메뉴 건너뛰기




Volumn 75, Issue 1, 2010, Pages 161-177

Comparison of Staphopain A (ScpA) and B (SspB) precursor activation mechanisms reveals unique secretion kinetics of proSspB (Staphopain B), and a different interaction with its cognate Staphostatin, SspC

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ELASTIN; STAPHOPAIN A; STAPHOPAIN B; STAPHOPAIN C; UNCLASSIFIED DRUG;

EID: 72949104561     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06974.x     Document Type: Article
Times cited : (32)

References (69)
  • 1
    • 0031925769 scopus 로고    scopus 로고
    • Staphylococcus aureus: A well-armed pathogen
    • Archer, G.L. (1998) Staphylococcus aureus: a well-armed pathogen. Clin Infect Dis 26 : 1179 1181.
    • (1998) Clin Infect Dis , vol.26 , pp. 1179-1181
    • Archer, G.L.1
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J. Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 : 195 201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 0037172403 scopus 로고    scopus 로고
    • Genome and virulence determinants of high virulence community-acquired MRSA
    • Baba, T., Takeuchi, F., Kuroda, M., Yuzawa, H., Aoki, K., Oguchi, A., et al. (2002) Genome and virulence determinants of high virulence community-acquired MRSA. Lancet 359 : 1819 1827.
    • (2002) Lancet , vol.359 , pp. 1819-1827
    • Baba, T.1    Takeuchi, F.2    Kuroda, M.3    Yuzawa, H.4    Aoki, K.5    Oguchi, A.6
  • 4
    • 37549035397 scopus 로고    scopus 로고
    • Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of Staphylococcal genomes: Polymorphism and evolution of two major pathogenicity islands
    • Baba, T., Bae, T., Schneewind, O., Takeuchi, F. Hiramatsu, K. (2008) Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of Staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands. J Bacteriol 190 : 300 310.
    • (2008) J Bacteriol , vol.190 , pp. 300-310
    • Baba, T.1    Bae, T.2    Schneewind, O.3    Takeuchi, F.4    Hiramatsu, K.5
  • 5
    • 67650358909 scopus 로고    scopus 로고
    • QMEAN server for protein model quality estimation
    • Benkert, P., Kunzli, M. Schwede, T. (2009) QMEAN server for protein model quality estimation. Nucleic Acids Res 37 : W510 W514.
    • (2009) Nucleic Acids Res , vol.37
    • Benkert, P.1    Kunzli, M.2    Schwede, T.3
  • 7
    • 36849064891 scopus 로고    scopus 로고
    • Poring over pores: Alpha-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia
    • Bubeck Wardenburg, J., Bae, T., Otto, M., Deleo, F.R. Schneewind, O. (2007) Poring over pores: alpha-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia. Nat Med 13 : 1405 1406.
    • (2007) Nat Med , vol.13 , pp. 1405-1406
    • Bubeck Wardenburg, J.1    Bae, T.2    Otto, M.3    Deleo, F.R.4    Schneewind, O.5
  • 8
    • 34047266670 scopus 로고    scopus 로고
    • Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection
    • Burlak, C., Hammer, C.H., Robinson, M.A., Whitney, A.R., McGavin, M.J., Kreiswirth, B.N. Deleo, F.R. (2007) Global analysis of community-associated methicillin-resistant Staphylococcus aureus exoproteins reveals molecules produced in vitro and during infection. Cell Microbiol 9 : 1172 1190.
    • (2007) Cell Microbiol , vol.9 , pp. 1172-1190
    • Burlak, C.1    Hammer, C.H.2    Robinson, M.A.3    Whitney, A.R.4    McGavin, M.J.5    Kreiswirth, B.N.6    Deleo, F.R.7
  • 10
    • 0037930846 scopus 로고    scopus 로고
    • Maturation processing and characterization of Streptopain
    • Chen, C.Y., Luo, S.C., Kuo, C.F., Lin, Y.S., Wu, J.J., Lin, M.T., et al. (2003) Maturation processing and characterization of Streptopain. J Biol Chem 278 : 17336 17343.
    • (2003) J Biol Chem , vol.278 , pp. 17336-17343
    • Chen, C.Y.1    Luo, S.C.2    Kuo, C.F.3    Lin, Y.S.4    Wu, J.J.5    Lin, M.T.6
  • 11
    • 34250370517 scopus 로고    scopus 로고
    • Distribution of Protein A on the surface of Staphylococcus aureus
    • DeDent, A.C., McAdow, M. Schneewind, O. (2007) Distribution of Protein A on the surface of Staphylococcus aureus. J Bacteriol 189 : 4473 4484.
    • (2007) J Bacteriol , vol.189 , pp. 4473-4484
    • Dedent, A.C.1    McAdow, M.2    Schneewind, O.3
  • 12
    • 54349128596 scopus 로고    scopus 로고
    • Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus
    • DeDent, A., Bae, T., Missiakas, D.M. Schneewind, O. (2008) Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus. EMBO J 27 : 2656 2668.
    • (2008) EMBO J , vol.27 , pp. 2656-2668
    • Dedent, A.1    Bae, T.2    Missiakas, D.M.3    Schneewind, O.4
  • 13
    • 0033168439 scopus 로고    scopus 로고
    • Autocatalytic processing of the Streptococcal cysteine protease zymogen: Processing mechanism and characterization of the autoproteolytic cleavage sites
    • Doran, J.D., Nomizu, M., Takebe, S., Menard, R., Griffith, D. Ziomek, E. (1999) Autocatalytic 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
    • 33846567123 scopus 로고    scopus 로고
    • The Staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity
    • Dubin, G., Wladyka, B., Stec-Niemczyk, J., Chmiel, D., Zdzalik, M., Dubin, A. Potempa, J. (2007) The Staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity. Biol Chem 388 : 227 235.
    • (2007) Biol Chem , vol.388 , pp. 227-235
    • Dubin, G.1    Wladyka, B.2    Stec-Niemczyk, J.3    Chmiel, D.4    Zdzalik, M.5    Dubin, A.6    Potempa, J.7
  • 15
    • 0034647756 scopus 로고    scopus 로고
    • Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases
    • Jr
    • Feltzer, R.E., Gray, R.D., Dean, W.L. Pierce, W.M., Jr (2000) Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases. J Biol Chem 275 : 21002 21009.
    • (2000) J Biol Chem , vol.275 , pp. 21002-21009
    • Feltzer, R.E.1    Gray, R.D.2    Dean, W.L.3    Pierce, W.M.4
  • 16
    • 0142039915 scopus 로고    scopus 로고
    • The Staphostatin-Staphopain complex: A forward binding inhibitor in complex with its target cysteine protease
    • Filipek, R., Rzychon, M., Oleksy, A., Gruca, M., Dubin, A., Potempa, J. Bochtler, M. (2003) The Staphostatin-Staphopain complex: a forward binding inhibitor in complex with its target cysteine protease. J Biol Chem 278 : 40959 40966.
    • (2003) J Biol Chem , vol.278 , pp. 40959-40966
    • Filipek, R.1    Rzychon, M.2    Oleksy, A.3    Gruca, M.4    Dubin, A.5    Potempa, J.6    Bochtler, M.7
  • 17
    • 8344267637 scopus 로고    scopus 로고
    • Prostaphopain B structure: A comparison of proregion-mediated and Staphostatin-mediated protease inhibition
    • Filipek, R., Szczepanowski, R., Sabat, A., Potempa, J. Bochtler, M. (2004) Prostaphopain B structure: a comparison of proregion-mediated and Staphostatin-mediated protease inhibition. Biochemistry 43 : 14306 14315.
    • (2004) Biochemistry , vol.43 , pp. 14306-14315
    • Filipek, R.1    Szczepanowski, R.2    Sabat, A.3    Potempa, J.4    Bochtler, M.5
  • 18
    • 17644400742 scopus 로고    scopus 로고
    • A comparison of Staphostatin B with standard mechanism serine protease inhibitors
    • Filipek, R., Potempa, J. Bochtler, M. (2005) A comparison of Staphostatin B with standard mechanism serine protease inhibitors. J Biol Chem 280 : 14669 14674.
    • (2005) J Biol Chem , vol.280 , pp. 14669-14674
    • Filipek, R.1    Potempa, J.2    Bochtler, M.3
  • 19
    • 34548091305 scopus 로고    scopus 로고
    • Potential associations between hematogenous complications and bacterial genotype in Staphylococcus aureus infection
    • Fowler, V.G. Nelson, C.L., McIntyre, L.M., Kreiswirth, B.N., Monk, A., Archer, G.L., et al. (2007) Potential associations between hematogenous complications and bacterial genotype in Staphylococcus aureus infection. J Infect Dis 196 : 738 747.
    • (2007) J Infect Dis , vol.196 , pp. 738-747
    • Fowler, V.G.1    Nelson, C.L.2    McIntyre, L.M.3    Kreiswirth, B.N.4    Monk, A.5    Archer, G.L.6
  • 20
    • 0034596066 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. the inhibitory and chaperone functions of the Subtilisin propeptide are not obligatorily linked
    • Fu, X., Inouye, M. Shinde, U. (2000) Folding pathway mediated by an intramolecular chaperone. The inhibitory and chaperone functions of the Subtilisin propeptide are not obligatorily linked. J Biol Chem 275 : 16871 16878.
    • (2000) J Biol Chem , vol.275 , pp. 16871-16878
    • Fu, X.1    Inouye, M.2    Shinde, U.3
  • 21
    • 10044261761 scopus 로고    scopus 로고
    • Genetic characterization of Staphopain genes in Staphylococcus aureus
    • Golonka, E., Filipek, R., Sabat, A., Sinczak, A. Potempa, J. (2004) Genetic characterization of Staphopain genes in Staphylococcus aureus. Biol Chem 385 : 1059 1067.
    • (2004) Biol Chem , vol.385 , pp. 1059-1067
    • Golonka, E.1    Filipek, R.2    Sabat, A.3    Sinczak, A.4    Potempa, J.5
  • 22
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J. Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter. J Bacteriol 177 : 4121 4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 23
    • 0026088819 scopus 로고
    • The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin
    • Guzzo, J., Duong, F., Wandersman, C., Murgier, M. Lazdunski, A. (1991) The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coli alpha-haemolysin. Mol Microbiol 5 : 447 453.
    • (1991) Mol Microbiol , vol.5 , pp. 447-453
    • Guzzo, J.1    Duong, F.2    Wandersman, C.3    Murgier, M.4    Lazdunski, A.5
  • 24
    • 0000796142 scopus 로고
    • Crystal structure of a thiol protease proteinase from Staphylococcus aureus V-8 in the E-64 inhibitor complex
    • Hofmann, B., Schomburg, D. Hecht, H.J. (1993) Crystal structure of a thiol protease proteinase from Staphylococcus aureus V-8 in the E-64 inhibitor complex. Acta Crystallogr A49 (Suppl 102.
    • (1993) Acta Crystallogr , vol.49 , Issue.SUPPL , pp. 102
    • Hofmann, B.1    Schomburg, D.2    Hecht, H.J.3
  • 25
    • 33646907087 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding
    • Horwich, A.L., Farr, G.W. Fenton, W.A. (2006) GroEL-GroES-mediated protein folding. Chem Rev 106 : 1917 1930.
    • (2006) Chem Rev , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 26
    • 0037122769 scopus 로고    scopus 로고
    • Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability
    • Jaswal, S.S., Sohl, J.L., Davis, J.H. Agard, D.A. (2002) Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature 415 : 343 346.
    • (2002) Nature , vol.415 , pp. 343-346
    • Jaswal, S.S.1    Sohl, J.L.2    Davis, J.H.3    Agard, D.A.4
  • 27
    • 14644412777 scopus 로고    scopus 로고
    • Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases
    • Jaswal, S.S., Truhlar, S.M., Dill, K.A. Agard, D.A. (2005) Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. J Mol Biol 347 : 355 366.
    • (2005) J Mol Biol , vol.347 , pp. 355-366
    • Jaswal, S.S.1    Truhlar, S.M.2    Dill, K.A.3    Agard, D.A.4
  • 28
    • 22644433729 scopus 로고    scopus 로고
    • SpeB-Spi: A novel protease-inhibitor pair from Streptococcus pyogenes
    • Kagawa, T.F., O'Toole, P.W. Cooney, J.C. (2005) SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes. Mol Microbiol 57 : 650 666.
    • (2005) Mol Microbiol , vol.57 , pp. 650-666
    • Kagawa, T.F.1    O'Toole, P.W.2    Cooney, J.C.3
  • 29
    • 0028021766 scopus 로고
    • The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor
    • Kessler, E. Safrin, M. (1994) The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor. J Biol Chem 269 : 22726 22731.
    • (1994) J Biol Chem , vol.269 , pp. 22726-22731
    • Kessler, E.1    Safrin, M.2
  • 30
    • 55849097322 scopus 로고    scopus 로고
    • Identification of the genetic basis for clinical menadione-auxotrophic small-colony variant isolates of Staphylococcus aureus
    • Lannergard, J., von Eiff, C., Sander, G., Cordes, T., Seggewiss, J., Peters, G., et al. (2008) Identification of the genetic basis for clinical menadione-auxotrophic small-colony variant isolates of Staphylococcus aureus. Antimicrob Agents Chemother 52 : 4017 4022.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 4017-4022
    • Lannergard, J.1    Von Eiff, C.2    Sander, G.3    Cordes, T.4    Seggewiss, J.5    Peters, G.6
  • 31
    • 0030831592 scopus 로고    scopus 로고
    • Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth
    • Leloup, L., Haddaoui el, A., Chambert, R. Petit-Glatron, M.F. (1997) Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth. Microbiology 143 : 3295 3303.
    • (1997) Microbiology , vol.143 , pp. 3295-3303
    • Leloup, L.1    Haddaoui El, A.2    Chambert, R.3    Petit-Glatron, M.F.4
  • 32
    • 0033025721 scopus 로고    scopus 로고
    • Kinetics of the secretion of Bacillus subtilis levanase overproduced during the exponential phase of growth
    • Leloup, L., Le Saux, J., Petit-Glatron, M.F. Chambert, R. (1999) Kinetics of the secretion of Bacillus subtilis levanase overproduced during the exponential phase of growth. Microbiology 145 : 613 619.
    • (1999) Microbiology , vol.145 , pp. 613-619
    • Leloup, L.1    Le Saux, J.2    Petit-Glatron, M.F.3    Chambert, R.4
  • 33
    • 65249172002 scopus 로고    scopus 로고
    • Evolution of virulence in epidemic community-associated methicillin-resistant Staphylococcus aureus
    • Li, M., Diep, B.A., Villaruz, A.E., Braughton, K.R., Jiang, X., DeLeo, F.R., et al. (2009) Evolution of virulence in epidemic community-associated methicillin-resistant Staphylococcus aureus. Proc Natl Acad Sci USA 106 : 5883 5888.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5883-5888
    • Li, M.1    Diep, B.A.2    Villaruz, A.E.3    Braughton, K.R.4    Jiang, X.5    Deleo, F.R.6
  • 34
    • 0000686715 scopus 로고
    • Streptococcal Proteinase: The zymogen to enzyme transfromation
    • Liu, T.Y. Elliott, S.D. (1965) Streptococcal Proteinase: the zymogen to enzyme transfromation. J Biol Chem 240 : 1138 1142.
    • (1965) J Biol Chem , vol.240 , pp. 1138-1142
    • Liu, T.Y.1    Elliott, S.D.2
  • 35
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy, F.D. (1998) Staphylococcus aureus infections. N Engl J Med 339 : 520 532.
    • (1998) N Engl J Med , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 36
    • 0024437119 scopus 로고
    • Construction, transfer and properties of a novel temperature-sensitive integrable plasmid for genomic analysis of Staphylococcus aureus
    • Luchansky, J.B., Benson, A.K. Atherly, A.G. (1989) Construction, transfer and properties of a novel temperature-sensitive integrable plasmid for genomic analysis of Staphylococcus aureus. Mol Microbiol 3 : 65 78.
    • (1989) Mol Microbiol , vol.3 , pp. 65-78
    • Luchansky, J.B.1    Benson, A.K.2    Atherly, A.G.3
  • 37
    • 0031004994 scopus 로고    scopus 로고
    • Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease
    • McGavin, M.J., Zahradka, C., Rice, K. Scott, J.E. (1997) Modification of the Staphylococcus aureus fibronectin binding phenotype by V8 protease. Infect Immun 65 : 2621 2628.
    • (1997) Infect Immun , vol.65 , pp. 2621-2628
    • McGavin, M.J.1    Zahradka, C.2    Rice, K.3    Scott, J.E.4
  • 38
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • McIver, K.S., Kessler, E., Olson, J.C. Ohman, D.E. (1995) The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol Microbiol 18 : 877 889.
    • (1995) Mol Microbiol , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 39
    • 0034017033 scopus 로고    scopus 로고
    • Staphylococcus aureus small colony variants, electron transport and persistent infections
    • McNamara, P.J. Proctor, R.A. (2000) Staphylococcus aureus small colony variants, electron transport and persistent infections. Int J Antimicrob Agents 14 : 117 122.
    • (2000) Int J Antimicrob Agents , vol.14 , pp. 117-122
    • McNamara, P.J.1    Proctor, R.A.2
  • 40
    • 0036830351 scopus 로고    scopus 로고
    • Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus
    • Massimi, I., Park, E., Rice, K., Muller-Esterl, W., Sauder, D. McGavin, M.J. (2002) Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus. J Biol Chem 277 : 41770 41777.
    • (2002) J Biol Chem , vol.277 , pp. 41770-41777
    • Massimi, I.1    Park, E.2    Rice, K.3    Muller-Esterl, W.4    Sauder, D.5    McGavin, M.J.6
  • 41
    • 36349012610 scopus 로고    scopus 로고
    • Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing
    • Nickerson, N.N., Prasad, L., Jacob, L., Delbaere, L.T. McGavin, M.J. (2007) Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing. J Biol Chem 282 : 34129 34138.
    • (2007) J Biol Chem , vol.282 , pp. 34129-34138
    • Nickerson, N.N.1    Prasad, L.2    Jacob, L.3    Delbaere, L.T.4    McGavin, M.J.5
  • 42
    • 50049092370 scopus 로고    scopus 로고
    • Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain
    • Nickerson, N.N., Joag, V. McGavin, M.J. (2008) Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain. Mol Microbiol 69 : 1530 1543.
    • (2008) Mol Microbiol , vol.69 , pp. 1530-1543
    • Nickerson, N.N.1    Joag, V.2    McGavin, M.J.3
  • 43
    • 0036947393 scopus 로고    scopus 로고
    • The protein encoded at the 3′ end of the serine protease gene of Aeromonas sobria functions as a chaperone in the production of the protease
    • Nomura, T., Fujii, Y., Yamanaka, H., Kobayashi, H. Okamoto, K. (2002) The protein encoded at the 3′ end of the serine protease gene of Aeromonas sobria functions as a chaperone in the production of the protease. J Bacteriol 184 : 7058 7061.
    • (2002) J Bacteriol , vol.184 , pp. 7058-7061
    • Nomura, T.1    Fujii, Y.2    Yamanaka, H.3    Kobayashi, H.4    Okamoto, K.5
  • 44
    • 0025837196 scopus 로고
    • Genetic systems in Staphylococci
    • Novick, R.P. (1991) Genetic systems in Staphylococci. Methods Enzymol 204 : 587 636.
    • (1991) Methods Enzymol , vol.204 , pp. 587-636
    • Novick, R.P.1
  • 45
    • 0027960065 scopus 로고
    • MSCRAMM-mediated adherence of microorganisms to host tissues
    • Patti, J.M., Allen, B.L., McGavin, M.J. Hook, M. (1994) MSCRAMM-mediated adherence of microorganisms to host tissues. Annu Rev Microbiol 48 : 585 617.
    • (1994) Annu Rev Microbiol , vol.48 , pp. 585-617
    • Patti, J.M.1    Allen, B.L.2    McGavin, M.J.3    Hook, M.4
  • 46
    • 0028074251 scopus 로고
    • Microbial adhesins recognizing extracellular matrix macromolecules
    • Patti, J.M. Hook, M. (1994) Microbial adhesins recognizing extracellular matrix macromolecules. Curr Opin Cell Biol 6 : 752 758.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 752-758
    • Patti, J.M.1    Hook, M.2
  • 47
    • 0023807526 scopus 로고
    • Cloning, characterization, and sequencing of an accessory gene regulator (agr) in Staphylococcus aureus
    • Peng, H.L., Novick, R.P., Kreiswirth, B., Kornblum, J. Schlievert, P. (1988) Cloning, characterization, and sequencing of an accessory gene regulator (agr) in Staphylococcus aureus. J Bacteriol 170 : 4365 4372.
    • (1988) J Bacteriol , vol.170 , pp. 4365-4372
    • Peng, H.L.1    Novick, R.P.2    Kreiswirth, B.3    Kornblum, J.4    Schlievert, P.5
  • 48
    • 0023149803 scopus 로고
    • Secretion of Bacillus subtilis levansucrase: A possible two-step mechanism
    • Petit-Glatron, M.F., Benyahia, F. Chambert, R. (1987) Secretion of Bacillus subtilis levansucrase: a possible two-step mechanism. Eur J Biochem 163 : 379 387.
    • (1987) Eur J Biochem , vol.163 , pp. 379-387
    • Petit-Glatron, M.F.1    Benyahia, F.2    Chambert, R.3
  • 49
    • 0025375220 scopus 로고
    • Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli
    • Phillips, G.J. Silhavy, T.J. (1990) Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. Nature 344 : 882 884.
    • (1990) Nature , vol.344 , pp. 882-884
    • Phillips, G.J.1    Silhavy, T.J.2
  • 50
    • 0023833788 scopus 로고
    • Degradation of elastin by a cysteine proteinase from Staphylococcus aureus
    • Potempa, J., Dubin, A., Korzus, G. Travis, J. (1988) Degradation of elastin by a cysteine proteinase from Staphylococcus aureus. J Biol Chem 263 : 2664 2667.
    • (1988) J Biol Chem , vol.263 , pp. 2664-2667
    • Potempa, J.1    Dubin, A.2    Korzus, G.3    Travis, J.4
  • 51
    • 22644435471 scopus 로고    scopus 로고
    • Fighting an enemy within: Cytoplasmic inhibitors of bacterial cysteine proteases
    • Potempa, J., Golonka, E., Filipek, R. Shaw, L.N. (2005) Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases. Mol Microbiol 57 : 605 610.
    • (2005) Mol Microbiol , vol.57 , pp. 605-610
    • Potempa, J.1    Golonka, E.2    Filipek, R.3    Shaw, L.N.4
  • 52
    • 33645084560 scopus 로고    scopus 로고
    • Small colony variants: A pathogenic form of bacteria that facilitates persistent and recurrent infections
    • Proctor, R.A., von Eiff, C., Kahl, B.C., Becker, K., McNamara, P., Herrmann, M. Peters, G. (2006) Small colony variants: a pathogenic form of bacteria that facilitates persistent and recurrent infections. Nat Rev Microbiol 4 : 295 305.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 295-305
    • Proctor, R.A.1    Von Eiff, C.2    Kahl, B.C.3    Becker, K.4    McNamara, P.5    Herrmann, M.6    Peters, G.7
  • 53
    • 0035167096 scopus 로고    scopus 로고
    • Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease
    • Rice, K., Peralta, R., Bast, D., de Azavedo, J. McGavin, M.J. (2001) Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. Infect Immun 69 : 159 169.
    • (2001) Infect Immun , vol.69 , pp. 159-169
    • Rice, K.1    Peralta, R.2    Bast, D.3    De Azavedo, J.4    McGavin, M.J.5
  • 54
    • 20144388398 scopus 로고    scopus 로고
    • Re-emergence of early pandemic Staphylococcus aureus as a community-acquired meticillin-resistant clone
    • Robinson, D.A., Kearns, A.M., Holmes, A., Morrison, D., Grundmann, G., Edwards, H., et al. (2005) Re-emergence of early pandemic Staphylococcus aureus as a community-acquired meticillin-resistant clone. Lancet 365 : 1256 1258.
    • (2005) Lancet , vol.365 , pp. 1256-1258
    • Robinson, D.A.1    Kearns, A.M.2    Holmes, A.3    Morrison, D.4    Grundmann, G.5    Edwards, H.6
  • 55
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch, J. Caparon, M. (2004) A microdomain for protein secretion in Gram-positive bacteria. Science 304 : 1513 1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 56
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: An organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch, J.W. Caparon, M.G. (2005) The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol Microbiol 58 : 959 968.
    • (2005) Mol Microbiol , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 57
    • 0042565975 scopus 로고    scopus 로고
    • Staphostatins: An expanding new group of proteinase inhibitors with a unique specificity for the regulation of Staphopains, Staphylococcus spp. cysteine proteinases
    • Rzychon, M., Sabat, A., Kosowska, K., Potempa, J. Dubin, A. (2003) Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of Staphopains, Staphylococcus spp. cysteine proteinases. Mol Microbiol 49 : 1051 1066.
    • (2003) Mol Microbiol , vol.49 , pp. 1051-1066
    • Rzychon, M.1    Sabat, A.2    Kosowska, K.3    Potempa, J.4    Dubin, A.5
  • 58
    • 14244266586 scopus 로고    scopus 로고
    • Cytoplasmic control of premature activation of a secreted protease zymogen: Deletion of Staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype
    • Shaw, L.N., Golonka, E., Szmyd, G., Foster, S.J., Travis, J. Potempa, J. (2005) Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of Staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype. J Bacteriol 187 : 1751 1762.
    • (2005) J Bacteriol , vol.187 , pp. 1751-1762
    • Shaw, L.N.1    Golonka, E.2    Szmyd, G.3    Foster, S.J.4    Travis, J.5    Potempa, J.6
  • 59
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E. Ehrlich, S.D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144 : 3097 3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 60
    • 33645504195 scopus 로고    scopus 로고
    • Identification of correct regions in protein models using structural, alignment, and consensus information
    • Wallner, B. Elofsson, A. (2006) Identification of correct regions in protein models using structural, alignment, and consensus information. Protein Sci 15 : 900 913.
    • (2006) Protein Sci , vol.15 , pp. 900-913
    • Wallner, B.1    Elofsson, A.2
  • 61
    • 39549121471 scopus 로고    scopus 로고
    • Vaccine protection against Staphylococcus aureus pneumonia
    • Wardenburg, J.B. Schneewind, O. (2008) Vaccine protection against Staphylococcus aureus pneumonia. J Exp Med 205 : 287 294.
    • (2008) J Exp Med , vol.205 , pp. 287-294
    • Wardenburg, J.B.1    Schneewind, O.2
  • 62
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of Gram-positive bacteria
    • van Wely, K.H., Swaving, J., Freudl, R. Driessen, A.J. (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.1    Swaving, J.2    Freudl, R.3    Driessen, A.J.4
  • 63
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild, J., Rossmeissl, P., Walter, W.A. Gross, C.A. (1996) Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J Bacteriol 178 : 3608 3613.
    • (1996) J Bacteriol , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 64
    • 12744279612 scopus 로고    scopus 로고
    • Efficient co-expression of a recombinant Staphopain A and its inhibitor Staphostatin A in Escherichia coli
    • Wladyka, B., Puzia, K. Dubin, A. (2005) Efficient co-expression of a recombinant Staphopain A and its inhibitor Staphostatin A in Escherichia coli. Biochem J 385 : 181 187.
    • (2005) Biochem J , vol.385 , pp. 181-187
    • Wladyka, B.1    Puzia, K.2    Dubin, A.3
  • 65
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin
    • Yabuta, Y., Takagi, H., Inouye, M. Shinde, U. (2001) Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J Biol Chem 276 : 44427 44434.
    • (2001) J Biol Chem , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.4
  • 66
    • 0035960883 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M
    • Yokoi, K., Kakikawa, M., Kimoto, H., Watanabe, K., Yasukawa, H., Yamakawa, A., et al. (2001) Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M. Gene 281 : 115 122.
    • (2001) Gene , vol.281 , pp. 115-122
    • Yokoi, K.1    Kakikawa, M.2    Kimoto, H.3    Watanabe, K.4    Yasukawa, H.5    Yamakawa, A.6
  • 67
  • 68
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou, H. Zhou, Y. (2002) Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 11 : 2714 2726.
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 69
    • 0028447557 scopus 로고
    • Purification of recombinant Shiga-like toxin type I, A1 fragment from Escherichia coli
    • Zollman, T.M., Austin, P.R., Jablonski, P.E. Hovde, C.J. (1994) Purification of recombinant Shiga-like toxin type I, A1 fragment from Escherichia coli. Protein Expr Purif 5 : 291 295.
    • (1994) Protein Expr Purif , vol.5 , pp. 291-295
    • Zollman, T.M.1    Austin, P.R.2    Jablonski, P.E.3    Hovde, C.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.