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Volumn 155, Issue 3, 2009, Pages 932-943

CpgA, EF-Tu and the stressosome protein YezB are substrates of the Ser/Thr kinase/phosphatase couple, PrkC/PrpC, in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; INITIATION FACTOR; INITIATION FACTOR TU; PHOSPHATASE; POLYLYSINE; POLYPEPTIDE; PROTEIN CPGA; PROTEIN PRKC; PROTEIN PRPC; PROTEIN SERINE THREONINE KINASE; PROTEIN YEZB; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; ELONGATION FACTOR TU; PHOSPHOPROTEIN PHOSPHATASE; SERINE; THREONINE;

EID: 64049118984     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.022475-0     Document Type: Article
Times cited : (55)

References (57)
  • 4
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C. & Spizizen, J. (1961). Requirements for transformation in Bacillus subtilis. J Bacteriol 81, 741-746.
    • (1961) J Bacteriol , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 6
    • 17144424245 scopus 로고    scopus 로고
    • Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes
    • Archambaud, C., Gouin, E., Pizarro-Cerda, J., Cossart, P. & Dussurget, O. (2005). Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes. Mol Microbiol 56, 383-396.
    • (2005) Mol Microbiol , vol.56 , pp. 383-396
    • Archambaud, C.1    Gouin, E.2    Pizarro-Cerda, J.3    Cossart, P.4    Dussurget, O.5
  • 7
    • 39149123853 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: Mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c
    • Canova, M. J., Veyron-Churlet, R., Zanella-Cleon, I., Cohen-Gonsaud, M., Cozzone, A. J., Becchi, M., Kremer, L. & Molle, V. (2008). The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c. Proteomics 8, 521-533.
    • (2008) Proteomics , vol.8 , pp. 521-533
    • Canova, M.J.1    Veyron-Churlet, R.2    Zanella-Cleon, I.3    Cohen-Gonsaud, M.4    Cozzone, A.J.5    Becchi, M.6    Kremer, L.7    Molle, V.8
  • 9
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E. A., Tate, E. & Stemmer, W. P. (1996). Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol 14, 315-319.
    • (1996) Nat Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 10
    • 32244443761 scopus 로고    scopus 로고
    • The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division
    • Dasgupta, A., Datta, P., Kundu, M. & Basu, J. (2006). The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. Microbiology 152, 493-504.
    • (2006) Microbiology , vol.152 , pp. 493-504
    • Dasgupta, A.1    Datta, P.2    Kundu, M.3    Basu, J.4
  • 12
    • 34648857991 scopus 로고    scopus 로고
    • Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis
    • Eymann, C., Becher, D., Bernhardt, J., Gronau, K., Klutzny, A. & Hecker, M. (2007). Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7, 3509-3526.
    • (2007) Proteomics , vol.7 , pp. 3509-3526
    • Eymann, C.1    Becher, D.2    Bernhardt, J.3    Gronau, K.4    Klutzny, A.5    Hecker, M.6
  • 14
    • 0036842045 scopus 로고    scopus 로고
    • The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells
    • Gaidenko, T. A., Kim, T.-J. & Price, C. W. (2002). The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J Bacteriol 184, 6109-6114.
    • (2002) J Bacteriol , vol.184 , pp. 6109-6114
    • Gaidenko, T.A.1    Kim, T.-J.2    Price, C.W.3
  • 15
    • 2342578723 scopus 로고    scopus 로고
    • Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller
    • Good, M. C., Greenstein, A. E., Young, T. A., Ng, H. L. & Alber, T. (2004). Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller. J Mol Biol 339, 459-469.
    • (2004) J Mol Biol , vol.339 , pp. 459-469
    • Good, M.C.1    Greenstein, A.E.2    Young, T.A.3    Ng, H.L.4    Alber, T.5
  • 16
    • 85047696182 scopus 로고    scopus 로고
    • Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Greenstein, A. E., Echols, N., Lombana, T. N., King, D. S. & Alber, T. (2007). Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis. J Biol Chem 282, 11427-11435.
    • (2007) J Biol Chem , vol.282 , pp. 11427-11435
    • Greenstein, A.E.1    Echols, N.2    Lombana, T.N.3    King, D.S.4    Alber, T.5
  • 17
    • 22244486672 scopus 로고
    • Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains
    • 2005
    • Grundner, C., Gay, L. M. & Alber, T. (2005). Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Sci 14, 1918-1921.
    • (1918) Protein Sci , vol.14
    • Grundner, C.1    Gay, L.M.2    Alber, T.3
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983). Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166, 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 19
    • 35848954992 scopus 로고    scopus 로고
    • SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria
    • Hecker, M., Pané-Farré, J. & Völker, U. (2007). SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria. Annu Rev Microbiol 61, 215-236.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 215-236
    • Hecker, M.1    Pané-Farré, J.2    Völker, U.3
  • 20
    • 0026542743 scopus 로고
    • Potentiation of epidermal growth factor receptor protein-tyrosine kinase activity by sulfate
    • Hubler, L., Kher, U. & Bertics, P. J. (1992). Potentiation of epidermal growth factor receptor protein-tyrosine kinase activity by sulfate. Biochim Biophys Acta 1133, 307-315.
    • (1992) Biochim Biophys Acta , vol.1133 , pp. 307-315
    • Hubler, L.1    Kher, U.2    Bertics, P.J.3
  • 21
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M. & Kuriyan, J. (2002). The conformational plasticity of protein kinases. Cell 109, 275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 23
    • 33645054791 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a eukaryotic-type serine/threonine kinase and its cognate phosphatase in Streptococcus pyogenes: Their biological functions and substrate identification
    • Jin, H. & Pancholi, V. (2006). Identification and biochemical characterization of a eukaryotic-type serine/threonine kinase and its cognate phosphatase in Streptococcus pyogenes: their biological functions and substrate identification. J Mol Biol 357, 1351-1372.
    • (2006) J Mol Biol , vol.357 , pp. 1351-1372
    • Jin, H.1    Pancholi, V.2
  • 24
    • 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. (2006). Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside. J Bacteriol 188, 7470-7476.
    • (2006) J Bacteriol , vol.188 , pp. 7470-7476
    • Jones, G.1    Dyson, P.2
  • 25
    • 23044488472 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape
    • Kang, C.-M., Abbott, D. W., Park, S. T., Dascher, C. C., Cantley, L. C. & Husson, R. N. (2005). The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev 19, 1692-1704.
    • (2005) Genes Dev , vol.19 , pp. 1692-1704
    • Kang, C.-M.1    Abbott, D.W.2    Park, S.T.3    Dascher, C.C.4    Cantley, L.C.5    Husson, R.N.6
  • 26
    • 42949164129 scopus 로고    scopus 로고
    • Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria
    • Kang, C. M., Nyayapathy, S., Lee, J. Y., Suh, J. W. & Husson, R. N. (2008). Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria. Microbiology 154, 725-735.
    • (2008) Microbiology , vol.154 , pp. 725-735
    • Kang, C.M.1    Nyayapathy, S.2    Lee, J.Y.3    Suh, J.W.4    Husson, R.N.5
  • 27
    • 33847675357 scopus 로고    scopus 로고
    • A eukaryotic-type Ser/Thr kinase in Enterococcus faecalis mediates antimicrobial resistance and intestinal persistence
    • Kristich, C. J., Wells, C. L. & Dunny, G. M. (2007). A eukaryotic-type Ser/Thr kinase in Enterococcus faecalis mediates antimicrobial resistance and intestinal persistence. Proc Natl Acad Sci U S A 104, 3508-3513.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3508-3513
    • Kristich, C.J.1    Wells, C.L.2    Dunny, G.M.3
  • 29
    • 0036268103 scopus 로고    scopus 로고
    • afsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3
    • Lee, P. C., Umeyama, T. & Horinouchi, S. (2002). afsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2). Mol Microbiol 43, 1413-1430.
    • (2002) Mol Microbiol , vol.43 , pp. 1413-1430
    • Lee, P.C.1    Umeyama, T.2    Horinouchi, S.3
  • 31
    • 33645688327 scopus 로고    scopus 로고
    • Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes
    • Lévine, A., Vannier, F., Absalon, C., Kuhn, L., Jackson, P., Scrivener, E., Labas, V., Vinh, J., Courtney, P. & other authors (2006). Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6, 2157-2173.
    • (2006) Proteomics , vol.6 , pp. 2157-2173
    • Lévine, A.1    Vannier, F.2    Absalon, C.3    Kuhn, L.4    Jackson, P.5    Scrivener, E.6    Labas, V.7    Vinh, J.8    Courtney, P.9
  • 34
    • 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. & Séror, S. (2002). Characterization of a membrane-linked Ser/ Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol Microbiol 46, 571-586.
    • (2002) Mol Microbiol , vol.46 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Séror, S.5
  • 35
    • 0038047139 scopus 로고    scopus 로고
    • Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis
    • Madec, E., Stensballe, A., Kjellström, S., Cladière, L., Obuchowski, M., Jensen, O. N. & Séror, S. J. (2003). Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis. J Mol Biol 330, 459-472.
    • (2003) J Mol Biol , vol.330 , pp. 459-472
    • Madec, E.1    Stensballe, A.2    Kjellström, S.3    Cladière, L.4    Obuchowski, M.5    Jensen, O.N.6    Séror, S.J.7
  • 37
    • 16344395006 scopus 로고    scopus 로고
    • How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF
    • Mijakovic, I., Petranovic, D. & Deutscher, J. (2004). How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF. J Mol Microbiol Biotechnol 8, 19-25.
    • (2004) J Mol Microbiol Biotechnol , vol.8 , pp. 19-25
    • Mijakovic, I.1    Petranovic, D.2    Deutscher, J.3
  • 39
  • 40
    • 0043162014 scopus 로고    scopus 로고
    • Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis
    • Molle, V., Girard-Blanc, C., Kremer, L., Doublet, P., Cozzone, A. J. & Prost, J.-F. (2003a). Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis. Biochem Biophys Res Commun 308, 820-825.
    • (2003) Biochem Biophys Res Commun , vol.308 , pp. 820-825
    • Molle, V.1    Girard-Blanc, C.2    Kremer, L.3    Doublet, P.4    Cozzone, A.J.5    Prost, J.-F.6
  • 41
    • 0348223992 scopus 로고    scopus 로고
    • An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Molle, V., Kremer, L., Girard-Blanc, C., Besra, G. S., Cozzone, A. J. & Prost, J.-F. (2003b). An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis. Biochemistry 42, 15300-15309.
    • (2003) Biochemistry , vol.42 , pp. 15300-15309
    • Molle, V.1    Kremer, L.2    Girard-Blanc, C.3    Besra, G.S.4    Cozzone, A.J.5    Prost, J.-F.6
  • 42
    • 2342467904 scopus 로고    scopus 로고
    • Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Molle, V., Soulat, D., Jault, J. M., Grangeasse, C., Cozzone, A. J. & Prost, J. F. (2004). Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis. FEMS Microbiol Lett 234, 215-223.
    • (2004) FEMS Microbiol Lett , vol.234 , pp. 215-223
    • Molle, V.1    Soulat, D.2    Jault, J.M.3    Grangeasse, C.4    Cozzone, A.J.5    Prost, J.F.6
  • 43
    • 26944443097 scopus 로고    scopus 로고
    • Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development
    • Nariya, H. & Inouye, S. (2005). Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development. Mol Microbiol 58, 367-379.
    • (2005) Mol Microbiol , vol.58 , pp. 367-379
    • Nariya, H.1    Inouye, S.2
  • 44
    • 33745275549 scopus 로고    scopus 로고
    • A protein Ser/Thr kinase cascade negatively regulates the DNA-binding activity of MrpC, a smaller form of which may be necessary for the Myxococcus xanthus development
    • Nariya, H. & Inouye, S. (2006). A protein Ser/Thr kinase cascade negatively regulates the DNA-binding activity of MrpC, a smaller form of which may be necessary for the Myxococcus xanthus development. Mol Microbiol 60, 1205-1217.
    • (2006) Mol Microbiol , vol.60 , pp. 1205-1217
    • Nariya, H.1    Inouye, S.2
  • 45
    • 14644398001 scopus 로고    scopus 로고
    • Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates
    • Novakova, L., Saskova, L., Pallova, P., Janecek, J., Novotna, J., Ulrych, A., Echenique, J., Trombe, M. C. & Branny, P. (2005). Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates. FEBS J 272, 1243-1254.
    • (2005) FEBS J , vol.272 , pp. 1243-1254
    • Novakova, L.1    Saskova, L.2    Pallova, P.3    Janecek, J.4    Novotna, J.5    Ulrych, A.6    Echenique, J.7    Trombe, M.C.8    Branny, P.9
  • 46
  • 47
    • 27944433764 scopus 로고    scopus 로고
    • The RsbRST stress module in bacteria: A signalling system that may interact with different output modules
    • Pane-Farre, J., Lewis, R. J. & Stulke, J. (2005). The RsbRST stress module in bacteria: a signalling system that may interact with different output modules. J Mol Microbiol Biotechnol 9, 65-76.
    • (2005) J Mol Microbiol Biotechnol , vol.9 , pp. 65-76
    • Pane-Farre, J.1    Lewis, R.J.2    Stulke, J.3
  • 49
    • 19944374470 scopus 로고    scopus 로고
    • Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae
    • Rajagopal, L., Vo, A., Silvestroni, A. & Rubens, C. E. (2005). Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae. Mol Microbiol 56, 1329-1346.
    • (2005) Mol Microbiol , vol.56 , pp. 1329-1346
    • Rajagopal, L.1    Vo, A.2    Silvestroni, A.3    Rubens, C.E.4
  • 50
    • 34249801777 scopus 로고    scopus 로고
    • Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae
    • Saskova, L., Novakova, L., Basler, M. & Branny, P. (2007). Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae. J Bacteriol 189, 4168-4179.
    • (2007) J Bacteriol , vol.189 , pp. 4168-4179
    • Saskova, L.1    Novakova, L.2    Basler, M.3    Branny, P.4
  • 51
    • 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. K. (2008). A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135, 486-496.
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.K.4
  • 52
    • 33745283362 scopus 로고    scopus 로고
    • EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis
    • Sharma, K., Gupta, M., Krupa, A., Srinivasan, N. & Singh, Y. (2006). EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis. FEBS J 273, 2711-2721.
    • (2006) FEBS J , vol.273 , pp. 2711-2721
    • Sharma, K.1    Gupta, M.2    Krupa, A.3    Srinivasan, N.4    Singh, Y.5
  • 53
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189, 113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 54
    • 33845966777 scopus 로고    scopus 로고
    • GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA
    • Thakur, M. & Chakraborti, P. K. (2006). GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA. J Biol Chem 281, 40107-40113.
    • (2006) J Biol Chem , vol.281 , pp. 40107-40113
    • Thakur, M.1    Chakraborti, P.K.2
  • 55
    • 10144255829 scopus 로고    scopus 로고
    • Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor
    • Yang, X., Kang, C. M., Brody, M. S. & Price, C. W. (1996). Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev 10, 2265-2275.
    • (1996) Genes Dev , vol.10 , pp. 2265-2275
    • Yang, X.1    Kang, C.M.2    Brody, M.S.3    Price, C.W.4
  • 56
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A beta-lactam-binding domain
    • Yeats, C., Finn, R. D. & Bateman, A. (2002). The PASTA domain: a beta-lactam-binding domain. Trends Biochem Sci 27, 438.
    • (2002) Trends Biochem Sci , vol.27 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 57
    • 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. (2003). Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat Struct Biol 10, 168-174.
    • (2003) Nat Struct Biol , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5


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