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Volumn , Issue , 2013, Pages 417-450

Type 3 secretion systems

Author keywords

E. coli; Effector; Injectisome; Shigella; Type III secretion system; Virulence

Indexed keywords


EID: 84941636958     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-397048-0.00014-0     Document Type: Chapter
Times cited : (3)

References (198)
  • 1
    • 0024323528 scopus 로고
    • A dual transcriptional activation system for the 230 kb plasmid genes coding for virulence-associated antigens of Shigella flexneri
    • Adler B., Sasakawa C., Tobe T., Makino S., Komatsu K., Yoshikawa M. A dual transcriptional activation system for the 230 kb plasmid genes coding for virulence-associated antigens of Shigella flexneri. Mol. Microbiol. 1989, 3(5):627-635.
    • (1989) Mol. Microbiol. , vol.3 , Issue.5 , pp. 627-635
    • Adler, B.1    Sasakawa, C.2    Tobe, T.3    Makino, S.4    Komatsu, K.5    Yoshikawa, M.6
  • 2
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a type 3 secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain C., Callebaut I., Journet L., et al. Characterization of a type 3 secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol. Microbiol. 2005, 56(1):54-67.
    • (2005) Mol. Microbiol. , vol.56 , Issue.1 , pp. 54-67
    • Agrain, C.1    Callebaut, I.2    Journet, L.3
  • 3
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type 3 secretion
    • Akeda Y., Galan J.E. Chaperone release and unfolding of substrates in type 3 secretion. Nature 2005, 437(7060):911-915.
    • (2005) Nature , vol.437 , Issue.7060 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 4
    • 15944376869 scopus 로고    scopus 로고
    • A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type 3 secretion
    • Allen-Vercoe E., Toh M.C., Waddell B., Ho H., DeVinney R. A carboxy-terminal domain of Tir from enterohemorrhagic Escherichia coli O157:H7 (EHEC O157:H7) required for efficient type 3 secretion. FEMS Microbiol. Lett. 2005, 243(2):355-364.
    • (2005) FEMS Microbiol. Lett. , vol.243 , Issue.2 , pp. 355-364
    • Allen-Vercoe, E.1    Toh, M.C.2    Waddell, B.3    Ho, H.4    DeVinney, R.5
  • 6
    • 66349124179 scopus 로고    scopus 로고
    • Sequence-based prediction of type 3 secreted proteins
    • Arnold R., Brandmaier S., Kleine F., et al. Sequence-based prediction of type 3 secreted proteins. PLoS Pathog. 2009, 5(4):e1000376.
    • (2009) PLoS Pathog. , vol.5 , Issue.4
    • Arnold, R.1    Brandmaier, S.2    Kleine, F.3
  • 7
    • 0030793819 scopus 로고    scopus 로고
    • Secretion of Ipa proteins by Shigella flexneri: inducer molecules and kinetics of activation
    • Bahrani F.K., Sansonetti P.J., Parsot C. Secretion of Ipa proteins by Shigella flexneri: inducer molecules and kinetics of activation. Infect. Immun. 1997, 65(10):4005-4010.
    • (1997) Infect. Immun. , vol.65 , Issue.10 , pp. 4005-4010
    • Bahrani, F.K.1    Sansonetti, P.J.2    Parsot, C.3
  • 8
    • 77954920256 scopus 로고    scopus 로고
    • FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type 3 secretion system
    • Bange G., Kummerer N., Engel C., Bozkurt G., Wild K., Sinning I. FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type 3 secretion system. Proc. Natl. Acad. Sci. USA 2010, 107(25):11295-11300.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , Issue.25 , pp. 11295-11300
    • Bange, G.1    Kummerer, N.2    Engel, C.3    Bozkurt, G.4    Wild, K.5    Sinning, I.6
  • 9
    • 28044448059 scopus 로고    scopus 로고
    • A positive regulatory loop controls expression of the locus of enterocyte effacement-encoded regulators Ler and GrlA
    • Barba J., Bustamante V.H., Flores-Valdez M.A., Deng W., Finlay B.B., Puente J.L. A positive regulatory loop controls expression of the locus of enterocyte effacement-encoded regulators Ler and GrlA. J. Bacteriol. 2005, 187(23):7918-7930.
    • (2005) J. Bacteriol. , vol.187 , Issue.23 , pp. 7918-7930
    • Barba, J.1    Bustamante, V.H.2    Flores-Valdez, M.A.3    Deng, W.4    Finlay, B.B.5    Puente, J.L.6
  • 10
    • 84860914359 scopus 로고    scopus 로고
    • Interaction of MxiG with the cytosolic complex of the type 3 secretion system controls Shigella virulence
    • Barison N., Lambers J., Hurwitz R., Kolbe M. Interaction of MxiG with the cytosolic complex of the type 3 secretion system controls Shigella virulence. FASEB J 2012, 26(4):1717-1726.
    • (2012) FASEB J , vol.26 , Issue.4 , pp. 1717-1726
    • Barison, N.1    Lambers, J.2    Hurwitz, R.3    Kolbe, M.4
  • 11
    • 84858283343 scopus 로고    scopus 로고
    • The structures of coiled-coil domains from type 3 secretion system translocators reveal homology to pore-forming toxins
    • Barta M.L., Dickenson N.E., Patil M., et al. The structures of coiled-coil domains from type 3 secretion system translocators reveal homology to pore-forming toxins. J. Mol. Biol. 2012, 417(5):395-405.
    • (2012) J. Mol. Biol. , vol.417 , Issue.5 , pp. 395-405
    • Barta, M.L.1    Dickenson, N.E.2    Patil, M.3
  • 12
    • 33646032683 scopus 로고    scopus 로고
    • Bacterially speaking
    • Bassler B.L., Losick R. Bacterially speaking. Cell 2006, 125(2):237-246.
    • (2006) Cell , vol.125 , Issue.2 , pp. 237-246
    • Bassler, B.L.1    Losick, R.2
  • 13
    • 80053591783 scopus 로고    scopus 로고
    • Quantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type 3 complex in enteropathogenic Escherichia coli
    • Biemans-Oldehinkel E., Sal-Man N., Deng W., Foster L.J., Finlay B.B. Quantitative proteomic analysis reveals formation of an EscL-EscQ-EscN type 3 complex in enteropathogenic Escherichia coli. J. Bacteriol. 2011, 193(19):5514-5519.
    • (2011) J. Bacteriol. , vol.193 , Issue.19 , pp. 5514-5519
    • Biemans-Oldehinkel, E.1    Sal-Man, N.2    Deng, W.3    Foster, L.J.4    Finlay, B.B.5
  • 14
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type 3 secretion ATPase YscN and its regulator, YscL
    • Blaylock B., Riordan K.E., Missiakas D.M., Schneewind O. Characterization of the Yersinia enterocolitica type 3 secretion ATPase YscN and its regulator, YscL. J. Bacteriol. 2006, 188(10):3525-3534.
    • (2006) J. Bacteriol. , vol.188 , Issue.10 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.E.2    Missiakas, D.M.3    Schneewind, O.4
  • 15
    • 0035133489 scopus 로고    scopus 로고
    • Structure and composition of the Shigella flexneri "needle complex", a part of its type 3 secreton
    • Blocker A., Jouihri N., Larquet E., et al. Structure and composition of the Shigella flexneri "needle complex", a part of its type 3 secreton. Mol. Microbiol. 2001, 39(3):652-663.
    • (2001) Mol. Microbiol. , vol.39 , Issue.3 , pp. 652-663
    • Blocker, A.1    Jouihri, N.2    Larquet, E.3
  • 16
    • 44349171953 scopus 로고    scopus 로고
    • What's the point of the type 3 secretion system needle?
    • Blocker A.J., Deane J.E., Veenendaal A.K., et al. What's the point of the type 3 secretion system needle?. Proc. Natl. Acad. Sci. USA 2008, 105(18):6507-6513.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.18 , pp. 6507-6513
    • Blocker, A.J.1    Deane, J.E.2    Veenendaal, A.K.3
  • 17
    • 56749182220 scopus 로고    scopus 로고
    • Spa32 interaction with the inner-membrane Spa40 component of the type 3 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 C.A., Boekema E.J., Allaoui A. Spa32 interaction with the inner-membrane Spa40 component of the type 3 secretion system of Shigella flexneri is required for the control of the needle length by a molecular tape measure mechanism. Mol. Microbiol. 2008, 70(6):1515-1528.
    • (2008) Mol. Microbiol. , vol.70 , Issue.6 , pp. 1515-1528
    • Botteaux, A.1    Sani, M.2    Kayath, C.A.3    Boekema, E.J.4    Allaoui, A.5
  • 18
    • 34547908488 scopus 로고    scopus 로고
    • Function and molecular architecture of the Yersinia injectisome tip complex
    • Broz P., Mueller C.A., Muller S.A., et al. Function and molecular architecture of the Yersinia injectisome tip complex. Mol. Microbiol. 2007, 65(5):1311-1320.
    • (2007) Mol. Microbiol. , vol.65 , Issue.5 , pp. 1311-1320
    • Broz, P.1    Mueller, C.A.2    Muller, S.A.3
  • 19
    • 0038593721 scopus 로고
    • The effect of Ca++ and Mg++ on lysis, growth, and production of virulence antigens by Pasteurella pestis
    • Brubaker R.R., Surgalla M.J. The effect of Ca++ and Mg++ on lysis, growth, and production of virulence antigens by Pasteurella pestis. J. Infect. Dis. 1964, 114:13-25.
    • (1964) J. Infect. Dis. , vol.114 , pp. 13-25
    • Brubaker, R.R.1    Surgalla, M.J.2
  • 20
    • 3843152683 scopus 로고    scopus 로고
    • Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica
    • Burghout P., Beckers F., de Wit E., et al. Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica. J. Bacteriol. 2004, 186(16):5366-5375.
    • (2004) J. Bacteriol. , vol.186 , Issue.16 , pp. 5366-5375
    • Burghout, P.1    Beckers, F.2    de Wit, E.3
  • 21
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysiological properties of the YscC secretin from the type 3 secretion system of Yersinia enterocolitica
    • Burghout P., van Boxtel R., Van Gelder P., et al. Structure and electrophysiological properties of the YscC secretin from the type 3 secretion system of Yersinia enterocolitica. J. Bacteriol. 2004, 186(14):4645-4654.
    • (2004) J. Bacteriol. , vol.186 , Issue.14 , pp. 4645-4654
    • Burghout, P.1    van Boxtel, R.2    Van Gelder, P.3
  • 22
    • 0035136207 scopus 로고    scopus 로고
    • Transcriptional regulation of type 3 secretion genes in enteropathogenic Escherichia coli: Ler antagonizes H-NS-dependent repression
    • Bustamante V.H., Santana F.J., Calva E., Puente J.L. Transcriptional regulation of type 3 secretion genes in enteropathogenic Escherichia coli: Ler antagonizes H-NS-dependent repression. Mol. Microbiol. 2001, 39(3):664-678.
    • (2001) Mol. Microbiol. , vol.39 , Issue.3 , pp. 664-678
    • Bustamante, V.H.1    Santana, F.J.2    Calva, E.3    Puente, J.L.4
  • 23
    • 37349055354 scopus 로고    scopus 로고
    • Structure of the Yersinia enterocolitica type 3 secretion translocator chaperone SycD
    • Buttner C.R., Sorg I., Cornelis G.R., Heinz D.W., Niemann H.H. Structure of the Yersinia enterocolitica type 3 secretion translocator chaperone SycD. J. Mol. Biol. 2008, 375(4):997-1012.
    • (2008) J. Mol. Biol. , vol.375 , Issue.4 , pp. 997-1012
    • Buttner, C.R.1    Sorg, I.2    Cornelis, G.R.3    Heinz, D.W.4    Niemann, H.H.5
  • 24
    • 84857649533 scopus 로고    scopus 로고
    • The evolution of the Escherichia coli phylogeny
    • Chaudhuri R.R., Henderson I.R. The evolution of the Escherichia coli phylogeny. Infect. Genet. Evol. 2012, 12(2):214-226.
    • (2012) Infect. Genet. Evol. , vol.12 , Issue.2 , pp. 214-226
    • Chaudhuri, R.R.1    Henderson, I.R.2
  • 25
    • 0042838231 scopus 로고    scopus 로고
    • Type 3 secretion of EspB in enterohemorrhagic Escherichia coli O157:H7
    • Chiu H.J., Lin W.S., Syu W.J. Type 3 secretion of EspB in enterohemorrhagic Escherichia coli O157:H7. Arch. Microbiol. 2003, 180(3):218-226.
    • (2003) Arch. Microbiol. , vol.180 , Issue.3 , pp. 218-226
    • Chiu, H.J.1    Lin, W.S.2    Syu, W.J.3
  • 27
    • 0038608020 scopus 로고    scopus 로고
    • Helical structure of the needle of the type 3 secretion system of Shigella flexneri
    • Cordes F.S., Komoriya K., Larquet E., et al. Helical structure of the needle of the type 3 secretion system of Shigella flexneri. J. Biol. Chem. 2003, 278(19):17103-17107.
    • (2003) J. Biol. Chem. , vol.278 , Issue.19 , pp. 17103-17107
    • Cordes, F.S.1    Komoriya, K.2    Larquet, E.3
  • 28
    • 0034729212 scopus 로고    scopus 로고
    • Type 3 secretion: a bacterial device for close combat with cells of their eukaryotic host
    • Cornelis G.R. Type 3 secretion: a bacterial device for close combat with cells of their eukaryotic host. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 2000, 355(1397):681-693.
    • (2000) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.355 , Issue.1397 , pp. 681-693
    • Cornelis, G.R.1
  • 29
    • 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. 1998, 30(1):47-56.
    • (1998) Mol. Microbiol. , vol.30 , Issue.1 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 30
    • 15944376254 scopus 로고    scopus 로고
    • Structural and functional studies of the enteropathogenic Escherichia coli type 3 needle complex protein EscJ
    • Crepin V.F., Prasannan S., Shaw R.K., et al. Structural and functional studies of the enteropathogenic Escherichia coli type 3 needle complex protein EscJ. Mol. Microbiol. 2005, 55(6):1658-1670.
    • (2005) Mol. Microbiol. , vol.55 , Issue.6 , pp. 1658-1670
    • Crepin, V.F.1    Prasannan, S.2    Shaw, R.K.3
  • 31
    • 0035206531 scopus 로고    scopus 로고
    • The filamentous type 3 secretion translocon of enteropathogenic Escherichia coli
    • Daniell S.J., Takahashi N., Wilson R., et al. The filamentous type 3 secretion translocon of enteropathogenic Escherichia coli. Cell Microbiol. 2001, 3(12):865-871.
    • (2001) Cell Microbiol. , vol.3 , Issue.12 , pp. 865-871
    • Daniell, S.J.1    Takahashi, N.2    Wilson, R.3
  • 32
    • 79960728151 scopus 로고    scopus 로고
    • The N-terminal amphipathic region of the Escherichia coli type 3 secretion system protein EspD is required for membrane insertion and function
    • Dasanayake D., Richaud M., Cyr N., et al. The N-terminal amphipathic region of the Escherichia coli type 3 secretion system protein EspD is required for membrane insertion and function. Mol. Microbiol. 2011, 81(3):734-750.
    • (2011) Mol. Microbiol. , vol.81 , Issue.3 , pp. 734-750
    • Dasanayake, D.1    Richaud, M.2    Cyr, N.3
  • 33
    • 33845938871 scopus 로고    scopus 로고
    • Mutations in the Yersinia pseudotuberculosis type 3 secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells
    • Davis A.J., Mecsas J. Mutations in the Yersinia pseudotuberculosis type 3 secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells. J. Bacteriol. 2007, 189(1):83-97.
    • (2007) J. Bacteriol. , vol.189 , Issue.1 , pp. 83-97
    • Davis, A.J.1    Mecsas, J.2
  • 34
    • 45149126804 scopus 로고    scopus 로고
    • Crystal structure of Spa40, the specificity switch for the Shigella flexneri type 3 secretion system
    • Deane J.E., Graham S.C., Mitchell E.P., Flot D., Johnson S., Lea S.M. Crystal structure of Spa40, the specificity switch for the Shigella flexneri type 3 secretion system. Mol. Microbiol. 2008, 69(1):267-276.
    • (2008) Mol. Microbiol. , vol.69 , Issue.1 , pp. 267-276
    • Deane, J.E.1    Graham, S.C.2    Mitchell, E.P.3    Flot, D.4    Johnson, S.5    Lea, S.M.6
  • 35
    • 33747613328 scopus 로고    scopus 로고
    • Molecular model of a type 3 secretion system needle: implications for host-cell sensing
    • Deane J.E., Roversi P., Cordes F.S., et al. Molecular model of a type 3 secretion system needle: implications for host-cell sensing. Proc. Natl. Acad. Sci. USA 2006, 103(33):12529-12533.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.33 , pp. 12529-12533
    • Deane, J.E.1    Roversi, P.2    Cordes, F.S.3
  • 36
    • 40849102234 scopus 로고    scopus 로고
    • Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues
    • Deane J.E., Roversi P., King C., Johnson S., Lea S.M. Structures of the Shigella flexneri type 3 secretion system protein MxiC reveal conformational variability amongst homologues. J. Mol. Biol. 2008, 377(4):985-992.
    • (2008) J. Mol. Biol. , vol.377 , Issue.4 , pp. 985-992
    • Deane, J.E.1    Roversi, P.2    King, C.3    Johnson, S.4    Lea, S.M.5
  • 37
    • 20144387135 scopus 로고    scopus 로고
    • Regulation of type 3 secretion hierarchy of translocators and effectors in attaching and effacing bacterial pathogens
    • Deng W., Li Y., Hardwidge P.R., et al. Regulation of type 3 secretion hierarchy of translocators and effectors in attaching and effacing bacterial pathogens. Infect. Immun. 2005, 73(4):2135-2146.
    • (2005) Infect. Immun. , vol.73 , Issue.4 , pp. 2135-2146
    • Deng, W.1    Li, Y.2    Hardwidge, P.R.3
  • 38
    • 1242328668 scopus 로고    scopus 로고
    • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
    • Derewenda U., Mateja A., Devedjiev Y., et al. The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure 2004, 12(2):301-306.
    • (2004) Structure , vol.12 , Issue.2 , pp. 301-306
    • Derewenda, U.1    Mateja, A.2    Devedjiev, Y.3
  • 39
    • 80053983313 scopus 로고    scopus 로고
    • The assembly of the export apparatus (YscR, S, T, U, V) of the Yersinia type 3 secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer
    • Diepold A., Wiesand U., Cornelis G.R. The assembly of the export apparatus (YscR, S, T, U, V) of the Yersinia type 3 secretion apparatus occurs independently of other structural components and involves the formation of an YscV oligomer. Mol. Microbiol. 2011, 82(2):502-514.
    • (2011) Mol. Microbiol. , vol.82 , Issue.2 , pp. 502-514
    • Diepold, A.1    Wiesand, U.2    Cornelis, G.R.3
  • 40
    • 0026674948 scopus 로고
    • Enteropathogenic Escherichia coli
    • Donnenberg M.S., Kaper J.B. Enteropathogenic Escherichia coli. Infect. Immun. 1992, 60(10):3953-3961.
    • (1992) Infect. Immun. , vol.60 , Issue.10 , pp. 3953-3961
    • Donnenberg, M.S.1    Kaper, J.B.2
  • 41
    • 0031015588 scopus 로고    scopus 로고
    • The locus of enterocyte effacement pathogenicity island of enteropathogenic Escherichia coli encodes secretion functions and remnants of transposons at its extreme right end
    • Donnenberg M.S., Lai L.C., Taylor K.A. The locus of enterocyte effacement pathogenicity island of enteropathogenic Escherichia coli encodes secretion functions and remnants of transposons at its extreme right end. Gene 1997, 184(1):107-114.
    • (1997) Gene , vol.184 , Issue.1 , pp. 107-114
    • Donnenberg, M.S.1    Lai, L.C.2    Taylor, K.A.3
  • 42
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: a universal regulator for a dynamic genome
    • Dorman C.J. H-NS: a universal regulator for a dynamic genome. Nat. Rev. Microbiol. 2004, 2(5):391-400.
    • (2004) Nat. Rev. Microbiol. , vol.2 , Issue.5 , pp. 391-400
    • Dorman, C.J.1
  • 44
    • 33846842428 scopus 로고    scopus 로고
    • Adaptation to the host environment: regulation of the SPI1 type 3 secretion system in Salmonella enterica serovar Typhimurium
    • Ellermeier J.R., Slauch J.M. Adaptation to the host environment: regulation of the SPI1 type 3 secretion system in Salmonella enterica serovar Typhimurium. Curr. Opin. Microbiol. 2007, 10(1):24-29.
    • (2007) Curr. Opin. Microbiol. , vol.10 , Issue.1 , pp. 24-29
    • Ellermeier, J.R.1    Slauch, J.M.2
  • 45
    • 0031895930 scopus 로고    scopus 로고
    • The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69
    • Elliott S.J., Wainwright L.A., McDaniel T.K., et al. The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69. Mol. Microbiol. 1998, 28(1):1-4.
    • (1998) Mol. Microbiol. , vol.28 , Issue.1 , pp. 1-4
    • Elliott, S.J.1    Wainwright, L.A.2    McDaniel, T.K.3
  • 47
    • 84861796152 scopus 로고    scopus 로고
    • Ultrastructural analysis of IpaD at the tip of the nascent MxiH type 3 secretion apparatus of Shigella flexneri
    • 420(1-2)
    • Epler C.R., Dickenson N.E., Bullitt E., Picking W.L. Ultrastructural analysis of IpaD at the tip of the nascent MxiH type 3 secretion apparatus of Shigella flexneri. J. Mol. Biol. 2012, 29(420(1-2)):29-39.
    • (2012) J. Mol. Biol. , vol.29 , pp. 29-39
    • Epler, C.R.1    Dickenson, N.E.2    Bullitt, E.3    Picking, W.L.4
  • 48
    • 77349103262 scopus 로고    scopus 로고
    • The role of the FliK molecular ruler in hook-length control in Salmonella enterica
    • Erhardt M., Hirano T., Su Y., et al. The role of the FliK molecular ruler in hook-length control in Salmonella enterica. Mol. Microbiol. 2010, 75(5):1272-1284.
    • (2010) Mol. Microbiol. , vol.75 , Issue.5 , pp. 1272-1284
    • Erhardt, M.1    Hirano, T.2    Su, Y.3
  • 49
    • 33748980226 scopus 로고    scopus 로고
    • High resolution structure of BipD: an invasion protein associated with the type 3 secretion system of Burkholderia pseudomallei
    • Erskine P.T., Knight M.J., Ruaux A., et al. High resolution structure of BipD: an invasion protein associated with the type 3 secretion system of Burkholderia pseudomallei. J. Mol. Biol. 2006, 363(1):125-136.
    • (2006) J. Mol. Biol. , vol.363 , Issue.1 , pp. 125-136
    • Erskine, P.T.1    Knight, M.J.2    Ruaux, A.3
  • 50
    • 84858633508 scopus 로고    scopus 로고
    • Structure of a type 3 secretion needle at 7-A resolution provides insights into its assembly and signaling mechanisms
    • Fujii T., Cheung M., Blanco A., Kato T., Blocker A.J., Namba K. Structure of a type 3 secretion needle at 7-A resolution provides insights into its assembly and signaling mechanisms. Proc. Natl. Acad. Sci. USA 2012, 109(12):4461-4466.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , Issue.12 , pp. 4461-4466
    • Fujii, T.1    Cheung, M.2    Blanco, A.3    Kato, T.4    Blocker, A.J.5    Namba, K.6
  • 51
    • 77649275030 scopus 로고    scopus 로고
    • The structure of the Salmonella typhimurium type 3 secretion system needle shows divergence from the flagellar system
    • Galkin V.E., Schmied W.H., Schraidt O., Marlovits T.C., Egelman E.H. The structure of the Salmonella typhimurium type 3 secretion system needle shows divergence from the flagellar system. J. Mol. Biol. 2010, 396(5):1392-1397.
    • (2010) J. Mol. Biol. , vol.396 , Issue.5 , pp. 1392-1397
    • Galkin, V.E.1    Schmied, W.H.2    Schraidt, O.3    Marlovits, T.C.4    Egelman, E.H.5
  • 52
    • 0038187635 scopus 로고    scopus 로고
    • Secretin of the enteropathogenic Escherichia coli type 3 secretion system requires components of the type 3 apparatus for assembly and localization
    • Gauthier A., Puente J.L., Finlay B.B. Secretin of the enteropathogenic Escherichia coli type 3 secretion system requires components of the type 3 apparatus for assembly and localization. Infect. Immun. 2003, 71(6):3310-3319.
    • (2003) Infect. Immun. , vol.71 , Issue.6 , pp. 3310-3319
    • Gauthier, A.1    Puente, J.L.2    Finlay, B.B.3
  • 53
    • 0028288278 scopus 로고
    • Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium
    • Ginocchio C.C., Olmsted S.B., Wells C.L., Galan J.E. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell 1994, 76(4):717-724.
    • (1994) Cell , vol.76 , Issue.4 , pp. 717-724
    • Ginocchio, C.C.1    Olmsted, S.B.2    Wells, C.L.3    Galan, J.E.4
  • 54
    • 0028912808 scopus 로고
    • A plasmid-encoded regulatory region activates chromosomal eaeA expression in enteropathogenic Escherichia coli
    • Gomez-Duarte O.G., Kaper J.B. A plasmid-encoded regulatory region activates chromosomal eaeA expression in enteropathogenic Escherichia coli. Infect. Immun. 1995, 63(5):1767-1776.
    • (1995) Infect. Immun. , vol.63 , Issue.5 , pp. 1767-1776
    • Gomez-Duarte, O.G.1    Kaper, J.B.2
  • 55
    • 84934438078 scopus 로고    scopus 로고
    • Roles of YopN, LcrG and LcrV in controlling Yops secretion by Yersinia pestis
    • Hamad M.A., Nilles M.L. Roles of YopN, LcrG and LcrV in controlling Yops secretion by Yersinia pestis. Adv. Exp. Med. Biol. 2007, 603:225-234.
    • (2007) Adv. Exp. Med. Biol. , vol.603 , pp. 225-234
    • Hamad, M.A.1    Nilles, M.L.2
  • 56
    • 0036488790 scopus 로고    scopus 로고
    • Prevalence of the new, SPI1-like, pathogenicity island ETT2 among Escherichia coli
    • Hartleib S., Prager R., Hedenstrom I., Lofdahl S., Tschape H. Prevalence of the new, SPI1-like, pathogenicity island ETT2 among Escherichia coli. Int. J. Med. Microbiol. 2003, 292(7-8):487-493.
    • (2003) Int. J. Med. Microbiol. , vol.292 , Issue.7-8 , pp. 487-493
    • Hartleib, S.1    Prager, R.2    Hedenstrom, I.3    Lofdahl, S.4    Tschape, H.5
  • 57
    • 14444287535 scopus 로고    scopus 로고
    • Genes encoding putative effector proteins of the type 3 secretion system of Salmonella pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages
    • Hensel M., Shea J.E., Waterman S.R., et al. Genes encoding putative effector proteins of the type 3 secretion system of Salmonella pathogenicity island 2 are required for bacterial virulence and proliferation in macrophages. Mol. Microbiol. 1998, 30(1):163-174.
    • (1998) Mol. Microbiol. , vol.30 , Issue.1 , pp. 163-174
    • Hensel, M.1    Shea, J.E.2    Waterman, S.R.3
  • 58
    • 66149119448 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout
    • Hodgkinson J.L., Horsley A., Stabat D., et al. Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. Nat. Struct. Mol. Biol. 2009, 16(5):477-485.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , Issue.5 , pp. 477-485
    • Hodgkinson, J.L.1    Horsley, A.2    Stabat, D.3
  • 59
    • 79952359941 scopus 로고    scopus 로고
    • Common architecture of the flagellar type 3 protein export apparatus and F- and V-type ATPases
    • Ibuki T., Imada K., Minamino T., Kato T., Miyata T., Namba K. Common architecture of the flagellar type 3 protein export apparatus and F- and V-type ATPases. Nat. Struct. Mol. Biol. 2011, 18(3):277-282.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , Issue.3 , pp. 277-282
    • Ibuki, T.1    Imada, K.2    Minamino, T.3    Kato, T.4    Miyata, T.5    Namba, K.6
  • 60
    • 0034775390 scopus 로고    scopus 로고
    • Characterization of translocation pores inserted into plasma membranes by type 3-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 3-secreted Esp proteins of enteropathogenic Escherichia coli. Cell Microbiol. 2001, 3(10):669-679.
    • (2001) Cell Microbiol. , vol.3 , Issue.10 , pp. 669-679
    • Ide, T.1    Laarmann, S.2    Greune, L.3    Schillers, H.4    Oberleithner, H.5    Schmidt, M.A.6
  • 61
    • 28044453495 scopus 로고    scopus 로고
    • A degenerate type 3 secretion system from septicemic Escherichia coli contributes to pathogenesis
    • Ideses D., Gophna U., Paitan Y., Chaudhuri R.R., Pallen M.J., Ron E.Z. A degenerate type 3 secretion system from septicemic Escherichia coli contributes to pathogenesis. J. Bacteriol. 2005, 187(23):8164-8171.
    • (2005) J. Bacteriol. , vol.187 , Issue.23 , pp. 8164-8171
    • Ideses, D.1    Gophna, U.2    Paitan, Y.3    Chaudhuri, R.R.4    Pallen, M.J.5    Ron, E.Z.6
  • 62
    • 33846314672 scopus 로고    scopus 로고
    • Structural similarity between the flagellar type 3 ATPase FliI and F1-ATPase subunits
    • Imada K., Minamino T., Tahara A., Namba K. Structural similarity between the flagellar type 3 ATPase FliI and F1-ATPase subunits. Proc. Natl. Acad. Sci. USA 2007, 104(2):485-490.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.2 , pp. 485-490
    • Imada, K.1    Minamino, T.2    Tahara, A.3    Namba, K.4
  • 63
    • 33748672462 scopus 로고    scopus 로고
    • The GrlR-GrlA regulatory system coordinately controls the expression of flagellar and LEE-encoded type 3 protein secretion systems in enterohemorrhagic Escherichia coli
    • Iyoda S., Koizumi N., Satou H., et al. The GrlR-GrlA regulatory system coordinately controls the expression of flagellar and LEE-encoded type 3 protein secretion systems in enterohemorrhagic Escherichia coli. J. Bacteriol. 2006, 188(16):5682-5692.
    • (2006) J. Bacteriol. , vol.188 , Issue.16 , pp. 5682-5692
    • Iyoda, S.1    Koizumi, N.2    Satou, H.3
  • 64
    • 4344696800 scopus 로고    scopus 로고
    • Positive effects of multiple pch genes on expression of the locus of enterocyte effacement genes and adherence of enterohaemorrhagic Escherichia coli O157:H7 to HEp-2 cells
    • Iyoda S., Watanabe H. Positive effects of multiple pch genes on expression of the locus of enterocyte effacement genes and adherence of enterohaemorrhagic Escherichia coli O157:H7 to HEp-2 cells. Microbiology 2004, 150(Pt 7):2357-2571.
    • (2004) Microbiology , vol.150 , pp. 2357-2571
    • Iyoda, S.1    Watanabe, H.2
  • 65
    • 80053296817 scopus 로고    scopus 로고
    • Structural characterization and membrane localization of ExsB from the type 3 secretion system (T3SS) of Pseudomonas aeruginosa
    • Izore T., Perdu C., Job V., Attree I., Faudry E., Dessen A. Structural characterization and membrane localization of ExsB from the type 3 secretion system (T3SS) of Pseudomonas aeruginosa. J. Mol. Biol. 2011, 413(1):236-246.
    • (2011) J. Mol. Biol. , vol.413 , Issue.1 , pp. 236-246
    • Izore, T.1    Perdu, C.2    Job, V.3    Attree, I.4    Faudry, E.5    Dessen, A.6
  • 66
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type 3 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 3 secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc. Natl. Acad. Sci. USA 1995, 92(17):7996-8000.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.17 , 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
  • 67
    • 77954407664 scopus 로고    scopus 로고
    • Structural basis of chaperone recognition of type 3 secretion system minor translocator proteins
    • Job V., Mattei P.J., Lemaire D., Attree I., Dessen A. Structural basis of chaperone recognition of type 3 secretion system minor translocator proteins. J. Biol. Chem. 2010, 285(30):23224-23232.
    • (2010) J. Biol. Chem. , vol.285 , Issue.30 , pp. 23224-23232
    • Job, V.1    Mattei, P.J.2    Lemaire, D.3    Attree, I.4    Dessen, A.5
  • 68
    • 41949121055 scopus 로고    scopus 로고
    • Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type 3 secretion proteins
    • Johnson D.L., Stone C.B., Mahony J.B. Interactions between CdsD, CdsQ, and CdsL, three putative Chlamydophila pneumoniae type 3 secretion proteins. J. Bacteriol. 2008, 190(8):2972-2980.
    • (2008) J. Bacteriol. , vol.190 , Issue.8 , pp. 2972-2980
    • Johnson, D.L.1    Stone, C.B.2    Mahony, J.B.3
  • 69
    • 49749089367 scopus 로고    scopus 로고
    • Characterization of soluble complexes of the Shigella flexneri type 3 secretion system ATPase
    • Johnson S., Blocker A. Characterization of soluble complexes of the Shigella flexneri type 3 secretion system ATPase. FEMS Microbiol. Lett. 2008, 286(2):274-278.
    • (2008) FEMS Microbiol. Lett. , vol.286 , Issue.2 , pp. 274-278
    • Johnson, S.1    Blocker, A.2
  • 70
    • 33947500141 scopus 로고    scopus 로고
    • Self-chaperoning of the type 3 secretion system needle tip proteins IpaD and BipD
    • Johnson S., Roversi P., Espina M., et al. Self-chaperoning of the type 3 secretion system needle tip proteins IpaD and BipD. J. Biol. Chem. 2007, 282(6):4035-4044.
    • (2007) J. Biol. Chem. , vol.282 , Issue.6 , pp. 4035-4044
    • Johnson, S.1    Roversi, P.2    Espina, M.3
  • 71
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L., Agrain C., Broz P., Cornelis G.R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 2003, 302(5651):1757-1760.
    • (2003) Science , vol.302 , Issue.5651 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 72
    • 0036335636 scopus 로고    scopus 로고
    • MxiE regulates intracellular expression of factors secreted by the Shigella flexneri 2a type 3 secretion system
    • Kane C.D., Schuch R., Day W.A., Maurelli A.T. MxiE regulates intracellular expression of factors secreted by the Shigella flexneri 2a type 3 secretion system. J. Bacteriol. 2002, 184(16):4409-4419.
    • (2002) J. Bacteriol. , vol.184 , Issue.16 , pp. 4409-4419
    • Kane, C.D.1    Schuch, R.2    Day, W.A.3    Maurelli, A.T.4
  • 73
  • 74
    • 30044445766 scopus 로고    scopus 로고
    • The needle component of the type 3 secreton of Shigella regulates the activity of the secretion apparatus
    • Kenjale R., Wilson J., Zenk S.F., et al. The needle component of the type 3 secreton of Shigella regulates the activity of the secretion apparatus. J. Biol. Chem. 2005, 280(52):42929-42937.
    • (2005) J. Biol. Chem. , vol.280 , Issue.52 , pp. 42929-42937
    • Kenjale, R.1    Wilson, J.2    Zenk, S.F.3
  • 75
    • 0030940269 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli protein secretion is induced in response to conditions similar to those in the gastrointestinal tract
    • Kenny B., Abe A., Stein M., Finlay B.B. Enteropathogenic Escherichia coli protein secretion is induced in response to conditions similar to those in the gastrointestinal tract. Infect. Immun. 1997, 65(7):2606-2612.
    • (1997) Infect. Immun. , vol.65 , Issue.7 , pp. 2606-2612
    • Kenny, B.1    Abe, A.2    Stein, M.3    Finlay, B.B.4
  • 76
    • 0029155828 scopus 로고
    • Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells
    • Kenny B., Finlay B.B. Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells. Proc. Natl. Acad. Sci. USA 1995, 92(17):7991-7995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.17 , pp. 7991-7995
    • Kenny, B.1    Finlay, B.B.2
  • 77
    • 0029972684 scopus 로고    scopus 로고
    • EspA, a protein secreted by enteropathogenic Escherichia coli, is required to induce signals in epithelial cells
    • Kenny B., Lai L.C., Finlay B.B., Donnenberg M.S. EspA, a protein secreted by enteropathogenic Escherichia coli, is required to induce signals in epithelial cells. Mol. Microbiol. 1996, 20(2):313-323.
    • (1996) Mol. Microbiol. , vol.20 , Issue.2 , pp. 313-323
    • Kenny, B.1    Lai, L.C.2    Finlay, B.B.3    Donnenberg, M.S.4
  • 78
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type 3 secretion components to needle complex formation
    • Kimbrough T.G., Miller S.I. Contribution of Salmonella typhimurium type 3 secretion components to needle complex formation. Proc. Natl. Acad. Sci. USA 2000, 97(20):11008-11013.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.20 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 79
    • 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., et al. A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 1998, 17(8):2166-2176.
    • (1998) EMBO J. , vol.17 , Issue.8 , pp. 2166-2176
    • Knutton, S.1    Rosenshine, I.2    Pallen, M.J.3
  • 80
    • 84856449393 scopus 로고    scopus 로고
    • Decoding the roles of pilotins and accessory proteins in secretin escort services
    • Koo J., Burrows L.L., Howell P.L. Decoding the roles of pilotins and accessory proteins in secretin escort services. FEMS Microbiol. Lett. 2012, 328(1):1-12.
    • (2012) FEMS Microbiol. Lett. , vol.328 , Issue.1 , pp. 1-12
    • Koo, J.1    Burrows, L.L.2    Howell, P.L.3
  • 81
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: dynamic channels for protein transport across membranes
    • Korotkov K.V., Gonen T., Hol W.G. Secretins: dynamic channels for protein transport across membranes. Trends. Biochem. Sci 2011, 36(8):433-443.
    • (2011) Trends. Biochem. Sci , vol.36 , Issue.8 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.3
  • 82
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov K.V., Pardon E., Steyaert J., Hol W.G. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 2009, 17(2):255-265.
    • (2009) Structure , vol.17 , Issue.2 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 83
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type 3 protein secretion system
    • Kubori T., Matsushima Y., Nakamura D., et al. Supramolecular structure of the Salmonella typhimurium type 3 protein secretion system. Science 1998, 280(5363):602-605.
    • (1998) Science , vol.280 , Issue.5363 , pp. 602-605
    • Kubori, T.1    Matsushima, Y.2    Nakamura, D.3
  • 84
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type 3 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 3 protein secretion system. Proc. Natl. Acad. Sci. USA 2000, 97(18):10225-10230.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.18 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 85
    • 0031009562 scopus 로고    scopus 로고
    • A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells
    • Lai L.C., Wainwright L.A., Stone K.D., Donnenberg M.S. A third secreted protein that is encoded by the enteropathogenic Escherichia coli pathogenicity island is required for transduction of signals and for attaching and effacing activities in host cells. Infect. Immun. 1997, 65(6):2211-2217.
    • (1997) Infect. Immun. , vol.65 , Issue.6 , pp. 2211-2217
    • Lai, L.C.1    Wainwright, L.A.2    Stone, K.D.3    Donnenberg, M.S.4
  • 86
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type 3 systems
    • Lara-Tejero M., Kato J., Wagner S., Liu X., Galan J.E. A sorting platform determines the order of protein secretion in bacterial type 3 systems. Science 2011, 331(6021):1188-1191.
    • (2011) Science , vol.331 , Issue.6021 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galan, J.E.5
  • 87
    • 17144387844 scopus 로고    scopus 로고
    • Structure and biochemical analysis of a secretin pilot protein
    • Lario P.I., Pfuetzner R.A., Frey E.A., et al. Structure and biochemical analysis of a secretin pilot protein. EMBO J. 2005, 24(6):1111-1121.
    • (2005) EMBO J. , vol.24 , Issue.6 , pp. 1111-1121
    • Lario, P.I.1    Pfuetzner, R.A.2    Frey, E.A.3
  • 88
    • 0036334915 scopus 로고    scopus 로고
    • Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type 3 secretion
    • Lavander M., Sundberg L., Edqvist P.J., Lloyd S.A., Wolf-Watz H., Forsberg A. Proteolytic cleavage of the FlhB homologue YscU of Yersinia pseudotuberculosis is essential for bacterial survival but not for type 3 secretion. J. Bacteriol. 2002, 184(16):4500-4509.
    • (2002) J. Bacteriol. , vol.184 , Issue.16 , pp. 4500-4509
    • Lavander, M.1    Sundberg, L.2    Edqvist, P.J.3    Lloyd, S.A.4    Wolf-Watz, H.5    Forsberg, A.6
  • 89
    • 33746275230 scopus 로고    scopus 로고
    • The discovery of SycO highlights a new function for type 3 secretion effector chaperones
    • Letzelter M., Sorg I., Mota L.J., et al. The discovery of SycO highlights a new function for type 3 secretion effector chaperones. EMBO J. 2006, 25(13):3223-3233.
    • (2006) EMBO J. , vol.25 , Issue.13 , pp. 3223-3233
    • Letzelter, M.1    Sorg, I.2    Mota, L.J.3
  • 91
    • 77953161216 scopus 로고    scopus 로고
    • A conserved domain in type 3 secretion links the cytoplasmic domain of InvA to elements of the basal body
    • Lilic M., Quezada C.M., Stebbins C.E. A conserved domain in type 3 secretion links the cytoplasmic domain of InvA to elements of the basal body. Acta. Crystallogr. D. Biol. Crystallogr. 2010, 66(Pt 6):709-713.
    • (2010) Acta. Crystallogr. D. Biol. Crystallogr. , vol.66 , Issue.PT 6 , pp. 709-713
    • Lilic, M.1    Quezada, C.M.2    Stebbins, C.E.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 C.E. A common structural motif in the binding of virulence factors to bacterial secretion chaperones. Mol. Cell. 2006, 21(5):653-664.
    • (2006) Mol. Cell. , vol.21 , Issue.5 , pp. 653-664
    • Lilic, M.1    Vujanac, M.2    Stebbins, C.E.3
  • 93
    • 0036197569 scopus 로고    scopus 로고
    • Molecular characterization of type 3 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 3 secretion signals via analysis of synthetic N-terminal amino acid sequences. Mol. Microbiol. 2002, 43(1):51-59.
    • (2002) Mol. Microbiol. , vol.43 , Issue.1 , pp. 51-59
    • Lloyd, S.A.1    Sjostrom, M.2    Andersson, S.3    Wolf-Watz, H.4
  • 94
    • 84862270506 scopus 로고    scopus 로고
    • Atomic model of the type 3 secretion system needle
    • Loquet A., Sgourakis N.G., Gupta R., et al. Atomic model of the type 3 secretion system needle. Nature 2012, 486(7402):276-279.
    • (2012) Nature , vol.486 , Issue.7402 , pp. 276-279
    • Loquet, A.1    Sgourakis, N.G.2    Gupta, R.3
  • 95
    • 59949084690 scopus 로고    scopus 로고
    • Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type 3 secretion
    • Lountos G.T., Austin B.P., Nallamsetty S., Waugh D.S. Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type 3 secretion. Protein. Sci. 2009, 18(2):467-474.
    • (2009) Protein. Sci. , vol.18 , Issue.2 , pp. 467-474
    • Lountos, G.T.1    Austin, B.P.2    Nallamsetty, S.3    Waugh, D.S.4
  • 96
    • 84857828509 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type 3 secretion system
    • Lountos G.T., Tropea J.E., Waugh D.S. Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type 3 secretion system. Acta. Crystallogr. D. Biol. Crystallogr. 2012, 68(Pt 3):201-209.
    • (2012) Acta. Crystallogr. D. Biol. Crystallogr. , vol.68 , Issue.PT 3 , pp. 201-209
    • Lountos, G.T.1    Tropea, J.E.2    Waugh, D.S.3
  • 97
    • 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. 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. 2011, 7(8):e1002163.
    • (2011) PLoS Pathog. , vol.7 , Issue.8
    • Lunelli, M.1    Hurwitz, R.2    Lambers, J.3    Kolbe, M.4
  • 98
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type 3 secretion translocator
    • Lunelli M., Lokareddy R.K., Zychlinsky A., Kolbe M. IpaB-IpgC interaction defines binding motif for type 3 secretion translocator. Proc. Natl. Acad. Sci. USA 2009, 106(24):9661-9666.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.24 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinsky, A.3    Kolbe, M.4
  • 99
    • 79958022702 scopus 로고    scopus 로고
    • Interactions and predicted host membrane topology of the enteropathogenic Escherichia coli translocator protein EspB
    • Luo W., Donnenberg M.S. Interactions and predicted host membrane topology of the enteropathogenic Escherichia coli translocator protein EspB. J. Bacteriol. 2011, 193(12):2972-2980.
    • (2011) J. Bacteriol. , vol.193 , Issue.12 , pp. 2972-2980
    • Luo, W.1    Donnenberg, M.S.2
  • 100
    • 0035180725 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the type 3 secretion chaperones CesT and SigE
    • Luo Y., Bertero M.G., Frey E.A., et al. Structural and biochemical characterization of the type 3 secretion chaperones CesT and SigE. Nat. Struct. Biol. 2001, 8(12):1031-1036.
    • (2001) Nat. Struct. Biol. , vol.8 , Issue.12 , pp. 1031-1036
    • Luo, Y.1    Bertero, M.G.2    Frey, E.A.3
  • 101
    • 0036282334 scopus 로고    scopus 로고
    • Spa32 regulates a switch in substrate specificity of the type 3 secreton of Shigella flexneri from needle components to Ipa proteins
    • Magdalena J., Hachani A., Chamekh M., et al. Spa32 regulates a switch in substrate specificity of the type 3 secreton of Shigella flexneri from needle components to Ipa proteins. J. Bacteriol. 2002, 184(13):3433-3441.
    • (2002) J. Bacteriol. , vol.184 , Issue.13 , pp. 3433-3441
    • Magdalena, J.1    Hachani, A.2    Chamekh, M.3
  • 102
    • 0038519642 scopus 로고    scopus 로고
    • Distribution of the secondary type 3 secretion system locus found in enterohemorrhagic Escherichia coli O157:H7 isolates among Shiga toxin-producing E. coli strains
    • Makino S., Tobe T., Asakura H., et al. Distribution of the secondary type 3 secretion system locus found in enterohemorrhagic Escherichia coli O157:H7 isolates among Shiga toxin-producing E. coli strains. J. Clin. Microbiol. 2003, 41(6):2341-2347.
    • (2003) J. Clin. Microbiol. , vol.41 , Issue.6 , pp. 2341-2347
    • Makino, S.1    Tobe, T.2    Asakura, H.3
  • 103
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type 3 secretion injectisome
    • Marlovits T.C., Kubori T., Lara-Tejero M., Thomas D., Unger V.M., Galan J.E. Assembly of the inner rod determines needle length in the type 3 secretion injectisome. Nature 2006, 441(7093):637-640.
    • (2006) Nature , vol.441 , Issue.7093 , 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
  • 104
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type 3 secretion needle complex
    • Marlovits T.C., Kubori T., Sukhan A., Thomas D.R., Galan J.E., Unger V.M. Structural insights into the assembly of the type 3 secretion needle complex. Science 2004, 306(5698):1040-1042.
    • (2004) Science , vol.306 , Issue.5698 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galan, J.E.5    Unger, V.M.6
  • 105
    • 77952742099 scopus 로고    scopus 로고
    • Modulation of Shigella virulence in response to available oxygen in vivo
    • Marteyn B., West N.P., Browning D.F., et al. Modulation of Shigella virulence in response to available oxygen in vivo. Nature 2010, 465(7296):355-358.
    • (2010) Nature , vol.465 , Issue.7296 , pp. 355-358
    • Marteyn, B.1    West, N.P.2    Browning, D.F.3
  • 106
    • 78751651347 scopus 로고    scopus 로고
    • Membrane targeting and pore formation by the type 3 secretion system translocon
    • Mattei P.J., Faudry E., Job V., Izore T., Attree I., Dessen A. Membrane targeting and pore formation by the type 3 secretion system translocon. FEBS J. 2011, 278(3):414-426.
    • (2011) FEBS J. , vol.278 , Issue.3 , pp. 414-426
    • Mattei, P.J.1    Faudry, E.2    Job, V.3    Izore, T.4    Attree, I.5    Dessen, A.6
  • 107
    • 0036276061 scopus 로고    scopus 로고
    • Regulation of transcription by the activity of the Shigella flexneri type 3 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 3 secretion apparatus. Mol. Microbiol. 2002, 43(6):1543-1553.
    • (2002) Mol. Microbiol. , vol.43 , Issue.6 , pp. 1543-1553
    • Mavris, M.1    Page, A.L.2    Tournebize, R.3    Demers, B.4    Sansonetti, P.5    Parsot, C.6
  • 108
    • 0028945803 scopus 로고
    • A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens
    • McDaniel T.K., Jarvis K.G., Donnenberg M.S., Kaper J.B. A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proc. Natl. Acad. Sci. USA 1995, 92(5):1664-1668.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.5 , pp. 1664-1668
    • McDaniel, T.K.1    Jarvis, K.G.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 109
    • 80052194653 scopus 로고    scopus 로고
    • Structural and functional studies on the N-terminal domain of the Shigella type 3 secretion protein MxiG
    • McDowell M.A., Johnson S., Deane J.E., et al. Structural and functional studies on the N-terminal domain of the Shigella type 3 secretion protein MxiG. J. Biol. Chem 2011, 286(35):30606-30614.
    • (2011) J. Biol. Chem , vol.286 , Issue.35 , pp. 30606-30614
    • McDowell, M.A.1    Johnson, S.2    Deane, J.E.3
  • 111
    • 0032998631 scopus 로고    scopus 로고
    • The Per regulon of enteropathogenic Escherichia coli: identification of a regulatory cascade and a novel transcriptional activator, the locus of enterocyte effacement (LEE)-encoded regulator (Ler)
    • Mellies J.L., Elliott S.J., Sperandio V., Donnenberg M.S., Kaper J.B. The Per regulon of enteropathogenic Escherichia coli: identification of a regulatory cascade and a novel transcriptional activator, the locus of enterocyte effacement (LEE)-encoded regulator (Ler). Mol. Microbiol. 1999, 33(2):296-306.
    • (1999) Mol. Microbiol. , vol.33 , Issue.2 , pp. 296-306
    • Mellies, J.L.1    Elliott, S.J.2    Sperandio, V.3    Donnenberg, M.S.4    Kaper, J.B.5
  • 112
    • 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. The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD. EMBO J. 1994, 13(22):5293-5302.
    • (1994) EMBO J. , vol.13 , Issue.22 , pp. 5293-5302
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3
  • 113
    • 0026335456 scopus 로고
    • Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica
    • Michiels T., Vanooteghem J.C., Lambert de Rouvroit C., et al. Analysis of virC, an operon involved in the secretion of Yop proteins by Yersinia enterocolitica. J. Bacteriol. 1991, 173(16):4994-5009.
    • (1991) J. Bacteriol. , vol.173 , Issue.16 , pp. 4994-5009
    • Michiels, T.1    Vanooteghem, J.C.2    Lambert de Rouvroit, C.3
  • 114
    • 58149347646 scopus 로고    scopus 로고
    • Mechanisms of type 3 protein export for bacterial flagellar assembly
    • Minamino T., Imada K., Namba K. Mechanisms of type 3 protein export for bacterial flagellar assembly. Mol. Biosyst. 2008, 4(11):1105-1115.
    • (2008) Mol. Biosyst. , vol.4 , Issue.11 , pp. 1105-1115
    • Minamino, T.1    Imada, K.2    Namba, K.3
  • 115
  • 116
    • 84155162801 scopus 로고    scopus 로고
    • Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export
    • Minamino T., Kinoshita M., Imada K., Namba K. Interaction between FliI ATPase and a flagellar chaperone FliT during bacterial flagellar protein export. Mol. Microbiol. 2012, 83(1):168-178.
    • (2012) Mol. Microbiol. , vol.83 , Issue.1 , pp. 168-178
    • Minamino, T.1    Kinoshita, M.2    Imada, K.3    Namba, K.4
  • 117
    • 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. 2000, 182(17):4906-4914.
    • (2000) J. Bacteriol. , vol.182 , Issue.17 , pp. 4906-4914
    • Minamino, T.1    Macnab, R.M.2
  • 118
    • 0033779545 scopus 로고    scopus 로고
    • FliH, a soluble component of the type 3 flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity
    • Minamino T., Macnab R.M. FliH, a soluble component of the type 3 flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity. Mol. Microbiol. 2000, 37(6):1494-1503.
    • (2000) Mol. Microbiol. , vol.37 , Issue.6 , pp. 1494-1503
    • Minamino, T.1    Macnab, R.M.2
  • 119
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • Minamino T., Namba K. Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export. Nature 2008, 451(7177):485-488.
    • (2008) Nature , vol.451 , Issue.7177 , pp. 485-488
    • Minamino, T.1    Namba, K.2
  • 120
    • 79957680663 scopus 로고    scopus 로고
    • The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type 3 secretion apparatus
    • Mizuno S., Amida H., Kobayashi N., Aizawa S., Tate S. The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type 3 secretion apparatus. J. Mol. Biol. 2011, 409(4):558-573.
    • (2011) J. Mol. Biol. , vol.409 , Issue.4 , pp. 558-573
    • Mizuno, S.1    Amida, H.2    Kobayashi, N.3    Aizawa, S.4    Tate, S.5
  • 122
    • 77954239967 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori
    • Moore S.A., Jia Y. Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori. J. Biol. Chem. 2010, 285(27):21060-21069.
    • (2010) J. Biol. Chem. , vol.285 , Issue.27 , pp. 21060-21069
    • Moore, S.A.1    Jia, Y.2
  • 123
    • 20044380517 scopus 로고    scopus 로고
    • Bacterial injectisomes: needle length does matter
    • Mota L.J., Journet L., Sorg I., Agrain C., Cornelis G.R. Bacterial injectisomes: needle length does matter. Science 2005, 307(5713):1278.
    • (2005) Science , vol.307 , Issue.5713 , pp. 1278
    • Mota, L.J.1    Journet, L.2    Sorg, I.3    Agrain, C.4    Cornelis, G.R.5
  • 124
    • 67651227317 scopus 로고    scopus 로고
    • Comparative analysis of the locus of enterocyte effacement and its flanking regions
    • Muller D., Benz I., Liebchen A., Gallitz I., Karch H., Schmidt M.A. Comparative analysis of the locus of enterocyte effacement and its flanking regions. Infect. Immun. 2009, 77(8):3501-3513.
    • (2009) Infect. Immun. , vol.77 , Issue.8 , pp. 3501-3513
    • Muller, D.1    Benz, I.2    Liebchen, A.3    Gallitz, I.4    Karch, H.5    Schmidt, M.A.6
  • 125
    • 3042661989 scopus 로고    scopus 로고
    • SepL, a protein required for enteropathogenic Escherichia coli type 3 translocation, interacts with secretion component SepD
    • O'Connell C.B., Creasey E.A., Knutton S., et al. SepL, a protein required for enteropathogenic Escherichia coli type 3 translocation, interacts with secretion component SepD. Mol. Microbiol. 2004, 52(6):1613-1625.
    • (2004) Mol. Microbiol. , vol.52 , Issue.6 , pp. 1613-1625
    • O'Connell, C.B.1    Creasey, E.A.2    Knutton, S.3
  • 126
    • 0033678558 scopus 로고    scopus 로고
    • Comparative analysis of the whole set of rRNA operons between an enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an Escherichia coli K-12 strain MG1655
    • Ohnishi M., Murata T., Nakayama K., et al. Comparative analysis of the whole set of rRNA operons between an enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an Escherichia coli K-12 strain MG1655. Syst. Appl. Microbiol. 2000, 23(3):315-324.
    • (2000) Syst. Appl. Microbiol. , vol.23 , Issue.3 , pp. 315-324
    • Ohnishi, M.1    Murata, T.2    Nakayama, K.3
  • 127
    • 53049084326 scopus 로고    scopus 로고
    • Structural characterization of the type-3 pilot-secretin complex from Shigella flexneri
    • Okon M., Moraes T.F., Lario P.I., et al. Structural characterization of the type-3 pilot-secretin complex from Shigella flexneri. Structure 2008, 16(10):1544-1554.
    • (2008) Structure , vol.16 , Issue.10 , pp. 1544-1554
    • Okon, M.1    Moraes, T.F.2    Lario, P.I.3
  • 128
    • 33947712323 scopus 로고    scopus 로고
    • Bile salts stimulate recruitment of IpaB to the Shigella flexneri surface, where it colocalizes with IpaD at the tip of the type 3 secretion needle
    • Olive A.J., Kenjale R., Espina M., Moore D.S., Picking W.L., Picking W.D. Bile salts stimulate recruitment of IpaB to the Shigella flexneri surface, where it colocalizes with IpaD at the tip of the type 3 secretion needle. Infect. Immun. 2007, 75(5):2626-2629.
    • (2007) Infect. Immun. , vol.75 , Issue.5 , pp. 2626-2629
    • Olive, A.J.1    Kenjale, R.2    Espina, M.3    Moore, D.S.4    Picking, W.L.5    Picking, W.D.6
  • 129
    • 33645519210 scopus 로고    scopus 로고
    • Evolutionary links between FliH/YscL-like proteins from bacterial type 3 secretion systems and second-stalk components of the FoF1 and vacuolar ATPases
    • Pallen M.J., Bailey C.M., Beatson S.A. Evolutionary links between FliH/YscL-like proteins from bacterial type 3 secretion systems and second-stalk components of the FoF1 and vacuolar ATPases. Protein. Sci. 2006, 15(4):935-941.
    • (2006) Protein. Sci. , vol.15 , Issue.4 , pp. 935-941
    • Pallen, M.J.1    Bailey, C.M.2    Beatson, S.A.3
  • 130
    • 38549088345 scopus 로고    scopus 로고
    • Energy source of flagellar type 3 secretion
    • Paul K., Erhardt M., Hirano T., Blair D.F., Hughes K.T. Energy source of flagellar type 3 secretion. Nature 2008, 451(7177):489-492.
    • (2008) Nature , vol.451 , Issue.7177 , pp. 489-492
    • Paul, K.1    Erhardt, M.2    Hirano, T.3    Blair, D.F.4    Hughes, K.T.5
  • 131
    • 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 W.L., Nishioka H., Hearn P.D., et al. 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. 2005, 73(3):1432-1440.
    • (2005) Infect. Immun. , vol.73 , Issue.3 , pp. 1432-1440
    • Picking, W.L.1    Nishioka, H.2    Hearn, P.D.3
  • 132
    • 0030717548 scopus 로고    scopus 로고
    • Differential regulation of the plasmid-encoded genes in the Shigella flexneri virulence regulon
    • Porter M.E., Dorman C.J. Differential regulation of the plasmid-encoded genes in the Shigella flexneri virulence regulon. Mol. Gen. Genet. 1997, 256(2):93-103.
    • (1997) Mol. Gen. Genet. , vol.256 , Issue.2 , pp. 93-103
    • Porter, M.E.1    Dorman, C.J.2
  • 133
    • 11844298461 scopus 로고    scopus 로고
    • The LEE1 promoters from both enteropathogenic and enterohemorrhagic Escherichia coli can be activated by PerC-like proteins from either organism
    • Porter M.E., Mitchell P., Free A., Smith D.G., Gally D.L. The LEE1 promoters from both enteropathogenic and enterohemorrhagic Escherichia coli can be activated by PerC-like proteins from either organism. J. Bacteriol. 2005, 187(2):458-472.
    • (2005) J. Bacteriol. , vol.187 , Issue.2 , pp. 458-472
    • Porter, M.E.1    Mitchell, P.2    Free, A.3    Smith, D.G.4    Gally, D.L.5
  • 134
    • 77954382595 scopus 로고    scopus 로고
    • Protein refolding is required for assembly of the type three secretion needle
    • Poyraz O., Schmidt H., Seidel K., et al. Protein refolding is required for assembly of the type three secretion needle. Nat. Struct. Mol. Biol. 2010, 17(7):788-792.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.7 , pp. 788-792
    • Poyraz, O.1    Schmidt, H.2    Seidel, K.3
  • 135
    • 34249942920 scopus 로고    scopus 로고
    • Structure of the heterotrimeric complex that regulates type 3 secretion needle formation
    • Quinaud M., Ple S., Job V., et al. Structure of the heterotrimeric complex that regulates type 3 secretion needle formation. Proc. Natl. Acad. Sci. USA 2007, 104(19):7803-7808.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.19 , pp. 7803-7808
    • Quinaud, M.1    Ple, S.2    Job, V.3
  • 136
  • 137
    • 2442646490 scopus 로고    scopus 로고
    • The ETT2 gene cluster, encoding a second type 3 secretion system from Escherichia coli, is present in the majority of strains but has undergone widespread mutational attrition
    • Ren C.P., Chaudhuri R.R., Fivian A., et al. The ETT2 gene cluster, encoding a second type 3 secretion system from Escherichia coli, is present in the majority of strains but has undergone widespread mutational attrition. J. Bacteriol. 2004, 186(11):3547-3560.
    • (2004) J. Bacteriol. , vol.186 , Issue.11 , pp. 3547-3560
    • Ren, C.P.1    Chaudhuri, R.R.2    Fivian, A.3
  • 138
    • 51049124329 scopus 로고    scopus 로고
    • The type 3 secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE
    • Rodgers L., Gamez A., Riek R., Ghosh P. The type 3 secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. J. Biol. Chem. 2008, 283(30):20857-20863.
    • (2008) J. Biol. Chem. , vol.283 , Issue.30 , pp. 20857-20863
    • Rodgers, L.1    Gamez, A.2    Riek, R.3    Ghosh, P.4
  • 139
    • 77950231693 scopus 로고    scopus 로고
    • The extreme C terminus of Shigella flexneri IpaB is required for regulation of type 3 secretion, needle tip composition, and binding
    • Roehrich A.D., Martinez-Argudo I., Johnson S., Blocker A.J., Veenendaal A.K. The extreme C terminus of Shigella flexneri IpaB is required for regulation of type 3 secretion, needle tip composition, and binding. Infect. Immun. 2010, 78(4):1682-1691.
    • (2010) Infect. Immun. , vol.78 , Issue.4 , pp. 1682-1691
    • Roehrich, A.D.1    Martinez-Argudo, I.2    Johnson, S.3    Blocker, A.J.4    Veenendaal, A.K.5
  • 140
    • 0026733626 scopus 로고
    • Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake
    • Rosenshine I., Donnenberg M.S., Kaper J.B., Finlay B.B. Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake. EMBO J. 1992, 11(10):3551-3560.
    • (1992) EMBO J. , vol.11 , Issue.10 , pp. 3551-3560
    • Rosenshine, I.1    Donnenberg, M.S.2    Kaper, J.B.3    Finlay, B.B.4
  • 141
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist R., Magnusson K.E., Wolf-Watz H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 1994, 13(4):964-972.
    • (1994) EMBO J. , vol.13 , Issue.4 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 142
    • 79955529365 scopus 로고    scopus 로고
    • A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC
    • Ross J.A., Plano G.V. A C-terminal region of Yersinia pestis YscD binds the outer membrane secretin YscC. J. Bacteriol. 2011, 193(9):2276-2289.
    • (2011) J. Bacteriol. , vol.193 , Issue.9 , pp. 2276-2289
    • Ross, J.A.1    Plano, G.V.2
  • 143
    • 77950244006 scopus 로고    scopus 로고
    • Structure of the cytoplasmic domain of FlhA and implication for flagellar type 3 protein export
    • Saijo-Hamano Y., Imada K., Minamino T., et al. Structure of the cytoplasmic domain of FlhA and implication for flagellar type 3 protein export. Mol. Microbiol. 2010, 76(1):260-268.
    • (2010) Mol. Microbiol. , vol.76 , Issue.1 , pp. 260-268
    • Saijo-Hamano, Y.1    Imada, K.2    Minamino, T.3
  • 144
    • 84856247471 scopus 로고    scopus 로고
    • EscI: a crucial component of the type 3 secretion system forms the inner rod structure in enteropathogenic Escherichia coli
    • Sal-Man N., Deng W., Finlay B.B. EscI: a crucial component of the type 3 secretion system forms the inner rod structure in enteropathogenic Escherichia coli. Biochem. J. 2012, 442(1):119-125.
    • (2012) Biochem. J. , vol.442 , Issue.1 , pp. 119-125
    • Sal-Man, N.1    Deng, W.2    Finlay, B.B.3
  • 145
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in Gram-negative bacteria
    • Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in Gram-negative bacteria. Trends. Biochem. Sci. 1993, 18(1):7-12.
    • (1993) Trends. Biochem. Sci. , vol.18 , Issue.1 , pp. 7-12
    • Salmond, G.P.1    Reeves, P.J.2
  • 146
    • 0035159912 scopus 로고    scopus 로고
    • The elements of the locus of enterocyte effacement in human and wild mammal isolates of Escherichia coli: evolution by assemblage or disruption?
    • Sandner L., Eguiarte L.E., Navarro A., Cravioto A., Souza V. The elements of the locus of enterocyte effacement in human and wild mammal isolates of Escherichia coli: evolution by assemblage or disruption?. Microbiology 2001, 147(Pt 11):3149-3158.
    • (2001) Microbiology , vol.147 , Issue.PT 11 , pp. 3149-3158
    • Sandner, L.1    Eguiarte, L.E.2    Navarro, A.3    Cravioto, A.4    Souza, V.5
  • 147
    • 79551681054 scopus 로고    scopus 로고
    • Interactions of the transmembrane polymeric rings of the Salmonella enterica serovar Typhimurium type 3 secretion system
    • pii: e00158-10
    • Sanowar S., Singh P., Pfuetzner R.A., et al. Interactions of the transmembrane polymeric rings of the Salmonella enterica serovar Typhimurium type 3 secretion system. M. Bio. 2009, 1(3). pii: e00158-10.
    • (2009) M. Bio. , vol.1 , Issue.3
    • Sanowar, S.1    Singh, P.2    Pfuetzner, R.A.3
  • 148
    • 0026035531 scopus 로고
    • Genetic and molecular basis of epithelial cell invasion by Shigella species
    • Sansonetti P.J. Genetic and molecular basis of epithelial cell invasion by Shigella species. Rev. Infect. Dis. 1991, 13(Suppl. 4):S285-S292.
    • (1991) Rev. Infect. Dis. , vol.13 , pp. S285-S292
    • Sansonetti, P.J.1
  • 149
    • 0020659378 scopus 로고
    • Alterations in the pathogenicity of Escherichia coli K-12 after transfer of plasmid and chromosomal genes from Shigella flexneri
    • Sansonetti P.J., Hale T.L., Dammin G.J., Kapfer C., Collins H.H., Formal S.B. Alterations in the pathogenicity of Escherichia coli K-12 after transfer of plasmid and chromosomal genes from Shigella flexneri. Infect. Immun. 1983, 39(3):1392-1402.
    • (1983) Infect. Immun. , vol.39 , Issue.3 , pp. 1392-1402
    • Sansonetti, P.J.1    Hale, T.L.2    Dammin, G.J.3    Kapfer, C.4    Collins, H.H.5    Formal, S.B.6
  • 150
    • 0020003681 scopus 로고
    • Involvement of a plasmid in the invasive ability of Shigella flexneri
    • Sansonetti P.J., Kopecko D.J., Formal S.B. Involvement of a plasmid in the invasive ability of Shigella flexneri. Infect. Immun. 1982, 35(3):852-860.
    • (1982) Infect. Immun. , vol.35 , Issue.3 , pp. 852-860
    • Sansonetti, P.J.1    Kopecko, D.J.2    Formal, S.B.3
  • 151
    • 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., et al. Virulence-associated genetic regions comprising 31 kilobases of the 230-kilobase plasmid in Shigella flexneri 2a. J. Bacteriol. 1988, 170(6):2480-2484.
    • (1988) J. Bacteriol. , vol.170 , Issue.6 , pp. 2480-2484
    • Sasakawa, C.1    Kamata, K.2    Sakai, T.3
  • 152
    • 0030474296 scopus 로고    scopus 로고
    • Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes
    • Schesser K., Frithz-Lindsten E., Wolf-Watz H. Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes. J. Bacteriol. 1996, 178(24):7227-7233.
    • (1996) J. Bacteriol. , vol.178 , Issue.24 , pp. 7227-7233
    • Schesser, K.1    Frithz-Lindsten, E.2    Wolf-Watz, H.3
  • 153
    • 77954067915 scopus 로고    scopus 로고
    • Topology and organization of the Salmonella typhimurium type 3 secretion needle complex components
    • Schraidt O., Lefebre M.D., Brunner M.J., et al. Topology and organization of the Salmonella typhimurium type 3 secretion needle complex components. PLoS Pathog. 2010, 6(4):e1000824.
    • (2010) PLoS Pathog. , vol.6 , Issue.4
    • Schraidt, O.1    Lefebre, M.D.2    Brunner, M.J.3
  • 154
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt O., Marlovits T.C. Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science 2011, 331(6021):1192-1195.
    • (2011) Science , vol.331 , Issue.6021 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 155
    • 0035213076 scopus 로고    scopus 로고
    • MxiM and MxiJ, base elements of the Mxi-Spa type 3 secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope
    • Schuch R., Maurelli A.T. MxiM and MxiJ, base elements of the Mxi-Spa type 3 secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope. J. Bacteriol. 2001, 183(24):6991-6998.
    • (2001) J. Bacteriol. , vol.183 , Issue.24 , pp. 6991-6998
    • Schuch, R.1    Maurelli, A.T.2
  • 156
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type 3 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 3 secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl. Acad. Sci. USA 2001, 98(20):11638-11643.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.20 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 158
    • 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. USA 1995, 92(26):11998-12002.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , Issue.26 , pp. 11998-12002
    • Sory, M.P.1    Boland, A.2    Lambermont, I.3    Cornelis, G.R.4
  • 159
    • 0033636187 scopus 로고    scopus 로고
    • Activation of enteropathogenic Escherichia coli (EPEC) LEE2 and LEE3 operons by Ler
    • Sperandio V., Mellies J.L., Delahay R.M., et al. Activation of enteropathogenic Escherichia coli (EPEC) LEE2 and LEE3 operons by Ler. Mol. Microbiol. 2000, 38(4):781-793.
    • (2000) Mol. Microbiol. , vol.38 , Issue.4 , pp. 781-793
    • Sperandio, V.1    Mellies, J.L.2    Delahay, R.M.3
  • 160
    • 0033592919 scopus 로고    scopus 로고
    • Quorum sensing controls expression of the type 3 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 3 secretion gene transcription and protein secretion in enterohemorrhagic and enteropathogenic Escherichia coli. Proc. Natl. Acad. Sci. USA 1999, 96(26):15196-15201.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.26 , pp. 15196-15201
    • Sperandio, V.1    Mellies, J.L.2    Nguyen, W.3    Shin, S.4    Kaper, J.B.5
  • 161
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the periplasmic rings in the type 3 secretion system
    • Spreter T., Yip C.K., Sanowar S., et al. A conserved structural motif mediates formation of the periplasmic rings in the type 3 secretion system. Nat. Struct. Mol. Biol. 2009, 16(5):468-476.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , Issue.5 , pp. 468-476
    • Spreter, T.1    Yip, C.K.2    Sanowar, S.3
  • 163
    • 0042338640 scopus 로고    scopus 로고
    • Priming virulence factors for delivery into the host
    • Stebbins C.E., Galan J.E. Priming virulence factors for delivery into the host. Nat. Rev. Mol. Cell Biol. 2003, 4(9):738-743.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.9 , pp. 738-743
    • Stebbins, C.E.1    Galan, J.E.2
  • 164
    • 79960941334 scopus 로고    scopus 로고
    • The cost of virulence: retarded growth of Salmonella Typhimurium cells expressing type 3 secretion system 1
    • Sturm A., Heinemann M., Arnoldini M., et al. The cost of virulence: retarded growth of Salmonella Typhimurium cells expressing type 3 secretion system 1. PLoS Pathog. 2011, 7(7):e1002143.
    • (2011) PLoS Pathog. , vol.7 , Issue.7
    • Sturm, A.1    Heinemann, M.2    Arnoldini, M.3
  • 165
    • 0038190990 scopus 로고    scopus 로고
    • Synthesis and localization of the Salmonella SPI-1 type 3 secretion needle complex proteins PrgI and PrgJ
    • Sukhan A., Kubori T., Galan J.E. Synthesis and localization of the Salmonella SPI-1 type 3 secretion needle complex proteins PrgI and PrgJ. J. Bacteriol. 2003, 185(11):3480-3483.
    • (2003) J. Bacteriol. , vol.185 , Issue.11 , pp. 3480-3483
    • Sukhan, A.1    Kubori, T.2    Galan, J.E.3
  • 166
    • 78649328894 scopus 로고    scopus 로고
    • Unraveling type 3 secretion systems in the highly versatile Burkholderia pseudomallei
    • Sun G.W., Gan Y.H. Unraveling type 3 secretion systems in the highly versatile Burkholderia pseudomallei. Trends. Microbiol. 2010, 18(12):561-568.
    • (2010) Trends. Microbiol. , vol.18 , Issue.12 , pp. 561-568
    • Sun, G.W.1    Gan, Y.H.2
  • 167
    • 40649128950 scopus 로고    scopus 로고
    • Structural characterization of the Yersinia pestis type 3 secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG
    • Sun P., Tropea J.E., Austin B.P., Cherry S., Waugh D.S. Structural characterization of the Yersinia pestis type 3 secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG. J. Mol. Biol. 2008, 377(3):819-830.
    • (2008) J. Mol. Biol. , vol.377 , Issue.3 , pp. 819-830
    • Sun, P.1    Tropea, J.E.2    Austin, B.P.3    Cherry, S.4    Waugh, D.S.5
  • 168
    • 0034128268 scopus 로고    scopus 로고
    • Role of EspB in experimental human enteropathogenic Escherichia coli infection
    • Tacket C.O., Sztein M.B., Losonsky G., et al. Role of EspB in experimental human enteropathogenic Escherichia coli infection. Infect. Immun. 2000, 68(6):3689-3695.
    • (2000) Infect. Immun. , vol.68 , Issue.6 , pp. 3689-3695
    • Tacket, C.O.1    Sztein, M.B.2    Losonsky, G.3
  • 169
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type 3 secretion machinery: the needle part is changeable in length and essential for delivery of effectors
    • Tamano K., Aizawa S., Katayama E., et al. Supramolecular structure of the Shigella type 3 secretion machinery: the needle part is changeable in length and essential for delivery of effectors. EMBO J. 2000, 19(15):3876-3887.
    • (2000) EMBO J. , vol.19 , Issue.15 , pp. 3876-3887
    • Tamano, K.1    Aizawa, S.2    Katayama, E.3
  • 170
    • 0036178888 scopus 로고    scopus 로고
    • Shigella Spa32 is an essential secretory protein for functional type 3 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 3 secretion machinery and uniformity of its needle length. J. Bacteriol. 2002, 184(5):1244-1252.
    • (2002) J. Bacteriol. , vol.184 , Issue.5 , pp. 1244-1252
    • Tamano, K.1    Katayama, E.2    Toyotome, T.3    Sasakawa, C.4
  • 171
    • 77956112515 scopus 로고    scopus 로고
    • Playing the Harp: evolution of our understanding of hrp/hrc genes
    • Tampakaki A.P., Skandalis N., Gazi A.D., et al. Playing the Harp: evolution of our understanding of hrp/hrc genes. Annu. Rev. Phytopathol. 2010, 48:347-370.
    • (2010) Annu. Rev. Phytopathol. , vol.48 , pp. 347-370
    • Tampakaki, A.P.1    Skandalis, N.2    Gazi, A.D.3
  • 172
    • 0027423585 scopus 로고
    • Transcriptional control of the invasion regulatory gene virB of Shigella flexneri: activation by virF and repression by H-NS
    • Tobe T., Yoshikawa M., Mizuno T., Sasakawa C. Transcriptional control of the invasion regulatory gene virB of Shigella flexneri: activation by virF and repression by H-NS. J. Bacteriol. 1993, 175(19):6142-6149.
    • (1993) J. Bacteriol. , vol.175 , Issue.19 , pp. 6142-6149
    • Tobe, T.1    Yoshikawa, M.2    Mizuno, T.3    Sasakawa, C.4
  • 174
    • 2942543052 scopus 로고    scopus 로고
    • Structure of Spa15, a type 3 secretion chaperone from Shigella flexneri with broad specificity
    • van Eerde A., Hamiaux C., Perez J., Parsot C., Dijkstra B.W. Structure of Spa15, a type 3 secretion chaperone from Shigella flexneri with broad specificity. EMBO Rep. 2004, 5(5):477-483.
    • (2004) EMBO Rep. , vol.5 , Issue.5 , pp. 477-483
    • van Eerde, A.1    Hamiaux, C.2    Perez, J.3    Parsot, C.4    Dijkstra, B.W.5
  • 175
    • 33947249049 scopus 로고    scopus 로고
    • The type 3 secretion system needle tip complex mediates host cell sensing and translocon insertion
    • Veenendaal A.K., Hodgkinson J.L., Schwarzer L., Stabat D., Zenk S.F., Blocker A.J. The type 3 secretion system needle tip complex mediates host cell sensing and translocon insertion. Mol. Microbiol. 2007, 63(6):1719-1730.
    • (2007) Mol. Microbiol. , vol.63 , Issue.6 , pp. 1719-1730
    • Veenendaal, A.K.1    Hodgkinson, J.L.2    Schwarzer, L.3    Stabat, D.4    Zenk, S.F.5    Blocker, A.J.6
  • 177
    • 0025822540 scopus 로고
    • Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits
    • Vogler A.P., Homma M., Irikura V.M., Macnab R.M. Salmonella typhimurium mutants defective in flagellar filament regrowth and sequence similarity of FliI to F0F1, vacuolar, and archaebacterial ATPase subunits. J. Bacteriol. 1991, 173(11):3564-3572.
    • (1991) J. Bacteriol. , vol.173 , Issue.11 , pp. 3564-3572
    • Vogler, A.P.1    Homma, M.2    Irikura, V.M.3    Macnab, R.M.4
  • 179
    • 33745860367 scopus 로고    scopus 로고
    • Structural polymorphism in bacterial EspA filaments revealed by cryo-EM and an improved approach to helical reconstruction
    • Wang Y.A., Yu X., Yip C., Strynadka N.C., Egelman E.H. Structural polymorphism in bacterial EspA filaments revealed by cryo-EM and an improved approach to helical reconstruction. Structure 2006, 14(7):1189-1196.
    • (2006) Structure , vol.14 , Issue.7 , pp. 1189-1196
    • Wang, Y.A.1    Yu, X.2    Yip, C.3    Strynadka, N.C.4    Egelman, E.H.5
  • 180
    • 0031278027 scopus 로고    scopus 로고
    • Insertion site of the locus of enterocyte effacement in enteropathogenic and enterohemorrhagic Escherichia coli differs in relation to the clonal phylogeny of the strains
    • Wieler L.H., McDaniel T.K., Whittam T.S., Kaper J.B. Insertion site of the locus of enterocyte effacement in enteropathogenic and enterohemorrhagic Escherichia coli differs in relation to the clonal phylogeny of the strains. FEMS Microbiol. Lett. 1997, 156(1):49-53.
    • (1997) FEMS Microbiol. Lett. , vol.156 , Issue.1 , pp. 49-53
    • Wieler, L.H.1    McDaniel, T.K.2    Whittam, T.S.3    Kaper, J.B.4
  • 181
    • 58149112120 scopus 로고    scopus 로고
    • Structure of the type 3 secretion recognition protein YscU from Yersinia enterocolitica
    • Wiesand U., Sorg I., Amstutz M., et al. Structure of the type 3 secretion recognition protein YscU from Yersinia enterocolitica. J. Mol. Biol. 2009, 385(3):854-866.
    • (2009) J. Mol. Biol. , vol.385 , Issue.3 , pp. 854-866
    • Wiesand, U.1    Sorg, I.2    Amstutz, M.3
  • 182
    • 34548561946 scopus 로고    scopus 로고
    • Induction of the Yersinia type 3 secretion system as an all-or-none phenomenon
    • Wiley D.J., Rosqvist R., Schesser K. Induction of the Yersinia type 3 secretion system as an all-or-none phenomenon. J. Mol. Biol. 2007, 373(1):27-37.
    • (2007) J. Mol. Biol. , vol.373 , Issue.1 , pp. 27-37
    • Wiley, D.J.1    Rosqvist, R.2    Schesser, K.3
  • 183
    • 33846438270 scopus 로고    scopus 로고
    • On the role of specific chaperones, the specific ATPase, and the proton motive force in type 3 secretion
    • Wilharm G., Dittmann S., Schmid A., Heesemann J. On the role of specific chaperones, the specific ATPase, and the proton motive force in type 3 secretion. Int. J. Med. Microbiol. 2007, 297(1):27-36.
    • (2007) Int. J. Med. Microbiol. , vol.297 , Issue.1 , pp. 27-36
    • Wilharm, G.1    Dittmann, S.2    Schmid, A.3    Heesemann, J.4
  • 184
    • 3042692057 scopus 로고    scopus 로고
    • Yersinia enterocolitica type 3 secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB
    • Wilharm G., Lehmann V., Krauss K., et al. Yersinia enterocolitica type 3 secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB. Infect. Immun. 2004, 72(7):4004-4009.
    • (2004) Infect. Immun. , vol.72 , Issue.7 , pp. 4004-4009
    • Wilharm, G.1    Lehmann, V.2    Krauss, K.3
  • 185
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn S., Allaoui A., Wattiau P., Cornelis G.R. YscN, the putative energizer of the Yersinia Yop secretion machinery. J. Bacteriol. 1994, 176(6):1561-1569.
    • (1994) J. Bacteriol. , vol.176 , Issue.6 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 186
    • 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. 1996, 20(6):1261-1271.
    • (1996) Mol. Microbiol. , vol.20 , Issue.6 , pp. 1261-1271
    • Woestyn, S.1    Sory, M.P.2    Boland, A.3    Lequenne, O.4    Cornelis, G.R.5
  • 187
    • 44949221276 scopus 로고    scopus 로고
    • YscP and YscU switch the substrate specificity of the Yersinia type 3 secretion system by regulating export of the inner rod protein YscI
    • Wood S.E., Jin J., Lloyd S.A. YscP and YscU switch the substrate specificity of the Yersinia type 3 secretion system by regulating export of the inner rod protein YscI. J. Bacteriol. 2008, 190(12):4252-4262.
    • (2008) J. Bacteriol. , vol.190 , Issue.12 , pp. 4252-4262
    • Wood, S.E.1    Jin, J.2    Lloyd, S.A.3
  • 188
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of the Salmonella type 3 secretion system export apparatus protein InvA
    • Worrall L.J., Vuckovic M., Strynadka N.C. Crystal structure of the C-terminal domain of the Salmonella type 3 secretion system export apparatus protein InvA. Protein. Sci. 2010, 19(5):1091-1096.
    • (2010) Protein. Sci. , vol.19 , Issue.5 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.3
  • 189
    • 28544440091 scopus 로고    scopus 로고
    • Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery
    • Yang F., Yang J., Zhang X., et al. Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery. Nucleic Acids Res. 2005, 33(19):6445-6458.
    • (2005) Nucleic Acids Res. , vol.33 , Issue.19 , pp. 6445-6458
    • Yang, F.1    Yang, J.2    Zhang, X.3
  • 190
    • 70349656403 scopus 로고    scopus 로고
    • The type 3 secretion system is involved in the invasion and intracellular survival of Escherichia coli K1 in human brain microvascular endothelial cells
    • Yao Y., Xie Y., Perace D., et al. The type 3 secretion system is involved in the invasion and intracellular survival of Escherichia coli K1 in human brain microvascular endothelial cells. FEMS Microbiol. Lett. 2009, 300(1):18-24.
    • (2009) FEMS Microbiol. Lett. , vol.300 , Issue.1 , pp. 18-24
    • Yao, Y.1    Xie, Y.2    Perace, D.3
  • 191
    • 11444263137 scopus 로고    scopus 로고
    • Structural characterization of a type 3 secretion system filament protein in complex with its chaperone
    • Yip C.K., Finlay B.B., Strynadka N.C. Structural characterization of a type 3 secretion system filament protein in complex with its chaperone. Nat. Struct. Mol. Biol. 2005, 12(1):75-81.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , Issue.1 , pp. 75-81
    • Yip, C.K.1    Finlay, B.B.2    Strynadka, N.C.3
  • 192
    • 20444488138 scopus 로고    scopus 로고
    • Structural characterization of the molecular platform for type 3 secretion system assembly
    • Yip C.K., Kimbrough T.G., Felise H.B., et al. Structural characterization of the molecular platform for type 3 secretion system assembly. Nature 2005, 435(7042):702-707.
    • (2005) Nature , vol.435 , Issue.7042 , pp. 702-707
    • Yip, C.K.1    Kimbrough, T.G.2    Felise, H.B.3
  • 193
    • 43049127811 scopus 로고    scopus 로고
    • Structural analysis of the essential self-cleaving type 3 secretion proteins EscU and SpaS
    • Zarivach R., Deng W., Vuckovic M., et al. Structural analysis of the essential self-cleaving type 3 secretion proteins EscU and SpaS. Nature 2008, 453(7191):124-127.
    • (2008) Nature , vol.453 , Issue.7191 , pp. 124-127
    • Zarivach, R.1    Deng, W.2    Vuckovic, M.3
  • 195
    • 9244233850 scopus 로고    scopus 로고
    • Regulators encoded in the Escherichia coli type 3 secretion system 2 gene cluster influence expression of genes within the locus for enterocyte effacement in enterohemorrhagic E. coli O157:H7
    • Zhang L., Chaudhuri R.R., Constantinidou C., et al. Regulators encoded in the Escherichia coli type 3 secretion system 2 gene cluster influence expression of genes within the locus for enterocyte effacement in enterohemorrhagic E. coli O157:H7. Infect. Immun. 2004, 72(12):7282-7293.
    • (2004) Infect. Immun. , vol.72 , Issue.12 , pp. 7282-7293
    • Zhang, L.1    Chaudhuri, R.R.2    Constantinidou, C.3
  • 196
    • 33646180623 scopus 로고    scopus 로고
    • Solution structure of monomeric BsaL, the type 3 secretion needle protein of Burkholderia pseudomallei
    • Zhang L., Wang Y., Picking W.L., Picking W.D., De Guzman R.N. Solution structure of monomeric BsaL, the type 3 secretion needle protein of Burkholderia pseudomallei. J. Mol. Biol. 2006, 359(2):322-330.
    • (2006) J. Mol. Biol. , vol.359 , Issue.2 , pp. 322-330
    • Zhang, L.1    Wang, Y.2    Picking, W.L.3    Picking, W.D.4    De Guzman, R.N.5
  • 197
    • 84864112952 scopus 로고    scopus 로고
    • The Salmonella type 3 secretion system inner rod protein PrgJ is partially folded
    • Zhong D., Lefebre M., Kaur K., et al. The Salmonella type 3 secretion system inner rod protein PrgJ is partially folded. J. Biol. Chem. 2012, 287(30):25303-25311.
    • (2012) J. Biol. Chem. , vol.287 , Issue.30 , pp. 25303-25311
    • Zhong, D.1    Lefebre, M.2    Kaur, K.3
  • 198
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky A., Prevost M.C., Sansonetti P.J. Shigella flexneri induces apoptosis in infected macrophages. Nature 1992, 358(6382):167-169.
    • (1992) Nature , vol.358 , Issue.6382 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3


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