메뉴 건너뛰기




Volumn 19, Issue 5, 2011, Pages 603-612

Biogenesis, regulation, and targeting of the type III secretion system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN 3SS; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 79955838725     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.03.015     Document Type: Review
Times cited : (103)

References (87)
  • 2
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • DOI 10.1038/nature03992, PII N03992
    • Y. Akeda, and J.E. Galán Chaperone release and unfolding of substrates in type III secretion Nature 437 2005 911 915 (Pubitemid 41486769)
    • (2005) Nature , vol.437 , Issue.7060 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 3
    • 77954556570 scopus 로고    scopus 로고
    • Evidence for alternative quaternary structure in a bacterial type III secretion system chaperone
    • M.L. Barta, L. Zhang, W.L. Picking, and B.V. Geisbrecht Evidence for alternative quaternary structure in a bacterial type III secretion system chaperone BMC Struct. Biol. 10 2010 21
    • (2010) BMC Struct. Biol. , vol.10 , pp. 21
    • Barta, M.L.1    Zhang, L.2    Picking, W.L.3    Geisbrecht, B.V.4
  • 4
    • 69249115197 scopus 로고    scopus 로고
    • Membrane protein structure determination using cryo-electron tomography and 3D image averaging
    • A. Bartesaghi, and S. Subramaniam Membrane protein structure determination using cryo-electron tomography and 3D image averaging Curr. Opin. Struct. Biol. 19 2009 402 407
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 402-407
    • Bartesaghi, A.1    Subramaniam, S.2
  • 5
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • DOI 10.1016/S1097-2765(02)00529-4
    • S.C. Birtalan, R.M. Phillips, and P. Ghosh Three-dimensional secretional signals in chaperone-effector complexes of bacterial pathogens Mol. Cell 9 2002 971 980 (Pubitemid 34632625)
    • (2002) Molecular Cell , vol.9 , Issue.5 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 6
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL
    • DOI 10.1128/JB.188.10.3525-3534.2006
    • B. Blaylock, K.E. Riordan, D.M. Missiakas, and O. Schneewind Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator J. Bacteriol. 188 2006 3525 3534 (Pubitemid 43726217)
    • (2006) Journal of Bacteriology , vol.188 , Issue.10 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.E.2    Missiakas, D.M.3    Schneewind, O.4
  • 9
    • 33645068849 scopus 로고    scopus 로고
    • Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion
    • J.E. Bröms, P.J. Edqvist, A. Forsberg, and M.S. Francis Tetratricopeptide repeats are essential for PcrH chaperone function in Pseudomonas aeruginosa type III secretion FEMS Microbiol. Lett. 256 2006 57 66
    • (2006) FEMS Microbiol. Lett. , vol.256 , pp. 57-66
    • Bröms, J.E.1    Edqvist, P.J.2    Forsberg, A.3    Francis, M.S.4
  • 10
    • 3843152683 scopus 로고    scopus 로고
    • Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica
    • DOI 10.1128/JB.186.16.5366-5375.2004
    • P. Burghout, F. Beckers, E. de Wit, R. van Boxtel, G.R. Cornelis, J. Tommassen, and M. Koster Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica J. Bacteriol. 186 2004 5366 5375 (Pubitemid 39038138)
    • (2004) Journal of Bacteriology , vol.186 , Issue.16 , pp. 5366-5375
    • Burghout, P.1    Beckers, F.2    De Wit, E.3    Van Boxtel, R.4    Cornelis, G.R.5    Tommassen, J.6    Koster, M.7
  • 11
    • 37349055354 scopus 로고    scopus 로고
    • Structure of the Yersinia enterocolitica Type III Secretion Translocator Chaperone SycD
    • DOI 10.1016/j.jmb.2007.11.009, PII S0022283607014696
    • C.R. Büttner, I. Sorg, G.R. Cornelis, D.W. Heinz, and H.H. Niemann Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD J. Mol. Biol. 375 2008 997 1012 (Pubitemid 350309395)
    • (2008) Journal of Molecular Biology , 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
  • 13
    • 34548108138 scopus 로고    scopus 로고
    • Targeting virulence: A new paradigm for antimicrobial therapy
    • DOI 10.1038/nchembio.2007.24, PII NCHEMBIO200724
    • A.E. Clatworthy, E. Pierson, and D.T. Hung Targeting virulence: a new paradigm for antimicrobial therapy Nat. Chem. Biol. 3 2007 541 548 (Pubitemid 47294400)
    • (2007) Nature Chemical Biology , vol.3 , Issue.9 , pp. 541-548
    • Clatworthy, A.E.1    Pierson, E.2    Hung, D.T.3
  • 15
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • DOI 10.1038/nrmicro1526, PII NRMICRO1526
    • G.R. Cornelis The type III secretion injectisome Nat. Rev. Microbiol. 4 2006 811 825 (Pubitemid 44593948)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.11 , pp. 811-825
    • Cornelis, G.R.1
  • 16
    • 76149128659 scopus 로고    scopus 로고
    • Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand
    • A.L. Cortajarena, J. Wang, and L. Regan Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand FEBS J. 277 2010 1058 1066
    • (2010) FEBS J. , vol.277 , pp. 1058-1066
    • Cortajarena, A.L.1    Wang, J.2    Regan, L.3
  • 19
    • 45149126804 scopus 로고    scopus 로고
    • Crystal structure of Spa40, the specificity switch for the Shigella flexneri type III secretion system
    • DOI 10.1111/j.1365-2958.2008.06293.x
    • J.E. Deane, S.C. Graham, E.P. Mitchell, D. Flot, S. Johnson, and S.M. Lea Crystal structure of Spa40, the specificity switch for the Shigella flexneri type III secretion system Mol. Microbiol. 69 2008 267 276 (Pubitemid 351832772)
    • (2008) Molecular Microbiology , 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
  • 20
    • 77950607053 scopus 로고    scopus 로고
    • Timing is everything: The regulation of type III secretion
    • J.E. Deane, P. Abrusci, S. Johnson, and S.M. Lea Timing is everything: the regulation of type III secretion Cell. Mol. Life Sci. 67 2010 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
  • 21
    • 77953123027 scopus 로고    scopus 로고
    • Deciphering the assembly of the Yersinia type III secretion injectisome
    • A. Diepold, M. Amstutz, S. Abel, I. Sorg, U. Jenal, and G.R. Cornelis Deciphering the assembly of the Yersinia type III secretion injectisome EMBO J. 29 2010 1928 1940
    • (2010) EMBO J. , vol.29 , pp. 1928-1940
    • Diepold, A.1    Amstutz, M.2    Abel, S.3    Sorg, I.4    Jenal, U.5    Cornelis, G.R.6
  • 23
    • 67649400561 scopus 로고    scopus 로고
    • Common themes in the design and function of bacterial effectors
    • J.E. Galán Common themes in the design and function of bacterial effectors Cell Host Microbe 5 2009 571 579
    • (2009) Cell Host Microbe , vol.5 , pp. 571-579
    • Galán, J.E.1
  • 26
    • 78650763169 scopus 로고    scopus 로고
    • Hijacking of the pleiotropic cytokine interferon-γ by the type III secretion system of Yersinia pestis
    • C. Gendrin, S. Sarrazzin, D. Bonnaffé, J.M. Jault, H. Lortat-Jacob, and A. Dessen Hijacking of the pleiotropic cytokine interferon-γ by the type III secretion system of Yersinia pestis PLoS One 5 2010 e15242
    • (2010) PLoS One , vol.5 , pp. 15242
    • Gendrin, C.1    Sarrazzin, S.2    Bonnaffé, D.3    Jault, J.M.4    Lortat-Jacob, H.5    Dessen, A.6
  • 30
    • 77954407664 scopus 로고    scopus 로고
    • Structural basis of chaperone recognition by type III secretion system minor translocator proteins
    • V. Job, P.J. Matteï, D. Lemaire, I. Attree, and A. Dessen Structural basis of chaperone recognition by type III secretion system minor translocator proteins J. Biol. Chem. 285 2010 23224 23232
    • (2010) J. Biol. Chem. , vol.285 , pp. 23224-23232
    • Job, V.1    Matteï, P.J.2    Lemaire, D.3    Attree, I.4    Dessen, A.5
  • 32
    • 69949149115 scopus 로고    scopus 로고
    • Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90
    • T. Kajander, J.N. Sachs, A. Goldman, and L. Regan Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90 J. Biol. Chem. 284 2009 25364 25374
    • (2009) J. Biol. Chem. , vol.284 , pp. 25364-25374
    • Kajander, T.1    Sachs, J.N.2    Goldman, A.3    Regan, L.4
  • 34
    • 0037350267 scopus 로고    scopus 로고
    • Targeting bacterial virulence: Inhibitors of type III secretion in Yersinia
    • DOI 10.1016/S1074-5521(03)00046-2
    • A.M. Kauppi, R. Nordfelth, H. Uvell, H. Wolf-Watz, and M. Elofsson Targeting bacterial virulence: inhibitors of type III secretion in Yersinia Chem. Biol. 10 2003 241 249 (Pubitemid 36380281)
    • (2003) Chemistry and Biology , vol.10 , Issue.3 , pp. 241-249
    • Kauppi, A.M.1    Nordfelth, R.2    Uvell, H.3    Wolf-Watz, H.4    Elofsson, M.5
  • 35
    • 44949215750 scopus 로고    scopus 로고
    • Virulence blockers as alternatives to antibiotics: Type III secretion inhibitors against Gram-negative bacteria
    • DOI 10.1111/j.1365-2796.2008.01941.x
    • P. Keyser, M. Elofsson, S. Rosell, and H. Wolf-Watz Virulence blockers as alternatives to antibiotics: type III secretion inhibitors against Gram-negative bacteria J. Intern. Med. 264 2008 17 29 (Pubitemid 351813482)
    • (2008) Journal of Internal Medicine , vol.264 , Issue.1 , pp. 17-29
    • Keyser, P.1    Elofsson, M.2    Rosell, S.3    Wolf-Watz, H.4
  • 36
    • 0036165971 scopus 로고    scopus 로고
    • Assembly of the type III secretion needle complex of Salmonella typhimurium
    • DOI 10.1016/S1286-4579(01)01512-X, PII S128645790101512X
    • T.G. Kimbrough, and S.I. Miller Assembly of the type III secretion needle complex of Salmonella typhimurium Microbes Infect. 4 2002 75 82 (Pubitemid 34127994)
    • (2002) Microbes and Infection , vol.4 , Issue.1 , pp. 75-82
    • Kimbrough, T.G.1    Miller, S.I.2
  • 37
    • 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
    • K.V. Korotkov, E. Pardon, J. Steyaert, and W.G.J. Hol Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody Structure 17 2009 255 265
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.J.4
  • 38
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
    • T. Kubori, A. Sukhan, S.-I. Aizawa, and J.E. Galán Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system Proc. Natl. Acad. Sci. USA 97 2000 10225 10230
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.-I.3    Galán, J.E.4
  • 39
    • 79952280754 scopus 로고    scopus 로고
    • A sorting platform determines the order of protein secretion in bacterial type III systems
    • M. Lara-Tejero, J. Kato, S. Wagner, X. Liu, and J.E. Galán A sorting platform determines the order of protein secretion in bacterial type III systems Science 331 2011 1188 1191
    • (2011) Science , vol.331 , pp. 1188-1191
    • Lara-Tejero, M.1    Kato, J.2    Wagner, S.3    Liu, X.4    Galán, J.E.5
  • 41
    • 77953161216 scopus 로고    scopus 로고
    • A conserved domain in type III secretion links the cytoplasmic domain of InvA to elements of the basal body
    • M. Lilic, C.M. Quezada, and C.E. Stebbins 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 2010 709 713
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 709-713
    • Lilic, M.1    Quezada, C.M.2    Stebbins, C.E.3
  • 43
    • 78650063483 scopus 로고    scopus 로고
    • Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB
    • R.K. Lokareddy, M. Lunelli, B. Eilers, V. Wolter, and M. Kolbe Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB J. Biol. Chem. 285 2010 39965 39975
    • (2010) J. Biol. Chem. , vol.285 , pp. 39965-39975
    • Lokareddy, R.K.1    Lunelli, M.2    Eilers, B.3    Wolter, V.4    Kolbe, M.5
  • 44
    • 62649095350 scopus 로고    scopus 로고
    • Functional characterization of the type III secretion ATPase from the plant pathogen Xanthomonas campestris pv. vesicatoria
    • C. Lorenz, and D. Büttner Functional characterization of the type III secretion ATPase from the plant pathogen Xanthomonas campestris pv. vesicatoria J. Bacteriol. 191 2009 1414 1428
    • (2009) J. Bacteriol. , vol.191 , pp. 1414-1428
    • Lorenz, C.1    Büttner, D.2
  • 45
    • 59949084690 scopus 로고    scopus 로고
    • Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion
    • G.T. Lountos, B.P. Austin, S. Nallamsetty, and D.S. Waugh Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion Protein Sci. 18 2009 467 474
    • (2009) Protein Sci. , vol.18 , pp. 467-474
    • Lountos, G.T.1    Austin, B.P.2    Nallamsetty, S.3    Waugh, D.S.4
  • 46
    • 67649861394 scopus 로고    scopus 로고
    • IpaB-IpgC interaction defines binding motif for type III secretion translocator
    • M. Lunelli, R.K. Lokareddy, A. Zychlinksy, and M. Kolbe IpaB-IpgC interaction defines binding motif for type III secretion translocator Proc. Natl. Acad. Sci. USA 106 2009 9661 9666
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9661-9666
    • Lunelli, M.1    Lokareddy, R.K.2    Zychlinksy, A.3    Kolbe, M.4
  • 47
    • 75249090025 scopus 로고    scopus 로고
    • Type III secretion systems shape up as they ship out
    • T.C. Marlovits, and C.E. Stebbins Type III secretion systems shape up as they ship out Curr. Opin. Microbiol. 13 2010 47 52
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 47-52
    • Marlovits, T.C.1    Stebbins, C.E.2
  • 48
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • DOI 10.1126/science.1102610
    • T.C. Marlovits, T. Kubori, A. Sukhan, D.R. Thomas, J.E. Galán, and V.M. Unger Structural insights into the assembly of the type III secretion needle complex Science 306 2004 1040 1042 (Pubitemid 39482908)
    • (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
  • 49
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type III secretion injectisome
    • DOI 10.1038/nature04822, PII N04822
    • T.C. Marlovits, T. Kubori, M. Lara-Tejero, D. Thomas, V.M. Unger, and J.E. Galán Assembly of the inner rod determines needle length in the type III secretion injectisome Nature 441 2006 637 640 (Pubitemid 43927295)
    • (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
  • 50
    • 78751651347 scopus 로고    scopus 로고
    • Membrane targeting and pore formation by the type III secretion system translocon
    • P.J. Matteï, E. Faudry, V. Job, T. Izoré, I. Attree, and A. Dessen Membrane targeting and pore formation by the type III secretion system translocon FEBS J. 278 2011 414 426
    • (2011) FEBS J. , vol.278 , pp. 414-426
    • Matteï, P.J.1    Faudry, E.2    Job, V.3    Izoré, T.4    Attree, I.5    Dessen, A.6
  • 51
    • 38549158887 scopus 로고    scopus 로고
    • Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export
    • T. Minamino, and K. Namba Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export Nature 451 2008 485 489
    • (2008) Nature , vol.451 , pp. 485-489
    • Minamino, T.1    Namba, K.2
  • 52
  • 53
    • 43449122166 scopus 로고    scopus 로고
    • The type III secretion system tip complex and translocon
    • DOI 10.1111/j.1365-2958.2008.06237.x
    • C.A. Mueller, P. Broz, and G.R. Cornelis The type III secretion system tip complex and translocon Mol. Microbiol. 68 2008 1085 1095 (Pubitemid 351670205)
    • (2008) Molecular Microbiology , vol.68 , Issue.5 , pp. 1085-1095
    • Mueller, C.A.1    Broz, P.2    Cornelis, G.R.3
  • 55
    • 78449265558 scopus 로고    scopus 로고
    • Crystal structure of Legionella DotD: Insights into the relationship between type IVb and type II/III secretion systems
    • N. Nakano, T. Kubori, M. Knoshita, K. Imada, and H. Nagai Crystal structure of Legionella DotD: insights into the relationship between type IVb and type II/III secretion systems PLoS Pathog. 6 2010 e1001129
    • (2010) PLoS Pathog. , vol.6 , pp. 1001129
    • Nakano, N.1    Kubori, T.2    Knoshita, M.3    Imada, K.4    Nagai, H.5
  • 56
    • 34547629449 scopus 로고    scopus 로고
    • Salicylidene acylhydrazides that affect type III protein secretion in Salmonella enterica serovar typhimurium
    • DOI 10.1128/AAC.00223-07
    • A. Negrea, E. Bjur, S.E. Ygberg, M. Elofsson, H. Wolf-Watz, and M. Rhen Salicylidene acylhydrazides that affect type III protein secretion in Salmonella enterica serovar typhimurium Antimicrob. Agents Chemother. 51 2007 2867 2876 (Pubitemid 47206224)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.8 , pp. 2867-2876
    • Negrea, A.1    Bjur, E.2    Ygberg, S.E.3    Elofsson, M.4    Wolf-Watz, H.5    Rhen, M.6
  • 57
    • 17644371042 scopus 로고    scopus 로고
    • Small-molecule inhibitors specifically targeting type III secretion
    • DOI 10.1128/IAI.73.5.3104-3114.2005
    • R. Nordfelth, A.M. Kauppi, H.A. Norberg, H. Wolf-Watz, and M. Elofsson Small-molecule Inhibitors specifically targeting type III secretion Infect. Immun. 73 2005 3104 3114 (Pubitemid 40570380)
    • (2005) Infection and Immunity , vol.73 , Issue.5 , pp. 3104-3114
    • Nordfelth, R.1    Kauppi, A.M.2    Norberg, H.A.3    Wolf-Watz, H.4    Elofsson, M.5
  • 59
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • DOI 10.1016/S1369-5274(02)00002-4
    • C. Parsot, C. Hamiaux, and A.-L. Page The various and varying roles of specific chaperones in type III secretion systems Curr. Opin. Microbiol. 6 2003 7 14 (Pubitemid 36258530)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.1 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.-L.3
  • 60
    • 77954394940 scopus 로고    scopus 로고
    • Co-chaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa
    • S. Plé, V. Job, A. Dessen, and I. Attree Co-chaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa J. Bacteriol. 192 2010 3801 3808
    • (2010) J. Bacteriol. , vol.192 , pp. 3801-3808
    • Plé, S.1    Job, V.2    Dessen, A.3    Attree, I.4
  • 64
  • 65
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • DOI 10.1016/S0092-8674(00)80830-2
    • C. Scheufler, A. Brinker, G. Bourenkov, S. Pergoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101 2000 199 210 (Pubitemid 32004747)
    • (2000) Cell , vol.101 , Issue.2 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl F.Ulrich7    Moarefi, I.8
  • 67
    • 34250840609 scopus 로고    scopus 로고
    • YscU recognizes translocators as export substrates of the Yersinia injectisome
    • DOI 10.1038/sj.emboj.7601731, PII 7601731
    • I. Sorg, S. Wagner, M. Amstutz, S.A. Muller, P. Broz, Y. Lussi, A. Engel, and G.R. Cornelis YscU recognizes translocators as export substrates of the Yersinia injectisome EMBO J. 26 2007 3015 3024 (Pubitemid 46975780)
    • (2007) EMBO Journal , vol.26 , Issue.12 , pp. 3015-3024
    • Sorg, I.1    Wagner, S.2    Amstutz, M.3    Muller, S.A.4    Broz, P.5    Lussi, Y.6    Engel, A.7    Cornelis, G.R.8
  • 69
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • DOI 10.1038/35102073
    • C.E. Stebbins, and J.E. Galán Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion Nature 414 2001 77 81 (Pubitemid 33041626)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 70
    • 0035145235 scopus 로고    scopus 로고
    • Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex
    • DOI 10.1128/JB.183.4.1159-1167.2001
    • A. Sukhan, T. Kubori, J. Wilson, and J.E. Galán Genetic analysis of assembly of the Salmonella enterica serovar Typhimurium type III secretion-associated needle complex J. Bacteriol. 183 2001 1159 1167 (Pubitemid 32107711)
    • (2001) Journal of Bacteriology , vol.183 , Issue.4 , pp. 1159-1167
    • Sukhan, A.1    Kubori, T.2    Wilson, J.3    Galan, J.E.4
  • 71
    • 40649128950 scopus 로고    scopus 로고
    • Structural characterization of the Yersinia pesits type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG
    • P. Sun, J.E. Tropea, B.P. Austin, S. Cherry, and D.S. Waugh Structural characterization of the Yersinia pesits type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG J. Mol. Biol. 377 2008 819 830
    • (2008) J. Mol. Biol. , vol.377 , pp. 819-830
    • Sun, P.1    Tropea, J.E.2    Austin, B.P.3    Cherry, S.4    Waugh, D.S.5
  • 72
    • 67749106086 scopus 로고    scopus 로고
    • Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila
    • Y.W. Tan, H.B. Yu, K.Y. Leung, J. Sivaraman, and Y.K. Mok Mapping of the chaperone AcrH binding regions of translocators AopB and AopD and characterization of oligomeric and metastable AcrH-AopB-AopD complexes in the type III secretion system of Aeromonas hydrophila Protein Sci. 18 2009 1724 1734
    • (2009) Protein Sci. , vol.18 , pp. 1724-1734
    • Tan, Y.W.1    Yu, H.B.2    Leung, K.Y.3    Sivaraman, J.4    Mok, Y.K.5
  • 73
    • 67650133652 scopus 로고    scopus 로고
    • Anti-activator ExsD forms a 1:1 complex with ExsA to inhibit transcription of type III secretion operons
    • J. Thibault, E. Faudry, C. Ebel, I. Attree, and S. Elsen Anti-activator ExsD forms a 1:1 complex with ExsA to inhibit transcription of type III secretion operons J. Biol. Chem. 284 2009 15762 15770
    • (2009) J. Biol. Chem. , vol.284 , pp. 15762-15770
    • Thibault, J.1    Faudry, E.2    Ebel, C.3    Attree, I.4    Elsen, S.5
  • 74
    • 42649087451 scopus 로고    scopus 로고
    • Structure of a widely conserved type IV pilus biogenesis factor which affects the stability of secretin multimers
    • M.B. Trindade, V. Job, C. Contreras-Martel, V. Pelicic, and A. Dessen Structure of a widely conserved type IV pilus biogenesis factor which affects the stability of secretin multimers J. Mol. Biol. 378 2008 1031 1039
    • (2008) J. Mol. Biol. , vol.378 , pp. 1031-1039
    • Trindade, M.B.1    Job, V.2    Contreras-Martel, C.3    Pelicic, V.4    Dessen, A.5
  • 75
    • 2942543052 scopus 로고    scopus 로고
    • Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specifity
    • DOI 10.1038/sj.embor.7400144
    • A. van Eerde, C. Hamiaux, J. Perez, C. Parsot, and B.W. Dijkstra Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity EMBO Rep. 5 2004 477 483 (Pubitemid 38745038)
    • (2004) EMBO Reports , vol.5 , Issue.5 , pp. 477-483
    • Van Eerde, A.1    Hamiaux, C.2    Perez, J.3    Parsot, C.4    Dijkstra, B.W.5
  • 76
    • 58649103547 scopus 로고    scopus 로고
    • Small-molecule type III secretion system inhibitors block assembly of the Shigella type III secreton
    • A.K.J. Veenendaal, C. Sundin, and A.J. Blocker Small-molecule type III secretion system inhibitors block assembly of the Shigella type III secreton J. Bacteriol. 191 2009 563 570
    • (2009) J. Bacteriol. , vol.191 , pp. 563-570
    • Veenendaal, A.K.J.1    Sundin, C.2    Blocker, A.J.3
  • 77
    • 77954572518 scopus 로고    scopus 로고
    • Analysis of the crystal structure of the ExsC.ExsE complex reveals distinctive binding interactions of the Pseudomonas aeruginosa type III secretion chaperone ExsC with ExsE and ExsD
    • N.J. Vogelaar, X. Jing, H.H. Robinson, and F.D. Schubot Analysis of the crystal structure of the ExsC.ExsE complex reveals distinctive binding interactions of the Pseudomonas aeruginosa type III secretion chaperone ExsC with ExsE and ExsD Biochemistry 49 2010 5870 5879
    • (2010) Biochemistry , vol.49 , pp. 5870-5879
    • Vogelaar, N.J.1    Jing, X.2    Robinson, H.H.3    Schubot, F.D.4
  • 79
    • 34547653543 scopus 로고    scopus 로고
    • Differences in the Electrostatic Surfaces of the Type III Secretion Needle Proteins PrgI, BsaL, and MxiH
    • DOI 10.1016/j.jmb.2007.06.034, PII S0022283607008297
    • Y. Wang, A.N. Ouellette, C.W. Egan, T. Rathinavelan, W. Im, and R.N. De Guzman Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH J. Mol. Biol. 371 2007 1304 1314 (Pubitemid 47208516)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.5 , pp. 1304-1314
    • Wang, Y.1    Ouellette, A.N.2    Egan, C.W.3    Rathinavelan, T.4    Im, W.5    De Guzman, R.N.6
  • 80
    • 33748490301 scopus 로고    scopus 로고
    • Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle
    • DOI 10.1111/j.1365-2958.2006.05347.x
    • K. Wolf, H.J. Betts, B. Chellas-Gery, S. Hower, C.N. Linton, and K.A. Fields Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle Mol. Microbiol. 61 2006 1543 1555 (Pubitemid 44359382)
    • (2006) Molecular Microbiology , vol.61 , Issue.6 , pp. 1543-1555
    • Wolf, K.1    Betts, H.J.2    Chellas-Gery, B.3    Hower, S.4    Linton, C.N.5    Fields, K.A.6
  • 81
    • 77954224937 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA
    • L.J. Worrall, M. Vuckovic, and N.C. Strynadka Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA Protein Sci. 19 2010 1091 1096
    • (2010) Protein Sci. , vol.19 , pp. 1091-1096
    • Worrall, L.J.1    Vuckovic, M.2    Strynadka, N.C.3
  • 83
    • 58149144382 scopus 로고    scopus 로고
    • A novel class of small molecule inhibitors of Hsp90
    • F. Yi, and L. Regan A novel class of small molecule inhibitors of Hsp90 ACS Chem. Biol. 3 2008 645 654
    • (2008) ACS Chem. Biol. , vol.3 , pp. 645-654
    • Yi, F.1    Regan, L.2
  • 86
    • 34547924922 scopus 로고    scopus 로고
    • Identification of minor inner-membrane components of the Shigella type III secretion system 'needle complex'
    • DOI 10.1099/mic.0.2007/007781-0
    • S.F. Zenk, D. Stabat, J.L. Hodgkinson, A.K. Veenendaal, S. Johnson, and A.J. Blocker Identification of minor inner-membrane components of the Shigella type III secretion system 'needle complex' Microbiology 153 2007 2405 2415 (Pubitemid 47262030)
    • (2007) Microbiology , vol.153 , Issue.8 , pp. 2405-2415
    • Zenk, S.F.1    Stabat, D.2    Hodgkinson, J.L.3    Veenendaal, A.K.J.4    Johnson, S.5    Blocker, A.J.6
  • 87
    • 33646180623 scopus 로고    scopus 로고
    • Solution structure of monomeric BsaL, the type III secretion needle protein of Burkholderia pseudomallei
    • L. Zhang, Y. Wang, W.L. Picking, W.D. Picking, and R.N. De Guzman Solution structure of monomeric BsaL, the type III secretion needle protein of Burkholderia pseudomallei J. Mol. Biol. 359 2006 322 330
    • (2006) J. Mol. Biol. , vol.359 , pp. 322-330
    • Zhang, L.1    Wang, Y.2    Picking, W.L.3    Picking, W.D.4    De Guzman, R.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.