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Volumn 23, Issue 1, 2015, Pages 161-172

The modular structure of the inner-membrane ring component PrgK facilitates assembly of the type III secretion system basal body

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PRGK PROTEIN; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; PRGH PROTEIN, SALMONELLA TYPHIMURIUM; PRGK PROTEIN, SALMONELLA TYPHIMURIUM;

EID: 84920986999     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.10.021     Document Type: Article
Times cited : (39)

References (39)
  • 1
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • F. Alber, F. Förster, D. Korkin, M. Topf, and A. Sali Integrating diverse data for structure determination of macromolecular assemblies Annu. Rev. Biochem. 77 2008 443 477
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 443-477
    • Alber, F.1    Förster, F.2    Korkin, D.3    Topf, M.4    Sali, A.5
  • 2
    • 0026496235 scopus 로고
    • MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins
    • A. Allaoui, P.J. Sansonetti, and C. Parsot MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins J. Bacteriol. 174 1992 7661 7669
    • (1992) J. Bacteriol. , vol.174 , pp. 7661-7669
    • Allaoui, A.1    Sansonetti, P.J.2    Parsot, C.3
  • 5
    • 34547563370 scopus 로고    scopus 로고
    • The RCI server: Rapid and accurate calculation of protein flexibility using chemical shifts
    • M.V. Berjanskii, and D.S. Wishart The RCI server: rapid and accurate calculation of protein flexibility using chemical shifts Nucleic Acids Res. 35 2007 W531 W537
    • (2007) Nucleic Acids Res. , vol.35 , pp. W531-W537
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 6
    • 84862556686 scopus 로고    scopus 로고
    • Protein export according to schedule: Architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria
    • D. Büttner Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria Microbiol. Mol. Biol. Rev. 76 2012 262 310
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 262-310
    • Büttner, D.1
  • 7
    • 33947129778 scopus 로고    scopus 로고
    • Salmonella, the host and disease: A brief review
    • B. Coburn, G.A. Grassl, and B.B. Finlay Salmonella, the host and disease: a brief review Immunol. Cell Biol. 85 2007 112 118
    • (2007) Immunol. Cell Biol. , vol.85 , pp. 112-118
    • Coburn, B.1    Grassl, G.A.2    Finlay, B.B.3
  • 9
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • A.M. Crago, and V. Koronakis Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization Mol. Microbiol. 30 1998 47 56
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 14
    • 84893745802 scopus 로고    scopus 로고
    • A substrate-fusion protein is trapped inside the Type III Secretion System channel in Shigella flexneri
    • K. Dohlich, A.B. Zumsteg, C. Goosmann, and M. Kolbe A substrate-fusion protein is trapped inside the Type III Secretion System channel in Shigella flexneri PLoS Pathog. 10 2014 e1003881
    • (2014) PLoS Pathog. , vol.10 , pp. e1003881
    • Dohlich, K.1    Zumsteg, A.B.2    Goosmann, C.3    Kolbe, M.4
  • 17
    • 44949215750 scopus 로고    scopus 로고
    • Virulence blockers as alternatives to antibiotics: Type III secretion inhibitors against Gram-negative bacteria
    • 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
    • (2008) J. Intern. Med. , vol.264 , pp. 17-29
    • Keyser, P.1    Elofsson, M.2    Rosell, S.3    Wolf-Watz, H.4
  • 18
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type III secretion components to needle complex formation
    • T.G. Kimbrough, and S.I. Miller Contribution of Salmonella typhimurium type III secretion components to needle complex formation Proc. Natl. Acad. Sci. USA 97 2000 11008 11013
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 19
    • 84863413409 scopus 로고    scopus 로고
    • The type III secretion system as a source of novel antibacterial drug targets
    • T. Kline, H.B. Felise, S. Sanowar, and S.I. Miller The type III secretion system as a source of novel antibacterial drug targets Curr. Drug Targets 13 2012 338 351
    • (2012) Curr. Drug Targets , vol.13 , pp. 338-351
    • Kline, T.1    Felise, H.B.2    Sanowar, S.3    Miller, S.I.4
  • 23
    • 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
    • M. Lunelli, R. Hurwitz, J. Lambers, and M. Kolbe Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands PLoS Pathog. 7 2011 e1002163
    • (2011) PLoS Pathog. , vol.7 , pp. e1002163
    • Lunelli, M.1    Hurwitz, R.2    Lambers, J.3    Kolbe, M.4
  • 24
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • 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
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    Sukhan, A.3    Thomas, D.R.4    Galán, J.E.5    Unger, V.M.6
  • 25
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation
    • J.A. Marsh, V.K. Singh, Z. Jia, and J.D. Forman-Kay Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation Protein Sci. 15 2006 2795 2804
    • (2006) Protein Sci. , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 26
    • 84892606269 scopus 로고    scopus 로고
    • Targeting the type III secretion system to treat bacterial infections
    • N.C. Marshall, and B.B. Finlay Targeting the type III secretion system to treat bacterial infections Expert Opin. Ther. Targets 18 2014 137 152
    • (2014) Expert Opin. Ther. Targets , vol.18 , pp. 137-152
    • Marshall, N.C.1    Finlay, B.B.2
  • 31
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • O. Schraidt, and T.C. Marlovits Three-dimensional model of Salmonella's needle complex at subnanometer resolution Science 331 2011 1192 1195
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 33
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure
    • K. Sekiya, M. Ohishi, T. Ogino, K. Tamano, C. Sasakawa, and A. Abe Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure Proc. Natl. Acad. Sci. USA 98 2001 11638 11643
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11638-11643
    • Sekiya, K.1    Ohishi, M.2    Ogino, T.3    Tamano, K.4    Sasakawa, C.5    Abe, A.6
  • 35
  • 37
    • 34547653543 scopus 로고    scopus 로고
    • Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH
    • 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
    • (2007) J. Mol. Biol. , vol.371 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.