메뉴 건너뛰기




Volumn 4, Issue 1, 2016, Pages

The structure and function of type III secretion systems

Author keywords

[No Author keywords available]

Indexed keywords

TYPE III SECRETION SYSTEM;

EID: 85006700085     PISSN: None     EISSN: 21650497     Source Type: Journal    
DOI: 10.1128/microbiolspec.VMBF-0004-2015     Document Type: Article
Times cited : (95)

References (172)
  • 1
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: bacterial devices for protein delivery into host cells
    • Galan JE, Collmer A. 1999. Type III secretion machines: bacterial devices for protein delivery into host cells. Science 284:1322-1328.
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 3
    • 0024323292 scopus 로고
    • Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells
    • Galan JE, Curtiss R, 3rd. 1989. Cloning and molecular characterization of genes whose products allow Salmonella typhimurium to penetrate tissue culture cells. Proc Natl Acad Sci USA 86:6383-6387.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6383-6387
    • Galan, J.E.1    Curtiss, R.2
  • 6
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan JE, Wolf-Watz H. 2006. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444:567-573.
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 7
    • 0036322385 scopus 로고    scopus 로고
    • Yersinia type III secretion: send in the effectors
    • Cornelis GR. 2002. Yersinia type III secretion: send in the effectors. J Cell Biol 158:401-408.
    • (2002) J Cell Biol , vol.158 , pp. 401-408
    • Cornelis, G.R.1
  • 9
    • 0042195926 scopus 로고    scopus 로고
    • Functions and effectors of the Salmonella pathogenicity island 2 type III secretion system
    • Waterman SR, Holden DW. 2003. Functions and effectors of the Salmonella pathogenicity island 2 type III secretion system. Cell Microbiol 5:501-511.
    • (2003) Cell Microbiol , vol.5 , pp. 501-511
    • Waterman, S.R.1    Holden, D.W.2
  • 10
    • 9944244618 scopus 로고    scopus 로고
    • Structural insights into bacterial modulation of the host cytoskeleton
    • Stebbins CE. 2004. Structural insights into bacterial modulation of the host cytoskeleton. Curr Opin Struct Biol 14:731-740.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 731-740
    • Stebbins, C.E.1
  • 11
    • 33749175594 scopus 로고    scopus 로고
    • Transcriptional regulation of the Pseudomonas aeruginosa type III secretion system
    • Yahr TL, Wolfgang MC. 2006. Transcriptional regulation of the Pseudomonas aeruginosa type III secretion system. Mol Microbiol 62: 631-640.
    • (2006) Mol Microbiol , vol.62 , pp. 631-640
    • Yahr, T.L.1    Wolfgang, M.C.2
  • 12
    • 35348992048 scopus 로고    scopus 로고
    • Manipulation of host-cell pathways by bacterial pathogens
    • Bhavsar AP, Guttman JA, Finlay BB. 2007. Manipulation of host-cell pathways by bacterial pathogens. Nature 449:827-834.
    • (2007) Nature , vol.449 , pp. 827-834
    • Bhavsar, A.P.1    Guttman, J.A.2    Finlay, B.B.3
  • 13
    • 33846842428 scopus 로고    scopus 로고
    • Adaptation to the host environment: regulation of the SPI1 type III secretion system in Salmonella enterica serovar Typhimurium
    • Ellermeier JR, Slauch JM. 2007. Adaptation to the host environment: regulation of the SPI1 type III secretion system in Salmonella enterica serovar Typhimurium. Curr Opin Microbiol 10:24-29.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 24-29
    • Ellermeier, J.R.1    Slauch, J.M.2
  • 14
    • 34447099537 scopus 로고    scopus 로고
    • SnapShot: effector proteins of type III secretion systems
    • Galan JE. 2007. SnapShot: effector proteins of type III secretion systems. Cell 130:192.
    • (2007) Cell , vol.130 , pp. 192
    • Galan, J.E.1
  • 15
    • 84862556686 scopus 로고    scopus 로고
    • Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant-and animal-pathogenic bacteria
    • Buttner D. 2012. Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant-and animal-pathogenic bacteria. Microbiol Mol Biol Rev 76:262-310.
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 262-310
    • Buttner, D.1
  • 17
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck CJ. 1998. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol Mol Biol Rev 62:379-433.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 18
  • 19
    • 84907563228 scopus 로고    scopus 로고
    • Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells
    • Galan JE, Lara-Tejero M, Marlovits TC, Wagner S. 2014. Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells. Annu Rev Microbiol 68:415-438.
    • (2014) Annu Rev Microbiol , vol.68 , pp. 415-438
    • Galan, J.E.1    Lara-Tejero, M.2    Marlovits, T.C.3    Wagner, S.4
  • 20
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab RM. 2003. How bacteria assemble flagella. Annu Rev Microbiol 57:77-100.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 21
    • 0141430076 scopus 로고    scopus 로고
    • Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events
    • Gophna U, Ron EZ, Graur D. 2003. Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events. Gene 312:151-163.
    • (2003) Gene , vol.312 , pp. 151-163
    • Gophna, U.1    Ron, E.Z.2    Graur, D.3
  • 25
    • 77951637036 scopus 로고    scopus 로고
    • Imaging type-III secretion reveals dynamics and spatial segregation of Salmonella effectors
    • Van Engelenburg SB, Palmer AE. 2010. Imaging type-III secretion reveals dynamics and spatial segregation of Salmonella effectors. Nat Methods 7:325-330.
    • (2010) Nat Methods , vol.7 , pp. 325-330
    • Van Engelenburg, S.B.1    Palmer, A.E.2
  • 26
  • 27
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt O, Marlovits TC. 2011. Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science 331:1192-1195.
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 31
    • 0027982037 scopus 로고
    • The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins
    • Kaniga K, Bossio JC, Galan JE. 1994. The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins. Mol Microbiol 13:555-568.
    • (1994) Mol Microbiol , vol.13 , pp. 555-568
    • Kaniga, K.1    Bossio, J.C.2    Galan, J.E.3
  • 32
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago AM, Koronakis V. 1998. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol Microbiol 30:47-56.
    • (1998) Mol Microbiol , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 33
    • 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. 1998. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol Microbiol 28:1367-1380.
    • (1998) Mol Microbiol , vol.28 , pp. 1367-1380
    • Daefler, S.1    Russel, M.2
  • 39
    • 75249090025 scopus 로고    scopus 로고
    • Type III secretion systems shape up as they ship out
    • Marlovits TC, Stebbins CE. 2010. Type III secretion systems shape up as they ship out. Curr Opin Microbiol 13:47-52.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 47-52
    • Marlovits, T.C.1    Stebbins, C.E.2
  • 42
    • 84860914359 scopus 로고    scopus 로고
    • Interaction of MxiG with the cytosolic complex of the type III secretion system controls Shigella virulence
    • Barison N, Lambers J, Hurwitz R, Kolbe M. 2012. Interaction of MxiG with the cytosolic complex of the type III secretion system controls Shigella virulence. FASEB J 26:1717-1726.
    • (2012) FASEB J , vol.26 , pp. 1717-1726
    • Barison, N.1    Lambers, J.2    Hurwitz, R.3    Kolbe, M.4
  • 43
    • 84868611292 scopus 로고    scopus 로고
    • Structure and interactions of the cytoplasmic domain of the Yersinia type III secretion protein YscD
    • Gamez A, Mukerjea R, Alayyoubi M, Ghassemian M, Ghosh P. 2012. Structure and interactions of the cytoplasmic domain of the Yersinia type III secretion protein YscD. J Bacteriol 194:5949-5958.
    • (2012) J Bacteriol , vol.194 , pp. 5949-5958
    • Gamez, A.1    Mukerjea, R.2    Alayyoubi, M.3    Ghassemian, M.4    Ghosh, P.5
  • 44
    • 84857828509 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type III secretion system
    • Lountos GT, Tropea JE, Waugh DS. 2012. Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type III secretion system. Acta Crystallogr D Biol Crystallogr 68:201-209.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , pp. 201-209
    • Lountos, G.T.1    Tropea, J.E.2    Waugh, D.S.3
  • 47
    • 77953161216 scopus 로고    scopus 로고
    • A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body
    • Lilic M, Quezada CM, Stebbins CE. 2010. A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body. Acta Crystallogr D Biol Crystallogr 66:709-713.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 709-713
    • Lilic, M.1    Quezada, C.M.2    Stebbins, C.E.3
  • 48
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA
    • Worrall LJ, Vuckovic M, Strynadka NC. 2010. Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA. Protein Sci 19:1091-1096.
    • (2010) Protein Sci , vol.19 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.3
  • 52
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type III secretion injectisome
    • Marlovits TC, Kubori T, Lara-Tejero M, Thomas D, Unger VM, Galan JE. 2006. Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441:637-640.
    • (2006) Nature , vol.441 , pp. 637-640
    • Marlovits, T.C.1    Kubori, T.2    Lara-Tejero, M.3    Thomas, D.4    Unger, V.M.5    Galan, J.E.6
  • 54
    • 84863637916 scopus 로고    scopus 로고
    • Type III secretion in Yersinia: injectisome or not?
    • Edgren T, Forsberg A, Rosqvist R, Wolf-Watz H. 2012. Type III secretion in Yersinia: injectisome or not? PLoS Pathog 8:e1002669. doi:10.1371/journal.ppat.1002669.
    • (2012) PLoS Pathog , vol.8
    • Edgren, T.1    Forsberg, A.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 55
  • 56
    • 84893745802 scopus 로고    scopus 로고
    • A substratefusion protein is trapped inside the type III secretion system channel in Shigella flexneri
    • Dohlich K, Zumsteg AB, Goosmann C, Kolbe M. 2014. A substratefusion protein is trapped inside the type III secretion system channel in Shigella flexneri. PLoS Pathog 10:e1003881. doi:10.1371/journal.ppat.1003881.
    • (2014) PLoS Pathog , vol.10
    • Dohlich, K.1    Zumsteg, A.B.2    Goosmann, C.3    Kolbe, M.4
  • 61
    • 84858633508 scopus 로고    scopus 로고
    • Structure of a type III secretion needle at 7-A resolution provides insights into its assembly and signaling mechanisms
    • Fujii T, Cheung M, Blanco A, Kato T, Blocker AJ, Namba K. 2012. Structure of a type III secretion needle at 7-A resolution provides insights into its assembly and signaling mechanisms. Proc Natl Acad Sci USA 109:4461-4466.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4461-4466
    • Fujii, T.1    Cheung, M.2    Blanco, A.3    Kato, T.4    Blocker, A.J.5    Namba, K.6
  • 63
    • 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 SI, Galan JE. 2000. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc Natl Acad Sci USA 97: 10225-10230.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 64
    • 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. 2002. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length. J Bacteriol 184:1244-1252.
    • (2002) J Bacteriol , vol.184 , pp. 1244-1252
    • Tamano, K.1    Katayama, E.2    Toyotome, T.3    Sasakawa, C.4
  • 65
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L, Agrain C, Broz P, Cornelis GR. 2003. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302:1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 66
    • 84892608956 scopus 로고    scopus 로고
    • The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system
    • Lefebre MD, Galan JE. 2014. The inner rod protein controls substrate switching and needle length in a Salmonella type III secretion system. Proc Natl Acad Sci USA 111:817-822.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 817-822
    • Lefebre, M.D.1    Galan, J.E.2
  • 68
    • 84861796152 scopus 로고    scopus 로고
    • Ultrastructural analysis of IpaD at the tip of the nascent MxiH type III secretion apparatus of Shigella flexneri
    • Epler CR, Dickenson NE, Bullitt E, Picking WL. 2012. Ultrastructural analysis of IpaD at the tip of the nascent MxiH type III secretion apparatus of Shigella flexneri. J Mol Biol 420:29-39.
    • (2012) J Mol Biol , vol.420 , pp. 29-39
    • Epler, C.R.1    Dickenson, N.E.2    Bullitt, E.3    Picking, W.L.4
  • 69
    • 22244476683 scopus 로고    scopus 로고
    • Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes
    • Goure J, Broz P, Attree O, Cornelis GR, Attree I. 2005. Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes. J Infect Dis 192:218-225.
    • (2005) J Infect Dis , vol.192 , pp. 218-225
    • Goure, J.1    Broz, P.2    Attree, O.3    Cornelis, G.R.4    Attree, I.5
  • 70
    • 43449122166 scopus 로고    scopus 로고
    • The type III secretion system tip complex and translocon
    • Mueller CA, Broz P, Cornelis GR. 2008. The type III secretion system tip complex and translocon. Mol Microbiol 68:1085-1095.
    • (2008) Mol Microbiol , vol.68 , pp. 1085-1095
    • Mueller, C.A.1    Broz, P.2    Cornelis, G.R.3
  • 71
    • 27344459420 scopus 로고
    • Immunization against plague by a specific fraction of Pasteurella pseudotuberculosis
    • Lawton WD, Surgalla MJ. 1963. Immunization against plague by a specific fraction of Pasteurella pseudotuberculosis. J Infect Dis 113:39-42.
    • (1963) J Infect Dis , vol.113 , pp. 39-42
    • Lawton, W.D.1    Surgalla, M.J.2
  • 75
    • 80052316924 scopus 로고    scopus 로고
    • Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands
    • Lunelli M, Hurwitz R, Lambers J, Kolbe M. 2011. Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands. PLoS Pathog 7:e1002163. doi:10.1371/journal.ppat.1002163.
    • (2011) PLoS Pathog , vol.7
    • Lunelli, M.1    Hurwitz, R.2    Lambers, J.3    Kolbe, M.4
  • 78
    • 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 MJ, Nisan I, Neves BC, Bain C, Wolff C, Dougan G, Frankel G. 1998. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J 17:2166-2176.
    • (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
  • 80
    • 15544376398 scopus 로고    scopus 로고
    • IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes
    • Picking WL, Nishioka H, Hearn PD, Baxter MA, Harrington AT, Blocker A, Picking WD. 2005. IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes. Infect Immun 73:1432-1440.
    • (2005) Infect Immun , vol.73 , pp. 1432-1440
    • Picking, W.L.1    Nishioka, H.2    Hearn, P.D.3    Baxter, M.A.4    Harrington, A.T.5    Blocker, A.6    Picking, W.D.7
  • 82
    • 46049089615 scopus 로고    scopus 로고
    • Signal pathway in salt-activated expression of the Salmonella pathogenicity island 1 type III secretion system in Salmonella enterica serovar Typhimurium
    • Mizusaki H, Takaya A, Yamamoto T, Aizawa S. 2008. Signal pathway in salt-activated expression of the Salmonella pathogenicity island 1 type III secretion system in Salmonella enterica serovar Typhimurium. J Bacteriol 190:4624-4631.
    • (2008) J Bacteriol , vol.190 , pp. 4624-4631
    • Mizusaki, H.1    Takaya, A.2    Yamamoto, T.3    Aizawa, S.4
  • 84
    • 66349123567 scopus 로고    scopus 로고
    • Accurate prediction of secreted substrates and identification of a conserved putative secretion signal for type III secretion systems
    • Samudrala R, Heffron F, McDermott JE. 2009. Accurate prediction of secreted substrates and identification of a conserved putative secretion signal for type III secretion systems. PLoS Pathog 5:e1000375. doi:10.1371/journal.ppat.1000375.
    • (2009) PLoS Pathog , vol.5
    • Samudrala, R.1    Heffron, F.2    McDermott, J.E.3
  • 86
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • Lloyd SA, Norman M, Rosqvist R, Wolf-Watz H. 2001. Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals. Mol Microbiol 39:520-531.
    • (2001) Mol Microbiol , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 87
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • Lee SH, Galan JE. 2004. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol Microbiol 51:483-495.
    • (2004) Mol Microbiol , vol.51 , pp. 483-495
    • Lee, S.H.1    Galan, J.E.2
  • 88
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins CE, Galan JE. 2001. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414:77-81.
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 89
    • 0042338640 scopus 로고    scopus 로고
    • Priming virulence factors for delivery into the host
    • Stebbins CE, Galan JE. 2003. Priming virulence factors for delivery into the host. Nat Rev Mol Cell Biol 4:738-743.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 738-743
    • Stebbins, C.E.1    Galan, J.E.2
  • 90
    • 79955838725 scopus 로고    scopus 로고
    • Biogenesis, regulation, and targeting of the type III secretion system
    • Izore T, Job V, Dessen A. 2011. Biogenesis, regulation, and targeting of the type III secretion system. Structure 19:603-612.
    • (2011) Structure , vol.19 , pp. 603-612
    • Izore, T.1    Job, V.2    Dessen, A.3
  • 91
    • 0034932732 scopus 로고    scopus 로고
    • Roles of LcrG and LcrV during type III targeting of effector Yops by Yersinia enterocolitica
    • DeBord KL, Lee VT, Schneewind O. 2001. Roles of LcrG and LcrV during type III targeting of effector Yops by Yersinia enterocolitica. J Bacteriol 183:4588-4598.
    • (2001) J Bacteriol , vol.183 , pp. 4588-4598
    • DeBord, K.L.1    Lee, V.T.2    Schneewind, O.3
  • 92
    • 33344459126 scopus 로고    scopus 로고
    • A common structural motif in the binding of virulence factors to bacterial secretion chaperones
    • Lilic M, Vujanac M, Stebbins CE. 2006. A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol Cell 21:653-664.
    • (2006) Mol Cell , vol.21 , pp. 653-664
    • Lilic, M.1    Vujanac, M.2    Stebbins, C.E.3
  • 93
    • 84873547335 scopus 로고    scopus 로고
    • Structure of the HopA1(21-102)-ShcA chaperone-effector complex of Pseudomonas syringae reveals conservation of a virulence factor binding motif from animal to plant pathogens
    • Janjusevic R, Quezada CM, Small J, Stebbins CE. 2013. Structure of the HopA1(21-102)-ShcA chaperone-effector complex of Pseudomonas syringae reveals conservation of a virulence factor binding motif from animal to plant pathogens. J Bacteriol 195:658-664.
    • (2013) J Bacteriol , vol.195 , pp. 658-664
    • Janjusevic, R.1    Quezada, C.M.2    Small, J.3    Stebbins, C.E.4
  • 94
    • 84857874120 scopus 로고    scopus 로고
    • A new means to identify type 3 secreted effectors: functionally interchangeable class IB chaperones recognize a conserved sequence
    • Costa SC, Schmitz AM, Jahufar FF, Boyd JD, Cho MY, Glicksman MA, Lesser CF. 2012. A new means to identify type 3 secreted effectors: functionally interchangeable class IB chaperones recognize a conserved sequence. MBio 3:e00243-11. doi:10.1128/mBio.00243-11.
    • (2012) MBio , vol.3
    • Costa, S.C.1    Schmitz, A.M.2    Jahufar, F.F.3    Boyd, J.D.4    Cho, M.Y.5    Glicksman, M.A.6    Lesser, C.F.7
  • 95
    • 0026065361 scopus 로고
    • Secretion of hybrid proteins by the Yersinia Yop export system
    • Michiels T, Cornelis GR. 1991. Secretion of hybrid proteins by the Yersinia Yop export system. J Bacteriol 173:1677-1685.
    • (1991) J Bacteriol , vol.173 , pp. 1677-1685
    • Michiels, T.1    Cornelis, G.R.2
  • 96
    • 33749241527 scopus 로고    scopus 로고
    • Optimization of the delivery of heterologous proteins by the Salmonella enterica serovar Typhimurium type III secretion system for vaccine development
    • Chen LM, Briones G, Donis RO, Galan JE. 2006. Optimization of the delivery of heterologous proteins by the Salmonella enterica serovar Typhimurium type III secretion system for vaccine development. Infect Immun 74:5826-5833.
    • (2006) Infect Immun , vol.74 , pp. 5826-5833
    • Chen, L.M.1    Briones, G.2    Donis, R.O.3    Galan, J.E.4
  • 98
    • 1842506700 scopus 로고    scopus 로고
    • Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains
    • Akeda Y, Galan JE. 2004. Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains. J Bacteriol 186:2402-2412.
    • (2004) J Bacteriol , vol.186 , pp. 2402-2412
    • Akeda, Y.1    Galan, J.E.2
  • 100
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret L, Calder SR, Higgins M, Hughes C. 2003. Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol Microbiol 48:1349-1355.
    • (2003) Mol Microbiol , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 101
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture of the flagellar type III protein export apparatus and F-and V-type ATPases
    • Ibuki T, Imada K, Minamino T, Kato T, Miyata T, Namba K. 2011. Common architecture of the flagellar type III protein export apparatus and F-and V-type ATPases. Nat Struct Mol Biol 18:277-282.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 277-282
    • Ibuki, T.1    Imada, K.2    Minamino, T.3    Kato, T.4    Miyata, T.5    Namba, K.6
  • 103
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda Y, Galan JE. 2005. Chaperone release and unfolding of substrates in type III secretion. Nature 437:911-915.
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 104
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino T, Namba K. 2008. Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 451:485-488.
    • (2008) Nature , vol.451 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 106
    • 84912081031 scopus 로고    scopus 로고
    • ATPaseindependent type-III protein secretion in Salmonella enterica
    • Erhardt M, Mertens ME, Fabiani FD, Hughes KT. 2014. ATPaseindependent type-III protein secretion in Salmonella enterica. PLoS Genet 10:e1004800. doi:10.1371/journal.pgen.1004800.
    • (2014) PLoS Genet , vol.10
    • Erhardt, M.1    Mertens, M.E.2    Fabiani, F.D.3    Hughes, K.T.4
  • 107
    • 84923371148 scopus 로고    scopus 로고
    • The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis
    • Minamino T, Morimoto YV, Kinoshita M, Aldridge PD, Namba K. 2014. The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis. Sci Rep 4:7579. doi:10.1038/srep07579.
    • (2014) Sci Rep , vol.4 , pp. 7579
    • Minamino, T.1    Morimoto, Y.V.2    Kinoshita, M.3    Aldridge, P.D.4    Namba, K.5
  • 109
    • 84889777894 scopus 로고    scopus 로고
    • Common and distinct structural features of Salmonella injectisome and flagellar basal body
    • Kawamoto A, Morimoto YV, Miyata T, Minamino T, Hughes KT, Kato T, Namba K. 2013. Common and distinct structural features of Salmonella injectisome and flagellar basal body. Sci Rep 3:3369. doi:10.1038/srep03369.
    • (2013) Sci Rep , vol.3 , pp. 3369
    • Kawamoto, A.1    Morimoto, Y.V.2    Miyata, T.3    Minamino, T.4    Hughes, K.T.5    Kato, T.6    Namba, K.7
  • 111
    • 3042692057 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB
    • Wilharm G, Lehmann V, Krauss K, Lehnert B, Richter S, Ruckdeschel K, Heesemann J, Trulzsch K. 2004. Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB. Infect Immun 72:4004-4009.
    • (2004) Infect Immun , vol.72 , pp. 4004-4009
    • Wilharm, G.1    Lehmann, V.2    Krauss, K.3    Lehnert, B.4    Richter, S.5    Ruckdeschel, K.6    Heesemann, J.7    Trulzsch, K.8
  • 112
    • 38849131977 scopus 로고    scopus 로고
    • Energizing type III secretion machines: what is the fuel?
    • Galan JE. 2008. Energizing type III secretion machines: what is the fuel? Nat Struct Mol Biol 15:127-128.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 127-128
    • Galan, J.E.1
  • 114
    • 84921824920 scopus 로고    scopus 로고
    • A Salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure
    • Roblin P, Dewitte F, Villeret V, Biondi EG, Bompard C. 2015. A Salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure. J Bacteriol 197:688-698.
    • (2015) J Bacteriol , vol.197 , pp. 688-698
    • Roblin, P.1    Dewitte, F.2    Villeret, V.3    Biondi, E.G.4    Bompard, C.5
  • 115
    • 84921812568 scopus 로고    scopus 로고
    • The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes
    • Tsai CL, Burkinshaw BJ, Strynadka NC, Tainer JA. 2015. The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes. J Bacteriol 197:672-675.
    • (2015) J Bacteriol , vol.197 , pp. 672-675
    • Tsai, C.L.1    Burkinshaw, B.J.2    Strynadka, N.C.3    Tainer, J.A.4
  • 117
    • 84878241251 scopus 로고    scopus 로고
    • Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion
    • Chen L, Ai X, Portaliou AG, Minetti CA, Remeta DP, Economou A, Kalodimos CG. 2013. Substrate-activated conformational switch on chaperones encodes a targeting signal in type III secretion. Cell Rep 3:709-715.
    • (2013) Cell Rep , vol.3 , pp. 709-715
    • Chen, L.1    Ai, X.2    Portaliou, A.G.3    Minetti, C.A.4    Remeta, D.P.5    Economou, A.6    Kalodimos, C.G.7
  • 118
    • 84879650647 scopus 로고    scopus 로고
    • A novel effector secretion mechanism based on proton-motive forcedependent type III secretion apparatus rotation
    • Ohgita T, Hayashi N, Hama S, Tsuchiya H, Gotoh N, Kogure K. 2013. A novel effector secretion mechanism based on proton-motive forcedependent type III secretion apparatus rotation. FASEB J 27:2862-2872.
    • (2013) FASEB J , vol.27 , pp. 2862-2872
    • Ohgita, T.1    Hayashi, N.2    Hama, S.3    Tsuchiya, H.4    Gotoh, N.5    Kogure, K.6
  • 121
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • Lara-Tejero M, Kato J, Wagner S, Liu X, Galan JE. 2011. A sorting platform determines the order of protein secretion in bacterial type III systems. Science 331:1188-1191.
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galan, J.E.5
  • 122
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo B, Fraser GM, Minamino T, Macnab RM. 2002. Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol Microbiol 45:967-982.
    • (2002) Mol Microbiol , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    Macnab, R.M.4
  • 123
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino T, MacNab RM. 2000. FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol Microbiol 37:1494-1503.
    • (2000) Mol Microbiol , vol.37 , pp. 1494-1503
    • Minamino, T.1    MacNab, R.M.2
  • 124
    • 33644853360 scopus 로고    scopus 로고
    • Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori
    • Lane MC, O'Toole PW, Moore SA. 2006. Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori. J Biol Chem 281:508-517.
    • (2006) J Biol Chem , vol.281 , pp. 508-517
    • Lane, M.C.1    O'Toole, P.W.2    Moore, S.A.3
  • 125
    • 72049109167 scopus 로고    scopus 로고
    • Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus
    • Minamino T, Yoshimura SD, Morimoto YV, Gonzalez-Pedrajo B, Kami-Ike N, Namba K. 2009. Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus. Mol Microbiol 74:1471-1483.
    • (2009) Mol Microbiol , vol.74 , pp. 1471-1483
    • Minamino, T.1    Yoshimura, S.D.2    Morimoto, Y.V.3    Gonzalez-Pedrajo, B.4    Kami-Ike, N.5    Namba, K.6
  • 126
    • 33749330451 scopus 로고    scopus 로고
    • The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex
    • McMurry JL, Murphy JW, Gonzalez-Pedrajo B. 2006. The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex. Biochemistry 45:11790-11798.
    • (2006) Biochemistry , vol.45 , pp. 11790-11798
    • McMurry, J.L.1    Murphy, J.W.2    Gonzalez-Pedrajo, B.3
  • 127
    • 0037701404 scopus 로고    scopus 로고
    • The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH
    • Minamino T, Gonzalez-Pedrajo B, Kihara M, Namba K, Macnab RM. 2003. The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. J Bacteriol 185: 3983-3988.
    • (2003) J Bacteriol , vol.185 , pp. 3983-3988
    • Minamino, T.1    Gonzalez-Pedrajo, B.2    Kihara, M.3    Namba, K.4    Macnab, R.M.5
  • 128
    • 84923284551 scopus 로고    scopus 로고
    • Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus
    • Bai F, Morimoto YV, Yoshimura SD, Hara N, Kami-Ike N, Namba K, Minamino T. 2014. Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus. Sci Rep 4:6528. doi:10.1038/srep06528.
    • (2014) Sci Rep , vol.4 , pp. 6528
    • Bai, F.1    Morimoto, Y.V.2    Yoshimura, S.D.3    Hara, N.4    Kami-Ike, N.5    Namba, K.6    Minamino, T.7
  • 129
    • 84922260211 scopus 로고    scopus 로고
    • Composition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisome
    • Diepold A, Kudryashev M, Delalez NJ, Berry RM, Armitage JP. 2015. Composition, formation, and regulation of the cytosolic c-ring, a dynamic component of the type III secretion injectisome. PLoS Biol 13: e1002039. doi:10.1371/journal.pbio.1002039.
    • (2015) PLoS Biol , vol.13
    • Diepold, A.1    Kudryashev, M.2    Delalez, N.J.3    Berry, R.M.4    Armitage, J.P.5
  • 131
    • 16844367441 scopus 로고    scopus 로고
    • Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima
    • Brown PN, Mathews MA, Joss LA, Hill CP, Blair DF. 2005. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima. J Bacteriol 187:2890-2902.
    • (2005) J Bacteriol , vol.187 , pp. 2890-2902
    • Brown, P.N.1    Mathews, M.A.2    Joss, L.A.3    Hill, C.P.4    Blair, D.F.5
  • 132
    • 84857553241 scopus 로고    scopus 로고
    • Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion
    • Bzymek KP, Hamaoka BY, Ghosh P. 2012. Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion. Biochemistry 51:1669-1677.
    • (2012) Biochemistry , vol.51 , pp. 1669-1677
    • Bzymek, K.P.1    Hamaoka, B.Y.2    Ghosh, P.3
  • 133
    • 33645233315 scopus 로고    scopus 로고
    • Organization of FliN subunits in the flagellar motor of Escherichia coli
    • Paul K, Blair DF. 2006. Organization of FliN subunits in the flagellar motor of Escherichia coli. J Bacteriol 188:2502-2511.
    • (2006) J Bacteriol , vol.188 , pp. 2502-2511
    • Paul, K.1    Blair, D.F.2
  • 134
    • 33745930219 scopus 로고    scopus 로고
    • Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching
    • Paul K, Harmon JG, Blair DF. 2006. Mutational analysis of the flagellar rotor protein FliN: identification of surfaces important for flagellar assembly and switching. J Bacteriol 188:5240-5248.
    • (2006) J Bacteriol , vol.188 , pp. 5240-5248
    • Paul, K.1    Harmon, J.G.2    Blair, D.F.3
  • 135
    • 63649127135 scopus 로고    scopus 로고
    • On the quaternary association of the type III secretion system HrcQB-C protein: experimental evidence differentiates among the various oligomerization models
    • Fadouloglou VE, Bastaki MN, Ashcroft AE, Phillips SE, Panopoulos NJ, Glykos NM, Kokkinidis M. 2009. On the quaternary association of the type III secretion system HrcQB-C protein: experimental evidence differentiates among the various oligomerization models. J Struct Biol 166:214-225.
    • (2009) J Struct Biol , vol.166 , pp. 214-225
    • Fadouloglou, V.E.1    Bastaki, M.N.2    Ashcroft, A.E.3    Phillips, S.E.4    Panopoulos, N.J.5    Glykos, N.M.6    Kokkinidis, M.7
  • 137
    • 84867815891 scopus 로고    scopus 로고
    • Structure of flagellar motor proteins in complex allows for insights into motor structure and switching
    • Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW. 2012. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching. J Biol Chem 287:35779-35783.
    • (2012) J Biol Chem , vol.287 , pp. 35779-35783
    • Vartanian, A.S.1    Paz, A.2    Fortgang, E.A.3    Abramson, J.4    Dahlquist, F.W.5
  • 138
    • 0036719968 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated protein InvE controls translocation of effector proteins into host cells
    • Kubori T, Galan JE. 2002. Salmonella type III secretion-associated protein InvE controls translocation of effector proteins into host cells. J Bacteriol 184:4699-4708.
    • (2002) J Bacteriol , vol.184 , pp. 4699-4708
    • Kubori, T.1    Galan, J.E.2
  • 139
    • 77950607053 scopus 로고    scopus 로고
    • Timing is everything: the regulation of type III secretion
    • Deane JE, Abrusci P, Johnson S, Lea SM. 2010. Timing is everything: the regulation of type III secretion. Cell Mol Life Sci 67:1065-1075.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1065-1075
    • Deane, J.E.1    Abrusci, P.2    Johnson, S.3    Lea, S.M.4
  • 140
    • 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. 2002. Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins. J Bacteriol 184:3433-3441.
    • (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
  • 141
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain C, Callebaut I, Journet L, Sorg I, Paroz C, Mota LJ, Cornelis GR. 2005. Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol Microbiol 56:54-67.
    • (2005) Mol Microbiol , vol.56 , pp. 54-67
    • Agrain, C.1    Callebaut, I.2    Journet, L.3    Sorg, I.4    Paroz, C.5    Mota, L.J.6    Cornelis, G.R.7
  • 142
    • 79957680663 scopus 로고    scopus 로고
    • The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type III secretion apparatus
    • Mizuno S, Amida H, Kobayashi N, Aizawa S, Tate S. 2011. The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type III secretion apparatus. J Mol Biol 409:558-573.
    • (2011) J Mol Biol , vol.409 , pp. 558-573
    • Mizuno, S.1    Amida, H.2    Kobayashi, N.3    Aizawa, S.4    Tate, S.5
  • 143
    • 84885445898 scopus 로고    scopus 로고
    • Functionally essential interaction between Yersinia YscO and the T3S4 domain of YscP
    • Mukerjea R, Ghosh P. 2013. Functionally essential interaction between Yersinia YscO and the T3S4 domain of YscP. J Bacteriol 195:4631-4638.
    • (2013) J Bacteriol , vol.195 , pp. 4631-4638
    • Mukerjea, R.1    Ghosh, P.2
  • 144
    • 56749182220 scopus 로고    scopus 로고
    • Spa32 interaction with the inner-membrane Spa40 component of the type III secretion system of Shigella flexneri is required for the control of the needle length by a molecular tape measure mechanism
    • Botteaux A, Sani M, Kayath CA, Boekema EJ, Allaoui A. 2008. Spa32 interaction with the inner-membrane Spa40 component of the type III secretion system of Shigella flexneri is required for the control of the needle length by a molecular tape measure mechanism. Mol Microbiol 70:1515-1528.
    • (2008) Mol Microbiol , vol.70 , pp. 1515-1528
    • Botteaux, A.1    Sani, M.2    Kayath, C.A.3    Boekema, E.J.4    Allaoui, A.5
  • 145
    • 44949221276 scopus 로고    scopus 로고
    • YscP and YscU switch the substrate specificity of the Yersinia type III secretion system by regulating export of the inner rod protein YscI
    • Wood SE, Jin J, Lloyd SA. 2008. YscP and YscU switch the substrate specificity of the Yersinia type III secretion system by regulating export of the inner rod protein YscI. J Bacteriol 190:4252-4262.
    • (2008) J Bacteriol , vol.190 , pp. 4252-4262
    • Wood, S.E.1    Jin, J.2    Lloyd, S.A.3
  • 146
    • 77956378439 scopus 로고    scopus 로고
    • The 33 carboxyl-terminal residues of Spa40 orchestrate the multi-step assembly process of the type III secretion needle complex in Shigella flexneri
    • Botteaux A, Kayath CA, Page AL, Jouihri N, Sani M, Boekema E, Biskri L, Parsot C, Allaoui A. 2010. The 33 carboxyl-terminal residues of Spa40 orchestrate the multi-step assembly process of the type III secretion needle complex in Shigella flexneri. Microbiology 156:2807-2817.
    • (2010) Microbiology , vol.156 , pp. 2807-2817
    • Botteaux, A.1    Kayath, C.A.2    Page, A.L.3    Jouihri, N.4    Sani, M.5    Boekema, E.6    Biskri, L.7    Parsot, C.8    Allaoui, A.9
  • 149
    • 58149302495 scopus 로고    scopus 로고
    • MxiC is secreted by and controls the substrate specificity of the Shigella flexneri type III secretion apparatus
    • Botteaux A, Sory MP, Biskri L, Parsot C, Allaoui A. 2009. MxiC is secreted by and controls the substrate specificity of the Shigella flexneri type III secretion apparatus. Mol Microbiol 71:449-460.
    • (2009) Mol Microbiol , vol.71 , pp. 449-460
    • Botteaux, A.1    Sory, M.P.2    Biskri, L.3    Parsot, C.4    Allaoui, A.5
  • 150
    • 0034864508 scopus 로고    scopus 로고
    • Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica
    • Cheng LW, Kay O, Schneewind O. 2001. Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica. J Bacteriol 183:5293-5301.
    • (2001) J Bacteriol , vol.183 , pp. 5293-5301
    • Cheng, L.W.1    Kay, O.2    Schneewind, O.3
  • 151
    • 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. 1992. A novel protein, LcrQ, involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH. J Bacteriol 174:3355-3363.
    • (1992) J Bacteriol , vol.174 , pp. 3355-3363
    • Rimpilainen, M.1    Forsberg, A.2    Wolf-Watz, H.3
  • 152
    • 0027229148 scopus 로고
    • LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis
    • Skryzpek E, Straley SC. 1993. LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis. J Bacteriol 175:3520-3528.
    • (1993) J Bacteriol , vol.175 , pp. 3520-3528
    • Skryzpek, E.1    Straley, S.C.2
  • 153
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot FD, Jackson MW, Penrose KJ, Cherry S, Tropea JE, Plano GV, Waugh DS. 2005. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J Mol Biol 346:1147-1161.
    • (2005) J Mol Biol , vol.346 , pp. 1147-1161
    • Schubot, F.D.1    Jackson, M.W.2    Penrose, K.J.3    Cherry, S.4    Tropea, J.E.5    Plano, G.V.6    Waugh, D.S.7
  • 154
    • 40849102234 scopus 로고    scopus 로고
    • Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues
    • Deane JE, Roversi P, King C, Johnson S, Lea SM. 2008. Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues. J Mol Biol 377:985-992.
    • (2008) J Mol Biol , vol.377 , pp. 985-992
    • Deane, J.E.1    Roversi, P.2    King, C.3    Johnson, S.4    Lea, S.M.5
  • 155
    • 84908240911 scopus 로고    scopus 로고
    • Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein
    • Weise CF, Login FH, Ho O, Grobner G, Wolf-Watz H, Wolf-Watz M. 2014. Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein. Biophys J 107:1950-1961.
    • (2014) Biophys J , vol.107 , pp. 1950-1961
    • Weise, C.F.1    Login, F.H.2    Ho, O.3    Grobner, G.4    Wolf-Watz, H.5    Wolf-Watz, M.6
  • 157
    • 0034443263 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium invasion is repressed in the presence of bile
    • Prouty AM, Gunn JS. 2000. Salmonella enterica serovar Typhimurium invasion is repressed in the presence of bile. Infect Immun 68:6763-6769.
    • (2000) Infect Immun , vol.68 , pp. 6763-6769
    • Prouty, A.M.1    Gunn, J.S.2
  • 158
    • 84856799133 scopus 로고    scopus 로고
    • Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure
    • Barta ML, Guragain M, Adam P, Dickenson NE, Patil M, Geisbrecht BV, Picking WL, Picking WD. 2012. Identification of the bile salt binding site on IpaD from Shigella flexneri and the influence of ligand binding on IpaD structure. Proteins 80:935-945.
    • (2012) Proteins , vol.80 , pp. 935-945
    • Barta, M.L.1    Guragain, M.2    Adam, P.3    Dickenson, N.E.4    Patil, M.5    Geisbrecht, B.V.6    Picking, W.L.7    Picking, W.D.8
  • 159
    • 78650765847 scopus 로고    scopus 로고
    • The crystal structures of the Salmonella type III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholate
    • Chatterjee S, Zhong D, Nordhues BA, Battaile KP, Lovell S, De Guzman RN. 2011. The crystal structures of the Salmonella type III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholate. Protein Sci 20:75-86.
    • (2011) Protein Sci , vol.20 , pp. 75-86
    • Chatterjee, S.1    Zhong, D.2    Nordhues, B.A.3    Battaile, K.P.4    Lovell, S.5    De Guzman, R.N.6
  • 160
    • 0028072943 scopus 로고
    • The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD
    • Menard R, Sansonetti P, Parsot C. 1994. The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD. EMBO J 13:5293-5302.
    • (1994) EMBO J , vol.13 , pp. 5293-5302
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3
  • 161
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist R, Magnusson KE, Wolf-Watz H. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J 13:964-972.
    • (1994) EMBO J , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 162
    • 0029090966 scopus 로고
    • Contact with cultured epithelial cells stimulates secretion of Salmonella typhimurium invasion protein InvJ
    • Zierler MK, Galan JE. 1995. Contact with cultured epithelial cells stimulates secretion of Salmonella typhimurium invasion protein InvJ. Infect Immun 63:4024-4028.
    • (1995) Infect Immun , vol.63 , pp. 4024-4028
    • Zierler, M.K.1    Galan, J.E.2
  • 163
    • 67650093032 scopus 로고    scopus 로고
    • Salmonella enterica serovar typhimurium pathogenicity island 1-encoded type III secretion system translocases mediate intimate attachment to nonphagocytic cells
    • Lara-Tejero M, Galan JE. 2009. Salmonella enterica serovar typhimurium pathogenicity island 1-encoded type III secretion system translocases mediate intimate attachment to nonphagocytic cells. Infect Immun 77:2635-2642.
    • (2009) Infect Immun , vol.77 , pp. 2635-2642
    • Lara-Tejero, M.1    Galan, J.E.2
  • 164
    • 67650090752 scopus 로고    scopus 로고
    • Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction
    • Epler CR, Dickenson NE, Olive AJ, Picking WL, Picking WD. 2009. Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction. Infect Immun 77:2754-2761.
    • (2009) Infect Immun , vol.77 , pp. 2754-2761
    • Epler, C.R.1    Dickenson, N.E.2    Olive, A.J.3    Picking, W.L.4    Picking, W.D.5
  • 167
    • 77952858676 scopus 로고    scopus 로고
    • pH sensing by intracellular Salmonella induces effector translocation
    • Yu XJ, McGourty K, Liu M, Unsworth KE, Holden DW. 2010. pH sensing by intracellular Salmonella induces effector translocation. Science 328:1040-1043.
    • (2010) Science , vol.328 , pp. 1040-1043
    • Yu, X.J.1    McGourty, K.2    Liu, M.3    Unsworth, K.E.4    Holden, D.W.5
  • 168
    • 84860521139 scopus 로고    scopus 로고
    • Functions of the Salmonella pathogenicity island 2 (SPI-2) type III secretion system effectors
    • Figueira R, Holden DW. 2012. Functions of the Salmonella pathogenicity island 2 (SPI-2) type III secretion system effectors. Microbiology 158:1147-1161.
    • (2012) Microbiology , vol.158 , pp. 1147-1161
    • Figueira, R.1    Holden, D.W.2
  • 169
    • 25144451293 scopus 로고    scopus 로고
    • The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion
    • Torruellas J, Jackson MW, Pennock JW, Plano GV. 2005. The Yersinia pestis type III secretion needle plays a role in the regulation of Yop secretion. Mol Microbiol 57:1719-1733.
    • (2005) Mol Microbiol , vol.57 , pp. 1719-1733
    • Torruellas, J.1    Jackson, M.W.2    Pennock, J.W.3    Plano, G.V.4
  • 170
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan SC, Phillips RM, Ghosh P. 2002. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol Cell 9:971-980.
    • (2002) Mol Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 171
    • 13444295356 scopus 로고    scopus 로고
    • Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2
    • Phan J, Tropea JE, Waugh DS. 2004. Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. Acta Crystallogr D Biol Crystallogr 60:1591-1599.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1591-1599
    • Phan, J.1    Tropea, J.E.2    Waugh, D.S.3
  • 172
    • 84862268306 scopus 로고    scopus 로고
    • Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD
    • Schreiner M, Niemann HH. 2012. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Struct Biol 12:13.
    • (2012) BMC Struct Biol , vol.12 , pp. 13
    • Schreiner, M.1    Niemann, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.