메뉴 건너뛰기




Volumn 288, Issue 43, 2013, Pages 30883-30891

Structural basis of mycobacterial inhibition by Cyclomarin A

Author keywords

[No Author keywords available]

Indexed keywords

COCRYSTAL STRUCTURE; HIGH RESOLUTION; IN-VITRO; MYCOBACTERIAL; N-TERMINAL DOMAINS; PULLDOWN; STRUCTURAL BASIS;

EID: 84886703421     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.493767     Document Type: Article
Times cited : (97)

References (33)
  • 2
    • 77953475812 scopus 로고    scopus 로고
    • Global tuberculosis drug development pipeline. The need and the reality
    • Ma, Z., Lienhardt, C., McIlleron, H., Nunn, A. J., and Wang, X. (2010) Global tuberculosis drug development pipeline. The need and the reality. Lancet 375, 2100-2109
    • (2010) Lancet , vol.375 , pp. 2100-2109
    • Ma, Z.1    Lienhardt, C.2    McIlleron, H.3    Nunn, A.J.4    Wang, X.5
  • 5
  • 6
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti, C. M., Boyd, D. H., and Rubin, E. J. (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48, 77-84
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 7
    • 34548695934 scopus 로고    scopus 로고
    • Comparative genomics of mycobacterial proteases
    • Ribeiro-Guimarães, M. L., and Pessolani, M. C. (2007) Comparative genomics of mycobacterial proteases. Microb. Pathog. 43, 173-178
    • (2007) Microb. Pathog. , vol.43 , pp. 173-178
    • Ribeiro-Guimarães, M.L.1    Pessolani, M.C.2
  • 8
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang, F., Mei, Z., Qi, Y., Yan, C., Hu, Q., Wang, J., and Shi, Y. (2011) Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 471, 331-335
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3    Yan, C.4    Hu, Q.5    Wang, J.6    Shi, Y.7
  • 9
    • 6344252715 scopus 로고    scopus 로고
    • Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation
    • Chandu, D., and Nandi, D. (2004) Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation. Res. Microbiol. 155, 710-719
    • (2004) Res. Microbiol. , vol.155 , pp. 710-719
    • Chandu, D.1    Nandi, D.2
  • 11
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J., and Horwich, A. (2006) Molecular chaperones and protein quality control. Cell 125, 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 12
    • 71749085013 scopus 로고    scopus 로고
    • Clp chaperone-proteases. Structure and function
    • Kress, W., Maglica, Z., and Weber-Ban, E. (2009) Clp chaperone-proteases. Structure and function. Res. Microbiol. 160, 618-628
    • (2009) Res. Microbiol. , vol.160 , pp. 618-628
    • Kress, W.1    Maglica, Z.2    Weber-Ban, E.3
  • 13
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases: ATP-fueled machines of protein destruction
    • Sauer, R. T., and Baker, T. A. (2011) AAA+ proteases: ATP-fueled machines of protein destruction. Annu. Rev. Biochem. 80, 587-612
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 14
    • 56849094648 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis ClpC1. Characterization and role of the Nterminal domain in its function
    • Kar, N. P., Sikriwal, D., Rath, P., Choudhary, R. K., and Batra, J. K. (2008) Mycobacterium tuberculosis ClpC1. Characterization and role of the Nterminal domain in its function. FEBS J. 275, 6149-6158
    • (2008) FEBS J. , vol.275 , pp. 6149-6158
    • Kar, N.P.1    Sikriwal, D.2    Rath, P.3    Choudhary, R.K.4    Batra, J.K.5
  • 15
    • 84858794930 scopus 로고    scopus 로고
    • The active ClpP protease from M tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring
    • Akopian, T., Kandror, O., Raju, R. M., Unnikrishnan, M., Rubin, E. J., and Goldberg, A. L. (2012) The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring. EMBO J. 31, 1529-1541
    • (2012) EMBO J. , vol.31 , pp. 1529-1541
    • Akopian, T.1    Kandror, O.2    Raju, R.M.3    Unnikrishnan, M.4    Rubin, E.J.5    Goldberg, A.L.6
  • 16
    • 84860909929 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection
    • Raju, R. M., Unnikrishnan, M., Rubin, D. H., Krishnamoorthy, V., Kandror, O., Akopian, T. N., Goldberg, A. L., and Rubin, E. J. (2012) Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection. PLoS Pathog. 8, e1002511
    • (2012) PLoS Pathog. , vol.8
    • Raju, R.M.1    Unnikrishnan, M.2    Rubin, D.H.3    Krishnamoorthy, V.4    Kandror, O.5    Akopian, T.N.6    Goldberg, A.L.7    Rubin, E.J.8
  • 22
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • Evans, P. R. (2011) An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D Biol. Crystallogr. 67, 282-292
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 26
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo, F., Maurizi, M. R., Esser, L., and Xia, D. (2002) Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277, 46743-46752
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 27
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state
    • Lee, S., Sowa, M. E., Watanabe, Y. H., Sigler, P. B., Chiu, W., Yoshida, M., and Tsai, F. T. (2003) The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state. Cell 115, 229-240
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.H.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.7
  • 28
    • 0037336274 scopus 로고    scopus 로고
    • Crystal structure of the E coli Hsp100 ClpB N-terminal domain
    • Li, J., and Sha, B. (2003) Crystal structure of the E. coli Hsp100 ClpB N-terminal domain. Structure. 11, 323-328
    • (2003) Structure. , vol.11 , pp. 323-328
    • Li, J.1    Sha, B.2
  • 29
    • 77957229353 scopus 로고    scopus 로고
    • Thermodynamics guided lead discovery and optimization
    • Ferenczy, G. G., and Keserũ, G. M. (2010) Thermodynamics guided lead discovery and optimization. Drug Discov. Today 15, 919-932
    • (2010) Drug Discov. Today , vol.15 , pp. 919-932
    • Ferenczy, G.G.1    Keserũ, G.M.2
  • 33
    • 0031030242 scopus 로고    scopus 로고
    • Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis
    • Turgay, K., Hamoen, L. W., Venema, G., and Dubnau, D. (1997) Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis. Genes Dev. 11, 119-128
    • (1997) Genes Dev. , vol.11 , pp. 119-128
    • Turgay, K.1    Hamoen, L.W.2    Venema, G.3    Dubnau, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.