메뉴 건너뛰기




Volumn 195, Issue 11, 2013, Pages 2452-2462

The rcs stress response and accessory envelope proteins are required for de novo generation of cell shape in escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; LYSOZYME; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 1B; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 84877996484     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00160-13     Document Type: Article
Times cited : (73)

References (82)
  • 1
    • 33749257121 scopus 로고    scopus 로고
    • The selective value of bacterial shape
    • Young KD. 2006. The selective value of bacterial shape. Microbiol. Mol. Biol. Rev. 70:660-703.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 660-703
    • Young, K.D.1
  • 2
    • 36549043573 scopus 로고    scopus 로고
    • Bacterial morphology: why have different shapes
    • Young KD. 2007. Bacterial morphology: why have different shapes. Curr. Opin. Microbiol. 10:596-600.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 596-600
    • Young, K.D.1
  • 3
    • 44349096261 scopus 로고    scopus 로고
    • Stars of the terrestrial deep subsurface: a novel 'star-shaped' bacterial morphotype from a South African platinum mine
    • Wanger G, Onstott TC, Southam G. 2008. Stars of the terrestrial deep subsurface: a novel 'star-shaped' bacterial morphotype from a South African platinum mine. Geobiology 6:325-330.
    • (2008) Geobiology , vol.6 , pp. 325-330
    • Wanger, G.1    Onstott, T.C.2    Southam, G.3
  • 5
    • 38049053061 scopus 로고    scopus 로고
    • Detection of intracellular bacterial communities in human urinary tract infection
    • doi:10.1371/journal.pmed.0040329
    • Rosen DA, Hooton TM, Stamm WE, Humphrey PA, Hultgren SJ. 2007. Detection of intracellular bacterial communities in human urinary tract infection. PLoS Med. 4:e329. doi:10.1371/journal.pmed.0040329.
    • (2007) PLoS Med. , vol.4
    • Rosen, D.A.1    Hooton, T.M.2    Stamm, W.E.3    Humphrey, P.A.4    Hultgren, S.J.5
  • 7
    • 77953265009 scopus 로고    scopus 로고
    • Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization
    • Sycuro LK, Pincus Z, Gutierrez KD, Biboy J, Stern CA, Vollmer W, Salama NR. 2010. Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. Cell 141:822-833.
    • (2010) Cell , vol.141 , pp. 822-833
    • Sycuro, L.K.1    Pincus, Z.2    Gutierrez, K.D.3    Biboy, J.4    Stern, C.A.5    Vollmer, W.6    Salama, N.R.7
  • 8
    • 84861220120 scopus 로고    scopus 로고
    • Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential
    • doi:10.1371/journal.ppat.1002603
    • Sycuro LK, Wyckoff TJ, Biboy J, Born P, Pincus Z, Vollmer W, Salama NR. 2012. Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential. PLoS Pathog. 8:e1002603. doi:10.1371/journal.ppat.1002603.
    • (2012) PLoS Pathog. , vol.8
    • Sycuro, L.K.1    Wyckoff, T.J.2    Biboy, J.3    Born, P.4    Pincus, Z.5    Vollmer, W.6    Salama, N.R.7
  • 10
    • 70349675410 scopus 로고    scopus 로고
    • Studies on the susceptibility of different culture morphotypes of Listeria monocytogenes to uptake and survival in human polymorphonuclear leukocytes
    • Rowan NJ, Kirf D, Tomkins P. 2009. Studies on the susceptibility of different culture morphotypes of Listeria monocytogenes to uptake and survival in human polymorphonuclear leukocytes. FEMS Immunol. Med. Microbiol. 57:183-192.
    • (2009) FEMS Immunol. Med. Microbiol. , vol.57 , pp. 183-192
    • Rowan, N.J.1    Kirf, D.2    Tomkins, P.3
  • 11
    • 77957963129 scopus 로고    scopus 로고
    • Bacterial shape: two-dimensional questions and possibilities
    • Young KD. 2010. Bacterial shape: two-dimensional questions and possibilities. Annu. Rev. Microbiol. 64:223-240.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 223-240
    • Young, K.D.1
  • 13
    • 69949158186 scopus 로고    scopus 로고
    • Sculpting the bacterial cell
    • Margolin W. 2009. Sculpting the bacterial cell. Curr. Biol. 19:R812-R822.
    • (2009) Curr. Biol. , vol.19
    • Margolin, W.1
  • 14
    • 33646420904 scopus 로고    scopus 로고
    • Orchestrating bacterial cell morphogenesis
    • Carballido-López R. 2006. Orchestrating bacterial cell morphogenesis. Mol. Microbiol. 60:815-819.
    • (2006) Mol. Microbiol. , vol.60 , pp. 815-819
    • Carballido-López, R.1
  • 15
    • 77949421358 scopus 로고    scopus 로고
    • MreB drives de novo rod morphogenesis in Caulobacter crescentus via remodeling of the cell wall
    • Takacs CN, Poggio S, Charbon G, Pucheault M, Vollmer W, Jacobs-Wagner C. 2010. MreB drives de novo rod morphogenesis in Caulobacter crescentus via remodeling of the cell wall. J. Bacteriol. 192:1671-1684.
    • (2010) J. Bacteriol. , vol.192 , pp. 1671-1684
    • Takacs, C.N.1    Poggio, S.2    Charbon, G.3    Pucheault, M.4    Vollmer, W.5    Jacobs-Wagner, C.6
  • 17
    • 0041664049 scopus 로고    scopus 로고
    • Bacterial shape
    • Young KD. 2003. Bacterial shape. Mol. Microbiol. 49:571-580.
    • (2003) Mol. Microbiol. , vol.49 , pp. 571-580
    • Young, K.D.1
  • 18
    • 4944246437 scopus 로고    scopus 로고
    • FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
    • Varma A, Young KD. 2004. FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli. J. Bacteriol. 186:6768-6774.
    • (2004) J. Bacteriol. , vol.186 , pp. 6768-6774
    • Varma, A.1    Young, K.D.2
  • 19
    • 84859443989 scopus 로고    scopus 로고
    • Escherichia coli lowmolecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching
    • Potluri L-P, de Pedro MA, Young KD. 2012. Escherichia coli lowmolecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching. Mol. Microbiol. 84:203-224.
    • (2012) Mol. Microbiol. , vol.84 , pp. 203-224
    • Potluri, L.-P.1    de Pedro, M.A.2    Young, K.D.3
  • 21
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: an intermediate filament-like function in cell shape
    • Ausmees N, Kuhn JR, Jacobs-Wagner C. 2003. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 115:705-713.
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 22
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-Lopez R, Errington J. 2001. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 23
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse T, Moller-Jensen J, Lobner-Olesen A, Gerdes K. 2003. Dysfunctional MreB inhibits chromosome segregation in Escherichia coli.EMBOJ. 22:5283-5292.
    • (2003) EMBOJ. , vol.22 , pp. 5283-5292
    • Kruse, T.1    Moller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 24
    • 70350139098 scopus 로고    scopus 로고
    • Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis
    • Kawai Y, Asai K, Errington J. 2009. Partial functional redundancy of MreB isoforms, MreB, Mbl and MreBH, in cell morphogenesis of Bacillus subtilis. Mol. Microbiol. 73:719-731.
    • (2009) Mol. Microbiol. , vol.73 , pp. 719-731
    • Kawai, Y.1    Asai, K.2    Errington, J.3
  • 25
    • 0141478044 scopus 로고
    • Protoplasts and L-type growth of Escherichia coli
    • Lederberg J, St Clair J. 1958. Protoplasts and L-type growth of Escherichia coli. J. Bacteriol. 75:143-160.
    • (1958) J. Bacteriol. , vol.75 , pp. 143-160
    • Lederberg, J.1    St Clair, J.2
  • 26
    • 79959395109 scopus 로고
    • Production of protoplasts of Escherichia coli by lysozyme treatment
    • U.S.A.
    • Zinder ND, Arndt WF. 1956. Production of protoplasts of Escherichia coli by lysozyme treatment. Proc. Natl. Acad. Sci. U. S. A. 42:586-590.
    • (1956) Proc. Natl. Acad. Sci. , vol.42 , pp. 586-590
    • Zinder, N.D.1    Arndt, W.F.2
  • 27
    • 0015424999 scopus 로고
    • Calcium requirement and magnesium stimulation of Escherichia coli L-form induction
    • Makemson JC, Darwish RZ. 1972. Calcium requirement and magnesium stimulation of Escherichia coli L-form induction. Infect. Immun. 6:880-882.
    • (1972) Infect.Immun. , vol.6 , pp. 880-882
    • Makemson, J.C.1    Darwish, R.Z.2
  • 28
    • 0021925531 scopus 로고
    • Fusion of bacterial spheroplasts by electric fields
    • Ruthe HJ, Adler J. 1985. Fusion of bacterial spheroplasts by electric fields. Biochim. Biophys. Acta 819:105-113.
    • (1985) Biochim. Biophys. Acta , vol.819 , pp. 105-113
    • Ruthe, H.J.1    Adler, J.2
  • 29
    • 0032985224 scopus 로고    scopus 로고
    • Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis
    • Denome SA, Elf PK, Henderson TA, Nelson DE, Young KD. 1999. Escherichia coli mutants lacking all possible combinations of eight penicillin binding proteins: viability, characteristics, and implications for peptidoglycan synthesis. J. Bacteriol. 181:3981-3993.
    • (1999) J. Bacteriol. , vol.181 , pp. 3981-3993
    • Denome, S.A.1    Elf, P.K.2    Henderson, T.A.3    Nelson, D.E.4    Young, K.D.5
  • 30
    • 0034810694 scopus 로고    scopus 로고
    • Reconstruction of Escherichia coli mrcA (PBP 1a) mutants lacking multiple combinations of penicillin binding proteins
    • Meberg BM, Sailer FC, Nelson DE, Young KD. 2001. Reconstruction of Escherichia coli mrcA (PBP 1a) mutants lacking multiple combinations of penicillin binding proteins. J. Bacteriol. 183:6148-6149.
    • (2001) J. Bacteriol. , vol.183 , pp. 6148-6149
    • Meberg, B.M.1    Sailer, F.C.2    Nelson, D.E.3    Young, K.D.4
  • 32
    • 80052551898 scopus 로고    scopus 로고
    • Using superfolder green fluorescent protein for periplasmic protein localization studies
    • Dinh T, Bernhardt TG. 2011. Using superfolder green fluorescent protein for periplasmic protein localization studies. J. Bacteriol. 193:4984-4987.
    • (2011) J. Bacteriol. , vol.193 , pp. 4984-4987
    • Dinh, T.1    Bernhardt, T.G.2
  • 34
    • 0014044956 scopus 로고
    • Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli
    • Birdsell DC, Cota-Robles EH. 1967. Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli. J. Bacteriol. 93:427-437.
    • (1967) J. Bacteriol. , vol.93 , pp. 427-437
    • Birdsell, D.C.1    Cota-Robles, E.H.2
  • 36
    • 84862815508 scopus 로고    scopus 로고
    • Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli
    • Li G, Young KD. 2012. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol. Microbiol. 84:276-295.
    • (2012) Mol. Microbiol. , vol.84 , pp. 276-295
    • Li, G.1    Young, K.D.2
  • 37
    • 84870593406 scopus 로고    scopus 로고
    • In situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids
    • Angew.Chem.Int.Ed.Engl.
    • Kuru E, Hughes HV, Brown PJ, Hall E, Tekkam S, Cava F, de Pedro MA, Brun YV, VanNieuwenhze MS. 2012. In situ probing of newly synthesized peptidoglycan in live bacteria with fluorescent D-amino acids. Angew. Chem. Int. Ed. Engl. 51:12519-12523.
    • (2012) , vol.51 , pp. 12519-12523
    • Kuru, E.1    Hughes, H.V.2    Brown, P.J.3    Hall, E.4    Tekkam, S.5    Cava, F.6    de Pedro, M.A.7    Brun, Y.V.8    Vannieuwenhze, M.S.9
  • 38
    • 84877937587 scopus 로고
    • Studies in the physiology and biochemistry of penicillin-induced spheroplasts of Escherichia coli
    • Hurwitz C, Reiner JM, Landau JV. 1958. Studies in the physiology and biochemistry of penicillin-induced spheroplasts of Escherichia coli. J. Bacteriol. 76:612-617.
    • (1958) J. Bacteriol. , vol.76 , pp. 612-617
    • Hurwitz, C.1    Reiner, J.M.2    Landau, J.V.3
  • 39
    • 0029841665 scopus 로고    scopus 로고
    • Effect of O side-chain length and composition on the virulence of Shigella flexneri
    • Sandlin RC, Goldberg MB, Maurelli AT. 1996. Effect of O side-chain length and composition on the virulence of Shigella flexneri 2a. Mol. Microbiol. 22:63-73.
    • (1996) Mol. Microbiol. , vol.22 , pp. 63-73
    • Sandlin, R.C.1    Goldberg, M.B.2    Maurelli, A.T.3
  • 40
    • 0028271240 scopus 로고
    • Role of the rfe gene in the synthesis of the O8 antigen in Escherichia coli K-12
    • Rick PD, Hubbard GL, Barr K. 1994. Role of the rfe gene in the synthesis of the O8 antigen in Escherichia coli K-12. J. Bacteriol. 176:2877-2884.
    • (1994) J. Bacteriol. , vol.176 , pp. 2877-2884
    • Rick, P.D.1    Hubbard, G.L.2    Barr, K.3
  • 41
    • 77955939137 scopus 로고    scopus 로고
    • The Rcs phosphorelay: more than just a two-component pathway
    • Clarke DJ. 2010. The Rcs phosphorelay: more than just a two-component pathway. Future Microbiol. 5:1173-1184.
    • (2010) Future Microbiol. , vol.5 , pp. 1173-1184
    • Clarke, D.J.1
  • 42
    • 40449091818 scopus 로고    scopus 로고
    • The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance
    • Laubacher ME, Ades SE. 2008. The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance. J. Bacteriol. 190:2065-2074.
    • (2008) J. Bacteriol. , vol.190 , pp. 2065-2074
    • Laubacher, M.E.1    Ades, S.E.2
  • 43
    • 77957342591 scopus 로고    scopus 로고
    • Antimicrobial peptides activate the Rcs regulon through the outer membrane lipoprotein RcsF
    • Farris C, Sanowar S, Bader MW, Pfuetzner R, Miller SI. 2010. Antimicrobial peptides activate the Rcs regulon through the outer membrane lipoprotein RcsF. J. Bacteriol. 192:4894-4903.
    • (2010) J. Bacteriol. , vol.192 , pp. 4894-4903
    • Farris, C.1    Sanowar, S.2    Bader, M.W.3    Pfuetzner, R.4    Miller, S.I.5
  • 44
    • 9144251714 scopus 로고    scopus 로고
    • Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis
    • Ize B, Porcelli I, Lucchini S, Hinton JC, Berks BC, Palmer T. 2004. Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis. J. Biol. Chem. 279:47543-47554.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47543-47554
    • Ize, B.1    Porcelli, I.2    Lucchini, S.3    Hinton, J.C.4    Berks, B.C.5    Palmer, T.6
  • 45
    • 63049110964 scopus 로고    scopus 로고
    • The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme
    • Callewaert L, Vanoirbeek KG, Lurquin I, Michiels CW, Aertsen A. 2009. The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme. J. Bacteriol. 191:1979-1981.
    • (2009) J. Bacteriol. , vol.191 , pp. 1979-1981
    • Callewaert, L.1    Vanoirbeek, K.G.2    Lurquin, I.3    Michiels, C.W.4    Aertsen, A.5
  • 48
    • 39149088656 scopus 로고    scopus 로고
    • The penicillinbinding proteins: structure and role in peptidoglycan biosynthesis
    • Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P. 2008. The penicillinbinding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol. Rev. 32:234-258.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 51
    • 0036437019 scopus 로고    scopus 로고
    • Regulation and mode of action of the second small RNA activator of RpoS translation, RprA
    • Majdalani N, Hernandez D, Gottesman S. 2002. Regulation and mode of action of the second small RNA activator of RpoS translation, RprA. Mol. Microbiol. 46:813-826.
    • (2002) Mol. Microbiol. , vol.46 , pp. 813-826
    • Majdalani, N.1    Hernandez, D.2    Gottesman, S.3
  • 52
    • 0033525526 scopus 로고    scopus 로고
    • Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli
    • Vollmer W, von Rechenberg M, Holtje JV. 1999. Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274:6726-6734.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6726-6734
    • Vollmer, W.1    von Rechenberg, M.2    Holtje, J.V.3
  • 54
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt TG, de Boer PA. 2003. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48:1171-1182.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 55
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E
    • Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA. 2007. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 63:1008-1025.
    • (2007) coli. Mol. Microbiol. , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    de Boer, P.A.5
  • 56
    • 0018205871 scopus 로고
    • Murein-lipoprotein of Escherichia coli: a protein involved in the stabilization of bacterial cell envelope
    • Suzuki H, Nishimura Y, Yasuda S, Nishimura A, Yamada M, Hirota Y. 1978. Murein-lipoprotein of Escherichia coli: a protein involved in the stabilization of bacterial cell envelope. Mol. Gen. Genet. 167:1-9.
    • (1978) Mol. Gen. Genet. , vol.167 , pp. 1-9
    • Suzuki, H.1    Nishimura, Y.2    Yasuda, S.3    Nishimura, A.4    Yamada, M.5    Hirota, Y.6
  • 57
    • 0037378572 scopus 로고    scopus 로고
    • Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli
    • Ghosh AS, Young KD. 2003. Sequences near the active site in chimeric penicillin binding proteins 5 and 6 affect uniform morphology of Escherichia coli. J. Bacteriol. 185:2178-2186.
    • (2003) J. Bacteriol. , vol.185 , pp. 2178-2186
    • Ghosh, A.S.1    Young, K.D.2
  • 58
    • 0035026549 scopus 로고    scopus 로고
    • Contributions of PBP 5 and DDcarboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli
    • Nelson DE, Young KD. 2001. Contributions of PBP 5 and DDcarboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli. J. Bacteriol. 183:3055-3064.
    • (2001) J. Bacteriol. , vol.183 , pp. 3055-3064
    • Nelson, D.E.1    Young, K.D.2
  • 59
    • 3142671582 scopus 로고    scopus 로고
    • Branching sites and morphological abnormalities behave as ectopic poles in shapedefective Escherichia coli
    • Nilsen T, Ghosh AS, Goldberg MB, Young KD. 2004. Branching sites and morphological abnormalities behave as ectopic poles in shapedefective Escherichia coli. Mol. Microbiol. 52:1045-1054.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1045-1054
    • Nilsen, T.1    Ghosh, A.S.2    Goldberg, M.B.3    Young, K.D.4
  • 60
    • 33746649568 scopus 로고    scopus 로고
    • Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli
    • Priyadarshini R, Popham DL, Young KD. 2006. Daughter cell separation by penicillin-binding proteins and peptidoglycan amidases in Escherichia coli. J. Bacteriol. 188:5345-5355.
    • (2006) J. Bacteriol. , vol.188 , pp. 5345-5355
    • Priyadarshini, R.1    Popham, D.L.2    Young, K.D.3
  • 61
    • 34548593404 scopus 로고    scopus 로고
    • Unstable Esche-richia coli L forms revisited: growth requires peptidoglycan synthesis
    • Joseleau-Petit D, Liebart JC, Ayala JA, D'Ari R. 2007. Unstable Esche-richia coli L forms revisited: growth requires peptidoglycan synthesis. J. Bacteriol. 189:6512-6520.
    • (2007) J. Bacteriol. , vol.189 , pp. 6512-6520
    • Joseleau-Petit, D.1    Liebart, J.C.2    Ayala, J.A.3    D'Ari, R.4
  • 62
    • 84155171318 scopus 로고    scopus 로고
    • The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus
    • Domínguez-Cuevas P, Mercier R, Leaver M, Kawai Y, Errington J. 2012. The rod to L-form transition of Bacillus subtilis is limited by a requirement for the protoplast to escape from the cell wall sacculus. Mol. Microbiol. 83:52-66.
    • (2012) Mol. Microbiol. , vol.83 , pp. 52-66
    • Domínguez-Cuevas, P.1    Mercier, R.2    Leaver, M.3    Kawai, Y.4    Errington, J.5
  • 63
    • 67650462306 scopus 로고    scopus 로고
    • Listeria monocytogenes L-forms respond to cell wall deficiency by modifying gene expression and the mode of division
    • Dell'Era S, Buchrieser C, Couve E, Schnell B, Briers Y, Schuppler M, Loessner MJ. 2009. Listeria monocytogenes L-forms respond to cell wall deficiency by modifying gene expression and the mode of division. Mol. Microbiol. 73:306-322.
    • (2009) Mol. Microbiol. , vol.73 , pp. 306-322
    • Dell'Era, S.1    Buchrieser, C.2    Couve, E.3    Schnell, B.4    Briers, Y.5    Schuppler, M.6    Loessner, M.J.7
  • 64
    • 70350223544 scopus 로고    scopus 로고
    • Insights into the molecular basis of L-form formation and survival in Escherichia coli
    • doi:10.1371/journal.pone.0007316
    • Glover WA, Yang Y, Zhang Y. 2009. Insights into the molecular basis of L-form formation and survival in Escherichia coli. PLoS One 4:e7316. doi:10.1371/journal.pone.0007316.
    • (2009) PLoS One , vol.4
    • Glover, W.A.1    Yang, Y.2    Zhang, Y.3
  • 65
    • 33645035845 scopus 로고    scopus 로고
    • The role of the Rcs phosphorelay in Enterobacteriaceae
    • Huang YH, Ferrieres L, Clarke DJ. 2006. The role of the Rcs phosphorelay in Enterobacteriaceae. Res. Microbiol. 157:206-212.
    • (2006) Res. Microbiol. , vol.157 , pp. 206-212
    • Huang, Y.H.1    Ferrieres, L.2    Clarke, D.J.3
  • 66
    • 0348147587 scopus 로고    scopus 로고
    • The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface
    • Ferrières L, Clarke DJ. 2003. The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K-12 and controls the expression of a regulon in response to growth on a solid surface. Mol. Microbiol. 50:1665-1682.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1665-1682
    • Ferrières, L.1    Clarke, D.J.2
  • 67
    • 84877983608 scopus 로고    scopus 로고
    • Envelope stress
    • Storz G, Hengge R (ed), Bacterial stress responses, 2nd ed.,ASM Press, Washington, DC
    • Ades SE, Hayden JD, Laubacher ME. 2011. Envelope stress, p 115-131. In Storz G, Hengge R (ed), Bacterial stress responses, 2nd ed. ASM Press, Washington, DC.
    • (2011) , pp. 115-131
    • Ades, S.E.1    Hayden, J.D.2    Laubacher, M.E.3
  • 68
    • 25144451503 scopus 로고    scopus 로고
    • The Rcs phosphorelay: a complex signal transduction system
    • Majdalani N, Gottesman S. 2005. The Rcs phosphorelay: a complex signal transduction system. Annu. Rev. Microbiol. 59:379-405.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 69
    • 33748798703 scopus 로고    scopus 로고
    • Loss of O-antigen increases cell shape abnormalities in penicillin-binding protein mutants of Escherichia coli
    • Ghosh AS, Melquist AL, Young KD. 2006. Loss of O-antigen increases cell shape abnormalities in penicillin-binding protein mutants of Escherichia coli. FEMS Microbiol. Lett. 263:252-257.
    • (2006) FEMS Microbiol. Lett. , vol.263 , pp. 252-257
    • Ghosh, A.S.1    Melquist, A.L.2    Young, K.D.3
  • 70
    • 84877942610 scopus 로고    scopus 로고
    • Outer membrane, American Society for Microbiology, Washington, DC.,In Neidhardt FC, Curtiss R, III, Ingraham JL, Lin CC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed)
    • Nikaido H. 1996. Outer membrane, p 1549. In Neidhardt FC, Curtiss R, III, Ingraham JL, Lin CC, Low KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella: cellular and molecular biology, vol 1. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: cellular and molecular biology , vol.1
    • Nikaido, H.1
  • 72
    • 0025123204 scopus 로고
    • Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB
    • Garcíadel Portillo F, de Pedro MA. 1990. Differential effect of mutational impairment of penicillin-binding proteins 1A and 1B on Escherichia coli strains harboring thermosensitive mutations in the cell division genes ftsA, ftsQ, ftsZ, and pbpB. J. Bacteriol. 172:5863-5870.
    • (1990) J. Bacteriol. , vol.172 , pp. 5863-5870
    • Garcíadel Portillo, F.1    de Pedro, M.A.2
  • 74
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming A. 1922. On a remarkable bacteriolytic element found in tissues and secretions. Proc. R. Soc. Lond. B 93:306-317.
    • (1922) Proc. R. Soc. Lond. B , vol.93 , pp. 306-317
    • Fleming, A.1
  • 75
    • 0016664344 scopus 로고
    • The distribution of muramidase (lysozyme) in human tissues
    • Mason DY, Taylor CR. 1975. The distribution of muramidase (lysozyme) in human tissues. J. Clin. Pathol. 28:124-132.
    • (1975) J. Clin. Pathol. , vol.28 , pp. 124-132
    • Mason, D.Y.1    Taylor, C.R.2
  • 76
  • 77
    • 0021747540 scopus 로고
    • Lysozyme concentration in tears-assessment of reference values in normal subjects
    • Aine E, Morsky P. 1984. Lysozyme concentration in tears-assessment of reference values in normal subjects. Acta Ophthalmol. (Copenh.) 62:932-938.
    • (1984) Acta Ophthalmol. (Copenh.) , vol.62 , pp. 932-938
    • Aine, E.1    Morsky, P.2
  • 78
    • 0000097445 scopus 로고    scopus 로고
    • Salivary lysozyme: a noninvasive marker for the study of the effects of stress of natural immunity
    • Perera S, Uddin M, Hayes JA. 1997. Salivary lysozyme: a noninvasive marker for the study of the effects of stress of natural immunity. Int. J. Behav. Med. 4:170-178.
    • (1997) Int. J. Behav. Med. , vol.4 , pp. 170-178
    • Perera, S.1    Uddin, M.2    Hayes, J.A.3
  • 79
    • 0035703976 scopus 로고    scopus 로고
    • Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation
    • Montagne P, Cuilliere ML, Mole C, Bene MC, Faure G. 2001. Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation. Adv. Exp. Med. Biol. 501:241-247.
    • (2001) Adv. Exp. Med. Biol. , vol.501 , pp. 241-247
    • Montagne, P.1    Cuilliere, M.L.2    Mole, C.3    Bene, M.C.4    Faure, G.5
  • 81
    • 0037114149 scopus 로고    scopus 로고
    • Cationic polypeptides are required for antibacterial activity of human airway fluid
    • Cole AM, Liao HI, Stuchlik O, Tilan J, Pohl J, Ganz T. 2002. Cationic polypeptides are required for antibacterial activity of human airway fluid. J. Immunol. 169:6985-6991.
    • (2002) J. Immunol. , vol.169 , pp. 6985-6991
    • Cole, A.M.1    Liao, H.I.2    Stuchlik, O.3    Tilan, J.4    Pohl, J.5    Ganz, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.