메뉴 건너뛰기




Volumn 289, Issue 45, 2014, Pages 31029-31042

The essential protein for bacterial flagella formation FlgJ functions as a β-N-acetylglucosaminidase

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYMES; PROTEINS;

EID: 84909952646     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.603944     Document Type: Article
Times cited : (52)

References (53)
  • 3
    • 0035863730 scopus 로고    scopus 로고
    • Flagellin, a novel mediator of Salmonella-induced epithelial activation and systemic inflammation: IκBα degradation, induction of nitric oxide synthase, induction of proinflammatory mediators, and cardiovascular dysfunction
    • Eaves-pyles, T., Murthy, K., Liaudet, L., Virág, L., Ross, G., Soriano, F. G., and Salzman, A. L. (2001) Flagellin, a novel mediator of Salmonella-induced epithelial activation and systemic inflammation: IκBα degradation, induction of nitric oxide synthase, induction of proinflammatory mediators, and cardiovascular dysfunction. J. Immunol. 166, 1248-1260
    • (2001) J. Immunol. , vol.166 , pp. 1248-1260
    • Eaves-pyles, T.1    Murthy, K.2    Liaudet, L.3    Virág, L.4    Ross, G.5    Soriano, F.G.6    Salzman, A.L.7
  • 4
    • 50049101426 scopus 로고    scopus 로고
    • Bringing order to a complex molecular machine: The assembly of the bacterial flagella
    • Apel, D., and Surette, M. G. (2008) Bringing order to a complex molecular machine: the assembly of the bacterial flagella. Biochim. Biophys. Acta 1778, 1851-1858
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1851-1858
    • Apel, D.1    Surette, M.G.2
  • 5
    • 0033033304 scopus 로고    scopus 로고
    • A new pathway for the secretion of virulence factors by bacteria: The flagellar export apparatus functions as a protein-secretion system
    • Young, G. M., Schmiel, D. H., and Miller, V. L. (1999) A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system. Proc. Natl. Acad. Sci. U.S.A. 96, 6456-6461
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3
  • 6
    • 33846923584 scopus 로고    scopus 로고
    • Plasticity of the domain structure in FlgJ, a bacterial protein involved in flagellar rod formation
    • Nambu, T., Inagaki, Y., and Kutsukake, K. (2006) Plasticity of the domain structure in FlgJ, a bacterial protein involved in flagellar rod formation. Genes Genet. Syst. 81, 381-389
    • (2006) Genes Genet. Syst. , vol.81 , pp. 381-389
    • Nambu, T.1    Inagaki, Y.2    Kutsukake, K.3
  • 7
    • 0026752989 scopus 로고
    • Morphological pathway of flagellar assembly in Salmonella typhimurium
    • Kubori, T., Shimamoto, N., Yamaguchi, S., Namba, K., and Aizawa, S. (1992) Morphological pathway of flagellar assembly in Salmonella typhimurium. J. Mol. Biol. 226, 433-446
    • (1992) J. Mol. Biol. , vol.226 , pp. 433-446
    • Kubori, T.1    Shimamoto, N.2    Yamaguchi, S.3    Namba, K.4    Aizawa, S.5
  • 8
    • 0017808121 scopus 로고
    • Incomplete flagellar structures in non-flagellate mutants of Salmonella typhimurium
    • Suzuki, T., Iino, T., Horiguchi, T., and Yamaguchi, S. (1978) Incomplete flagellar structures in non-flagellate mutants of Salmonella typhimurium. J. Bacteriol. 133, 904-915
    • (1978) J. Bacteriol. , vol.133 , pp. 904-915
    • Suzuki, T.1    Iino, T.2    Horiguchi, T.3    Yamaguchi, S.4
  • 9
    • 0032464279 scopus 로고    scopus 로고
    • A structural feature in the central channel of the bacterial flagellar FliF ring complex is implicated in type III protein export
    • Suzuki, H., Yonekura, K., Murata, K., Hirai, T., Oosawa, K., and Namba, K. (1998) A structural feature in the central channel of the bacterial flagellar FliF ring complex is implicated in type III protein export. J. Struct. Biol. 124, 104-114
    • (1998) J. Struct. Biol. , vol.124 , pp. 104-114
    • Suzuki, H.1    Yonekura, K.2    Murata, K.3    Hirai, T.4    Oosawa, K.5    Namba, K.6
  • 10
    • 0030047151 scopus 로고    scopus 로고
    • The permeability of the wall fabric of Escherichia coli and Bacillus subtilis
    • Demchick, P., and Koch, A. L. (1996) The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J. Bacteriol. 178, 768-773
    • (1996) J. Bacteriol. , vol.178 , pp. 768-773
    • Demchick, P.1    Koch, A.L.2
  • 11
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer, W., and Bertsche, U. (2008) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1778, 1714-1734
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 12
    • 84455162073 scopus 로고    scopus 로고
    • Peptidoglycan hydrolases of Escherichia coli
    • van Heijenoort, J. (2011) Peptidoglycan hydrolases of Escherichia coli. Microbiol. Mol. Biol. Rev. 75, 636-663
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 636-663
    • Van Heijenoort, J.1
  • 14
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Höltje, J.-V., Mirelman, D., Sharon, N., and Schwarz, U. (1975) Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124, 1067-1076
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Höltje, J.-V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 15
  • 16
    • 0033053893 scopus 로고    scopus 로고
    • Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium
    • Nambu, T., Minamino, T., Macnab, R. M., and Kutsukake, K. (1999) Peptidoglycan-hydrolyzing activity of the FlgJ protein, essential for flagellar rod formation in Salmonella typhimurium. J. Bacteriol. 181, 1555-1561
    • (1999) J. Bacteriol. , vol.181 , pp. 1555-1561
    • Nambu, T.1    Minamino, T.2    Macnab, R.M.3    Kutsukake, K.4
  • 17
    • 0029842085 scopus 로고    scopus 로고
    • Peptidoglycan as a barrier to transenvelope transport
    • Dijkstra, A. J., and Keck, W. (1996) Peptidoglycan as a barrier to transenvelope transport. J. Bacteriol. 178, 5555-5562
    • (1996) J. Bacteriol. , vol.178 , pp. 5555-5562
    • Dijkstra, A.J.1    Keck, W.2
  • 18
    • 0032453569 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the flagellin core protein and other genes encoding structural proteins of the Vibrio cholerae flagellum
    • Das, M., Chopra, A. K., Wood, T., and Peterson, J. W. (1998) Cloning, sequencing and expression of the flagellin core protein and other genes encoding structural proteins of the Vibrio cholerae flagellum. FEMS Microbiol. Lett. 165, 239-246
    • (1998) FEMS Microbiol. Lett. , vol.165 , pp. 239-246
    • Das, M.1    Chopra, A.K.2    Wood, T.3    Peterson, J.W.4
  • 19
    • 0035860359 scopus 로고    scopus 로고
    • The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific muramidase
    • 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, 359-369
    • (2001) J. Mol. Biol. , vol.312 , pp. 359-369
    • Hirano, T.1    Minamino, T.2    Macnab, R.M.3
  • 21
    • 77955263894 scopus 로고    scopus 로고
    • Mutational studies of the peptidoglycan hydrolase FlgJ of Sphingomonas sp. Strain A1
    • Maruyama, Y., Ochiai, A., Itoh, T., Mikami, B., Hashimoto, W., and Murata, K. (2010) Mutational studies of the peptidoglycan hydrolase FlgJ of Sphingomonas sp. strain A1. J. Basic Microbiol. 50, 311-317
    • (2010) J. Basic Microbiol. , vol.50 , pp. 311-317
    • Maruyama, Y.1    Ochiai, A.2    Itoh, T.3    Mikami, B.4    Hashimoto, W.5    Murata, K.6
  • 23
    • 36549017697 scopus 로고    scopus 로고
    • The flagellar muramidase from the photosynthetic bacterium Rhodobacter sphaeroides
    • de la Mora, J., Ballado, T., González-Pedrajo, B., Camarena, L., and Dreyfus, G. (2007) The flagellar muramidase from the photosynthetic bacterium Rhodobacter sphaeroides. J. Bacteriol. 189, 7998-8004
    • (2007) J. Bacteriol. , vol.189 , pp. 7998-8004
    • De La Mora, J.1    Ballado, T.2    González-Pedrajo, B.3    Camarena, L.4    Dreyfus, G.5
  • 24
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase
    • Mark, B. L., Vocadlo, D. J., Knapp, S., Triggs-Raine, B. L., Withers, S. G., and James, M. N. (2001) Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase. J. Biol. Chem. 276, 10330-10337
    • (2001) J. Biol. Chem. , vol.276 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 25
    • 84866324619 scopus 로고    scopus 로고
    • The C terminus of the flagellar muramidase SltF modulates the interaction with FlgJ in Rhodobacter sphaeroides
    • de la Mora, J., Osorio-Valeriano, M., González-Pedrajo, B., Ballado, T., Camarena, L., and Dreyfus, G. (2012) The C terminus of the flagellar muramidase SltF modulates the interaction with FlgJ in Rhodobacter sphaeroides. J. Bacteriol. 194, 4513-4520
    • (2012) J. Bacteriol. , vol.194 , pp. 4513-4520
    • De La Mora, J.1    Osorio-Valeriano, M.2    González-Pedrajo, B.3    Ballado, T.4    Camarena, L.5    Dreyfus, G.6
  • 26
    • 0037487270 scopus 로고    scopus 로고
    • A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole
    • Viollier, P. H., and Shapiro, L. (2003) A lytic transglycosylase homologue, PleA, is required for the assembly of pili and the flagellum at the Caulobacter crescentus cell pole. Mol. Microbiol. 49, 331-345
    • (2003) Mol. Microbiol. , vol.49 , pp. 331-345
    • Viollier, P.H.1    Shapiro, L.2
  • 27
    • 0027293346 scopus 로고
    • Compositional analysis of peptidoglycan by high performance anion-exchange chromatography
    • Clarke A. J. (1993) Compositional analysis of peptidoglycan by high performance anion-exchange chromatography. Anal. Biochem. 212, 344-350
    • (1993) Anal. Biochem. , vol.212 , pp. 344-350
    • Clarke, A.J.1
  • 28
    • 0014060395 scopus 로고
    • Measurement of bacteriolytic enzymes
    • Hash, J. H. (1967) Measurement of bacteriolytic enzymes. J. Bacteriol. 93, 1201-1202
    • (1967) J. Bacteriol. , vol.93 , pp. 1201-1202
    • Hash, J.H.1
  • 29
    • 0034633271 scopus 로고    scopus 로고
    • Assay for lytic transglycosylases: A family of peptidoglycan lyases
    • Blackburn, N. T., and Clarke, A. J. (2000) Assay for lytic transglycosylases: a family of peptidoglycan lyases. Anal. Biochem. 284, 388-393
    • (2000) Anal. Biochem. , vol.284 , pp. 388-393
    • Blackburn, N.T.1    Clarke, A.J.2
  • 30
    • 84901256994 scopus 로고    scopus 로고
    • A highly active and negatively charged Streptococcus pyogenes lysine with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia
    • Lood, R., Raz, A., Molina, H., Euler, C. W., and Fischetti, V. A. (2014) A highly active and negatively charged Streptococcus pyogenes lysine with a rare D-alanyl-L-alanine endopeptidase activity protects mice against streptococcal bacteremia. Antimicrob. Agents Chemother. 58, 3073-3084
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 3073-3084
    • Lood, R.1    Raz, A.2    Molina, H.3    Euler, C.W.4    Fischetti, V.A.5
  • 33
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey, R. M., Herbert, A. D., Sternberg, M. J., and Kelley, L. A. (2008) Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70, 611-625
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4
  • 34
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L. A., MacCallum, R. M., and Sternberg, M. J. (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299, 499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 77951243041 scopus 로고    scopus 로고
    • O-Acetylation of peptidoglycan in Gram-negative bacteria: Identification and characterization of peptidoglycan O-acetyltransferase in Neisseria gonorrhoeae
    • Moynihan, P. J., and Clarke, A. J. (2010) O-Acetylation of peptidoglycan in Gram-negative bacteria: identification and characterization of peptidoglycan O-acetyltransferase in Neisseria gonorrhoeae. J. Biol. Chem. 285, 13264-13273
    • (2010) J. Biol. Chem. , vol.285 , pp. 13264-13273
    • Moynihan, P.J.1    Clarke, A.J.2
  • 37
    • 84873845734 scopus 로고    scopus 로고
    • Mechanism of action of Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, an SGNH serine esterase
    • Pfeffer, J. M., Weadge, J. T., and Clarke, A. J. (2013) Mechanism of action of Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, an SGNH serine esterase. J. Biol. Chem. 288, 2605-2613
    • (2013) J. Biol. Chem. , vol.288 , pp. 2605-2613
    • Pfeffer, J.M.1    Weadge, J.T.2    Clarke, A.J.3
  • 38
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of helical and strand segments in proteins using CD spectroscopy
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (1999) Estimation of the number of helical and strand segments in proteins using CD spectroscopy. Protein Sci. 8, 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 39
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (2000) Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis. Anal. Biochem. 287, 243-251
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 41
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn, N. T., and Clarke, A. J. (2001) Identification of four families of peptidoglycan lytic transglycosylases. J. Mol. Evol. 52, 78-84
    • (2001) J. Mol. Evol. , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 42
    • 0037154093 scopus 로고    scopus 로고
    • Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa
    • Blackburn, N. T., and Clarke, A. J. (2002) Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa. Biochemistry 41, 1001-1013
    • (2002) Biochemistry , vol.41 , pp. 1001-1013
    • Blackburn, N.T.1    Clarke, A.J.2
  • 43
    • 43049098925 scopus 로고    scopus 로고
    • Polar, peritrichous, and lateral flagella belong to three distinguishable flagellar families
    • Fujii, M., Shibata, S., and Aizawa, S-I. (2008) Polar, peritrichous, and lateral flagella belong to three distinguishable flagellar families. J. Mol. Biol. 379, 273-283
    • (2008) J. Mol. Biol. , vol.379 , pp. 273-283
    • Fujii, M.1    Shibata, S.2    Aizawa, S.-I.3
  • 44
    • 0028016327 scopus 로고
    • Dimorphic transistion in Escherichia coli and Salmonella typhimurium: Surface-induced differentiation into hyperflagellate swarmer cells
    • Harshey, R. M., and Matsuyama, T. (1994) Dimorphic transistion in Escherichia coli and Salmonella typhimurium: surface-induced differentiation into hyperflagellate swarmer cells. Proc. Natl. Acad. Sci. U.S.A. 91, 8631-8635
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8631-8635
    • Harshey, R.M.1    Matsuyama, T.2
  • 45
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., and Dijkstra, B. W. (1995) Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and x-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry 34, 15619-15623
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 46
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S., and Vorgias, C. E. (1996) Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3, 638-648
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 47
    • 0031466989 scopus 로고    scopus 로고
    • Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation
    • Drouillard, S., Armand, S., Davies, G. J., Vorgias, C. E., and Henrissat, B. (1997) Serratia marcescens chitobiase is a retaining glycosidase utilizing substrate acetamido group participation. Biochem. J. 328, 945-949
    • (1997) Biochem. J. , vol.328 , pp. 945-949
    • Drouillard, S.1    Armand, S.2    Davies, G.J.3    Vorgias, C.E.4    Henrissat, B.5
  • 49
    • 70349140472 scopus 로고    scopus 로고
    • Molecular properties of the glucosaminidase AcmA from Lactococcus lactis MG1363: Mutational and biochemical analyses
    • Inagaki, N., Iguchi, A., Yokoyama, T., Yokoi, K. J., Ono, Y., Yamakawa, A., Taketo, A., and Kodaira, K. (2009) Molecular properties of the glucosaminidase AcmA from Lactococcus lactis MG1363: mutational and biochemical analyses. Gene 447, 61-71
    • (2009) Gene , vol.447 , pp. 61-71
    • Inagaki, N.1    Iguchi, A.2    Yokoyama, T.3    Yokoi, K.J.4    Ono, Y.5    Yamakawa, A.6    Taketo, A.7    Kodaira, K.8
  • 50
    • 84906546265 scopus 로고    scopus 로고
    • Structure of pneumococcal peptidoglycan hydrolase LytB reveals insights into the bacterial cell wall remodeling and pathogenesis
    • Bai, X.-H., Chen, H.-J., Jiang, Y. L., Wen, Z., Huang, Y., Cheng, W., Li, Q., Lei, Q., Zhang, J.-R., Chen, Y., and Zhou, C. Z. (2014) Structure of pneumococcal peptidoglycan hydrolase LytB reveals insights into the bacterial cell wall remodeling and pathogenesis. J. Biol. Chem. 289, 23403-23416
    • (2014) J. Biol. Chem. , vol.289 , pp. 23403-23416
    • Bai, X.-H.1    Chen, H.-J.2    Jiang, Y.L.3    Wen, Z.4    Huang, Y.5    Cheng, W.6    Li, Q.7    Lei, Q.8    Zhang, J.-R.9    Chen, Y.10    Zhou, C.Z.11
  • 51
    • 43049179699 scopus 로고    scopus 로고
    • Molecular properties of the putative autolysin Atl(WM) encoded by Staphylococcus warneri M: Mutational and biochemical analyses of the amidase and glucosaminidase domains
    • Yokoi, K. J., Sugahara, K., Iguchi, A., Nishitani, G., Ikeda, M., Shimada, T., Inagaki, N., Yamakawa, A., Taketo, A., and Kodaira, K. (2008) Molecular properties of the putative autolysin Atl(WM) encoded by Staphylococcus warneri M: mutational and biochemical analyses of the amidase and glucosaminidase domains. Gene 416, 66-76
    • (2008) Gene , vol.416 , pp. 66-76
    • Yokoi, K.J.1    Sugahara, K.2    Iguchi, A.3    Nishitani, G.4    Ikeda, M.5    Shimada, T.6    Inagaki, N.7    Yamakawa, A.8    Taketo, A.9    Kodaira, K.10
  • 52
    • 62449111582 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes
    • Bublitz, M., Polle, L., Holland, C., Heinz, D. W., Nimtz, M., and Schubert, W. D. (2009) Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes. Mol. Microbiol. 71, 1509-1522
    • (2009) Mol. Microbiol. , vol.71 , pp. 1509-1522
    • Bublitz, M.1    Polle, L.2    Holland, C.3    Heinz, D.W.4    Nimtz, M.5    Schubert, W.D.6
  • 53


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.