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Volumn 58, Issue 10, 2012, Pages 1183-1194

Changes in peptidoglycan structure and metabolism during differentiation of Proteus mirabilis into swarmer cells

Author keywords

Autolysinss; Lytic transglycosylases; Murein; O acetylation; Peptidoglycan; Swarming

Indexed keywords

AUTOLYSIN; LIPOPROTEIN; PEPTIDOGLYCAN;

EID: 84867848076     PISSN: 00084166     EISSN: 14803275     Source Type: Journal    
DOI: 10.1139/w2012-102     Document Type: Article
Times cited : (13)

References (46)
  • 1
    • 0020312345 scopus 로고
    • Changes in the organization of the outer membrane of Proteus mirabilis during swarming: Freeze-fracture structure and membrane fluidity analysis
    • PMID:6279575
    • Armitage, J.P. 1982. Changes in the organization of the outer membrane of Proteus mirabilis during swarming: freeze-fracture structure and membrane fluidity analysis. J. Bacteriol. 150(2): 900-904. PMID:6279575.
    • (1982) J. Bacteriol , vol.150 , Issue.2 , pp. 900-904
    • Armitage, J.P.1
  • 2
    • 0016531490 scopus 로고
    • Indirect evidence for cell wall and membrane differences between filamentious swarming cells and short non-swarming cells of Proteus mirabilis
    • doi:10.1099/00221287-89-1-199. PMID:1097593
    • Armitage, J.P., Rowbury, R.J., and Smith, D.G. 1975. Indirect evidence for cell wall and membrane differences between filamentious swarming cells and short non-swarming cells of Proteus mirabilis. J. Gen. Microbiol. 89(1): 199-202. doi:10.1099/00221287-89-1-199. PMID:1097593
    • (1975) J. Gen. Microbiol , vol.89 , Issue.1 , pp. 199-202
    • Armitage, J.P.1    Rowbury, R.J.2    Smith, D.G.3
  • 3
    • 0018396418 scopus 로고
    • Alterations in the cell envelope composition of Proteus mirabilis during the development of swarmer cells
    • doi:10.1016/0304-4165(79)90115-6. PMID:378265
    • Armitage, J.P., Smith, D.G., and Rowbury, R.J. 1979. Alterations in the cell envelope composition of Proteus mirabilis during the development of swarmer cells. Biochim. Biophys. Acta, 584(3): 389-397. doi:10.1016/0304-4165(79)90115-6. PMID:378265
    • (1979) Biochim. Biophys. Acta , vol.584 , Issue.3 , pp. 389-397
    • Armitage, J.P.1    Smith, D.G.2    Rowbury, R.J.3
  • 4
    • 0028906663 scopus 로고
    • Genetic analysis of Proteus mirabilis mutants defective in swarmer cell elongation
    • PMID:7836320
    • Belas, R., Goldman, M., and Ashliman, K. 1995. Genetic analysis of Proteus mirabilis mutants defective in swarmer cell elongation. J. Bacteriol. 177(3): 823-828. PMID:7836320
    • (1995) J. Bacteriol , vol.177 , Issue.3 , pp. 823-828
    • Belas, R.1    Goldman, M.2    Ashliman, K.3
  • 5
    • 0031785679 scopus 로고    scopus 로고
    • Characterization of Proteus mirabilis precocious swarming mutants: Identification of rsbA, encoding a regular of swarming behavior
    • PMID:9829920
    • Belas, R., Schneider, R., and Melch, M. 1998. Characterization of Proteus mirabilis precocious swarming mutants: identification of rsbA, encoding a regular of swarming behavior. J. Bacteriol. 180(23): 6126-6139. PMID:9829920
    • (1998) J. Bacteriol , vol.180 , Issue.23 , pp. 6126-6139
    • Belas, R.1    Schneider, R.2    Melch, M.3
  • 6
    • 0028093382 scopus 로고
    • Analysis of the sodium dodecyl sulfate-stable peptidogylcan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis
    • PMID: 7915268
    • Bernadsky, G., Beveridge, T.J., and Clarke, A.J. 1994. Analysis of the sodium dodecyl sulfate-stable peptidogylcan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis. J. Bacteriol. 176(17): 5225-5232. PMID: 7915268
    • (1994) J. Bacteriol , vol.176 , Issue.17 , pp. 5225-5232
    • Bernadsky, G.1    Beveridge, T.J.2    Clarke, A.J.3
  • 7
    • 0037154093 scopus 로고    scopus 로고
    • Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa
    • doi: 10.1021/bi011833k. PMID:11790124
    • Blackburn, N.T., and Clarke, A.J. 2002a. Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa. Biochemistry, 41(3): 1001-1013. doi: 10.1021/bi011833k. PMID:11790124
    • (2002) Biochemistry , vol.41 , Issue.3 , pp. 1001-1013
    • Blackburn, N.T.1    Clarke, A.J.2
  • 8
    • 85037421452 scopus 로고    scopus 로고
    • Families of lytic tranglycosylases
    • Blackburn, N.T., and Clarke, A.J. 2002b. Families of lytic tranglycosylases. J. Mol. Evol. 52: 78-84.
    • (2002) J. Mol. Evol , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 9
    • 0019127047 scopus 로고
    • The peptidoglycan of Neisseria gonorrhoeae: O-acetyl groups and lysozyme sensitivity
    • doi:10.1111/j.1574-6968.1980.tb05648.x
    • Blundell, J.K., Smith, G.J., and Perkins, H.R. 1980. The peptidoglycan of Neisseria gonorrhoeae: O-acetyl groups and lysozyme sensitivity. FEMS Microbiol. Lett. 9(4): 259-261. doi:10.1111/j.1574-6968.1980.tb05648.x
    • (1980) FEMS Microbiol. Lett , vol.9 , Issue.4 , pp. 259-261
    • Blundell, J.K.1    Smith, G.J.2    Perkins, H.R.3
  • 10
    • 0027279951 scopus 로고
    • Extent of peptidoglycan O-acetylation in the tribe Proteeae
    • PMID:8331084
    • Clarke, A.J. 1993a. Extent of peptidoglycan O-acetylation in the tribe Proteeae. J. Bacteriol. 175(14): 4550-4553. PMID:8331084
    • (1993) J. Bacteriol , vol.175 , Issue.14 , pp. 4550-4553
    • Clarke, A.J.1
  • 11
    • 0027293346 scopus 로고
    • Compositional analysis of peptidoglycan by highperformance anion-exchange chromatography
    • doi:10.1006/abio.1993.1339. PMID:8214575
    • Clarke, A.J. 1993b. Compositional analysis of peptidoglycan by highperformance anion-exchange chromatography. Anal. Biochem. 212(2): 344-350. doi:10.1006/abio.1993.1339. PMID:8214575
    • (1993) Anal. Biochem , vol.212 , Issue.2 , pp. 344-350
    • Clarke, A.J.1
  • 12
    • 0026605558 scopus 로고
    • O-Acetylated peptidoglycan: Its occurrence, pathobiological significance and biosynthesis
    • doi:10.1139/m92-014. PMID:1521192
    • Clarke, A.J., and Dupont, C. 1992. O-Acetylated peptidoglycan: Its occurrence, pathobiological significance and biosynthesis. Can. J. Microbiol. 38(2): 85-91. doi:10.1139/m92-014. PMID:1521192.
    • (1992) Can. J. Microbiol , vol.38 , Issue.2 , pp. 85-91
    • Clarke, A.J.1    Dupont, C.2
  • 13
    • 84862942115 scopus 로고    scopus 로고
    • Perturbation of FliL interferes with Proteus mirabilis swarmer cell gene expression and differentiation
    • doi:10.1128/JB.05998-11. PMID:22081397
    • Cusick, K., Lee, Y.-Y., Youchak, B., and Belas, R. 2012. Perturbation of FliL interferes with Proteus mirabilis swarmer cell gene expression and differentiation. J. Bacteriol. 194(2): 437-447. doi:10.1128/JB.05998-11. PMID:22081397
    • (2012) J. Bacteriol , vol.194 , Issue.2 , pp. 437-447
    • Cusick, K.1    Lee, Y.-Y.2    Youchak, B.3    Belas, R.4
  • 14
    • 36549017697 scopus 로고    scopus 로고
    • The flagellar muramidase from the photosynthetic bacterium Rhodobacter sphaeroides
    • doi:10.1128/JB.01073-07. PMID:17873041
    • de la Mora, J., Ballado, T., Gonzalez-Pedrajo, B., Camarena, L., and Dreyfus, G. 2007. The flagellar muramidase from the photosynthetic bacterium Rhodobacter sphaeroides. J. Bacteriol. 189(22): 7998-8004. doi:10.1128/JB.01073-07. PMID:17873041
    • (2007) J. Bacteriol , vol.189 , Issue.22 , pp. 7998-8004
    • de la Mora, J.1    Ballado, T.2    Gonzalez-Pedrajo, B.3    Camarena, L.4    Dreyfus, G.5
  • 15
    • 0025972046 scopus 로고
    • Dependence of lysozyme catalyzed solubilization of Proteus mirabilis peptidoglycan on the extent of O-acetylation
    • doi:10.1111/j.1432-1033.1991.tb15764.x. PMID:1999194
    • Dupont, C., and Clarke, A.J. 1991. Dependence of lysozyme catalyzed solubilization of Proteus mirabilis peptidoglycan on the extent of O-acetylation. Eur. J. Biochem. 195(3): 763-769. doi:10.1111/j.1432-1033.1991.tb15764.x. PMID:1999194
    • (1991) Eur. J. Biochem , vol.195 , Issue.3 , pp. 763-769
    • Dupont, C.1    Clarke, A.J.2
  • 16
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high performance liquid chromatography
    • doi:10.1016/0003-2697(88)90468-X. PMID:3056100
    • Glauner, B. 1988. Separation and quantification of muropeptides with high performance liquid chromatography. Anal. Biochem. 172(2): 451-464. doi:10.1016/0003-2697(88)90468-X. PMID:3056100
    • (1988) Anal. Biochem , vol.172 , Issue.2 , pp. 451-464
    • Glauner, B.1
  • 17
    • 0035797871 scopus 로고    scopus 로고
    • Bacterial swarming: A biochemical time-resolved FTIR-ATR study of Proteus mirabilis swarm-cell differentiation
    • doi:10.1021/bi010434m. PMID:11570895
    • Gué, M., Dupont, V., Dufour, A., and Sire, O. 2001. Bacterial swarming: a biochemical time-resolved FTIR-ATR study of Proteus mirabilis swarm-cell differentiation. Biochemistry, 40(39): 11938-11945. doi:10.1021/bi010434m. PMID:11570895
    • (2001) Biochemistry , vol.40 , Issue.39 , pp. 11938-11945
    • Gué, M.1    Dupont, V.2    Dufour, A.3    Sire, O.4
  • 18
    • 0028799808 scopus 로고
    • A cell-surface polysaccharide that facilitates rapid population migration by differentiated swarm cells of Proteus mirabilis
    • doi:10.1111/j.1365-2958.1995.mmi_17061167.x. PMID:8594335
    • Gygi, D., Rahman, M.M., Lai, S.-C., Carlson, R., Guard-Petter, J., and Hughes, C. 1995. A cell-surface polysaccharide that facilitates rapid population migration by differentiated swarm cells of Proteus mirabilis. Mol. Microbiol. 17(6): 1167-1175. doi:10.1111/j.1365-2958.1995.mmi_17061167.x. PMID:8594335
    • (1995) Mol. Microbiol , vol.17 , Issue.6 , pp. 1167-1175
    • Gygi, D.1    Rahman, M.M.2    Lai, S.-C.3    Carlson, R.4    Guard-Petter, J.5    Hughes, C.6
  • 20
    • 0035860359 scopus 로고    scopus 로고
    • The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase
    • doi:10.1006/jmbi.2001.4963. PMID:11554792
    • Hirano, T., Minamino, T., and Macnab, R.M. 2001. The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase. J. Mol. Biol. 312(2): 359-369. doi:10.1006/jmbi.2001.4963. PMID:11554792
    • (2001) J. Mol. Biol , vol.312 , Issue.2 , pp. 359-369
    • Hirano, T.1    Minamino, T.2    Macnab, R.M.3
  • 21
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli
    • PMID:9529891
    • Höltje, J.-V. 1998. Growth of the stress-bearing and shapemaintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62(1): 181-203. PMID:9529891
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , Issue.1 , pp. 181-203
    • Höltje, J.-V.1
  • 22
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • PMID:357
    • Höltje, J.-V., Mirelman, D., Sharon, N., and Schwarz, U. 1975. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124(3): 1067-1076. PMID:357
    • (1975) J. Bacteriol , vol.124 , Issue.3 , pp. 1067-1076
    • Höltje, J.-V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 23
    • 38549128203 scopus 로고    scopus 로고
    • Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis
    • doi:10.1128/CMR.00019-07. PMID:18202436
    • Jacobsen, S.M., Stickler, D.J., Mobley, H.L., and Shirtliff, M.E. 2008. Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis. Clin. Microbiol. Rev. 21(1): 26-59. doi:10.1128/CMR.00019-07. PMID:18202436
    • (2008) Clin. Microbiol. Rev , vol.21 , Issue.1 , pp. 26-59
    • Jacobsen, S.M.1    Stickler, D.J.2    Mobley, H.L.3    Shirtliff, M.E.4
  • 24
    • 20944436886 scopus 로고    scopus 로고
    • The RssAB two-component signal transduction system in Serratia marcescens regulates swarming motility and cell envelope architecture in response to exogenous saturated fatty acids
    • doi:10.1128/JB.187.10.3407-3414.2005. PMID:15866926
    • Lai, H.C., Soo, P.C., Wei, J.R., Yi, W.C., Liaw, S.J., Horng, Y.T., et al. 2005. The RssAB two-component signal transduction system in Serratia marcescens regulates swarming motility and cell envelope architecture in response to exogenous saturated fatty acids. J. Bacteriol. 187(10): 3407-3414. doi:10.1128/JB.187.10.3407-3414.2005. PMID:15866926
    • (2005) J. Bacteriol , vol.187 , Issue.10 , pp. 3407-3414
    • Lai, H.C.1    Soo, P.C.2    Wei, J.R.3    Yi, W.C.4    Liaw, S.J.5    Horng, Y.T.6
  • 25
    • 34447538362 scopus 로고    scopus 로고
    • Overproduction of penicillin-binding protein 2 and its inactive variants causes morphological changes and lysis in Escherichia coli
    • doi:10.1128/JB.00207-07. PMID:17513478
    • Legaree, B.A., Adams, C., and Clarke, A.J. 2007. Overproduction of penicillin-binding protein 2 and its inactive variants causes morphological changes and lysis in Escherichia coli. J. Bacteriol. 189(14): 4975-4983. doi:10.1128/JB.00207-07. PMID:17513478
    • (2007) J. Bacteriol , vol.189 , Issue.14 , pp. 4975-4983
    • Legaree, B.A.1    Adams, C.2    Clarke, A.J.3
  • 26
    • 77955263894 scopus 로고    scopus 로고
    • Mutational studies on the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1
    • doi:10.1002/jobm.200900249. PMID:20586063
    • Marauyama, Y., Ochiai, A., Itoh, T., Mikami, B., Hashimoto, W., and Murata, K. 2010. Mutational studies on the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1. J. Basic Microbiol. 50(4): 311-317. doi:10.1002/jobm.200900249. PMID:20586063
    • (2010) J. Basic Microbiol , vol.50 , Issue.4 , pp. 311-317
    • Marauyama, Y.1    Ochiai, A.2    Itoh, T.3    Mikami, B.4    Hashimoto, W.5    Murata, K.6
  • 27
    • 77955132811 scopus 로고    scopus 로고
    • Regulation of gene expression during swarmer cell differentiation in Proteus mirabilis
    • PMID:20497230
    • Morgenstein, R.M., Szostek, B., and Rather, P.N. 2010. Regulation of gene expression during swarmer cell differentiation in Proteus mirabilis. FEMS Microbiol. Rev. 34(5): 753-763. PMID:20497230
    • (2010) FEMS Microbiol. Rev , vol.34 , Issue.5 , pp. 753-763
    • Morgenstein, R.M.1    Szostek, B.2    Rather, P.N.3
  • 28
    • 80255137078 scopus 로고    scopus 로고
    • O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems
    • doi:10.1016/j.biocel.2011.08.007. PMID:21889603
    • Moynihan, P.J., and Clarke, A.J. 2011. O-Acetylated peptidoglycan: controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems. Int. J. Biochem. Cell Biol. 43(12): 1655-1659. doi:10.1016/j.biocel.2011.08.007. PMID:21889603
    • (2011) Int. J. Biochem. Cell Biol , vol.43 , Issue.12 , pp. 1655-1659
    • Moynihan, P.J.1    Clarke, A.J.2
  • 29
    • 0033053893 scopus 로고    scopus 로고
    • Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium
    • PMID:10049388
    • Nambu, T., Minamino, T., Mcnab, R.M., and Kutukake, K. 1999. Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium. J. Bacteriol. 181(5): 1555-1561. PMID:10049388
    • (1999) J. Bacteriol , vol.181 , Issue.5 , pp. 1555-1561
    • Nambu, T.1    Minamino, T.2    McNab, R.M.3    Kutukake, K.4
  • 30
    • 77955654591 scopus 로고    scopus 로고
    • Host-pathogen interactions in urinary tract infection
    • doi:10.1038/nrurol.2010.101. PMID:20647992
    • Nielubowicz, G.R., and Mobley, H.L. 2010. Host-pathogen interactions in urinary tract infection. Nat. Rev. Urol. 7: 430-441. doi:10.1038/nrurol.2010.101. PMID:20647992
    • (2010) Nat. Rev. Urol , vol.7 , pp. 430-441
    • Nielubowicz, G.R.1    Mobley, H.L.2
  • 31
    • 0026728871 scopus 로고
    • A new mercury penicillin V derivative as a probe for ultrastructural localization of penicillin-binding proteins in Escherichia coli
    • PMID:1624457
    • Paul, T., Halligan, N., Blaszczak, L., Parr, T., Jr, and Beveridge, T.J. 1992. A new mercury penicillin V derivative as a probe for ultrastructural localization of penicillin-binding proteins in Escherichia coli. J. Bacteriol. 174(14): 4689-4700. PMID:1624457
    • (1992) J. Bacteriol , vol.174 , Issue.14 , pp. 4689-4700
    • Paul, T.1    Halligan, N.2    Blaszczak, L.3    Parr Jr., T.4    Beveridge, T.J.5
  • 32
    • 0029738252 scopus 로고    scopus 로고
    • The role of Oacetylation in the metabolism of peptidoglycan in Providencia stuartii
    • doi:10.1089/mdr.1996.2.135. PMID:9158736
    • Payie, K.G., Strating, H., and Clarke, A.J. 1996. The role of Oacetylation in the metabolism of peptidoglycan in Providencia stuartii. Microb. Drug Resist. 2(1): 135-140. doi:10.1089/mdr.1996.2.135. PMID:9158736
    • (1996) Microb. Drug Resist , vol.2 , Issue.1 , pp. 135-140
    • Payie, K.G.1    Strating, H.2    Clarke, A.J.3
  • 33
    • 77952702307 scopus 로고    scopus 로고
    • Transciptome of swarming Proteus mirabilis
    • doi:10.1128/IAI.01222-09. PMID:20368347
    • Pearson, M.M., Rasko, D.A., Smith, S.N., and Mobley, L.T. 2010. Transciptome of swarming Proteus mirabilis. Infect. Immun. 78(6): 2834-2845. doi:10.1128/IAI.01222-09. PMID:20368347
    • (2010) Infect. Immun , vol.78 , Issue.6 , pp. 2834-2845
    • Pearson, M.M.1    Rasko, D.A.2    Smith, S.N.3    Mobley, L.T.4
  • 34
    • 31344451043 scopus 로고    scopus 로고
    • Peptidoglcyan O-acetylation and autolysin profile of Enterococcus faecalis in the viable but nonculturable state
    • doi:10.1128/JB.188.3.902-908.2006. PMID:16428393
    • Pfeffer, J.M., Strating, H., Weadge, J.T., and Clarke, A.J. 2006. Peptidoglcyan O-acetylation and autolysin profile of Enterococcus faecalis in the viable but nonculturable state. J. Bacteriol. 188(3): 902-908. doi:10.1128/JB.188.3.902-908.2006. PMID:16428393
    • (2006) J. Bacteriol , vol.188 , Issue.3 , pp. 902-908
    • Pfeffer, J.M.1    Strating, H.2    Weadge, J.T.3    Clarke, A.J.4
  • 35
    • 0028878573 scopus 로고
    • Variability of peptidoglycan structural parameters in Gram-negative bacteria
    • doi:10.1111/j.1574-6968.1995.tb07341.x. PMID:7867925
    • Quintela, J.C., Caparrós, M., and de Pedro, M.A. 1995. Variability of peptidoglycan structural parameters in Gram-negative bacteria. FEMS Microbiol. Lett. 125(1): 95-100. doi:10.1111/j.1574-6968.1995.tb07341.x. PMID:7867925
    • (1995) FEMS Microbiol. Lett , vol.125 , Issue.1 , pp. 95-100
    • Quintela, J.C.1    Caparrós, M.2    de Pedro, M.A.3
  • 36
    • 0020028114 scopus 로고
    • Strainrelated differences in lysozyme sensitivity and extent of Oacetylation of gonococcal peptidoglycan
    • PMID:6811442
    • Rosenthal, R.S., Blundell, J.K., and Perkins, H.R. 1982. Strainrelated differences in lysozyme sensitivity and extent of Oacetylation of gonococcal peptidoglycan. Infect. Immun. 37(2): 826-829. PMID:6811442
    • (1982) Infect. Immun , vol.37 , Issue.2 , pp. 826-829
    • Rosenthal, R.S.1    Blundell, J.K.2    Perkins, H.R.3
  • 37
    • 0020632077 scopus 로고
    • Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes
    • PMID:6406367
    • Rosenthal, R.S., Folkening, W.J., Miller, D.R., and Swim, S.C. 1983. Resistance of O-acetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes. Infect. Immun. 40(3): 826-829. PMID:6406367
    • (1983) Infect. Immun , vol.40 , Issue.3 , pp. 826-829
    • Rosenthal, R.S.1    Folkening, W.J.2    Miller, D.R.3    Swim, S.C.4
  • 38
    • 43749112959 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase
    • doi:10.1074/jbc.M710135200. PMID:18234673
    • Scheurwater, E.M., and Clarke, A.J. 2008. The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase. J. Biol. Chem. 283(13): 8363-8373. doi:10.1074/jbc.M710135200. PMID:18234673
    • (2008) J. Biol. Chem , vol.283 , Issue.13 , pp. 8363-8373
    • Scheurwater, E.M.1    Clarke, A.J.2
  • 39
    • 39649099979 scopus 로고    scopus 로고
    • Lytic transglycosylases: Bacterial space-making autolysins
    • doi:10.1016/j.biocel.2007.03.018. PMID:17468031
    • Scheurwater, E.M., Reid, C.W., and Clarke, A.J. 2008. Lytic transglycosylases: bacterial space-making autolysins. Int. J. Biochem. Cell Biol. 40(4): 586-591. doi:10.1016/j.biocel.2007.03.018. PMID:17468031
    • (2008) Int. J. Biochem. Cell Biol , vol.40 , Issue.4 , pp. 586-591
    • Scheurwater, E.M.1    Reid, C.W.2    Clarke, A.J.3
  • 40
    • 0029846597 scopus 로고    scopus 로고
    • Modified peptidoglycan chemical composition in shape-altered Escherichia coli
    • doi:10.1099/13500872-142-8-1919. PMID:8760906
    • Signoretto, C., Di Stefano, F., and Canepari, P. 1996. Modified peptidoglycan chemical composition in shape-altered Escherichia coli. Microbiology, 142(8): 1919-1926. doi:10.1099/13500872-142-8-1919. PMID:8760906
    • (1996) Microbiology , vol.142 , Issue.8 , pp. 1919-1926
    • Signoretto, C.1    Di Stefano, F.2    Canepari, P.3
  • 41
    • 23944431508 scopus 로고    scopus 로고
    • Characterization of the dapA-nlpB genetic locus involved in regulation of swarming motility, cell envelope architecture, hemolysin production, and cell attachment ability in Serratia marcescens
    • doi:10.1128/IAI.73.9.6075-6084.2005. PMID:16113328
    • Soo, P.C., Wei, J.R., Horng, Y.T., Hsieh, S.C., Ho, S.W., and Lai, H.C. 2005. Characterization of the dapA-nlpB genetic locus involved in regulation of swarming motility, cell envelope architecture, hemolysin production, and cell attachment ability in Serratia marcescens. Infect. Immun. 73(9): 6075-6084. doi:10.1128/IAI.73.9.6075-6084.2005. PMID:16113328
    • (2005) Infect. Immun , vol.73 , Issue.9 , pp. 6075-6084
    • Soo, P.C.1    Wei, J.R.2    Horng, Y.T.3    Hsieh, S.C.4    Ho, S.W.5    Lai, H.C.6
  • 42
    • 0035312006 scopus 로고    scopus 로고
    • Differentiation of bacterial autolysins by zymogram analysis
    • doi:10.1006/abio.2001.5007. PMID:11262168
    • Strating, H., and Clarke, A.J. 2001. Differentiation of bacterial autolysins by zymogram analysis. Anal. Biochem. 291(1): 149-154. doi:10.1006/abio.2001.5007. PMID:11262168
    • (2001) Anal. Biochem , vol.291 , Issue.1 , pp. 149-154
    • Strating, H.1    Clarke, A.J.2
  • 43
    • 0021033685 scopus 로고
    • Strain distribution in extents of lysozyme resistance and Oacetylation of gonocccal peptidoglycan determined by highperformance liquid chromatography
    • Swim, S.G., Gfell, M.A., Wilde, C.E., III, and Rosenthal, R.S. 1993. Strain distribution in extents of lysozyme resistance and Oacetylation of gonocccal peptidoglycan determined by highperformance liquid chromatography. Infect. Immun. 42: 446-452.
    • (1993) Infect. Immun , vol.42 , pp. 446-452
    • Swim, S.G.1    Gfell, M.A.2    Wilde, C.E.3    Rosenthal, R.S.4
  • 44
    • 31044439427 scopus 로고    scopus 로고
    • Identification and characterization of O-acetylpeptidoglycan esterase: A novel enzyme discovered in Neisseria gonorrhoeae
    • doi: 10.1021/bi051679s. PMID:16411760
    • Weadge, J.T., and Clarke, A.J. 2006. Identification and characterization of O-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry, 45(3): 839-851. doi: 10.1021/bi051679s. PMID:16411760
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 839-851
    • Weadge, J.T.1    Clarke, A.J.2
  • 45
    • 24344487095 scopus 로고    scopus 로고
    • Identification of a new family of enzymes with potential O-acetylpeptidoglycan esterase activity in both Gram-positive and Gram-negative bacteria
    • doi:10.1186/1471-2180-5-49. PMID: 16111493
    • Weadge, J.T., Pfeffer, J.M., and Clarke, A.J. 2005. Identification of a new family of enzymes with potential O-acetylpeptidoglycan esterase activity in both Gram-positive and Gram-negative bacteria. BMC Microbiol. 5(1): 49. doi:10.1186/1471-2180-5-49. PMID: 16111493
    • (2005) BMC Microbiol , vol.5 , Issue.1 , pp. 49
    • Weadge, J.T.1    Pfeffer, J.M.2    Clarke, A.J.3
  • 46
    • 0017091185 scopus 로고
    • Evidence for a role of Nacetylmuramyl- L-alanine amidase in septum separation in Escherichia coli
    • PMID:61961
    • Wolf-Watz, H., and Normark, S. 1976. Evidence for a role of Nacetylmuramyl- L-alanine amidase in septum separation in Escherichia coli. J. Bacteriol. 128(2): 580-586. PMID:61961
    • (1976) J. Bacteriol , vol.128 , Issue.2 , pp. 580-586
    • Wolf-Watz, H.1    Normark, S.2


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