메뉴 건너뛰기




Volumn 72, Issue 4, 2009, Pages 895-904

Evidence for a dual role of PBP1 in the cell division and cell separation of Staphylococcus aureus

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA GLUTAMYLTRANSFERASE; MUTANT PROTEIN; PENICILLIN BINDING PROTEIN;

EID: 65549166382     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06687.x     Document Type: Article
Times cited : (51)

References (46)
  • 1
    • 35648932478 scopus 로고    scopus 로고
    • Perturbation of cell wall synthesis suppresses autolysis in Staphylococcus aureus: Evidence for coregulation of cell wall synthetic and hydrolytic enzymes
    • DOI 10.1128/JB.01048-07
    • Antignac, A., Sieradzki, K. Tomasz, A. (2007) Perturbation of cell wall synthesis suppresses autolysis in Staphylococcus aureus: evidence for coregulation of cell wall synthetic and hydrolytic enzymes. J Bacteriol 189 : 7573 7580. (Pubitemid 350035066)
    • (2007) Journal of Bacteriology , vol.189 , Issue.21 , pp. 7573-7580
    • Antignac, A.1    Sieradzki, K.2    Tomasz, A.3
  • 2
    • 0022998431 scopus 로고
    • Characterization of an isogenic set of methicillin-resistant and susceptible mutants of Staphylococcus aureus
    • Berger-Bachi, B., Strassle, A. Kayser, F.H. (1986) Characterization of an isogenic set of methicillin-resistant and susceptible mutants of Staphylococcus aureus. Eur J Clin Microbiol 5 : 697 701. (Pubitemid 17213584)
    • (1986) European Journal of Clinical Microbiology , vol.5 , Issue.6 , pp. 697-701
    • Berger-Bachi, B.1    Strassle, A.2    Kayser, F.H.3
  • 3
    • 0019511038 scopus 로고
    • Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation
    • Botta, G.A. Park, J.T. (1981) Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation. J Bacteriol 145 : 333 340. (Pubitemid 11140310)
    • (1981) Journal of Bacteriology , vol.145 , Issue.1 , pp. 333-340
    • Botta, G.A.1    Park, J.T.2
  • 4
    • 53849143253 scopus 로고    scopus 로고
    • Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain
    • Costa, T., Priyadarshini, R. Jacobs-Wagner, C. (2008) Localization of PBP3 in Caulobacter crescentus is highly dynamic and largely relies on its functional transpeptidase domain. Mol Microbiol 70 : 634 651.
    • (2008) Mol Microbiol , vol.70 , pp. 634-651
    • Costa, T.1    Priyadarshini, R.2    Jacobs-Wagner, C.3
  • 5
    • 0033985396 scopus 로고    scopus 로고
    • Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis
    • DOI 10.1046/j.1365-2958.2000.01724.x
    • Daniel, R.A., Harry, E.J. Errington, J. (2000) Role of penicillin-binding protein PBP 2B in assembly and functioning of the division machinery of Bacillus subtilis. Mol Microbiol 35 : 299 311. (Pubitemid 30055227)
    • (2000) Molecular Microbiology , vol.35 , Issue.2 , pp. 299-311
    • Daniel, R.A.1    Harry, E.J.2    Errington, J.3
  • 6
    • 36549008206 scopus 로고    scopus 로고
    • New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus
    • DOI 10.1128/JB.00645-07
    • Dubrac, S., Boneca, I.G., Poupel, O. Msadek, T. (2007) New insights into the WalK/WalR (YycG/YycF) essential signal transduction pathway reveal a major role in controlling cell wall metabolism and biofilm formation in Staphylococcus aureus. J Bacteriol 189 : 8257 8269. (Pubitemid 350178938)
    • (2007) Journal of Bacteriology , vol.189 , Issue.22 , pp. 8257-8269
    • Dubrac, S.1    Boneca, I.G.2    Poupel, O.3    Msadek, T.4
  • 7
    • 56749173808 scopus 로고    scopus 로고
    • A matter of life and death: Cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway
    • Dubrac, S., Bisicchia, P., Devine, K.M. Msadek, T. (2008) A matter of life and death: cell wall homeostasis and the WalKR (YycGF) essential signal transduction pathway. Mol Microbiol 70 : 1307 1322.
    • (2008) Mol Microbiol , vol.70 , pp. 1307-1322
    • Dubrac, S.1    Bisicchia, P.2    Devine, K.M.3    Msadek, T.4
  • 8
    • 33748808682 scopus 로고    scopus 로고
    • A link in transcription between the native pbpB and the acquired mecA gene in a strain of Staphylococcus aureus
    • DOI 10.1099/mic.0.29078-0
    • Gardete, S., de Lencastre, H. Tomasz, A. (2006) A link in transcription between the native pbpB and the acquired mecA gene in a strain of Staphylococcus aureus. Microbiology 152 : 2549 2558. (Pubitemid 44405080)
    • (2006) Microbiology , vol.152 , Issue.9 , pp. 2549-2558
    • Gardete, S.1    De Lencastre, H.2    Tomasz, A.3
  • 10
    • 0026049801 scopus 로고
    • Serine beta-lactamases and penicillin-binding proteins
    • Ghuysen, J.M. (1991) Serine beta-lactamases and penicillin-binding proteins. Annu Rev Microbiol 45 : 37 67.
    • (1991) Annu Rev Microbiol , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 11
    • 0031767816 scopus 로고    scopus 로고
    • Staphylococcal cell wall: Morphogenesis and fatal variations in the presence of penicillin
    • Giesbrecht, P., Kersten, T., Maidhof, H. Wecke, J. (1998) Staphylococcal cell wall: morphogenesis and fatal variations in the presence of penicillin. Microbiol Mol Biol Rev 62 : 1371 1414. (Pubitemid 28558303)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.4 , pp. 1371-1414
    • Giesbrecht, P.1    Kersten, T.2    Maidhof, H.3    Wecke, J.4
  • 12
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • Goffin, C. Ghuysen, J.M. (1998) Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62 : 1079 1093. (Pubitemid 28558293)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.4 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.-M.2
  • 13
    • 0037348664 scopus 로고    scopus 로고
    • Stable low-copy-number Staphylococcus aureus shuttle vectors
    • DOI 10.1099/mic.0.25951-0
    • Grkovic, S., Brown, M.H., Hardie, K.M., Firth, N. Skurray, R.A. (2003) Stable low-copy-number Staphylococcus aureus shuttle vectors. Microbiology 149 : 785 794. (Pubitemid 36395112)
    • (2003) Microbiology , vol.149 , Issue.3 , pp. 785-794
    • Grkovic, S.1    Brown, M.H.2    Hardie, K.M.3    Firth, N.4    Skurray, R.A.5
  • 14
    • 0021361020 scopus 로고
    • Low-affinity penicillin-binding protein associated with β-lactam resistance in Staphylococcus aureus
    • Hartman, B.J. Tomasz, A. (1984) Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus. J Bacteriol 158 : 513 516. (Pubitemid 14147618)
    • (1984) Journal of Bacteriology , vol.158 , Issue.2 , pp. 513-516
    • Hartman, B.J.1    Tomasz, A.2
  • 15
    • 33750444279 scopus 로고    scopus 로고
    • Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: Inside versus outside
    • DOI 10.1128/JB.00800-06
    • Jones, G. Dyson, P. (2006) Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside. J Bacteriol 188 : 7470 7476. (Pubitemid 44646246)
    • (2006) Journal of Bacteriology , vol.188 , Issue.21 , pp. 7470-7476
    • Jones, G.1    Dyson, P.2
  • 16
    • 0026088721 scopus 로고
    • Suppression of autolysis and cell wall turnover in heterogeneous Tn551 mutants of a methicillin-resistant Staphylococcus aureus strain
    • de Jonge, B.L., de Lencastre, H. Tomasz, A. (1991) Suppression of autolysis and cell wall turnover in heterogeneous Tn551 mutants of a methicillin-resistant Staphylococcus aureus strain. J Bacteriol 173 : 1105 1110.
    • (1991) J Bacteriol , vol.173 , pp. 1105-1110
    • De Jonge, B.L.1    De Lencastre, H.2    Tomasz, A.3
  • 17
    • 0026639828 scopus 로고
    • Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. the role of penicillin binding protein 2A
    • de Jonge, B.L., Chang, Y.S., Gage, D. Tomasz, A. (1992) Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. The role of penicillin binding protein 2A. J Biol Chem 267 : 11248 11254.
    • (1992) J Biol Chem , vol.267 , pp. 11248-11254
    • De Jonge, B.L.1    Chang, Y.S.2    Gage, D.3    Tomasz, A.4
  • 19
    • 0017361278 scopus 로고
    • Formation of regular packets of Staphylococcus aureus cells
    • Koyama, T., Yamada, M. Matsuhashi, M. (1977) Formation of regular packets of Staphylococcus aureus cells. J Bacteriol 129 : 1518 1523. (Pubitemid 8065046)
    • (1977) Journal of Bacteriology , vol.129 , Issue.3 , pp. 1518-1523
    • Koyama, T.1    Yamada, M.2    Matsuhashi, M.3
  • 20
    • 14244254169 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: Evidence for the cooperative functioning of PBP2, PBP4, and PBP2A
    • DOI 10.1128/JB.187.5.1815-1824.2005
    • Leski, T.A. Tomasz, A. (2005) Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: evidence for the cooperative functioning of PBP2, PBP4, and PBP2A. J Bacteriol 187 : 1815 1824. (Pubitemid 40289383)
    • (2005) Journal of Bacteriology , vol.187 , Issue.5 , pp. 1815-1824
    • Leski, T.A.1    Tomasz, A.2
  • 21
    • 1642442760 scopus 로고    scopus 로고
    • The D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
    • DOI 10.1046/j.1365-2958.2003.03953.x
    • Morlot, C., Noirclerc-Savoye, M., Zapun, A., Dideberg, O. Vernet, T. (2004) The d,d-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol Microbiol 51 : 1641 1648. (Pubitemid 38406538)
    • (2004) Molecular Microbiology , vol.51 , Issue.6 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 22
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • DOI 10.1038/nsb0396-284
    • Pares, S., Mouz, N., Petillot, Y., Hakenbeck, R. Dideberg, O. (1996) X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat Struct Biol 3 : 284 289. (Pubitemid 26081712)
    • (1996) Nature Structural Biology , vol.3 , Issue.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Petillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 24
    • 4444297890 scopus 로고    scopus 로고
    • Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli
    • DOI 10.1128/JB.186.18.6110-6117.2004
    • Piette, A., Fraipont, C., Den Blaauwen, T., Aarsman, M.E., Pastoret, S. Nguyen-Disteche, M. (2004) Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. J Bacteriol 186 : 6110 6117. (Pubitemid 39186999)
    • (2004) Journal of Bacteriology , vol.186 , Issue.18 , pp. 6110-6117
    • Piette, A.1    Fraipont, C.2    Den Blaauwen, T.3    Aarsman, M.E.G.4    Pastoret, S.5    Nguyen-Disteche, M.6
  • 25
    • 0242606152 scopus 로고    scopus 로고
    • Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery
    • DOI 10.1046/j.1365-2958.2003.03719.x
    • Pinho, M.G. Errington, J. (2003) Dispersed mode of Staphylococcus aureus cell wall synthesis in the absence of the division machinery. Mol Microbiol 50 : 871 881. (Pubitemid 37372250)
    • (2003) Molecular Microbiology , vol.50 , Issue.3 , pp. 871-881
    • Pinho, M.G.1    Errington, J.2
  • 26
    • 13444259776 scopus 로고    scopus 로고
    • Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
    • DOI 10.1111/j.1365-2958.2004.04420.x
    • Pinho, M.G. Errington, J. (2005) Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates. Mol Microbiol 55 : 799 807. (Pubitemid 40203695)
    • (2005) Molecular Microbiology , vol.55 , Issue.3 , pp. 799-807
    • Pinho, M.G.1    Errington, J.2
  • 28
    • 0034748911 scopus 로고    scopus 로고
    • Complementation of the essential peptidoglycan transpeptidase function of penicillin-binding protein 2 (PBP2) by the drug resistance protein PBP2A in Staphylococcus aureus
    • DOI 10.1128/JB.183.22.6525-6531.2001
    • Pinho, M.G., Filipe, S.R., de Lencastre, H. Tomasz, A. (2001b) Complementation of the essential peptidoglycan transpeptidase function of penicillin-binding protein 2 (PBP2) by the drug resistance protein PBP2A in Staphylococcus aureus. J Bacteriol 183 : 6525 6531. (Pubitemid 33026741)
    • (2001) Journal of Bacteriology , vol.183 , Issue.22 , pp. 6525-6531
    • Pinho, M.G.1    Filipe, S.R.2    De Lencastre, H.3    Tomasz, A.4
  • 29
    • 33846007687 scopus 로고    scopus 로고
    • The bacterial cytoskeleton
    • DOI 10.1187/cbe.06-09-0188
    • Pogliano, J. (2008) The bacterial cytoskeleton. Curr Opin Cell Biol 20 : 19 27. (Pubitemid 46047498)
    • (2006) CBE Life Sciences Education , vol.5 , Issue.4 , pp. 306-310
    • Watters, C.1
  • 30
    • 0031006866 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of lytM, a unique autolytic gene of Staphylococcus aureus
    • Ramadurai, L. Jayaswal, R.K. (1997) Molecular cloning, sequencing, and expression of lytM, a unique autolytic gene of Staphylococcus aureus. J Bacteriol 179 : 3625 3631. (Pubitemid 27233002)
    • (1997) Journal of Bacteriology , vol.179 , Issue.11 , pp. 3625-3631
    • Ramadurai, L.1    Jayaswal, R.K.2
  • 31
    • 70449232353 scopus 로고
    • Etude au microscope electronique de plasmas contenant de l'acide desoxyribonucleique
    • Ryter, A., Kellenberger, E., Birchandersen, A. Maaloe, O. (1958) Etude au microscope electronique de plasmas contenant de l'acide desoxyribonucleique. Z Naturforsch B 13B : 597 605.
    • (1958) Z Naturforsch B , vol.13 B , pp. 597-605
    • Ryter, A.1    Kellenberger, E.2    Birchandersen, A.3    Maaloe, O.4
  • 32
    • 0033516654 scopus 로고    scopus 로고
    • Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus
    • Sieradzki, K., Pinho, M.G. Tomasz, A. (1999) Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus. J Biol Chem 274 : 18942 18946. (Pubitemid 129519311)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.27 , pp. 18942-18946
    • Sieradzki, K.1    Pinho, M.G.2    Tomasz, A.3
  • 33
    • 0041353701 scopus 로고    scopus 로고
    • Normally functioning murF is essential for the optimal expression of methicillin resistance in Staphylococcus aureus
    • Sobral, R.G., Ludovice, A.M., Gardete, S., Tabei, K., de Lencastre, H. Tomasz, A. (2003) Normally functioning murF is essential for the optimal expression of methicillin resistance in Staphylococcus aureus. Microb Drug Resist 9 : 231 241. (Pubitemid 37048544)
    • (2003) Microbial Drug Resistance , vol.9 , Issue.3 , pp. 231-241
    • Sobral, R.G.1    Ludovice, A.M.2    Gardete, S.3    Tabei, K.4    De Lencastre, H.5    Tomasz, A.6
  • 34
    • 0013096299 scopus 로고
    • Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12
    • Spratt, B.G. (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci USA 72 : 2999 3003.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2999-3003
    • Spratt, B.G.1
  • 35
    • 0028986933 scopus 로고
    • Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus
    • Sugai, M., Komatsuzawa, H., Akiyama, T., Hong, Y.M., Oshida, T., Miyake, Y. et al. (1995) Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus. J Bacteriol 177 : 1491 1496.
    • (1995) J Bacteriol , vol.177 , pp. 1491-1496
    • Sugai, M.1    Komatsuzawa, H.2    Akiyama, T.3    Hong, Y.M.4    Oshida, T.5    Miyake, Y.6
  • 36
    • 0000726755 scopus 로고
    • The fine structure of Diplococcus pneumoniae
    • Tomasz, A., Jamieson, J.D. Ottolenghi, E. (1964) The fine structure of Diplococcus pneumoniae. J Cell Biol 22 : 453 467.
    • (1964) J Cell Biol , vol.22 , pp. 453-467
    • Tomasz, A.1    Jamieson, J.D.2    Ottolenghi, E.3
  • 37
    • 0017356210 scopus 로고
    • Geometry of cell division in Staphylococcus aureus
    • Tzagoloff, H. Novick, R. (1977) Geometry of cell division in Staphylococcus aureus. J Bacteriol 129 : 343 350. (Pubitemid 8018601)
    • (1977) Journal of Bacteriology , vol.129 , Issue.1 , pp. 343-350
    • Tzagoloff, H.1    Novick, R.2
  • 39
    • 0031949367 scopus 로고    scopus 로고
    • Penicillin-binding protein 1 of Staphylococcus aureus is essential for growth
    • Wada, A. Watanabe, H. (1998) Penicillin-binding protein 1 of Staphylococcus aureus is essential for growth. J Bacteriol 180 : 2759 2765. (Pubitemid 28213279)
    • (1998) Journal of Bacteriology , vol.180 , Issue.10 , pp. 2759-2765
    • Wada, A.1    Watanabe, H.2
  • 40
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss, D.S., Chen, J.C., Ghigo, J.M., Boyd, D. Beckwith, J. (1999) Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J Bacteriol 181 : 508 520. (Pubitemid 29045142)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.-M.3    Boyd, D.4    Beckwith, J.5
  • 41
    • 0026317589 scopus 로고
    • The role of two surface exposed loops in transcription activation by the Escherichia coli CRP and FNR proteins
    • Wientjes, F.B. Nanninga, N. (1991) On the role of the high molecular weight penicillin-binding proteins in the cell cycle of Escherichia coli. Res Microbiol 142 : 333 344. (Pubitemid 21913103)
    • (1991) Nucleic Acids Research , vol.19 , Issue.24 , pp. 6705-6712
    • Williams, R.1    Bell, A.2    Sims, G.3    Busby, S.4
  • 42
    • 0347915664 scopus 로고    scopus 로고
    • Genetic Analysis of the Cell Division Protein FtsI (PBP3): Amino Acid Substitutions that Impair Septal Localization of FtsI and Recruitment of FtsN
    • DOI 10.1128/JB.186.2.490-502.2004
    • Wissel, M.C. Weiss, D.S. (2004) Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J Bacteriol 186 : 490 502. (Pubitemid 38076440)
    • (2004) Journal of Bacteriology , vol.186 , Issue.2 , pp. 490-502
    • Wissel, M.C.1    Weiss, D.S.2
  • 43
    • 11144318755 scopus 로고    scopus 로고
    • The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring
    • DOI 10.1128/JB.187.1.320-328.2005
    • Wissel, M.C., Wendt, J.L., Mitchell, C.J. Weiss, D.S. (2005) The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J Bacteriol 187 : 320 328. (Pubitemid 40024208)
    • (2005) Journal of Bacteriology , vol.187 , Issue.1 , pp. 320-328
    • Wissel, M.C.1    Wendt, J.L.2    Mitchell, C.J.3    Weiss, D.S.4
  • 45
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A beta-lactam-binding domain
    • Yeats, C., Finn, R.D. Bateman, A. (2002) The PASTA domain: a beta-lactam-binding domain. Trends Biochem Sci 27 : 438 440.
    • (2002) Trends Biochem Sci , vol.27 , pp. 438-440
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 46
    • 38749102811 scopus 로고    scopus 로고
    • Penicillin-binding proteins and cell wall composition in beta-lactam-sensitive and - Resistant strains of Staphylococcus sciuri
    • Zhou, Y., Antignac, A., Wu, S.W. Tomasz, A. (2008) Penicillin-binding proteins and cell wall composition in beta-lactam-sensitive and - resistant strains of Staphylococcus sciuri. J Bacteriol 190 : 508 514.
    • (2008) J Bacteriol , vol.190 , pp. 508-514
    • Zhou, Y.1    Antignac, A.2    Wu, S.W.3    Tomasz, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.