메뉴 건너뛰기




Volumn 72, Issue 3, 2004, Pages 1618-1625

Role for Serine Protease HtrA (DegP) of Streptococcus pyogenes in the Biogenesis of Virulence Factors SpeB and the Hemolysin Streptolysin S

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE PROTEINASE; SERINE PROTEASE HTRA; SERINE PROTEINASE; SPEB VIRULENCE FACTOR; STREPTOLYSIN S; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 1342323730     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.72.3.1618-1625.2004     Document Type: Article
Times cited : (85)

References (56)
  • 1
    • 0034777396 scopus 로고    scopus 로고
    • Absence of a cysteine protease effect on bacterial virulence in two murine models of human invasive group A streptococcal infection
    • Ashbaugh, C. D., and M. R. Wessels. 2001. Absence of a cysteine protease effect on bacterial virulence in two murine models of human invasive group A streptococcal infection. Infect. Immun. 69:6683-6688.
    • (2001) Infect. Immun. , vol.69 , pp. 6683-6688
    • Ashbaugh, C.D.1    Wessels, M.R.2
  • 2
    • 0029670766 scopus 로고    scopus 로고
    • Multicopy suppressors of prc mutant Escherichia coli include twoHtrA (DegP) protease homologs (HhoAB), DksA, and a truncated RlpA
    • Bass, S., Q. Gu, and A. Christen. 1996. Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated RlpA. J. Bacteriol. 178:1154-1161,
    • (1996) J. Bacteriol. , vol.178 , pp. 1154-1161
    • Bass, S.1    Gu, Q.2    Christen, A.3
  • 3
    • 0346251029 scopus 로고    scopus 로고
    • Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes
    • Brenot, A., K. Y. King, B. Janowiak, O. Griffith, and M. Caparon. 2004. Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes. Infect. Immun. 72:408-413.
    • (2004) Infect. Immun. , vol.72 , pp. 408-413
    • Brenot, A.1    King, K.Y.2    Janowiak, B.3    Griffith, O.4    Caparon, M.5
  • 4
    • 0026633880 scopus 로고
    • Murine model of cutaneous infection with gram-positive cocci
    • Bunce, C., L. Wheeler, G. Reed, J. Musser, and N. Barg. 1992. Murine model of cutaneous infection with gram-positive cocci. Infect. Immun. 60:2636-2640.
    • (1992) Infect. Immun. , vol.60 , pp. 2636-2640
    • Bunce, C.1    Wheeler, L.2    Reed, G.3    Musser, J.4    Barg, N.5
  • 5
    • 0025774825 scopus 로고
    • Role of M protein in adherence of group A streptococci
    • Caparon, M. G., D. S. Stephens, A. Olsén, and J. R. Scott. 1991. Role of M protein in adherence of group A streptococci. Infect. Immun. 59:1811-1817.
    • (1991) Infect. Immun. , vol.59 , pp. 1811-1817
    • Caparon, M.G.1    Stephens, D.S.2    Olsén, A.3    Scott, J.R.4
  • 6
    • 0030948560 scopus 로고    scopus 로고
    • Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion
    • Chaussee, M. S., E. R. Phillips, and J. J. Ferretti. 1997. Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion. Infect. Immun. 65:1956-1959.
    • (1997) Infect. Immun. , vol.65 , pp. 1956-1959
    • Chaussee, M.S.1    Phillips, E.R.2    Ferretti, J.J.3
  • 7
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • Clausen, T., C. Southan, and M. Ehrmann. 2002. The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell. 10:443-455.
    • (2002) Mol. Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 8
    • 0038782015 scopus 로고    scopus 로고
    • Extracellular enzymes with immunomodulating activities: Variations on a theme in Streptococcus pyogenes
    • Collin, M., and A. Olsén. 2003. Extracellular enzymes with immunomodulating activities: variations on a theme in Streptococcus pyogenes. Infect. Immun. 71:2983-2992.
    • (2003) Infect. Immun. , vol.71 , pp. 2983-2992
    • Collin, M.1    Olsén, A.2
  • 9
    • 0033923852 scopus 로고    scopus 로고
    • Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein
    • Collin, M., and A. Olsén. 2000. Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein. Mol. Microbiol. 36:1306-1318.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1306-1318
    • Collin, M.1    Olsén, A.2
  • 10
    • 0036716436 scopus 로고    scopus 로고
    • Role of the htrA gene in Klebsiella pneumoniae virulence
    • Cortes, G., B. de Astorza, V. J. Benedi, and S. Alberti. 2002. Role of the htrA gene in Klebsiella pneumoniae virulence. Infect. Immun. 70:4772-4776.
    • (2002) Infect. Immun. , vol.70 , pp. 4772-4776
    • Cortes, G.1    De Astorza, B.2    Benedi, V.J.3    Alberti, S.4
  • 11
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. 2000. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13:470-511.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 12
    • 0035899883 scopus 로고    scopus 로고
    • HtrA protease and processing of extracellular proteins of Streptococcus mutans
    • Diaz-Torres, M. L., and R. R. Russell. 2001. HtrA protease and processing of extracellular proteins of Streptococcus mutans. FEMS Microbiol. Lett. 204:23-28.
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 23-28
    • Diaz-Torres, M.L.1    Russell, R.R.2
  • 13
    • 0033168439 scopus 로고    scopus 로고
    • Auotcatalytic processing of the streptococcal cysteine protease zymogen: Processing mechanism and characterization of the autoproteolytic cleavage sites
    • Doran, J. D., M. Nomizu, S. Takebe, R. Menard, D. Griffith, and E. Ziomek. 1999. Auotcatalytic processing of the streptococcal cysteine protease zymogen: processing mechanism and characterization of the autoproteolytic cleavage sites. Eur. J. Biochem. 263:145-151.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 145-151
    • Doran, J.D.1    Nomizu, M.2    Takebe, S.3    Menard, R.4    Griffith, D.5    Ziomek, E.6
  • 14
    • 0029908161 scopus 로고    scopus 로고
    • The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes
    • Elzer, P. H., R. W. Phillips, G. T. Robertson, and R. M. Roop II. 1996. The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes. Infect. Immun. 64:4838-4841.
    • (1996) Infect. Immun. , vol.64 , pp. 4838-4841
    • Elzer, P.H.1    Phillips, R.W.2    Robertson, G.T.3    Roop II, R.M.4
  • 16
    • 0141557576 scopus 로고    scopus 로고
    • Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal MDR proteins
    • Gajic, O., G. B. Buist, M. Kojíc, L. Topisirovic, O. P. Kuipers, and J. Kok. 2003. Novel mechanism of bacteriocin secretion and immunity carried out by lactococcal MDR proteins. J. Biol. Chem. 278:34291-34298.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34291-34298
    • Gajic, O.1    Buist, G.B.2    Kojíc, M.3    Topisirovic, L.4    Kuipers, O.P.5    Kok, J.6
  • 17
    • 0031937326 scopus 로고    scopus 로고
    • Organization around the dnaA gene of Streptococcus pneumoniae
    • Gasc, A.-M., P. Biammarinaro, S. Richter, and M. Sicard. 1998. Organization around the dnaA gene of Streptococcus pneumoniae. Microbiology 144:433-439.
    • (1998) Microbiology , vol.144 , pp. 433-439
    • Gasc, A.-M.1    Biammarinaro, P.2    Richter, S.3    Sicard, M.4
  • 18
    • 0021016755 scopus 로고
    • Isolation and characterization of erythrogenic toxins. V. Communication: Identity of erythrogenic toxin type B and streptococcal proteinase precursor
    • Gerlach, D., H. Knoll, W. Kohler, J. H. Ozegowski, and V. Hribalova. 1983. Isolation and characterization of erythrogenic toxins. V. Communication: identity of erythrogenic toxin type B and streptococcal proteinase precursor. Zentbl. Bakteriol. Mikrobiol. Hyg. A 255:221-233.
    • (1983) Zentbl. Bakteriol. Mikrobiol. Hyg. A , vol.255 , pp. 221-233
    • Gerlach, D.1    Knoll, H.2    Kohler, W.3    Ozegowski, J.H.4    Hribalova, V.5
  • 20
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 21
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., S. Wickner, and M. R. Maurizi. 1997. Protein quality control: triage by chaperones and proteases. Genes Dev. 11:815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 22
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski, E., P. A. Horwitz, and M. G. Caparon. 1992. Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect. Immun. 60:5119-5125.
    • (1992) Infect. Immun. , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horwitz, P.A.2    Caparon, M.G.3
  • 23
    • 0025350533 scopus 로고
    • Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor
    • Hauser, A. R., and P. M. Schlievert. 1990. Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor. J. Bacteriol. 172:4536-4542.
    • (1990) J. Bacteriol. , vol.172 , pp. 4536-4542
    • Hauser, A.R.1    Schlievert, P.M.2
  • 24
    • 0012344768 scopus 로고
    • The oxygen-stable haemolysin of group A haemolytic streptococci (streptolysin S)
    • Herbert, D., and E. W. Todd. 1944. The oxygen-stable haemolysin of group A haemolytic streptococci (streptolysin S). Br. J. Exp. Pathol. 25:242-254.
    • (1944) Br. J. Exp. Pathol. , vol.25 , pp. 242-254
    • Herbert, D.1    Todd, E.W.2
  • 25
    • 0035794607 scopus 로고    scopus 로고
    • Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili
    • Huang, D. L., T. L. Raivio, C. H. Jones, T. J. Silhavy, and S. J. Hultgren. 2001. Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili. EMBO J. 20:1508-1518.
    • (2001) EMBO J. , vol.20 , pp. 1508-1518
    • Huang, D.L.1    Raivio, T.L.2    Jones, C.H.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 27
    • 0028168515 scopus 로고
    • spo0J is required for normal chromosome segregation as well as the initiation of sporulation in Bacillus subtilis
    • Ireton, K., H. W. T. Gunther, and A. D. Grossman. 1994. spo0J is required for normal chromosome segregation as well as the initiation of sporulation in Bacillus subtilis. J. Bacteriol. 176:5320-5329.
    • (1994) J. Bacteriol. , vol.176 , pp. 5320-5329
    • Ireton, K.1    Gunther, H.W.T.2    Grossman, A.D.3
  • 28
    • 9044220226 scopus 로고    scopus 로고
    • C5a peptidase alters clearance and trafficking of group A streptococci by infected mice
    • Ji, Y., L. McLandsborough, A. Kondagunta, and P. P. Cleary. 1996. C5a peptidase alters clearance and trafficking of group A streptococci by infected mice. Infect. Immun. 64:503-510.
    • (1996) Infect. Immun. , vol.64 , pp. 503-510
    • Ji, Y.1    McLandsborough, L.2    Kondagunta, A.3    Cleary, P.P.4
  • 30
    • 0034868619 scopus 로고    scopus 로고
    • Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
    • Jones, C. H., T. C. Bolken, K. F. Jones, G. O. Zeller, and D. E. Hruby. 2001. Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes. Infect. Immun. 69:5538-5545.
    • (2001) Infect. Immun. , vol.69 , pp. 5538-5545
    • Jones, C.H.1    Bolken, T.C.2    Jones, K.F.3    Zeller, G.O.4    Hruby, D.E.5
  • 31
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer, T., M. Garrido-Franco, R. Huber, M. Ehrmann, and T. Clausen. 2002. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416:455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 32
    • 0002846133 scopus 로고
    • An improved method for transformation of Escherichia coli with ColE1-derived plasmids
    • H. W. Boyer, and S. Micosia (ed.). Elsevier-North Holland Biomedical Press, New York, N.Y.
    • Kushner, S. R. 1978. An improved method for transformation of Escherichia coli with ColE1-derived plasmids, p. 17-23. In H. W. Boyer, and S. Micosia (ed.), Genetic engineering. Elsevier-North Holland Biomedical Press, New York, N.Y.
    • (1978) Genetic Engineering , pp. 17-23
    • Kushner, S.R.1
  • 33
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • Lei, B., S. Mackie, S. Lukomski, and J. M. Musser. 2000. Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect. Immun. 68:6807-6818.
    • (2000) Infect. Immun. , vol.68 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4
  • 34
    • 0029947971 scopus 로고    scopus 로고
    • Construction and characterization of a Yersinia enterocolitica 0:8 high-temperature requirement (htrA) isogenic mutant
    • Li, S. R., N. Dorrell, P. H. Everest, G. Dougan, and B. W. Wren. 1996. Construction and characterization of a Yersinia enterocolitica 0:8 high-temperature requirement (htrA) isogenic mutant. Infect. Immun. 64:2088-2094.
    • (1996) Infect. Immun. , vol.64 , pp. 2088-2094
    • Li, S.R.1    Dorrell, N.2    Everest, P.H.3    Dougan, G.4    Wren, B.W.5
  • 36
    • 0033789226 scopus 로고    scopus 로고
    • Role of streptolysin O in a mouse model of invasive group A streptococcal disease
    • Limbago, B., V. Penumalli, B. Weinrick, and J. R. Scott. 2000. Role of streptolysin O in a mouse model of invasive group A streptococcal disease. Infect. Immun. 68:6384-6390.
    • (2000) Infect. Immun. , vol.68 , pp. 6384-6390
    • Limbago, B.1    Penumalli, V.2    Weinrick, B.3    Scott, J.R.4
  • 37
    • 0000686715 scopus 로고
    • Streptococcal protease: The zymogen to enzyme transformation
    • Liu, T.-Y., and S. D. Elliot. 1965. Streptococcal protease: the zymogen to enzyme transformation. J. Biol. Chem. 240:1138-1142.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1138-1142
    • Liu, T.-Y.1    Elliot, S.D.2
  • 38
    • 0032476656 scopus 로고    scopus 로고
    • A role for Trigger Factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W. R., C. M. Gibson, and M. G. Caparon. 1998. A role for Trigger Factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17:6263-6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 39
    • 0035726295 scopus 로고    scopus 로고
    • Mutation of luxS affects growth and virulence factor expression in Streptococcus pyogenes
    • Lyon, W. R., J. C. Madden, J. C. Levin, J. L. Stein, and M. G. Caparon. 2001. Mutation of luxS affects growth and virulence factor expression in Streptococcus pyogenes. Mol. Microbiol. 42:145-157.
    • (2001) Mol. Microbiol. , vol.42 , pp. 145-157
    • Lyon, W.R.1    Madden, J.C.2    Levin, J.C.3    Stein, J.L.4    Caparon, M.G.5
  • 40
    • 0033973889 scopus 로고    scopus 로고
    • Microbial metalloproteases and pathogenesis
    • Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microbes Infect. 2:91-98.
    • (2000) Microbes Infect. , vol.2 , pp. 91-98
    • Miyoshi, S.1    Shinoda, S.2
  • 41
    • 0036966408 scopus 로고    scopus 로고
    • Streptococcal beta-hemolysins: Genetics and role in disease pathogenesis
    • Nizet, V. 2002. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 10:575-580.
    • (2002) Trends Microbiol. , vol.10 , pp. 575-580
    • Nizet, V.1
  • 43
    • 0035156736 scopus 로고    scopus 로고
    • YkdA and YvtA, HtrA-like serine proteases in Bacillus subtilis, engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression
    • Noone, D., A. Howell, R. Collery, and K. M. Devine. 2001. YkdA and YvtA, HtrA-like serine proteases in Bacillus subtilis, engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression. J. Bacteriol. 183:654-663.
    • (2001) J. Bacteriol. , vol.183 , pp. 654-663
    • Noone, D.1    Howell, A.2    Collery, R.3    Devine, K.M.4
  • 44
    • 0034049557 scopus 로고    scopus 로고
    • Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated
    • Noone, D., A. Howell, and K. M. Devine. 2000. Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated. J. Bacteriol. 182:1592-1599.
    • (2000) J. Bacteriol. , vol.182 , pp. 1592-1599
    • Noone, D.1    Howell, A.2    Devine, K.M.3
  • 45
    • 0025188767 scopus 로고
    • Inability of toxin inhibitors to neutralize enhanced toxicity caused by bacteria adherent to tissue culture cells
    • Ofek, I., D. Zafriri, J. Goldhar, and B. I. Eisenstein. 1990. Inability of toxin inhibitors to neutralize enhanced toxicity caused by bacteria adherent to tissue culture cells. Infect. Immun. 58:3737-3742.
    • (1990) Infect. Immun. , vol.58 , pp. 3737-3742
    • Ofek, I.1    Zafriri, D.2    Goldhar, J.3    Eisenstein, B.I.4
  • 46
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M. J., and B. W. Wren. 1997. The HtrA family of serine proteases. Mol. Microbiol. 26:209-221.
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 47
    • 0034108191 scopus 로고    scopus 로고
    • HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing
    • Poquet, I., V. Saint, E. Seznec, N. Simoes, A. Bolotin, and A. Gruss. 2000. HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing. Mol. Microbiol. 35:1042-1051.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1042-1051
    • Poquet, I.1    Saint, V.2    Seznec, E.3    Simoes, N.4    Bolotin, A.5    Gruss, A.6
  • 48
    • 0036839640 scopus 로고    scopus 로고
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
    • Purdy, G. E., M. Hong, and S. M. Payne. 2002. Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread. Infect. Immun. 70:6355-6364.
    • (2002) Infect. Immun. , vol.70 , pp. 6355-6364
    • Purdy, G.E.1    Hong, M.2    Payne, S.M.3
  • 49
    • 0029957927 scopus 로고    scopus 로고
    • Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection
    • Schrager, H. M., J. G. Rheinwald, and M. R. Wessels. 1996. Hyaluronic acid capsule and the role of streptococcal entry into keratinocytes in invasive skin infection. J. Clin. Investig. 98:1954-1958.
    • (1996) J. Clin. Investig. , vol.98 , pp. 1954-1958
    • Schrager, H.M.1    Rheinwald, J.G.2    Wessels, M.R.3
  • 50
    • 0036074050 scopus 로고    scopus 로고
    • Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopharyngeal colonization
    • Sebert, M. E., L. M. Palmer, M. Fosenberg, and J. N. Weiser. 2002. Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopharyngeal colonization. Infect. Immun. 70:4059-4067.
    • (2002) Infect. Immun. , vol.70 , pp. 4059-4067
    • Sebert, M.E.1    Palmer, L.M.2    Fosenberg, M.3    Weiser, J.N.4
  • 51
    • 0032825302 scopus 로고    scopus 로고
    • The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress
    • Skorko-Glonek, J., D. Zurawa, E. Kuxzwara, M. Wozniak, and Z. Wypych. 1999. The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol. Gen. Genet. 262:342-350.
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 342-350
    • Skorko-Glonek, J.1    Zurawa, D.2    Kuxzwara, E.3    Wozniak, M.4    Wypych, Z.5
  • 52
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., A. Beil, and M. Ehrmann. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 53
    • 0033744193 scopus 로고    scopus 로고
    • Role for a secreted cysteine proteinase in the establishment of host tissue tropism by group A streptococci
    • Svensson, M. D., D. A. Scaramuzzino, U. Sjöbring, A. Olsén, C. Frank, and D. E. Bessen. 2000. Role for a secreted cysteine proteinase in the establishment of host tissue tropism by group A streptococci. Mol. Microbiol. 38:242-253.
    • (2000) Mol. Microbiol. , vol.38 , pp. 242-253
    • Svensson, M.D.1    Scaramuzzino, D.A.2    Sjöbring, U.3    Olsén, A.4    Frank, C.5    Bessen, D.E.6
  • 54
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H., A. Bolhuis, J. D. H. Jongbloed, S. Bron, and J. M. van Dijl. 2000. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64:515-547.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    Van Dijl, J.M.5
  • 55
    • 0034615573 scopus 로고    scopus 로고
    • Bacterial proteinases as targets for the development of second-generation antibiotics
    • Travis, J., and J. Potempa. 2000. Bacterial proteinases as targets for the development of second-generation antibiotics. Biochem. Biophys. Acta 1477:35-50.
    • (2000) Biochem. Biophys. Acta , vol.1477 , pp. 35-50
    • Travis, J.1    Potempa, J.2
  • 56
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of Gram-positive bacteria
    • van Wely, K. H. M., J. Swaving, R. Fruedl, and A. J. M. Driessen. 2001. Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol. Rev. 25:437-454.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 437-454
    • Van Wely, K.H.M.1    Swaving, J.2    Fruedl, R.3    Driessen, A.J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.