메뉴 건너뛰기




Volumn 197, Issue 4, 2015, Pages 762-773

Mep72, a metzincin protease that is preferentially secreted by biofilms of Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

ALGINIC ACID; ALKALINE PROTEINASE; CARBOHYDRATE BINDING PROTEIN; MEP72 PROTEIN; PROTEINASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR; BACTERIAL PROTEIN; BACTERIAL SECRETION SYSTEM; PEPTIDE HYDROLASE;

EID: 84921780616     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02404-14     Document Type: Article
Times cited : (20)

References (55)
  • 1
    • 0018896292 scopus 로고
    • Production of mucoid microcolonies by Pseudomonas aeruginosa within infected lungs in cystic fibrosis
    • Lam J, Chan R, Lam K, Costerton JW. 1980. Production of mucoid microcolonies by Pseudomonas aeruginosa within infected lungs in cystic fibrosis. Infect Immun 28:546-556.
    • (1980) Infect Immun , vol.28 , pp. 546-556
    • Lam, J.1    Chan, R.2    Lam, K.3    Costerton, J.W.4
  • 2
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan JR, Deretic V. 1996. Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol Rev 60:539-574.
    • (1996) Microbiol Rev , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 3
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: a common cause of persistent infections
    • Costerton JW, Stewart PS, Greenberg EP. 1999. Bacterial biofilms: a common cause of persistent infections. Science 284:1318-1322. http://dx.doi.org/10.1126/science.284.5418.1318.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 4
    • 0034641962 scopus 로고    scopus 로고
    • Quorum-sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms
    • Singh PK, Schaefer AL, Parsek MR, Moninger TO, Welsh MJ, Greenberg EP. 2000. Quorum-sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms. Nature 407:762-764. http://dx.doi.org/10.1038/35037627.
    • (2000) Nature , vol.407 , pp. 762-764
    • Singh, P.K.1    Schaefer, A.L.2    Parsek, M.R.3    Moninger, T.O.4    Welsh, M.J.5    Greenberg, E.P.6
  • 5
    • 0035077009 scopus 로고    scopus 로고
    • Riddle of biofilm resistance
    • Lewis K. 2001. Riddle of biofilm resistance. Antimicrob Agents Chemother 45:999-1007. http://dx.doi.org/10.1128/AAC.45.4.999-1007.2001.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 999-1007
    • Lewis, K.1
  • 6
    • 0242523776 scopus 로고    scopus 로고
    • Bacterial biofilms: an emerging link to disease pathogenesis
    • Parsek MR, Singh PK. 2003. Bacterial biofilms: an emerging link to disease pathogenesis. Annu Rev Microbiol 57:677-701. http://dx.doi.org/10.1146/annurev.micro.57.030502.090720.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 677-701
    • Parsek, M.R.1    Singh, P.K.2
  • 8
    • 0036157549 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm
    • Sauer K, Camper AK, Ehrlich GD, Costerton JW, Davies DG. 2002. Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm. J Bacteriol 184:1140-1154. http://dx.doi.org/10.1128/jb.184.4.1140-1154.2002.
    • (2002) J Bacteriol , vol.184 , pp. 1140-1154
    • Sauer, K.1    Camper, A.K.2    Ehrlich, G.D.3    Costerton, J.W.4    Davies, D.G.5
  • 9
    • 20644457332 scopus 로고    scopus 로고
    • Transcriptome analysis of Pseudomonas aeruginosa biofilm development: anaerobic respiration and iron limitation
    • Hentzer M, Eberl L, Givskov M. 2005. Transcriptome analysis of Pseudomonas aeruginosa biofilm development: anaerobic respiration and iron limitation. Biofilms 2:37-61. http://dx.doi.org/10.1017/S1479050505001699.
    • (2005) Biofilms , vol.2 , pp. 37-61
    • Hentzer, M.1    Eberl, L.2    Givskov, M.3
  • 10
    • 24944506408 scopus 로고    scopus 로고
    • Transcriptome analysis of Pseudomonas aeruginosa growth: comparison of gene expression in planktonic cultures and developing and mature biofilms
    • Waite RD, Papakonstantinopoulou A, Littler E, Curtis MA. 2005. Transcriptome analysis of Pseudomonas aeruginosa growth: comparison of gene expression in planktonic cultures and developing and mature biofilms. J Bacteriol 187:6571-6576. http://dx.doi.org/10.1128/JB.187.18.6571-6576.2005.
    • (2005) J Bacteriol , vol.187 , pp. 6571-6576
    • Waite, R.D.1    Papakonstantinopoulou, A.2    Littler, E.3    Curtis, M.A.4
  • 11
    • 64049084921 scopus 로고    scopus 로고
    • Biofilms and type III secretion are not mutually exclusive in Pseudomonas aeruginosa
    • Mikkelsen H, Bond NJ, Skindersoe ME, Givskov M, Lilley KS, Welch M. 2009. Biofilms and type III secretion are not mutually exclusive in Pseudomonas aeruginosa. Microbiology 155:687-698. http://dx.doi.org/10.1099/mic.0.025551-0.
    • (2009) Microbiology , vol.155 , pp. 687-698
    • Mikkelsen, H.1    Bond, N.J.2    Skindersoe, M.E.3    Givskov, M.4    Lilley, K.S.5    Welch, M.6
  • 13
    • 78649760128 scopus 로고    scopus 로고
    • Comparative microarray analysis reveals that the core biofilm-associated transcriptome of Pseudomonas aeruginosa comprises relatively few genes
    • Patell S, Gu M, Davenport P, Givskov M, Waite RD, Welch M. 2010. Comparative microarray analysis reveals that the core biofilm-associated transcriptome of Pseudomonas aeruginosa comprises relatively few genes. Environ Microbiol Rep 2:440-448. http://dx.doi.org/10.1111/j.1758-2229.2010.00158.x.
    • (2010) Environ Microbiol Rep , vol.2 , pp. 440-448
    • Patell, S.1    Gu, M.2    Davenport, P.3    Givskov, M.4    Waite, R.D.5    Welch, M.6
  • 14
    • 0031729127 scopus 로고    scopus 로고
    • Cell-to-cell signaling and Pseudomonas aeruginosa infections
    • Van Delden C, Iglewski BH. 1998. Cell-to-cell signaling and Pseudomonas aeruginosa infections. Emerg Infect Dis 4:551-560. http://dx.doi.org/10.3201/eid0404.980405.
    • (1998) Emerg Infect Dis , vol.4 , pp. 551-560
    • Van Delden, C.1    Iglewski, B.H.2
  • 15
    • 78549236798 scopus 로고    scopus 로고
    • Protein secretion systems in Pseudomonas aeruginosa: a wealth of pathogenic weapons
    • Bleves S, Viarre V, Salacha R, Michel GPF, Filloux A, Voulhoux R. 2010. Protein secretion systems in Pseudomonas aeruginosa: a wealth of pathogenic weapons. Int J Med Microbiol 300:534-543. http://dx.doi.org/10.1016/j.ijmm.2010.08.005.
    • (2010) Int J Med Microbiol , vol.300 , pp. 534-543
    • Bleves, S.1    Viarre, V.2    Salacha, R.3    Michel, G.P.F.4    Filloux, A.5    Voulhoux, R.6
  • 16
    • 0029801248 scopus 로고    scopus 로고
    • Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway
    • Yahr TL, Goranson J, Frank DW. 1996. Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway. Mol Microbiol 22:991-1003. http://dx.doi.org/10.1046/j.1365-2958.1996.01554.x.
    • (1996) Mol Microbiol , vol.22 , pp. 991-1003
    • Yahr, T.L.1    Goranson, J.2    Frank, D.W.3
  • 17
    • 0030731178 scopus 로고    scopus 로고
    • Identification of type III secreted products of the Pseudomonas aeruginosa exoenzyme S regulon
    • Yahr TL, Mende-Mueller LM, Friese MB, Frank DW. 1997. Identification of type III 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
  • 18
    • 0036191393 scopus 로고    scopus 로고
    • Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa
    • Hauser AR, Cobb E, Bodi M, Mariscal D, Vallés J, Engel JN, Rello J. 2002. Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa. Crit Care Med 30:521-528. http://dx.doi.org/10.1097/00003246-200203000-00005.
    • (2002) Crit Care Med , vol.30 , pp. 521-528
    • Hauser, A.R.1    Cobb, E.2    Bodi, M.3    Mariscal, D.4    Vallés, J.5    Engel, J.N.6    Rello, J.7
  • 20
    • 7744220530 scopus 로고    scopus 로고
    • A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa
    • Goodman AL, Kulasekara B, Rietsch A, Boyd D, Smith RS, Lory S. 2004. A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa. Dev Cell 7:745-754. http://dx.doi.org/10.1016/j.devcel.2004.08.020.
    • (2004) Dev Cell , vol.7 , pp. 745-754
    • Goodman, A.L.1    Kulasekara, B.2    Rietsch, A.3    Boyd, D.4    Smith, R.S.5    Lory, S.6
  • 22
    • 32444447802 scopus 로고    scopus 로고
    • Keeping their options open: acute versus persistent infections
    • Furukawa S, Kuchma SL, O'Toole GA. 2006. Keeping their options open: acute versus persistent infections. J Bacteriol 188:1211-1217. http://dx.doi.org/10.1128/JB.188.4.1211-1217.2006.
    • (2006) J Bacteriol , vol.188 , pp. 1211-1217
    • Furukawa, S.1    Kuchma, S.L.2    O'Toole, G.A.3
  • 24
    • 41949122329 scopus 로고    scopus 로고
    • In situ growth rates and biofilm development of Pseudomonas aeruginosa populations in chronic lung infections
    • Yang L, Haagensen JAJ, Jelsbak L, Johansen HK, Sternberg C, Høiby N, Molin S. 2008. In situ growth rates and biofilm development of Pseudomonas aeruginosa populations in chronic lung infections. J Bacteriol 190:2767-2776. http://dx.doi.org/10.1128/JB.01581-07.
    • (2008) J Bacteriol , vol.190 , pp. 2767-2776
    • Yang, L.1    Haagensen, J.A.J.2    Jelsbak, L.3    Johansen, H.K.4    Sternberg, C.5    Høiby, N.6    Molin, S.7
  • 25
    • 84867315903 scopus 로고    scopus 로고
    • Calcium chelation by alginate activates the type III secretion system in mucoid Pseudomonas aeruginosa biofilms
    • Horsman SR, Moore RA, Lewenza S. 2012. Calcium chelation by alginate activates the type III secretion system in mucoid Pseudomonas aeruginosa biofilms. PLoS One 7:e46826. http://dx.doi.org/10.1371/journal.pone.0046826.
    • (2012) PLoS One , vol.7
    • Horsman, S.R.1    Moore, R.A.2    Lewenza, S.3
  • 26
    • 0347182852 scopus 로고    scopus 로고
    • Identification of quorum-sensing regulated proteins in the opportunistic pathogen Pseudomonas aeruginosa by proteomics
    • Arevalo-Ferro C, Hentzer M, Reil G, Görg A, Kjelleberg S, Givskov M, Riedel K, Eberl L. 2003. Identification of quorum-sensing regulated proteins in the opportunistic pathogen Pseudomonas aeruginosa by proteomics. Environ Microbiol 5:1350-1369. http://dx.doi.org/10.1046/j.1462-2920.2003.00532.x.
    • (2003) Environ Microbiol , vol.5 , pp. 1350-1369
    • Arevalo-Ferro, C.1    Hentzer, M.2    Reil, G.3    Görg, A.4    Kjelleberg, S.5    Givskov, M.6    Riedel, K.7    Eberl, L.8
  • 27
    • 0038486028 scopus 로고    scopus 로고
    • Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1
    • Nouwens AS, Beatson SA, Whitchurch CB, Walsh BJ, Schweizer HP, Mattick JS, Cordwell SJ. 2003. Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1. Microbiology 149:1311-1322. http://dx.doi.org/10.1099/mic.0.25967-0.
    • (2003) Microbiology , vol.149 , pp. 1311-1322
    • Nouwens, A.S.1    Beatson, S.A.2    Whitchurch, C.B.3    Walsh, B.J.4    Schweizer, H.P.5    Mattick, J.S.6    Cordwell, S.J.7
  • 28
    • 17644395614 scopus 로고    scopus 로고
    • Expression of the quorum-sensing regulatory protein LasR is strongly affected by iron and oxygen concentrations in cultures of Pseudomonas aeruginosa irrespective of cell density
    • Kim E-J, Wang W, Deckwer W-D, Zeng A-P. 2005. Expression of the quorum-sensing regulatory protein LasR is strongly affected by iron and oxygen concentrations in cultures of Pseudomonas aeruginosa irrespective of cell density. Microbiology 151:1127-1138. http://dx.doi.org/10.1099/mic.0.27566-0.
    • (2005) Microbiology , vol.151 , pp. 1127-1138
    • Kim, E.-J.1    Wang, W.2    Deckwer, W.-D.3    Zeng, A.-P.4
  • 29
    • 33646452555 scopus 로고    scopus 로고
    • Quorum-sensing antagonistic activities of azithromycin in Pseudomonas aeruginosa PAO1: a global approach
    • Nalca Y, Jänsch L, Bredenbruch F, Geffers R, Buer J, Häussler S. 2006. Quorum-sensing antagonistic activities of azithromycin in Pseudomonas aeruginosa PAO1: a global approach. Antimicrob Agents Chemother 50:1680-1688. http://dx.doi.org/10.1128/AAC.50.5.1680-1688.2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1680-1688
    • Nalca, Y.1    Jänsch, L.2    Bredenbruch, F.3    Geffers, R.4    Buer, J.5    Häussler, S.6
  • 30
    • 84867467871 scopus 로고    scopus 로고
    • Identification of proteins associated with the Pseudomonas aeruginosa biofilm extracellular matrix
    • Toyofuku M, Roschitzki B, Riedel K, Eberl L. 2012. Identification of proteins associated with the Pseudomonas aeruginosa biofilm extracellular matrix. J Proteome Res 11:4906-4915. http://dx.doi.org/10.1021/pr300395j.
    • (2012) J Proteome Res , vol.11 , pp. 4906-4915
    • Toyofuku, M.1    Roschitzki, B.2    Riedel, K.3    Eberl, L.4
  • 31
    • 21144449112 scopus 로고    scopus 로고
    • Calcium-induced virulence factors associated with the extracellular matrix of mucoid Pseudomonas aeruginosa biofilms
    • Sarkisova S, Patrauchan MA, Berglund D, Nivens DE, Franklin MJ. 2005. Calcium-induced virulence factors associated with the extracellular matrix of mucoid Pseudomonas aeruginosa biofilms. J Bacteriol 187::4327-4337. http://dx.doi.org/10.1128/JB.187.13.4327-4337.2005.
    • (2005) J Bacteriol , vol.187 , pp. 4327-4337
    • Sarkisova, S.1    Patrauchan, M.A.2    Berglund, D.3    Nivens, D.E.4    Franklin, M.J.5
  • 32
    • 84870673207 scopus 로고    scopus 로고
    • Flexible survival strategies of Pseudomonas aeruginosa in biofilms result in increased fitness compared with Candida albicans
    • Purschke FG, Hiller E, Trick I, Rupp S. 2012. Flexible survival strategies of Pseudomonas aeruginosa in biofilms result in increased fitness compared with Candida albicans. Mol Cell Proteomics 11:1652-1669. http://dx.doi.org/10.1074/mcp. M112.017673.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1652-1669
    • Purschke, F.G.1    Hiller, E.2    Trick, I.3    Rupp, S.4
  • 33
    • 76449122382 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa uses a cyclic-di-GMPregulated adhesin to reinforce the biofilm extracellular matrix
    • Borlee BR, Goldman AD, Murakami K, Samudrala R, Wozniak DJ, Parsek MR. 2010. Pseudomonas aeruginosa uses a cyclic-di-GMPregulated adhesin to reinforce the biofilm extracellular matrix. Mol Microbiol 75:827-842. http://dx.doi.org/10.1111/j.1365-2958.2009.06991.x.
    • (2010) Mol Microbiol , vol.75 , pp. 827-842
    • Borlee, B.R.1    Goldman, A.D.2    Murakami, K.3    Samudrala, R.4    Wozniak, D.J.5    Parsek, M.R.6
  • 34
    • 84888221457 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas aeruginosa metalloendopeptidase, Mep72, a member of the Vfr regulon
    • Balyimez A, Colmer-Hamood JA, Francisco MS, Hamood AN. 2013. Characterization of the Pseudomonas aeruginosa metalloendopeptidase, Mep72, a member of the Vfr regulon. BMC Microbiol 13:269. http://dx.doi.org/10.1186/1471-2180-13-269.
    • (2013) BMC Microbiol , vol.13 , pp. 269
    • Balyimez, A.1    Colmer-Hamood, J.A.2    Francisco, M.S.3    Hamood, A.N.4
  • 35
    • 33947181889 scopus 로고    scopus 로고
    • Interrelationships between colonies, biofilms, and planktonic cells of Pseudomonas aeruginosa
    • Mikkelsen H, Duck Z, Lilley KS, Welch M. 2007. Interrelationships between colonies, biofilms, and planktonic cells of Pseudomonas aeruginosa. J Bacteriol 189:2411-2416. http://dx.doi.org/10.1128/JB.01687-06.
    • (2007) J Bacteriol , vol.189 , pp. 2411-2416
    • Mikkelsen, H.1    Duck, Z.2    Lilley, K.S.3    Welch, M.4
  • 36
    • 33646462432 scopus 로고    scopus 로고
    • Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1
    • Kwon DH, Lu C-D. 2006. Polyamines induce resistance to cationic peptide, aminoglycoside, and quinolone antibiotics in Pseudomonas aeruginosa PAO1. Antimicrob Agents Chemother 50:1615-1622. http://dx.doi.org/10.1128/AAC.50.5.1615-1622.2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1615-1622
    • Kwon, D.H.1    Lu, C.-D.2
  • 37
    • 33646461534 scopus 로고    scopus 로고
    • Polyamines increase antibiotic susceptibility in Pseudomonas aeruginosa
    • Kwon DH, Lu C-D. 2006. Polyamines increase antibiotic susceptibility in Pseudomonas aeruginosa. Antimicrob Agents Chemother 50:1623-1627. http://dx.doi.org/10.1128/AAC.50.5.1623-1627.2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1623-1627
    • Kwon, D.H.1    Lu, C.-D.2
  • 38
    • 34250176184 scopus 로고    scopus 로고
    • Polyamine effects on antibiotic susceptibility in bacteria
    • Kwon D-H, Lu C-D. 2007. Polyamine effects on antibiotic susceptibility in bacteria. Antimicrob Agents Chemother 51:2070-2077. http://dx.doi.org/10.1128/AAC.01472-06.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2070-2077
    • Kwon, D.-H.1    Lu, C.-D.2
  • 39
    • 0034873465 scopus 로고    scopus 로고
    • Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa
    • Wilderman PJ, Vasil AI, Johnson Z, Wilson MJ, Cunliffe HE, Lamont IL, Vasil ML. 2001. Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa. Infect Immun 69::5385-5394. http://dx.doi.org/10.1128/IAI.69.9.5385-5394.2001.
    • (2001) Infect Immun , vol.69 , pp. 5385-5394
    • Wilderman, P.J.1    Vasil, A.I.2    Johnson, Z.3    Wilson, M.J.4    Cunliffe, H.E.5    Lamont, I.L.6    Vasil, M.L.7
  • 40
    • 0033953969 scopus 로고    scopus 로고
    • Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa
    • Folders J, Tommassen J, van Loon LC, Bitter W. 2000. Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa. J Bacteriol 182:1257-1263. http://dx.doi.org/10.1128/JB.182.5.1257-1263.2000.
    • (2000) J Bacteriol , vol.182 , pp. 1257-1263
    • Folders, J.1    Tommassen, J.2    van Loon, L.C.3    Bitter, W.4
  • 41
    • 58149200939 scopus 로고    scopus 로고
    • DOOR: a database for prokaryotic operons
    • Mao F, Dam P, Chou J, Olman V, Xu Y. 2009. DOOR: a database for prokaryotic operons. Nucleic Acids Res 37:D459-D463. http://dx.doi.org/10.1093/nar/gkn757.
    • (2009) Nucleic Acids Res , vol.37 , pp. D459-D463
    • Mao, F.1    Dam, P.2    Chou, J.3    Olman, V.4    Xu, Y.5
  • 42
    • 0026671355 scopus 로고
    • Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry
    • Murzin AG. 1992. Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. Proteins 14:191-201. http://dx.doi.org/10.1002/prot.340140206.
    • (1992) Proteins , vol.14 , pp. 191-201
    • Murzin, A.G.1
  • 43
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor
    • Yeats C, Bentley S, Bateman A. 2003. New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor. BMC Microbiol 3:3. http://dx.doi.org/10.1186/1471-2180-3-3.
    • (2003) BMC Microbiol , vol.3 , pp. 3
    • Yeats, C.1    Bentley, S.2    Bateman, A.3
  • 44
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. 2001. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310:243-257. http://dx.doi.org/10.1006/jmbi.2001.4762.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 46
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Rüth FX. 2003. Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotechnol 24:157-202. http://dx.doi.org/10.1385/MB:24:2:157.
    • (2003) Mol Biotechnol , vol.24 , pp. 157-202
    • Gomis-Rüth, F.X.1
  • 47
    • 0025804758 scopus 로고
    • Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families
    • Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Warren RA. 1991. Domains in microbial beta-1,4-glycanases: sequence conservation, function, and enzyme families. Microbiol Rev 55:303-315.
    • (1991) Microbiol Rev , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller, R.C.4    Warren, R.A.5
  • 48
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball G, Chapon-Hervé V, Bleves S, Michel G, Bally M. 1999. Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J Bacteriol 181:382-388.
    • (1999) J Bacteriol , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Hervé, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 49
    • 0034647756 scopus 로고    scopus 로고
    • Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases
    • Feltzer RE, Gray RD, Dean WL, Pierce WM. 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. http://dx.doi.org/10.1074/jbc. M002088200.
    • (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
  • 50
    • 0035860712 scopus 로고    scopus 로고
    • Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond
    • Hege T, Feltzer RE, Gray RD, Baumann U. 2001. Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond. J Biol Chem 276:35087-35092. http://dx.doi.org/10.1074/jbc. M104020200.
    • (2001) J Biol Chem , vol.276 , pp. 35087-35092
    • Hege, T.1    Feltzer, R.E.2    Gray, R.D.3    Baumann, U.4
  • 51
    • 84855848528 scopus 로고    scopus 로고
    • Inhibition of Pseudomonas aeruginosa virulence: characterization of the AprA-AprI interface and species selectivity
    • Bardoel BW, van Kessel KPM, van Strijp JAG, Milder FJ. 2012. Inhibition of Pseudomonas aeruginosa virulence: characterization of the AprA-AprI interface and species selectivity. J Mol Biol 415:573-583. http://dx.doi.org/10.1016/j.jmb.2011.11.039.
    • (2012) J Mol Biol , vol.415 , pp. 573-583
    • Bardoel, B.W.1    van Kessel, K.P.M.2    van Strijp, J.A.G.3    Milder, F.J.4
  • 52
    • 0035869555 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa protease IV enzyme assays and comparison to other Pseudomonas proteases
    • Caballero AR, Moreau JM, Engel LS, Marquart ME, Hill JM, O'Callaghan RJ. 2001. Pseudomonas aeruginosa protease IV enzyme assays and comparison to other Pseudomonas proteases. Anal Biochem 290::330-337. http://dx.doi.org/10.1006/abio.2001.4999.
    • (2001) Anal Biochem , vol.290 , pp. 330-337
    • Caballero, A.R.1    Moreau, J.M.2    Engel, L.S.3    Marquart, M.E.4    Hill, J.M.5    O'Callaghan, R.J.6
  • 53
    • 0032515142 scopus 로고    scopus 로고
    • Elastase and the LasA protease of Pseudomonas aeruginosa are secreted with their propeptides
    • Kessler E, Safrin M, Gustin JK, Ohman DE. 1998. Elastase and the LasA protease of Pseudomonas aeruginosa are secreted with their propeptides. J Biol Chem 273:30225-30231. http://dx.doi.org/10.1074/jbc.273.46.30225.
    • (1998) J Biol Chem , vol.273 , pp. 30225-30231
    • Kessler, E.1    Safrin, M.2    Gustin, J.K.3    Ohman, D.E.4
  • 54
    • 0031781189 scopus 로고    scopus 로고
    • Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa
    • Braun P, de Groot A, Bitter W, Tommassen J. 1998. Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J Bacteriol 180:3467-3469.
    • (1998) J Bacteriol , vol.180 , pp. 3467-3469
    • Braun, P.1    de Groot, A.2    Bitter, W.3    Tommassen, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.