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Volumn 10, Issue 21, 2010, Pages 3910-3915

An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates

Author keywords

Mass spectrometry; Microbiology; Mycobacterium; Phosphoproteomics; Ser Thr protein kinase

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN GROEL2; PROTEIN HSPX; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 78049378075     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000316     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Av-Gay, Y., Everett, M., The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 2000, 8, 238-244.
    • (2000) Trends Microbiol. , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 2
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S. T., Brosch, R., Parkhill, J., Garnier, T. et al., Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4
  • 3
    • 77349099314 scopus 로고    scopus 로고
    • Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way
    • Molle, V., Kremer, L., Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way. Mol. Microbiol. 2010, 75, 1064-1077.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1064-1077
    • Molle, V.1    Kremer, L.2
  • 4
    • 38149136540 scopus 로고    scopus 로고
    • Mycobacterial Ser/Thr protein kinases and phosphatases: physiological roles and therapeutic potential
    • Wehenkel, A., Bellinzoni, M., Grana, M., Duran, R. et al., Mycobacterial Ser/Thr protein kinases and phosphatases: physiological roles and therapeutic potential. Biochim. Biophys. Acta 2008, 1784, 193-202.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 193-202
    • Wehenkel, A.1    Bellinzoni, M.2    Grana, M.3    Duran, R.4
  • 5
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom, N., Sicheritz-Ponten, T., Gupta, R., Gammeltoft, S. et al., Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 2004, 4, 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4
  • 6
    • 38149109895 scopus 로고    scopus 로고
    • Insights from site-specific phosphoproteomics in bacteria
    • Soufi, B., Jers, C., Hansen, M. E., Petranovic, D. et al., Insights from site-specific phosphoproteomics in bacteria. Biochim. Biophys. Acta 2008, 1784, 186-192.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 186-192
    • Soufi, B.1    Jers, C.2    Hansen, M.E.3    Petranovic, D.4
  • 7
    • 2942562627 scopus 로고    scopus 로고
    • The phosphorylation site database: a guide to the serine-, threonine-, and/or tyrosine-phosphorylated proteins in prokaryotic organisms
    • Wurgler-Murphy, S. M., King, D. M., Kennelly, P. J., The phosphorylation site database: a guide to the serine-, threonine-, and/or tyrosine-phosphorylated proteins in prokaryotic organisms. Proteomics 2004, 4, 1562-1570.
    • (2004) Proteomics , vol.4 , pp. 1562-1570
    • Wurgler-Murphy, S.M.1    King, D.M.2    Kennelly, P.J.3
  • 8
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U., Molecular chaperones in cellular protein folding. Nature 1996, 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 10
    • 0036773739 scopus 로고    scopus 로고
    • Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays
    • Stewart, G. R., Wernisch, L., Stabler, R., Mangan, J. A. et al., Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays. Microbiology 2002, 148, 3129-3138.
    • (2002) Microbiology , vol.148 , pp. 3129-3138
    • Stewart, G.R.1    Wernisch, L.2    Stabler, R.3    Mangan, J.A.4
  • 12
    • 0035133932 scopus 로고    scopus 로고
    • Differential expression of mycobacterial proteins following phagocytosis by macrophages
    • Monahan, I. M., Betts, J., Banerjee, D. K., Butcher, P. D., Differential expression of mycobacterial proteins following phagocytosis by macrophages. Microbiology 2001, 147, 459-471.
    • (2001) Microbiology , vol.147 , pp. 459-471
    • Monahan, I.M.1    Betts, J.2    Banerjee, D.K.3    Butcher, P.D.4
  • 13
    • 0035183063 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain
    • Lewthwaite, J. C., Coates, A. R., Tormay, P., Singh, M. et al., Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain. Infect. Immun. 2001, 69, 7349-7355.
    • (2001) Infect. Immun. , vol.69 , pp. 7349-7355
    • Lewthwaite, J.C.1    Coates, A.R.2    Tormay, P.3    Singh, M.4
  • 14
    • 67651215965 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages
    • Hickey, T. B., Thorson, L. M., Speert, D. P., Daffe, M. et al., Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages. Infect. Immun. 2009, 77, 3389-3401.
    • (2009) Infect. Immun. , vol.77 , pp. 3389-3401
    • Hickey, T.B.1    Thorson, L.M.2    Speert, D.P.3    Daffe, M.4
  • 15
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang, Z., Primm, T. P., Jakana, J., Lee, I. H. et al., Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J. Biol. Chem. 1996, 271, 7218-7223.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4
  • 16
    • 0029785912 scopus 로고    scopus 로고
    • Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial α-crystallin homolog
    • Yuan, Y., Crane, D. D., Barry, C. E., 3rd, Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial α-crystallin homolog. J. Bacteriol. 1996, 178, 4484-4492.
    • (1996) J. Bacteriol. , vol.178 , pp. 4484-4492
    • Yuan, Y.1    Crane, D.D.2    Barry 3rd, C.E.3
  • 17
    • 0032483025 scopus 로고    scopus 로고
    • The 16-kDa α-crystallin (Acr) protein of Mycobacterium tuberculosis is required for growth in macrophages
    • Yuan, Y., Crane, D. D., Simpson, R. M., Zhu, Y. Q. et al., The 16-kDa α-crystallin (Acr) protein of Mycobacterium tuberculosis is required for growth in macrophages. Proc. Natl. Acad. Sci. USA 1998, 95, 9578-9583.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9578-9583
    • Yuan, Y.1    Crane, D.D.2    Simpson, R.M.3    Zhu, Y.Q.4
  • 18
    • 65249125696 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases
    • Canova, M. J., Kremer, L., Molle, V., The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser/Thr protein kinases. J. Bacteriol. 2009, 191, 2876-2883.
    • (2009) J. Bacteriol. , vol.191 , pp. 2876-2883
    • Canova, M.J.1    Kremer, L.2    Molle, V.3
  • 19
    • 49949091451 scopus 로고    scopus 로고
    • pETPhos: a customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates
    • Canova, M. J., Kremer, L., Molle, V., pETPhos: a customized expression vector designed for further characterization of Ser/Thr/Tyr protein kinases and their substrates. Plasmid 2008, 60, 149-153.
    • (2008) Plasmid , vol.60 , pp. 149-153
    • Canova, M.J.1    Kremer, L.2    Molle, V.3
  • 20
    • 33749570515 scopus 로고    scopus 로고
    • The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation
    • Molle, V., Brown, A. K., Besra, G. S., Cozzone, A. J. et al., The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J. Biol. Chem. 2006, 281, 30094-30103.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30094-30103
    • Molle, V.1    Brown, A.K.2    Besra, G.S.3    Cozzone, A.J.4
  • 21
    • 65249174626 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue
    • Veyron-Churlet, R., Molle, V., Taylor, R. C., Brown, A. K. et al., The Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J. Biol. Chem. 2009, 284, 6414-6424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6414-6424
    • Veyron-Churlet, R.1    Molle, V.2    Taylor, R.C.3    Brown, A.K.4
  • 22
    • 77951212397 scopus 로고    scopus 로고
    • Phosphorylation of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis
    • Veyron-Churlet, R., Zanella-Cleon, I., Cohen-Gonsaud, M., Molle, V. et al., Phosphorylation of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis. J. Biol. Chem. 2010, 285, 12714-12725.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12714-12725
    • Veyron-Churlet, R.1    Zanella-Cleon, I.2    Cohen-Gonsaud, M.3    Molle, V.4
  • 23
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • Macek, B., Gnad, F., Soufi, B., Kumar, C. et al., Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell. Proteomics 2008, 7, 299-307.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4
  • 24
    • 0022774381 scopus 로고
    • Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis
    • Cortay, J. C., Rieul, C., Duclos, B., Cozzone, A. J., Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis. Eur. J. Biochem. 1986, 159, 227-237.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 227-237
    • Cortay, J.C.1    Rieul, C.2    Duclos, B.3    Cozzone, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.