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Volumn 22, Issue 14, 2015, Pages 1698-1709

Exit from mycobacterial dormancy: A structural perspective

Author keywords

Dormancy; Mycobacteria; Resuscitation; Structure

Indexed keywords

HYDROLASE; PEPTIDOGLYCAN;

EID: 84931263248     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867322666150209153027     Document Type: Article
Times cited : (18)

References (98)
  • 1
    • 84867988931 scopus 로고    scopus 로고
    • Genomic determinants of sporulation in Bacilli and Clostridia: Towards the minimal set of sporulation-specific genes
    • Galperin, M. Y.; Mekhedov, S. L.; Puigbo, P.; Smirnov, S.; Wolf, Y. I.; Rigden, D. J. Genomic determinants of sporulation in Bacilli and Clostridia: Towards the minimal set of sporulation-specific genes. Environ. Microbiol., 2012, 14(11), 2870-2890
    • (2012) Environ. Microbiol. , vol.14 , Issue.11 , pp. 2870-2890
    • Galperin, M.Y.1    Mekhedov, S.L.2    Puigbo, P.3    Smirnov, S.4    Wolf, Y.I.5    Rigden, D.J.6
  • 2
    • 31344441136 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptormediated transcytosis without altering the integrity of tight junctions
    • Menozzi FD, Reddy VM, Cayet D, Raze D, Debrie AS, Dehouck MP, Cecchelli R & Locht C (2006) Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptormediated transcytosis without altering the integrity of tight junctions. Microbes Infect 8, 1-9.
    • (2006) Microbes Infect , vol.8 , pp. 1-9
    • Menozzi, F.D.1    Reddy, V.M.2    Cayet, D.3    Raze, D.4    Debrie, A.S.5    Dehouck, M.P.6    Cecchelli, R.7    Locht, C.8
  • 3
    • 79959729031 scopus 로고    scopus 로고
    • Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation
    • Esposito, C.; Marasco, D.; Delogu, G.; Pedone, E.; Berisio, R. Heparin-binding hemagglutinin HBHA from Mycobacterium tuberculosis affects actin polymerisation. Biochem. Biophys. Res. Commun., 2011, 410(2), 339-344.
    • (2011) Biochem. Biophys. Res. Commun. , vol.410 , Issue.2 , pp. 339-344
    • Esposito, C.1    Marasco, D.2    Delogu, G.3    Pedone, E.4    Berisio, R.5
  • 4
    • 77950371492 scopus 로고    scopus 로고
    • Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: Implications for bacterial agglutination
    • Esposito C, Carullo P, Pedone E, Graziano G, Del Vecchio P & Berisio R (2010) Dimerisation and structural integrity of Heparin Binding Hemagglutinin A from Mycobacterium tuberculosis: implications for bacterial agglutination. FEBS Lett., 2010, 584(6), 1091-1096.
    • (2010) FEBS Lett. 2010 , vol.584 , Issue.6 , pp. 1091-1096
    • Esposito, C.1    Carullo, P.2    Pedone, E.3    Graziano, G.4    Vecchio, P.D.5    Berisio, R.6
  • 5
    • 46049101224 scopus 로고    scopus 로고
    • Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis
    • Esposito, C.; Pethoukov, M. V.; Svergun, D. I.; Ruggiero, A.; Pedone, C.; Pedone, E.; Berisio, R. Evidence for an elongated dimeric structure of heparin-binding hemagglutinin from Mycobacterium tuberculosis. J. Bacteriol., 2008, 190(13), 4749-4753.
    • (2008) J. Bacteriol. , vol.190 , Issue.13 , pp. 4749-4753
    • Esposito, C.1    Pethoukov, M.V.2    Svergun, D.I.3    Ruggiero, A.4    Pedone, C.5    Pedone, E.6    Berisio, R.7
  • 7
    • 79251589638 scopus 로고    scopus 로고
    • The challenge of new drug discovery for tuberculosis
    • Koul, A.; Arnoult, E.; Lounis, N.; Guillemont, J.; Andries, K. The challenge of new drug discovery for tuberculosis. Nature, 2011, 469(7331), 483-490.
    • (2011) Nature , vol.469 , Issue.7331 , pp. 483-490
    • Koul, A.1    Arnoult, E.2    Lounis, N.3    Guillemont, J.4    Andries, K.5
  • 8
    • 17644388063 scopus 로고    scopus 로고
    • Annulling a dangerous liaison: Vaccination strategies against AIDS and tuberculosis
    • Kaufmann, S. H.; McMichael, A. J. Annulling a dangerous liaison: vaccination strategies against AIDS and tuberculosis. Nat. Med., 2005, 11(4), S33-S44.
    • (2005) Nat. Med. , vol.11 , Issue.4 , pp. S33-S44
    • Kaufmann, S.H.1    McMichael, A.J.2
  • 11
    • 0027205450 scopus 로고
    • Why is Chlamydia sensitive to penicillin in the absence of peptidoglycan
    • Moulder, J. W. Why is Chlamydia sensitive to penicillin in the absence of peptidoglycan? Infect. Agents Dis., 1993, 2(2), 87-99.
    • (1993) Infect. Agents Dis. , vol.2 , Issue.2 , pp. 87-99
    • Moulder, J.W.1
  • 12
    • 0016748566 scopus 로고
    • Covalent lipoprotein from the outer membrane of Escherichia coli
    • Braun, V. Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim. Biophys. Acta, 1975, 415(3), 335-377.
    • (1975) Biochim. Biophys. Acta , vol.415 , Issue.3 , pp. 335-377
    • Braun, V.1
  • 13
    • 0020653625 scopus 로고
    • Structure, function, and assembly of cell walls of gram-positive bacteria
    • Shockman, G. D.; Barrett, J. F. Structure, function, and assembly of cell walls of gram-positive bacteria. Annu. Rev. Microbiol., 1983, 37, 501-527.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 501-527
    • Shockman, G.D.1    Barrett, J.F.2
  • 14
    • 0026071729 scopus 로고
    • Freezesubstitution of gram-negative eubacteria: General cell morphology and envelope profiles
    • Graham, L. L.; Harris, R.; Villiger, W.; Beveridge, T. J. Freezesubstitution of gram-negative eubacteria: general cell morphology and envelope profiles. J. Bacteriol., 1991, 173(5), 1623-1633.
    • (1991) J. Bacteriol. , vol.173 , Issue.5 , pp. 1623-1633
    • Graham, L.L.1    Harris, R.2    Villiger, W.3    Beveridge, T.J.4
  • 15
    • 84868090447 scopus 로고    scopus 로고
    • Targeting the mycobacterial envelope for tuberculosis drug development
    • Favrot, L.; Ronning, D. R.; Targeting the mycobacterial envelope for tuberculosis drug development. Expert Rev. Anti Infect. Ther., 2012, 10(9), 1023-1036.
    • (2012) Expert Rev. Anti Infect. Ther. , vol.10 , Issue.9 , pp. 1023-1036
    • Favrot, L.1    Ronning, D.R.2
  • 18
    • 84886920443 scopus 로고    scopus 로고
    • Inhibition of the First Step in Synthesis of the Mycobacterial Cell Wall Core, Catalyzed by the GlcNAc-1-phosphate Transferase WecA, by the Novel Caprazamycin Derivative CPZEN-45
    • Ishizaki, Y.; Hayashi, C.; Inoue, K.; Igarashi, M.; Takahashi, Y.; Pujari, V.; Crick, D. C.; Brennan, P. J.; Nomoto, A. Inhibition of the First Step in Synthesis of the Mycobacterial Cell Wall Core, Catalyzed by the GlcNAc-1-phosphate Transferase WecA, by the Novel Caprazamycin Derivative CPZEN-45. J. Biol. Chem., 2013, 288(42), 30309-30319.
    • (2013) J. Biol. Chem. , vol.288 , Issue.42 , pp. 30309-30319
    • Ishizaki, Y.1    Hayashi, C.2    Inoue, K.3    Igarashi, M.4    Takahashi, Y.5    Pujari, V.6    Crick, D.C.7    Brennan, P.J.8    Nomoto, A.9
  • 19
    • 0029738191 scopus 로고    scopus 로고
    • The convergence of murein recycling research with betalactamase research
    • Park, J. T. The convergence of murein recycling research with betalactamase research. Microb. Drug Resist., 1996, 2(1), 105-112.
    • (1996) Microb. Drug Resist. , vol.2 , Issue.1 , pp. 105-112
    • Park, J.T.1
  • 20
    • 84873775015 scopus 로고
    • Bagshaped macromolecules-A new outlook on bacterial cell walls
    • Weidel, W.; Pelzer, H. Bagshaped Macromolecules-a New Outlook on Bacterial Cell Walls. Adv. Enzymol. Relat. Areas Mol. Biol., 1964, 26, 193-232.
    • (1964) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.26 , pp. 193-232
    • Weidel, W.1    Pelzer, H.2
  • 21
    • 0015848145 scopus 로고
    • The chain length of the glycans in bacterial cell walls
    • Ward, J. B. The chain length of the glycans in bacterial cell walls. Biochem. J., 1973, 133(2), 395-398.
    • (1973) Biochem. J. , vol.133 , Issue.2 , pp. 395-398
    • Ward, J.B.1
  • 22
  • 23
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah, I. M.; Laaberki, M. H.; Popham, D. L.; Dworkin, J. A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell, 2008, 135(3), 486-496.
    • (2008) Cell , vol.135 , Issue.3 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 24
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, Dtranspeptidation
    • Lavollay, M.; Arthur, M.; Fourgeaud, M.; Dubost, L.; Marie, A.; Veziris, N.; Blanot, D.; Gutmann, L.; Mainardi, J. L. The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, Dtranspeptidation. J. Bacteriol., 2008, 190(12), 4360-4366.
    • (2008) J. Bacteriol. , vol.190 , Issue.12 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5    Veziris, N.6    Blanot, D.7    Gutmann, L.8    Mainardi, J.L.9
  • 26
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • Gupta, R.; Lavollay, M.; Mainardi, J. L.; Arthur, M.; Bishai, W. R.; Lamichhane, G. The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat. Med., 2010, 16(4), 466-469.
    • (2010) Nat. Med. , vol.16 , Issue.4 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5    Lamichhane, G.6
  • 27
    • 84861049632 scopus 로고    scopus 로고
    • Dynamics induced by beta-lactam antibiotics in the active site of Bacillus subtilis L, D-transpeptidase
    • Lecoq, L.; Bougault, C.; Hugonnet, J. E.; Veckerle, C.; Pessey, O.; Arthur, M.;Simorre, J. P. Dynamics induced by beta-lactam antibiotics in the active site of Bacillus subtilis L, D-transpeptidase. Structure, 2012, 20(5), 850-861.
    • (2012) Structure , vol.20 , Issue.5 , pp. 850-861
    • Lecoq, L.1    Bougault, C.2    Hugonnet, J.E.3    Veckerle, C.4    Pessey, O.5    Arthur, M.6    Simorre, J.P.7
  • 28
    • 50349098601 scopus 로고    scopus 로고
    • Role of Nacetylglucosaminidase and N-acetylmuramidase activities in Enterococcus faecalis peptidoglycan metabolism
    • Mesnage, S.; Chau, F.; Dubost, L.; Arthur, M. Role of Nacetylglucosaminidase and N-acetylmuramidase activities in Enterococcus faecalis peptidoglycan metabolism. J. Biol. Chem., 2008, 283(28), 19845-19853.
    • (2008) J. Biol. Chem. , vol.283 , Issue.28 , pp. 19845-19853
    • Mesnage, S.1    Chau, F.2    Dubost, L.3    Arthur, M.4
  • 29
    • 84887103834 scopus 로고    scopus 로고
    • Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-L-alanine amidase 3717 point to a role in peptidoglycan fragment recycling
    • Prigozhin, D. M.; Mavrici, D.; Huizar, J. P.; Vansell, H. J.; Alber, T. Structural and biochemical analyses of Mycobacterium tuberculosis N-acetylmuramyl-L-alanine amidase Rv3717 point to a role in peptidoglycan fragment recycling. J. Biol. Chem., 2013, 288(44), 31549-31555.
    • (2013) J. Biol. Chem. , vol.288 , Issue.44 , pp. 31549-31555
    • Prigozhin, D.M.1    Mavrici, D.2    Huizar, J.P.3    Vansell, H.J.4    Alber, T.5
  • 30
    • 84885389572 scopus 로고    scopus 로고
    • The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain
    • Rocaboy, M.; Herman, R.; Sauvage, E.; Remaut, H.; Moonens, K.; Terrak, M.; Charlier, P.; Kerff, F. The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain. Mol. Microbiol., 2013, 90(2), 267-277.
    • (2013) Mol. Microbiol. , vol.90 , Issue.2 , pp. 267-277
    • Rocaboy, M.1    Herman, R.2    Sauvage, E.3    Remaut, H.4    Moonens, K.5    Terrak, M.6    Charlier, P.7    Kerff, F.8
  • 31
    • 34250549335 scopus 로고
    • The mucopeptide turnover in the cell walls of growing cultures of Bacillus megaterium KM
    • Chaloupka, J.; Kreckova, P.; Rihova, L. The mucopeptide turnover in the cell walls of growing cultures of Bacillus megaterium KM. Experientia, 1962, 18, 362-363.
    • (1962) Experientia , vol.18 , pp. 362-363
    • Chaloupka, J.1    Kreckova, P.2    Rihova, L.3
  • 32
    • 52449146320 scopus 로고
    • Changes in the character of the cell wall in growth of Bacillus megaterium cultures
    • Chaloupka, J.; Kreckova, P.; Rihova, L. Changes in the character of the cell wall in growth of Bacillus megaterium cultures. Folia Microbiol. (Praha), 1962, 7, 269-274.
    • (1962) Folia Microbiol. (Praha) , vol.7 , pp. 269-274
    • Chaloupka, J.1    Kreckova, P.2    Rihova, L.3
  • 33
    • 0014036586 scopus 로고
    • The structure and biosynthesis of the components of the cell walls of gram-positive bacteria
    • Rogers, H. J. The structure and biosynthesis of the components of the cell walls of gram-positive bacteria. Folia Microbiol. (Praha), 1967, 12(3), 191-200.
    • (1967) Folia Microbiol. (Praha) , vol.12 , Issue.3 , pp. 191-200
    • Rogers, H.J.1
  • 34
    • 0015239261 scopus 로고
    • Turnover of the cell wall of Grampositive bacteria
    • Mauck, J.; Chan, L.; Glaser, L. Turnover of the cell wall of Grampositive bacteria. J. Biol. Chem., 1971, 246(6), 1820-1827.
    • (1971) J. Biol. Chem. , vol.246 , Issue.6 , pp. 1820-1827
    • Mauck, J.1    Chan, L.2    Glaser, L.3
  • 36
    • 0024234561 scopus 로고
    • Turnover of cell walls in microorganisms
    • Doyle, R. J.; Chaloupka, J.; Vinter, V. Turnover of cell walls in microorganisms. Microbiol. Rev., 1988, 52(4), 554-567.
    • (1988) Microbiol. Rev. , vol.52 , Issue.4 , pp. 554-567
    • Doyle, R.J.1    Chaloupka, J.2    Vinter, V.3
  • 37
    • 0024544714 scopus 로고
    • Cell wall assembly in Bacillus subtilis: Visualization of old and new wall material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid
    • Merad, T.; Archibald, A. R.; Hancock, I. C.; Harwood, C. R.; Hobot, J. A.; Cell wall assembly in Bacillus subtilis: visualization of old and new wall material by electron microscopic examination of samples stained selectively for teichoic acid and teichuronic acid. J. Gen. Microbiol., 1989, 135(6), 645-655.
    • (1989) J. Gen. Microbiol. , vol.135 , Issue.6 , pp. 645-655
    • Merad, T.1    Archibald, A.R.2    Hancock, I.C.3    Harwood, C.R.4    Hobot, J.A.5
  • 38
    • 0017229378 scopus 로고
    • Turnover and spreading of old wall during surface growth of Bacillus subtilis
    • Pooley, H. M. Turnover and spreading of old wall during surface growth of Bacillus subtilis. J. Bacteriol., 1976, 125(3), 1127-1138.
    • (1976) J. Bacteriol. , vol.125 , Issue.3 , pp. 1127-1138
    • Pooley, H.M.1
  • 39
    • 0028288896 scopus 로고
    • Structural differentiation of the Bacillus subtilis 168 cell wall
    • Graham, L. L.; Beveridge, T. J. Structural differentiation of the Bacillus subtilis 168 cell wall. J. Bacteriol., 1994, 176(5), 1413-1421.
    • (1994) J. Bacteriol. , vol.176 , Issue.5 , pp. 1413-1421
    • Graham, L.L.1    Beveridge, T.J.2
  • 40
    • 33748777110 scopus 로고    scopus 로고
    • Z ring as executor of bacterial cell division
    • Dajkovic, A.; Lutkenhaus, J. Z ring as executor of bacterial cell division. J. Mol. Microbiol. Biotechnol., 2006, 11(3-5), 140-151.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , Issue.3-5 , pp. 140-151
    • Dajkovic, A.1    Lutkenhaus, J.2
  • 41
    • 0018972825 scopus 로고
    • Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ)
    • Lutkenhaus, J. F.; Wolf-Watz, H.; Donachie, W. D. Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ). J. Bacteriol., 1980, 142(2), 615-620.
    • (1980) J. Bacteriol. , vol.142 , Issue.2 , pp. 615-620
    • Lutkenhaus, J.F.1    Wolf-Watz, H.2    Donachie, W.D.3
  • 42
    • 84891344282 scopus 로고    scopus 로고
    • The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
    • Loose, M.; Mitchison, T. J. The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns. Nat. Cell Biol., 2014, 16(1), 38-46.
    • (2014) Nat. Cell Biol. , vol.16 , Issue.1 , pp. 38-46
    • Loose, M.1    Mitchison, T.J.2
  • 43
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin, W. FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol, 2005, 6(11), 862-871.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.11 , pp. 862-871
    • Margolin, W.1
  • 44
    • 1242275409 scopus 로고    scopus 로고
    • R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division
    • Koppelman, C. M.; Aarsman. M. E.; Postmus, J.; Pas, E.; Muijsers, A. O.; Scheffers, D. J.; Nanninga, N.; den, Blaauwen. T. R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division. Mol. Microbiol., 2004, 51(3), 645-657.
    • (2004) Mol. Microbiol. , vol.51 , Issue.3 , pp. 645-657
    • Koppelman, C.M.1    Aarsman, M.E.2    Postmus, J.3    Pas, E.4    Muijsers, A.O.5    Scheffers, D.J.6    Nanninga, N.7    Den Blaauwen, T.8
  • 45
    • 1242275409 scopus 로고    scopus 로고
    • R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division
    • Koppelman, C. M.; Aarsman, M. E.; Postmus, J.; Pas, E.; Muijsers, A. O.; Scheffers, D. J.; Nanninga, N.; den Blaauwen, T. R174 of Escherichia coli FtsZ is involved in membrane interaction and protofilament bundling, and is essential for cell division. Mol. Microbiol., 2004, 51(3), 645-657.
    • (2004) Mol. Microbiol. , vol.51 , Issue.3 , pp. 645-657
    • Koppelman, C.M.1    Aarsman, M.E.2    Postmus, J.3    Pas, E.4    Muijsers, A.O.5    Scheffers, D.J.6    Nanninga, N.7    Den Blaauwen, T.8
  • 46
    • 40849118255 scopus 로고    scopus 로고
    • Bacterial growth and cell division: A mycobacterial perspective
    • Hett, E. C.; Rubin, E. J. Bacterial growth and cell division: A mycobacterial perspective. MMBR, 2008, 72(1), 126-156.
    • (2008) MMBR , vol.72 , Issue.1 , pp. 126-156
    • Hett, E.C.1    Rubin, E.J.2
  • 47
    • 0038141823 scopus 로고    scopus 로고
    • Conditional expression of Mycobacterium smegmatis ftsZ, an essential cell division gene
    • Dziadek, J.; Rutherford, S. A.; Madiraju, M. V.; Atkinson, M. A.; Rajagopalan, M. Conditional expression of Mycobacterium smegmatis ftsZ, an essential cell division gene. Microbiology, 2003, 149(Pt. 6), 1593-1603.
    • (2003) Microbiology , vol.149 , pp. 1593-1603
    • Dziadek, J.1    Rutherford, S.A.2    Madiraju, M.V.3    Atkinson, M.A.4    Rajagopalan, M.5
  • 51
    • 33646372958 scopus 로고    scopus 로고
    • Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis
    • Tufariello, J. M.; Mi, K.; Xu, J.; Manabe, Y. C.; Kesavan, A. K.; Drumm, J.; Tanaka, K.; Jacobs, W. R. Jr.; Chan, J. Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis. Infect. Immun., 2006, 74(5), 2985-2995.
    • (2006) Infect. Immun. , vol.74 , Issue.5 , pp. 2985-2995
    • Tufariello, J.M.1    Mi, K.2    Xu, J.3    Manabe, Y.C.4    Kesavan, A.K.5    Drumm, J.6    Tanaka, K.7    Jacobs, Jr.W.R.8    Chan, J.9
  • 52
    • 57749173148 scopus 로고    scopus 로고
    • Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. Tuberculosis
    • Ruggiero, A.; Tizzano, B.; Pedone, E.; Pedone, C.; Wilmanns, M.; Berisio, R. Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. Tuberculosis. 2009, J. Mol. Biol., 385(1), 153-162.
    • (2009) J. Mol. Biol. , vol.385 , Issue.1 , pp. 153-162
    • Ruggiero, A.1    Tizzano, B.2    Pedone, E.3    Pedone, C.4    Wilmanns, M.5    Berisio, R.6
  • 54
    • 84900402701 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis RpfE crystal structure reveals a positively charged catalytic cleft
    • Mavrici, D.; Prigozhin, D. M.; Alber, T. Mycobacterium tuberculosis RpfE crystal structure reveals a positively charged catalytic cleft. Protein Sci., 2014, 23(4), 481-487.
    • (2014) Protein Sci. , vol.23 , Issue.4 , pp. 481-487
    • Mavrici, D.1    Prigozhin, D.M.2    Alber, T.3
  • 56
    • 84979146389 scopus 로고
    • Stereochemistry and mechanism of enzymatic reactions
    • Koshland, D. E. Stereochemistry and mechanism of enzymatic reactions. Biol Rev., 1953, 28(4), 416-436.
    • (1953) Biol Rev. , vol.28 , Issue.4 , pp. 416-436
    • Koshland, D.E.1
  • 57
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo, D. J.; Davies, G. J.; Laine, R.; Withers, S. G. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature, 2001, 412(6849), 835-838.
    • (2001) Nature , vol.412 , Issue.6849 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 58
    • 0026734541 scopus 로고
    • Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: Structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35
    • Inoue, M.; Yamada, H.; Yasukochi, T.; Kuroki, R.; Miki, T.; Horiuchi, T.; Imoto, T. Multiple role of hydrophobicity of tryptophan-108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid-35. Biochemistry, 1992, 31(24), 5545-5553.
    • (1992) Biochemistry , vol.31 , Issue.24 , pp. 5545-5553
    • Inoue, M.1    Yamada, H.2    Yasukochi, T.3    Kuroki, R.4    Miki, T.5    Horiuchi, T.6    Imoto, T.7
  • 59
    • 0028934071 scopus 로고
    • Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity
    • Maenaka, K.; Matsushima, M.; Song, H.; Sunada, F.; Watanabe, K.; Kumagai, I. Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity. J. Mol. Biol., 1995, 247, 281-293.
    • (1995) J. Mol. Biol. , vol.247 , pp. 281-293
    • Maenaka, K.1    Matsushima, M.2    Song, H.3    Sunada, F.4    Watanabe, K.5    Kumagai, I.6
  • 60
    • 84878888480 scopus 로고    scopus 로고
    • Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses
    • Squeglia, F.; Romano, M.; Ruggiero, A.; Vitagliano, L.; De Simone, A.; Berisio, R. Carbohydrate recognition by RpfB from Mycobacterium tuberculosis unveiled by crystallographic and molecular dynamics analyses. Biophys. J., 2013, 104(11), 2530-2539.
    • (2013) Biophys. J. , vol.104 , Issue.11 , pp. 2530-2539
    • Squeglia, F.1    Romano, M.2    Ruggiero, A.3    Vitagliano, L.4    De Simone, A.5    Berisio, R.6
  • 62
    • 40349106168 scopus 로고    scopus 로고
    • A mycobacterial enzyme essential for cell division synergizes with resuscitationpromoting factor
    • Hett, E. C.; Chao, M. C.; Deng, L. L.; Rubin, E. J. A mycobacterial enzyme essential for cell division synergizes with resuscitationpromoting factor. PLoS Pathog., 2008, 4(2), e1000001.
    • (2008) PLoS Pathog. , vol.4 , Issue.2 , pp. e1000001
    • Hett, E.C.1    Chao, M.C.2    Deng, L.L.3    Rubin, E.J.4
  • 63
    • 77956331325 scopus 로고    scopus 로고
    • Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation
    • Ruggiero, A.; Marasco, D.; Squeglia, F.; Soldini, S.; Pedone, E.; Pedone, C.; Berisio, R. Structure and functional regulation of RipA, a mycobacterial enzyme essential for daughter cell separation. Structure, 2010, 18(9), 1184-1190.
    • (2010) Structure , vol.18 , Issue.9 , pp. 1184-1190
    • Ruggiero, A.1    Marasco, D.2    Squeglia, F.3    Soldini, S.4    Pedone, E.5    Pedone, C.6    Berisio, R.7
  • 65
  • 66
    • 45549087223 scopus 로고    scopus 로고
    • Identification and characterization of novel cell wall hydrolase CwlT: A two-domain autolysin exhibiting n-acetylmuramidase and DL-endopeptidase activities
    • Fukushima, T.; Kitajima, T.; Yamaguchi, H.; Ouyang, Q.; Furuhata, K.; Yamamoto, H.; Shida, T.; Sekiguchi, J. Identification and characterization of novel cell wall hydrolase CwlT: A two-domain autolysin exhibiting n-acetylmuramidase and DL-endopeptidase activities. J. Biol. Chem., 2008, 283(17), 11117-11125.
    • (2008) J. Biol. Chem. , vol.283 , Issue.17 , pp. 11117-11125
    • Fukushima, T.1    Kitajima, T.2    Yamaguchi, H.3    Ouyang, Q.4    Furuhata, K.5    Yamamoto, H.6    Shida, T.7    Sekiguchi, J.8
  • 68
    • 77952163865 scopus 로고    scopus 로고
    • Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide
    • Eldholm, V.; Johnsborg, O.; Straume, D.; Ohnstad, H. S.; Berg, K. H.; Hermoso, J. A.; Havarstein, L. S. Pneumococcal CbpD is a murein hydrolase that requires a dual cell envelope binding specificity to kill target cells during fratricide. Mol. Microbiol., 2010, 76(4), 905-917.
    • (2010) Mol. Microbiol , vol.76 , Issue.4 , pp. 905-917
    • Eldholm, V.1    Johnsborg, O.2    Straume, D.3    Ohnstad, H.S.4    Berg, K.H.5    Hermoso, J.A.6    Havarstein, L.S.7
  • 70
    • 84907016009 scopus 로고    scopus 로고
    • Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: Evidence for the L-to-D inversion of configuration of the catalytic cysteine
    • Squeglia, F.; Ruggiero, A.; Romano, M.; Vitagliano, L; Berisio, R. Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine. Acta Crystallogr. D Biol. Crystallogr., 2014, 70, 2295-2300.
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 2295-2300
    • Squeglia, F.1    Ruggiero, A.2    Romano, M.3    Vitagliano, L.4    Berisio, R.5
  • 71
    • 84880954944 scopus 로고    scopus 로고
    • Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria
    • Chao, M. C.; Kieser, K. J.; Minami, S.; Mavrici, D.; Aldridge, B. B.; Fortune, S. M.; Alber, T.; Rubin, E. J. Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria. PLoS Pathog., 2013, 9(2), e1003197.
    • (2013) PLoS Pathog. , vol.9 , Issue.2 , pp. e1003197
    • Chao, M.C.1    Kieser, K.J.2    Minami, S.3    Mavrici, D.4    Aldridge, B.B.5    Fortune, S.M.6    Alber, T.7    Rubin, E.J.8
  • 72
    • 32444437484 scopus 로고    scopus 로고
    • A eukaryotic-type serine/threonine protein kinase is required for biofilm formation, genetic competence, and acid resistance in Streptococcus mutans
    • Hussain, H.; Branny, P.; Allan, E. A eukaryotic-type serine/threonine protein kinase is required for biofilm formation, genetic competence, and acid resistance in Streptococcus mutans. J. Bacteriol., 2006, 188(4), 1628-1632.
    • (2006) J. Bacteriol. , vol.188 , Issue.4 , pp. 1628-1632
    • Hussain, H.1    Branny, P.2    Allan, E.3
  • 73
    • 49649128879 scopus 로고    scopus 로고
    • From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division
    • Fiuza, M.; Canova, M. J.; Zanella-Cleon, I.; Becchi, M.; Cozzone, A. J.; Mateos, L. M.; Kremer, L.; Gil, J A.; Molle, V. From the characterization of the four serine/threonine protein kinases (PknA/B/G/L) of Corynebacterium glutamicum toward the role of PknA and PknB in cell division. J. Biol. Chem., 2008, 283(26), 18099-18112.
    • (2008) J. Biol. Chem. , vol.283 , Issue.26 , pp. 18099-18112
    • Fiuza, M.1    Canova, M.J.2    Zanella-Cleon, I.3    Becchi, M.4    Cozzone, A.J.5    Mateos, L.M.6    Kremer, L.7    Gil, J.A.8    Molle, V.9
  • 74
    • 61349099574 scopus 로고    scopus 로고
    • The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum
    • Fiuza, M.; Canova, M. J.; Patin, D.; Letek, M.; Zanella-Cleon, I.; Becchi, M.; Mateos, L. M.; Mengin-Lecreulx, D.; Molle, V.; Gil J. A. The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum. J. Biol, Chem., 2008, 283(5), 36553-36563.
    • (2008) J. Biol, Chem. , vol.283 , Issue.5 , pp. 36553-36563
    • Fiuza, M.1    Canova, M.J.2    Patin, D.3    Letek, M.4    Zanella-Cleon, I.5    Becchi, M.6    Mateos, L.M.7    Mengin-Lecreulx, D.8    Molle, V.9    Gil, J.A.10
  • 75
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes
    • Madec, E.; Laszkiewicz, A.; Iwanicki, A.; Obuchowski, M.; Seror, S. Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol. Microbiol., 2002, 46(2), 571-586.
    • (2002) Mol. Microbiol. , vol.46 , Issue.2 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Seror, S.5
  • 76
    • 0038047139 scopus 로고    scopus 로고
    • Mass spectrometry and sitedirected mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis
    • Madec, E.; Stensballe, A.; Kjellstrom, S.; Cladiere, L.; Obuchowski, M.; Jensen, O. N.; Seror, S. J. Mass spectrometry and sitedirected mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis. J. Mol. Biol., 2003, 330(3), 459-472.
    • (2003) J. Mol. Biol. , vol.330 , Issue.3 , pp. 459-472
    • Madec, E.1    Stensballe, A.2    Kjellstrom, S.3    Cladiere, L.4    Obuchowski, M.5    Jensen, O.N.6    Seror, S.J.7
  • 77
    • 64049118984 scopus 로고    scopus 로고
    • CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis
    • Absalon, C.; Obuchowski, M.; Madec, E.; Delattre, D.; Holland, I. B.; Seror, S. J. CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis. Microbiology, 2009, 155(pt3), 932-943.
    • (2009) Microbiology , vol.155 , pp. 932-943
    • Absalon, C.1    Obuchowski, M.2    Madec, E.3    Delattre, D.4    Holland, I.B.5    Seror, S.J.6
  • 78
    • 33750444279 scopus 로고    scopus 로고
    • Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: Inside versus outside
    • Jones, G.; Dyson, P. Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside. J. Bacteriol., 2006, 188(21), 7470-7476.
    • (2006) J. Bacteriol. , vol.188 , Issue.21 , pp. 7470-7476
    • Jones, G.1    Dyson, P.2
  • 79
    • 79952848730 scopus 로고    scopus 로고
    • X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus
    • Ruggiero, A.; Squeglia, F.; Marasco, D.; Marchetti, R.; Molinaro, A.; Berisio, R. X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus. Biochem. J., 2011, 435(1), 33-41.
    • (2011) Biochem. J. , vol.435 , Issue.1 , pp. 33-41
    • Ruggiero, A.1    Squeglia, F.2    Marasco, D.3    Marchetti, R.4    Molinaro, A.5    Berisio, R.6
  • 81
    • 84898955995 scopus 로고    scopus 로고
    • Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis
    • Calvanese, L.; Falcigno, L.; Maglione, C.; Marasco, D.; Ruggiero, A.; Squeglia, F.; Berisio, R.; D'Auria, G. Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis. Biopolymers, 2014, 101(7), 712-719
    • (2014) Biopolymers , vol.101 , Issue.7 , pp. 712-719
    • Calvanese, L.1    Falcigno, L.2    Maglione, C.3    Marasco, D.4    Ruggiero, A.5    Squeglia, F.6    Berisio, R.7    D'Auria, G.8
  • 82
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A betalactam-binding domain
    • Yeats, C.; Finn, R. D.; Bateman, A. The PASTA domain: A betalactam-binding domain. Trends Biochem. Sci., 2002, 27(9), 438.
    • (2002) Trends Biochem. Sci. , vol.27 , Issue.9 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 83
    • 77954005502 scopus 로고    scopus 로고
    • A role for the class A penicillinbinding protein PonA2 in the survival of Mycobacterium smegmatis under conditions of nonreplication
    • Patru, M. M.; Pavelka, M. S. Jr. A role for the class A penicillinbinding protein PonA2 in the survival of Mycobacterium smegmatis under conditions of nonreplication. J. Bacteriol., 2010, 192(12), 3043-3054.
    • (2010) J. Bacteriol. , vol.192 , Issue.12 , pp. 3043-3054
    • Patru, M.M.1    Pavelka, Jr.M.S.2
  • 84
    • 79960964670 scopus 로고    scopus 로고
    • The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization
    • Mir, M.; Asong, J.; Li, X.; Cardot, J.; Boons, G.; Husson, R. N. The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLOS Pathog., 7(7), e1002182
    • PLOS Pathog. , vol.7 , Issue.7 , pp. 1002182
    • Mir, M.1    Asong, J.2    Li, X.3    Cardot, J.4    Boons, G.5    Husson, R.N.6
  • 85
    • 33646378677 scopus 로고    scopus 로고
    • Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins
    • Lim, J. H.; Kim, M. S.; Kim, H. E.; Yano, T.; Oshima, Y.; Aggarwal, K.; Goldman, W. E.; Silverman, N.; Kurata, S.; Oh, B. H. Structural basis for preferential recognition of diaminopimelic acid-type peptidoglycan by a subset of peptidoglycan recognition proteins. J. Biol. Chem., 2006, 281(12), 8286-8295.
    • (2006) J. Biol. Chem. , vol.281 , Issue.12 , pp. 8286-8295
    • Lim, J.H.1    Kim, M.S.2    Kim, H.E.3    Yano, T.4    Oshima, Y.5    Aggarwal, K.6    Goldman, W.E.7    Silverman, N.8    Kurata, S.9    Oh, B.H.10
  • 86
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard, S. R.; Till, J. H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem., 2000, 69, 373-398.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 87
    • 0028838012 scopus 로고
    • Dimerization of cell-surface receptors in signal-transduction
    • Heldin, C. H. Dimerization of Cell-Surface Receptors in Signal-Transduction. Cell, 1995, 80(2), 213-223.
    • (1995) Cell , vol.80 , Issue.2 , pp. 213-223
    • Heldin, C.H.1
  • 88
    • 79953890803 scopus 로고    scopus 로고
    • The structural biology of toll-like receptors
    • Botos, I.; Segal, D. M.; Davies, D. R. The Structural Biology of Toll-like Receptors. Structure, 2011, 19(4), 447-459.
    • (2011) Structure , vol.19 , Issue.4 , pp. 447-459
    • Botos, I.1    Segal, D.M.2    Davies, D.R.3
  • 89
    • 57149120752 scopus 로고    scopus 로고
    • Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase
    • Mieczkowski, C.; Iavarone, A. T.; Alber, T. Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase. Embo J., 27(23), 3186-3197.
    • Embo J. , vol.27 , Issue.23 , pp. 3186-3197
    • Mieczkowski, C.1    Iavarone, A.T.2    Alber, T.3
  • 90
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young, T. A.; Delagoutte, B.; Endrizzi, J. A.; Falick, A. M.; Alber, T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struc. Biol., 2003, 10(3), 168-174.
    • (2003) Nat. Struc. Biol. , vol.10 , Issue.3 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 91
    • 84904617793 scopus 로고    scopus 로고
    • Mechanism of autophosphorylation of mycobacterial PknB explored by molecular dynamics simulations
    • Damle, N. P.; Mohanty, D. Mechanism of autophosphorylation of mycobacterial PknB explored by molecular dynamics simulations. Biochemistry, 2014, 53, 4715-4726.
    • (2014) Biochemistry , vol.53 , pp. 4715-4726
    • Damle, N.P.1    Mohanty, D.2
  • 92
    • 77952657885 scopus 로고    scopus 로고
    • The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation
    • Barthe, P.; Mukamolova, G. V.; Roumestand, C.; Cohen-Gonsaud, M. The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation. Structure, 2010, 18(5), 606-615.
    • (2010) Structure , vol.18 , Issue.5 , pp. 606-615
    • Barthe, P.1    Mukamolova, G.V.2    Roumestand, C.3    Cohen-Gonsaud, M.4
  • 94
    • 0032824605 scopus 로고    scopus 로고
    • The role of peptidoglycan structure and structural dynamics during endospore dormancy and germination
    • Atrih, A.; Foster, S. J. The role of peptidoglycan structure and structural dynamics during endospore dormancy and germination. Antonie Van Leeuwenhoek, 1999, 75(4), 299-307.
    • (1999) Antonie Van Leeuwenhoek , vol.75 , Issue.4 , pp. 299-307
    • Atrih, A.1    Foster, S.J.2
  • 96
    • 84875134300 scopus 로고    scopus 로고
    • Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis
    • Ruggiero, A.; Marchant, J.; Squeglia, F.; Makarov, V.; De Simone, A.; Berisio, R. Molecular determinants of inactivation of the resuscitation promoting factor B from Mycobacterium tuberculosis. J. Biomol. Struct. Dyn., 2013, 31(2), 195-205.
    • (2013) J. Biomol. Struct. Dyn. , vol.31 , Issue.2 , pp. 195-205
    • Ruggiero, A.1    Marchant, J.2    Squeglia, F.3    Makarov, V.4    De Simone, A.5    Berisio, R.6
  • 97
  • 98
    • 80052345448 scopus 로고    scopus 로고
    • A delicate dance: Host response to mycobacteria
    • Huynh, K. K.; Joshi, S. A.; Brown, E. J. A delicate dance: host response to mycobacteria. Curr. Opin. Immunol., 2011, 23(4), 464-472.
    • (2011) Curr. Opin. Immunol. , vol.23 , Issue.4 , pp. 464-472
    • Huynh, K.K.1    Joshi, S.A.2    Brown, E.J.3


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