E. Complex function for SicA, a Salmonella enterica serovar typhimurium type III secretion-associated chaperone. J. Bacteriol. 182:2000;2262-2268
    • (2000) J. Bacteriol. , vol.182 , pp. 2262-2268
    • Tucker, S.C.1    Galan, J.E.2
  • 262
    • 0035145294 scopus 로고    scopus 로고
    • SigE is a chaperone for the Salmonella enterica serovar typhimurium invasion protein SigD
    • Darwin K.H., Robinson L.S., Miller V.L. SigE is a chaperone for the Salmonella enterica serovar typhimurium invasion protein SigD. J. Bacteriol. 183:2001;1452-1454
    • (2001) J. Bacteriol. , vol.183 , pp. 1452-1454
    • Darwin, K.H.1    Robinson, L.S.2    Miller, V.L.3
  • 263
    • 0038530831 scopus 로고    scopus 로고
    • SseA is a chaperone for the SseB and SseD translocon components of the Salmonella pathogenicity-island-2-encoded type III secretion system
    • Ruiz-Albert J., Mundy R., Yu X.L., Beuzon C.R., Holden D.W. SseA is a chaperone for the SseB and SseD translocon components of the Salmonella pathogenicity-island-2-encoded type III secretion system. Microbiology. 149:2003;1103-1111
    • (2003) Microbiology , vol.149 , pp. 1103-1111
    • Ruiz-Albert, J.1    Mundy, R.2    Yu, X.L.3    Beuzon, C.R.4    Holden, D.W.5
  • 264
    • 0038354852 scopus 로고    scopus 로고
    • IcsB, secreted via the type III secretion system, is chaperoned by IpgA and required at the post-invasion stage of Shigella pathogenicity
    • Ogawa M., Suzuki T., Tatsuno I., Abe H., Sasakawa C. IcsB, secreted via the type III secretion system, is chaperoned by IpgA and required at the post-invasion stage of Shigella pathogenicity. Mol. Microbiol. 48:2003;913-931
    • (2003) Mol. Microbiol. , vol.48 , pp. 913-931
    • Ogawa, M.1    Suzuki, T.2    Tatsuno, I.3    Abe, H.4    Sasakawa, C.5
  • 265
    • 0036951970 scopus 로고    scopus 로고
    • Identification of the cis-acting site involved in activation of promoters regulated by activity of the type III secretion apparatus in Shigella flexneri
    • Mavris M., Sansonetti P.J., Parsot C. Identification of the cis-acting site involved in activation of promoters regulated by activity of the type III secretion apparatus in Shigella flexneri. J. Bacteriol. 184:2002;6751-6759
    • (2002) J. Bacteriol. , vol.184 , pp. 6751-6759
    • Mavris, M.1    Sansonetti, P.J.2    Parsot, C.3
  • 266
    • 0033809933 scopus 로고    scopus 로고
    • IpgD, a protein secreted by the type III secretion machinery of Shigella flexneri, is chaperoned by IpgE and implicated in entry focus formation
    • Niebuhr K., Jouihri N., Allaoui A., Gounon P., Sansonetti P.J., Parsot C. IpgD, a protein secreted by the type III secretion machinery of Shigella flexneri, is chaperoned by IpgE and implicated in entry focus formation. Mol. Microbiol. 38:2000;8-19
    • (2000) Mol. Microbiol. , vol.38 , pp. 8-19
    • Niebuhr, K.1    Jouihri, N.2    Allaoui, A.3    Gounon, P.4    Sansonetti, P.J.5    Parsot, C.6
  • 267
    • 0036267949 scopus 로고    scopus 로고
    • Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway
    • Page A.L., Sansonetti P., Parsot C. Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway. Mol. Microbiol. 43:2002;1533-1542
    • (2002) Mol. Microbiol. , vol.43 , pp. 1533-1542
    • Page, A.L.1    Sansonetti, P.2    Parsot, C.3
  • 268
    • 0037379441 scopus 로고    scopus 로고
    • CesD2 of enteropathogenic Escherichia coli is a second chaperone for the type III secretion translocator protein EspD
    • Neves B.C., Mundy R., Petrovska L., Dougan G., Knutton S., Frankel G. CesD2 of enteropathogenic Escherichia coli is a second chaperone for the type III secretion translocator protein EspD. Infect. Immun. 71:2003;2130-2141
    • (2003) Infect. Immun. , vol.71 , pp. 2130-2141
    • Neves, B.C.1    Mundy, R.2    Petrovska, L.3    Dougan, G.4    Knutton, S.5    Frankel, G.6
  • 270
    • 0029944323 scopus 로고    scopus 로고
    • The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes
    • Woestyn S., Sory M.P., Boland A., Lequenne O., Cornelis G.R. The cytosolic SycE and SycH chaperones of Yersinia protect the region of YopE and YopH involved in translocation across eukaryotic cell membranes. Mol. Microbiol. 20:1996;1261-1271
    • (1996) Mol. Microbiol. , vol.20 , pp. 1261-1271
    • Woestyn, S.1    Sory, M.P.2    Boland, A.3    Lequenne, O.4    Cornelis, G.R.5
  • 271
    • 0031766236 scopus 로고    scopus 로고
    • A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis
    • Day J.B., Plano G.V. A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis. Mol. Microbiol. 30:1998;777-788
    • (1998) Mol. Microbiol. , vol.30 , pp. 777-788
    • Day, J.B.1    Plano, G.V.2
  • 272
    • 0034864508 scopus 로고    scopus 로고
    • Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica
    • Cheng L.W., Kay O., Schneewind O. Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica. J. Bacteriol. 183:2001;5293-5301
    • (2001) J. Bacteriol. , vol.183 , pp. 5293-5301
    • Cheng, L.W.1    Kay, O.2    Schneewind, O.3
  • 273
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells
    • Iriarte M., Cornelis G.R. YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol. Microbiol. 29:1998;915-929
    • (1998) Mol. Microbiol. , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.