메뉴 건너뛰기




Volumn 67, Issue 10, 1999, Pages 5395-5408

Virulence role of V antigen of Yersinia pestis at the bacterial surface

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN;

EID: 0032833608     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.10.5395-5408.1999     Document Type: Article
Times cited : (120)

References (80)
  • 1
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D. M., and O. Schneewind. 1997. A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278:1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 2
    • 0030913232 scopus 로고    scopus 로고
    • cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16:2730-2744.
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 3
    • 0026041767 scopus 로고
    • The V antigen of yersiniae: An overview
    • Brubaker, R. R. 1991. The V antigen of yersiniae: an overview. Contrib. Microbiol. Immunol. 12:127-133.
    • (1991) Contrib. Microbiol. Immunol. , vol.12 , pp. 127-133
    • Brubaker, R.R.1
  • 4
    • 37049227034 scopus 로고
    • Pasteurella pestis: Role of pesticin I and iron in experimental plague
    • Brubaker, R. R., E. D. Beesley, and M. J. Surgalla. 1965. Pasteurella pestis: role of pesticin I and iron in experimental plague. Science 149:422-424.
    • (1965) Science , vol.149 , pp. 422-424
    • Brubaker, R.R.1    Beesley, E.D.2    Surgalla, M.J.3
  • 5
    • 0000680216 scopus 로고
    • The basis of virulence in Pasteurella pestis: An antigen determining virulence
    • Burrows, T. W., and G. A. Bacon. 1956. The basis of virulence in Pasteurella pestis: an antigen determining virulence. Br. J. Exp. Pathol. 37:481-493.
    • (1956) Br. J. Exp. Pathol. , vol.37 , pp. 481-493
    • Burrows, T.W.1    Bacon, G.A.2
  • 6
    • 0000972368 scopus 로고
    • The role of multiplication of Pasteurella pestis in mononuclear phagocytes in the pathogenesis of fleaborne plague
    • Cavanaugh, D. C., and R. Randall. 1959. The role of multiplication of Pasteurella pestis in mononuclear phagocytes in the pathogenesis of fleaborne plague. J. Immunol. 83:348-363.
    • (1959) J. Immunol. , vol.83 , pp. 348-363
    • Cavanaugh, D.C.1    Randall, R.2
  • 7
    • 0030967331 scopus 로고    scopus 로고
    • Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica
    • Cheng, L. W., D. M. Anderson, and O. Schneewind. 1997. Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica. Mol. Microbiol. 24:757-765.
    • (1997) Mol. Microbiol. , vol.24 , pp. 757-765
    • Cheng, L.W.1    Anderson, D.M.2    Schneewind, O.3
  • 8
    • 0031771288 scopus 로고    scopus 로고
    • The Yersinia deadly kiss
    • Cornelis, G. R. 1998. The Yersinia deadly kiss. J. Bacteriol. 180:5495-5504.
    • (1998) J. Bacteriol. , vol.180 , pp. 5495-5504
    • Cornelis, G.R.1
  • 10
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R., and H. Wolf-Watz. 1997. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23:861-867.
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 12
    • 0345009691 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Kentucky, Lexington
    • Fields, K. A. 1999. Ph.D. thesis. University of Kentucky, Lexington.
    • (1999)
    • Fields, K.A.1
  • 13
    • 0032797583 scopus 로고    scopus 로고
    • LcrV of Yersinia pestis enters infected eukaryotic cells by a virulence plasmid-independent mechanism
    • Fields, K. A., and S. C. Straley. 1999. LcrV of Yersinia pestis enters infected eukaryotic cells by a virulence plasmid-independent mechanism. Infect. Immun. 67:4801-4813.
    • (1999) Infect. Immun. , vol.67 , pp. 4801-4813
    • Fields, K.A.1    Straley, S.C.2
  • 14
    • 0030954706 scopus 로고    scopus 로고
    • Failure to detect binding of LcrH to the V antigen of Yersinia pestis
    • Fields, K. A., A. W. Williams, and S. C. Straley. 1997. Failure to detect binding of LcrH to the V antigen of Yersinia pestis. Infect. Immun. 65:3954-3957.
    • (1997) Infect. Immun. , vol.65 , pp. 3954-3957
    • Fields, K.A.1    Williams, A.W.2    Straley, S.C.3
  • 15
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotubercubsis
    • Forsberg, A., A. M. Viltanen, M. Skurnik, and H. Wolf-Watz. 1991. The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotubercubsis. Mol. Microbiol. 5:977-986.
    • (1991) Mol. Microbiol. , vol.5 , pp. 977-986
    • Forsberg, A.1    Viltanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 16
    • 0345440797 scopus 로고    scopus 로고
    • Personal communication
    • Frank, D. W. Personal communication.
    • Frank, D.W.1
  • 18
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Håkansson, S., E. E. Galyov, R. Rosqvist, and H. Wolf-Watz. 1996. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20: 593-603.
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Håkansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 19
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • Hanahan, D., J. Jessee, and F. R. Bloom. 1991. Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol. 204:63-113.
    • (1991) Methods Enzymol. , vol.204 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 21
    • 0030777667 scopus 로고    scopus 로고
    • Regions of Yersinia pestis V antigen that contribute to protection against plague identified by passive and active immunization
    • Hill, J., S. E. C. Leary, K. F. Griffin, E. D. Williamson, and R. W. Titball. 1997. Regions of Yersinia pestis V antigen that contribute to protection against plague identified by passive and active immunization. Infect. Immun. 65:4476-4482.
    • (1997) Infect. Immun. , vol.65 , pp. 4476-4482
    • Hill, J.1    Leary, S.E.C.2    Griffin, K.F.3    Williamson, E.D.4    Titball, R.W.5
  • 23
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells
    • Iriarte, M., and G. R. Cornelis. 1998. YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol. Microbiol. 29:915-929.
    • (1998) Mol. Microbiol. , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2
  • 24
    • 0032055051 scopus 로고    scopus 로고
    • TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • Iriarte, M., M. P. Sory, A. Boland, A. P. Boyd, S. D. Mills, I. Lambermont, and G. R. Cornells. 1998. TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. EMBO J. 17:1907-1918.
    • (1998) EMBO J. , vol.17 , pp. 1907-1918
    • Iriarte, M.1    Sory, M.P.2    Boland, A.3    Boyd, A.P.4    Mills, S.D.5    Lambermont, I.6    Cornells, G.R.7
  • 25
    • 0019433725 scopus 로고
    • Rapid procedure for detection and isolation of large and small plasmids
    • Kado, C. I., and S. T. Liu. 1981. Rapid procedure for detection and isolation of large and small plasmids. J. Bacteriol. 145:1365-1373.
    • (1981) J. Bacteriol. , vol.145 , pp. 1365-1373
    • Kado, C.I.1    Liu, S.T.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0026542646 scopus 로고
    • Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica
    • Lambert de Rouvroit, C. L., C. Sluiters, and G. R. Cornelis. 1992. Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol. Microbiol. 6:395-409.
    • (1992) Mol. Microbiol. , vol.6 , pp. 395-409
    • Lambert De Rouvroit, C.L.1    Sluiters, C.2    Cornelis, G.R.3
  • 29
    • 0031970595 scopus 로고    scopus 로고
    • Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: One-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone
    • Lee, V. T., D. M. Anderson, and O. Schneewind. 1998. Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Mol. Microbiol. 28:593-601.
    • (1998) Mol. Microbiol. , vol.28 , pp. 593-601
    • Lee, V.T.1    Anderson, D.M.2    Schneewind, O.3
  • 30
    • 0025358996 scopus 로고
    • Yersinia pestis pH6 antigen: Genetic, biochemical, and virulence characterization of a protein involved in pathogenesis in bubonic plague
    • Lindler, L. E., M. S. Klempner, and S. C. Straley. 1990. Yersinia pestis pH6 antigen: genetic, biochemical, and virulence characterization of a protein involved in pathogenesis in bubonic plague. Infect. Immun. 58:2569-2577.
    • (1990) Infect. Immun. , vol.58 , pp. 2569-2577
    • Lindler, L.E.1    Klempner, M.S.2    Straley, S.C.3
  • 32
    • 0344147262 scopus 로고    scopus 로고
    • Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria
    • Metcalf, W. W., W. Jiang, L. L. Daniels, S.-K. Kim, A. Haldimann, and B. L. Wanner. 1996. Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria. Mol. Microbiol. 24:73-91.
    • (1996) Mol. Microbiol. , vol.24 , pp. 73-91
    • Metcalf, W.W.1    Jiang, W.2    Daniels, L.L.3    Kim, S.-K.4    Haldimann, A.5    Wanner, B.L.6
  • 35
    • 0028058806 scopus 로고
    • Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide
    • Motin, V. L., R. Nakajima, G. B. Smirnov, and R. R. Brubaker. 1994. Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide. Infect. Immun. 62:4192-4201.
    • (1994) Infect. Immun. , vol.62 , pp. 4192-4201
    • Motin, V.L.1    Nakajima, R.2    Smirnov, G.B.3    Brubaker, R.R.4
  • 36
    • 0027534069 scopus 로고
    • Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha
    • Nakajima, R., and R. R. Brubaker. 1993. Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha. Infect. Immun. 61:21-31.
    • (1993) Infect. Immun. , vol.61 , pp. 21-31
    • Nakajima, R.1    Brubaker, R.R.2
  • 37
    • 0029021978 scopus 로고
    • Suppression of cytokines in mice by protein A-V antigen fusion and restoration of synthesis by active immunization
    • Nakajima, R., V. L. Motin, and R. R. Brubaker. 1995. Suppression of cytokines in mice by protein A-V antigen fusion and restoration of synthesis by active immunization. Infect. Immun. 63:3021-3029.
    • (1995) Infect. Immun. , vol.63 , pp. 3021-3029
    • Nakajima, R.1    Motin, V.L.2    Brubaker, R.R.3
  • 38
    • 0030946572 scopus 로고    scopus 로고
    • Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: Amplification of interleukin-10
    • Nedialkov, Y. A., V. L. Motin, and R. R. Brubaker. 1997. Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: amplification of interleukin-10. Infect. Immun. 65:1196-1203.
    • (1997) Infect. Immun. , vol.65 , pp. 1196-1203
    • Nedialkov, Y.A.1    Motin, V.L.2    Brubaker, R.R.3
  • 39
    • 0031019824 scopus 로고    scopus 로고
    • Effect of Yersinia pestis YopM on experimental plague
    • Nemeth, J., and S. C. Straley. 1997. Effect of Yersinia pestis YopM on experimental plague. Infect. Immun. 65:924-930.
    • (1997) Infect. Immun. , vol.65 , pp. 924-930
    • Nemeth, J.1    Straley, S.C.2
  • 40
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocates YopB and YopB
    • Neyt, C., and G. R. Cornelis. 1999. Role of SycD, the chaperone of the Yersinia Yop translocates YopB and YopB. Mol. Microbiol. 31:143-156.
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 41
    • 0031802098 scopus 로고    scopus 로고
    • The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG
    • Nilles, M. L., K. A. Fields, and S. C. Straley. 1998. The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG. J. Bacteriol. 180:3410-3420.
    • (1998) J. Bacteriol. , vol.180 , pp. 3410-3420
    • Nilles, M.L.1    Fields, K.A.2    Straley, S.C.3
  • 44
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis - Etiologic agent of plague
    • Perry, R. D., and J. D. Fetherston. 1997. Yersinia pestis - etiologic agent of plague. Clin. Microbiol. Rev. 10:35-66.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 45
    • 0024992438 scopus 로고
    • Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis
    • Perry, R. D., M. Pendrak, and P. Schuetze. 1990. Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis. J. Bacteriol. 172:5929-5937.
    • (1990) J. Bacteriol. , vol.172 , pp. 5929-5937
    • Perry, R.D.1    Pendrak, M.2    Schuetze, P.3
  • 47
    • 0030978909 scopus 로고    scopus 로고
    • cas and FAK, and the associated accumulation of these proteins in focal adhesions
    • cas and FAK, and the associated accumulation of these proteins in focal adhesions. EMBO J. 16:2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 50
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • Plano, G. V., S. S. Barve, and S. C. Straley. 1991. LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J. Bacteriol. 173:7293-7303.
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 51
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1995. Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis. J. Bacteriol. 177:3843-3854.
    • (1995) J. Bacteriol. , vol.177 , pp. 3843-3854
    • Plano, G.V.1    Straley, S.C.2
  • 53
    • 0024437782 scopus 로고
    • Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis
    • Price, S. B., K. Y. Leung, S. S. Barve, and S. C. Straley. 1989. Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis. J. Bacteriol. 171:5646-5653.
    • (1989) J. Bacteriol. , vol.171 , pp. 5646-5653
    • Price, S.B.1    Leung, K.Y.2    Barve, S.S.3    Straley, S.C.4
  • 54
    • 0026772670 scopus 로고
    • 1 involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH
    • 1 involved in the low-calcium response of Yersinia pseudotuberculosis shows extensive homology to YopH. J. Bacteriol. 174:3355-3363.
    • (1992) J. Bacteriol. , vol.174 , pp. 3355-3363
    • Rimpilainen, M.1    Forsberg, A.2    Wolf-Watz, H.3
  • 56
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist, R., Å. Forsberg, and H. Wolf-Watz. 1991. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59:4562-4569.
    • (1991) Infect. Immun. , vol.59 , pp. 4562-4569
    • Rosqvist, R.1    Forsberg, A.2    Wolf-Watz, H.3
  • 57
    • 0032489918 scopus 로고    scopus 로고
    • Yersinia enterocolitica impairs activation of transcription factor NF-kB: Involvment in the induction of programmed cell death and in the suppression of macrophage TNF-α production
    • Ruckdeschel, K., S. Harb, A. Roggenkamp, M. Hornef, R. Zumbihl, S. Kohler, J. Heesemann, and B. Rouot. 1998. Yersinia enterocolitica impairs activation of transcription factor NF-kB: involvment in the induction of programmed cell death and in the suppression of macrophage TNF-α production. J. Exp. Med. 187:1069-1079.
    • (1998) J. Exp. Med. , vol.187 , pp. 1069-1079
    • Ruckdeschel, K.1    Harb, S.2    Roggenkamp, A.3    Hornef, M.4    Zumbihl, R.5    Kohler, S.6    Heesemann, J.7    Rouot, B.8
  • 60
    • 0031885218 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD
    • Sarker, M., C. Neyt, I. Stainier, and G. R. Cornelis. 1998. The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J. Bacteriol. 180:1207-1214.
    • (1998) J. Bacteriol. , vol.180 , pp. 1207-1214
    • Sarker, M.1    Neyt, C.2    Stainier, I.3    Cornelis, G.R.4
  • 61
    • 0031811818 scopus 로고    scopus 로고
    • LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells
    • Sarker, M., M. Sory, A. P. Boyd, M. Iriarte, and G. R. Cornelis. 1998. LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells. Infect. Immun. 66:2976-2979.
    • (1998) Infect. Immun. , vol.66 , pp. 2976-2979
    • Sarker, M.1    Sory, M.2    Boyd, A.P.3    Iriarte, M.4    Cornelis, G.R.5
  • 62
    • 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., E. Frithz-Lindsten, and H. Wolf-Watz. 1996. Delineation and mutational analysis of the Yersinia pseudotuberculosis YopE domains which mediate translocation across bacterial and eukaryotic cellular membranes. J. Bacteriol. 178:7227-7233.
    • (1996) J. Bacteriol. , vol.178 , pp. 7227-7233
    • Schesser, K.1    Frithz-Lindsten, E.2    Wolf-Watz, H.3
  • 63
    • 0031770757 scopus 로고    scopus 로고
    • Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus
    • Skrzypek, E., C. Cowan, and S. C. Straley. 1998. Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus. Mol. Microbiol. 30:1051-1065.
    • (1998) Mol. Microbiol. , vol.30 , pp. 1051-1065
    • Skrzypek, E.1    Cowan, C.2    Straley, S.C.3
  • 64
    • 0027229148 scopus 로고
    • LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis
    • Skrzypek, E., and S. C. Straley. 1993. LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis. J. Bacteriol. 175:3520-3528.
    • (1993) J. Bacteriol. , vol.175 , pp. 3520-3528
    • Skrzypek, E.1    Straley, S.C.2
  • 65
    • 0029031698 scopus 로고
    • 2+ response, and virulence of Yersinia pestis
    • 2+ response, and virulence of Yersinia pestis. J. Bacteriol. 177:2530-2542.
    • (1995) J. Bacteriol. , vol.177 , pp. 2530-2542
    • Skrzypek, E.1    Straley, S.C.2
  • 66
    • 0023715723 scopus 로고
    • Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis
    • Sodeinde, O. A., and J. D. Goguen. 1988. Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis. Infect. Immun. 56:2743-2748.
    • (1988) Infect. Immun. , vol.56 , pp. 2743-2748
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 67
    • 0023807278 scopus 로고
    • Plasminogen activator/coagulase of Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins
    • Sodeinde, O., A. K. Sample, R. R. Brubaker, and J. D. Goguen. 1988. Plasminogen activator/coagulase of Yersinia pestis is responsible for degradation of plasmid-encoded outer membrane proteins. Infect. Immun. 56:2749-2752.
    • (1988) Infect. Immun. , vol.56 , pp. 2749-2752
    • Sodeinde, O.1    Sample, A.K.2    Brubaker, R.R.3    Goguen, J.D.4
  • 68
    • 0030698085 scopus 로고    scopus 로고
    • YscM1 and YscM2, two Yersinia enterocolitica proteins causing down regulation of yop transcription
    • Stainier, I., M. Iriarte, and G. R. Cornelis. 1997. YscM1 and YscM2, two Yersinia enterocolitica proteins causing down regulation of yop transcription. Mol. Microbiol. 26:833-843.
    • (1997) Mol. Microbiol. , vol.26 , pp. 833-843
    • Stainier, I.1    Iriarte, M.2    Cornelis, G.R.3
  • 69
    • 0001405461 scopus 로고
    • The plasmid-encoded outer-membrane proteins of Yersinia pestis
    • Straley, S. C. 1988. The plasmid-encoded outer-membrane proteins of Yersinia pestis. Rev. Infect. Dis. 10(Suppl. 2):S323-S326.
    • (1988) Rev. Infect. Dis. , vol.10 , Issue.SUPPL. 2
    • Straley, S.C.1
  • 70
    • 0022629859 scopus 로고
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins. Infect. Immun. 51:445-454.
    • (1986) Infect. Immun. , vol.51 , pp. 445-454
    • Straley, S.C.1    Bowmer, W.S.2
  • 71
    • 0014142953 scopus 로고
    • Influence of unsaturation on fibrinolytic activity of salts of fatty acids
    • Surgalla, M. J., E. D. Beesley, and R. R. Brubaker. 1967. Influence of unsaturation on fibrinolytic activity of salts of fatty acids. Proc. Soc. Exp. Biol. Med. 126:256-258.
    • (1967) Proc. Soc. Exp. Biol. Med. , vol.126 , pp. 256-258
    • Surgalla, M.J.1    Beesley, E.D.2    Brubaker, R.R.3
  • 72
    • 0009482260 scopus 로고
    • Electophoretic transfer of proteins from polacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electophoretic transfer of proteins from polacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 74
    • 0023085635 scopus 로고
    • Role of V antigen in promoting virulence in yersiniae
    • Une, T., and R. R. Brubaker. 1987. Role of V antigen in promoting virulence in yersiniae. Contrib. Microbiol. Immunol. 9:179-185.
    • (1987) Contrib. Microbiol. Immunol. , vol.9 , pp. 179-185
    • Une, T.1    Brubaker, R.R.2
  • 77
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • Williams, A. W., and S. C. Straley. 1998. YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J. Bacteriol. 180:350-358.
    • (1998) J. Bacteriol. , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2
  • 78
    • 0030731178 scopus 로고    scopus 로고
    • Identification of type IIIH secreted products of the Pseudomonas aeruginosa exoenzyme S regulon
    • Yahr, T. L., L. M. Mende-Mueller, M. B. Friese, and D. W. Frank. 1997. Identification of type IIIH secreted products of the Pseudomonas aeruginosa exoenzyme S regulon. J. Bacteriol. 179:7165-7168.
    • (1997) J. Bacteriol. , vol.179 , pp. 7165-7168
    • Yahr, T.L.1    Mende-Mueller, L.M.2    Friese, M.B.3    Frank, D.W.4
  • 79


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.