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Volumn 5, Issue 5, 2010, Pages

A framework for classification of prokaryotic protein kinases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SERINE THREONINE KINASE;

EID: 77956534307     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0010608     Document Type: Article
Times cited : (19)

References (126)
  • 1
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the ''eukaryotic'' protein kinase superfamily
    • Leonard CJ, Aravind L, Koonin EV (1998) Novel families of putative protein kinases in bacteria and archaea: evolution of the ''eukaryotic'' protein kinase superfamily. Genome Res 8: 1038-1047.
    • (1998) Genome Res , vol.8 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 2
    • 0035849669 scopus 로고    scopus 로고
    • On the origin of Ser/Thr kinases in a prokaryote
    • Han G, Zhang CC (2001) On the origin of Ser/Thr kinases in a prokaryote. FEMS Microbiol Lett 200: 79-84.
    • (2001) FEMS Microbiol Lett , vol.200 , pp. 79-84
    • Han, G.1    Zhang, C.C.2
  • 3
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • Kennelly PJ (2002) Protein kinases and protein phosphatases in prokaryotes: a genomic perspective. FEMS Microbiol Lett 206: 1-8.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 4
    • 0036100787 scopus 로고    scopus 로고
    • Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases
    • Krupa A, Srinivasan N (2002) Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases. Protein Sci 11: 1580-1584.
    • (2002) Protein Sci , vol.11 , pp. 1580-1584
    • Krupa, A.1    Srinivasan, N.2
  • 5
    • 25444460385 scopus 로고    scopus 로고
    • Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes
    • Krupa A, Srinivasan N (2005) Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes. BMC Genomics 6: 129.
    • (2005) BMC Genomics , vol.6 , pp. 129
    • Krupa, A.1    Srinivasan, N.2
  • 7
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: An emerging regulatory device of bacterial physiology
    • Grangeasse C, Cozzone AJ, Deutscher J, Mijakovic I (2007) Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem Sci 32: 86-94.
    • (2007) Trends Biochem Sci , vol.32 , pp. 86-94
    • Grangeasse, C.1    Cozzone, A.J.2    Deutscher, J.3    Mijakovic, I.4
  • 8
    • 54949108269 scopus 로고    scopus 로고
    • Identification of the idiosyncratic bacterial protein tyrosine kinase (BY-kinase) family signature
    • Jadeau F, Bechet E, Cozzone AJ, Deleage G, Grangeasse C, et al. (2008) Identification of the idiosyncratic bacterial protein tyrosine kinase (BY-kinase) family signature. Bioinformatics 24: 2427-2430.
    • (2008) Bioinformatics , vol.24 , pp. 2427-2430
    • Jadeau, F.1    Bechet, E.2    Cozzone, A.J.3    Deleage, G.4    Grangeasse, C.5
  • 9
    • 66549090908 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA
    • Bach H, Wong D, Av-Gay Y (2009) Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA. Biochem J 420: 155-160.
    • (2009) Biochem J , vol.420 , pp. 155-160
    • Bach, H.1    Wong, D.2    Av-Gay, Y.3
  • 10
    • 0024598750 scopus 로고
    • Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria
    • Bourret RB, Hess JF, Borkovich KA, Pakula AA, Simon MI (1989) Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria. J Biol Chem 264: 7085-7088.
    • (1989) J Biol Chem , vol.264 , pp. 7085-7088
    • Bourret, R.B.1    Hess, J.F.2    Borkovich, K.A.3    Pakula, A.A.4    Simon, M.I.5
  • 11
    • 0025908814 scopus 로고
    • Signal transduction pathways involving protein phosphorylation in prokaryotes
    • Bourret RB, Borkovich KA, Simon MI (1991) Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu Rev Biochem 60: 401-441.
    • (1991) Annu Rev Biochem , vol.60 , pp. 401-441
    • Bourret, R.B.1    Borkovich, K.A.2    Simon, M.I.3
  • 12
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch JA (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3: 165-170.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 13
    • 0024257073 scopus 로고
    • The phosphoenolpyruvate:Sugar phosphotransferase system in gram-positive bacteria: Properties, mechanism, and regulation
    • Reizer J, Saier MH, Jr., Deutscher J, Grenier F, Thompson J, et al. (1988) The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation. Crit Rev Microbiol 15: 297-338.
    • (1988) Crit Rev Microbiol , vol.15 , pp. 297-338
    • Reizer, J.1    Saier Jr., M.H.2    Deutscher, J.3    Grenier, F.4    Thompson, J.5
  • 14
    • 0033981191 scopus 로고    scopus 로고
    • No longer an exclusive club: Eukaryotic signaling domains in bacteria
    • Bakal CJ, Davies JE (2000) No longer an exclusive club: eukaryotic signaling domains in bacteria. Trends Cell Biol 10: 32-38.
    • (2000) Trends Cell Biol , vol.10 , pp. 32-38
    • Bakal, C.J.1    Davies, J.E.2
  • 15
    • 0027411095 scopus 로고
    • Eukaryotic-like protein serine/threonine kinases in Myxococcus xanthus, a developmental bacterium exhibiting social behavior
    • Munoz-Dorado J, Inouye S, Inouye M (1993) Eukaryotic-like protein serine/threonine kinases in Myxococcus xanthus, a developmental bacterium exhibiting social behavior. J Cell Biochem 51: 29-33.
    • (1993) J Cell Biochem , vol.51 , pp. 29-33
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 16
    • 0027980597 scopus 로고
    • Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase
    • Matsumoto A, Hong SK, Ishizuka H, Horinouchi S, Beppu T (1994) Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase. Gene 146: 47-56.
    • (1994) Gene , vol.146 , pp. 47-56
    • Matsumoto, A.1    Hong, S.K.2    Ishizuka, H.3    Horinouchi, S.4    Beppu, T.5
  • 17
    • 0029743605 scopus 로고    scopus 로고
    • Fancy meeting you here! A fresh look at ''prokaryotic'' protein phosphorylation
    • Kennelly PJ, Potts M (1996) Fancy meeting you here! A fresh look at ''prokaryotic'' protein phosphorylation. J Bacteriol 178: 4759-4764.
    • (1996) J Bacteriol , vol.178 , pp. 4759-4764
    • Kennelly, P.J.1    Potts, M.2
  • 18
    • 0032529472 scopus 로고    scopus 로고
    • Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome
    • Zhang CC, Gonzalez L, Phalip V (1998) Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome. Nucleic Acids Res 26: 3619-3625.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3619-3625
    • Zhang, C.C.1    Gonzalez, L.2    Phalip, V.3
  • 19
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Av-Gay Y, Everett M (2000) The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol 8: 238-244.
    • (2000) Trends Microbiol , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 20
    • 0038039713 scopus 로고    scopus 로고
    • Eukaryotic-type protein kinases in Streptomyces coelicolor: Variations on a common theme
    • Petrickova K, Petricek M (2003) Eukaryotic-type protein kinases in Streptomyces coelicolor: variations on a common theme. Microbiology 149: 1609-1621.
    • (2003) Microbiology , vol.149 , pp. 1609-1621
    • Petrickova, K.1    Petricek, M.2
  • 21
    • 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, Villarino A, et al. (2008) Mycobacterial Ser/Thr protein kinases and phosphatases: physiological roles and therapeutic potential. Biochim Biophys Acta 1784: 193-202.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 193-202
    • Wehenkel, A.1    Bellinzoni, M.2    Grana, M.3    Duran, R.4    Villarino, A.5
  • 23
    • 0021766191 scopus 로고
    • Protein phosphorylation in the archaebacterium Sulfolobus acidocaldarius
    • Skorko R (1984) Protein phosphorylation in the archaebacterium Sulfolobus acidocaldarius. Eur J Biochem 145: 617-622.
    • (1984) Eur J Biochem , vol.145 , pp. 617-622
    • Skorko, R.1
  • 24
    • 0028964131 scopus 로고
    • Identification of a eukaryotic-like protein kinase gene in Archaebacteria
    • Smith RF, King KY (1995) Identification of a eukaryotic-like protein kinase gene in Archaebacteria. Protein Sci 4: 126-129.
    • (1995) Protein Sci , vol.4 , pp. 126-129
    • Smith, R.F.1    King, K.Y.2
  • 25
    • 0020851355 scopus 로고
    • ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes
    • Deutscher J, Saier MH, Jr. (1983) ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc Natl Acad Sci U S A 80: 6790-6794.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6790-6794
    • Deutscher, J.1    Saier Jr., M.H.2
  • 26
    • 0027975371 scopus 로고
    • Light-Dependent Tyrosine Phosphorylation in the Cyanobacterium Prochlorothrix hollandica
    • Warner KM, Bullerjahn GS (1994) Light-Dependent Tyrosine Phosphorylation in the Cyanobacterium Prochlorothrix hollandica. Plant Physiol 105: 629-633.
    • (1994) Plant Physiol , vol.105 , pp. 629-633
    • Warner, K.M.1    Bullerjahn, G.S.2
  • 27
    • 0028364945 scopus 로고
    • Tyrosine kinase activity in Pseudomonas aeruginosa
    • South SL, Nichols R, Montie TC (1994) Tyrosine kinase activity in Pseudomonas aeruginosa. Mol Microbiol 12: 903-910.
    • (1994) Mol Microbiol , vol.12 , pp. 903-910
    • South, S.L.1    Nichols, R.2    Montie, T.C.3
  • 28
    • 0030009174 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote
    • Frasch SC, Dworkin M (1996) Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote. J Bacteriol 178: 4084-4088.
    • (1996) J Bacteriol , vol.178 , pp. 4084-4088
    • Frasch, S.C.1    Dworkin, M.2
  • 29
    • 0033539643 scopus 로고    scopus 로고
    • A novel bacterial tyrosine kinase essential for cell division and differentiation
    • Wu J, Ohta N, Zhao JL, Newton A (1999) A novel bacterial tyrosine kinase essential for cell division and differentiation. Proc Natl Acad Sci U S A 96: 13068-13073.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13068-13073
    • Wu, J.1    Ohta, N.2    Zhao, J.L.3    Newton, A.4
  • 30
    • 0036040203 scopus 로고    scopus 로고
    • Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces
    • Umeyama T, Lee PC, Horinouchi S (2002) Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces. Appl Microbiol Biotechnol 59: 419-425.
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 419-425
    • Umeyama, T.1    Lee, P.C.2    Horinouchi, S.3
  • 31
    • 0036228110 scopus 로고    scopus 로고
    • StoPK-1, a serine/threonine protein kinase from the glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009, affects oxidative stress response
    • Neu JM, MacMillan SV, Nodwell JR, Wright GD (2002) StoPK-1, a serine/threonine protein kinase from the glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009, affects oxidative stress response. Mol Microbiol 44: 417-430.
    • (2002) Mol Microbiol , vol.44 , pp. 417-430
    • Neu, J.M.1    Macmillan, S.V.2    Nodwell, J.R.3    Wright, G.D.4
  • 32
    • 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 (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    Seror, S.5
  • 33
    • 0036886406 scopus 로고    scopus 로고
    • Activation of 6-phosphofructokinase via phosphorylation by Pkn4, a protein Ser/Thr kinase of Myxococcus xanthus
    • Nariya H, Inouye S (2002) Activation of 6-phosphofructokinase via phosphorylation by Pkn4, a protein Ser/Thr kinase of Myxococcus xanthus. Mol Microbiol 46: 1353-1366.
    • (2002) Mol Microbiol , vol.46 , pp. 1353-1366
    • Nariya, H.1    Inouye, S.2
  • 34
    • 0037487186 scopus 로고    scopus 로고
    • An effective sporulation of Myxococcus Xanthus requires glycogen consumption via Pkn4-activated 6-phosphofructokinase
    • Nariya H, Inouye S (2003) An effective sporulation of Myxococcus Xanthus requires glycogen consumption via Pkn4-activated 6-phosphofructokinase. Mol Microbiol 49: 517-528.
    • (2003) Mol Microbiol , vol.49 , pp. 517-528
    • Nariya, H.1    Inouye, S.2
  • 35
    • 1542269017 scopus 로고    scopus 로고
    • HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria
    • Poncet S, Mijakovic I, Nessler S, Gueguen-Chaignon V, Chaptal V, et al. (2004) HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria. Biochim Biophys Acta 1697: 123-135.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 123-135
    • Poncet, S.1    Mijakovic, I.2    Nessler, S.3    Gueguen-Chaignon, V.4    Chaptal, V.5
  • 36
    • 18244401112 scopus 로고    scopus 로고
    • Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: Implications in glucose transport and cell division
    • Deol P, Vohra R, Saini AK, Singh A, Chandra H, et al. (2005) Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division. J Bacteriol 187: 3415-3420.
    • (2005) J Bacteriol , vol.187 , pp. 3415-3420
    • Deol, P.1    Vohra, R.2    Saini, A.K.3    Singh, A.4    Chandra, H.5
  • 37
    • 19944374470 scopus 로고    scopus 로고
    • Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae
    • Rajagopal L, Vo A, Silvestroni A, Rubens CE (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
  • 38
    • 0027535009 scopus 로고
    • A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant
    • Galyov EE, Hakansson S, Forsberg A, Wolf-Watz H (1993) A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant. Nature 361: 730-732.
    • (1993) Nature , vol.361 , pp. 730-732
    • Galyov, E.E.1    Hakansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 39
    • 33750492300 scopus 로고    scopus 로고
    • Regulation of cytotoxin expression by converging eukaryotic-type and two-component signaling mechanisms in Streptococcus agalactiae
    • Rajagopal L, Vo A, Silvestroni A, Rubens CE (2006) Regulation of cytotoxin expression by converging eukaryotic-type and two-component signaling mechanisms in Streptococcus agalactiae. Mol Microbiol 62: 941-957.
    • (2006) Mol Microbiol , vol.62 , pp. 941-957
    • Rajagopal, L.1    Vo, A.2    Silvestroni, A.3    Rubens, C.E.4
  • 40
    • 33747780120 scopus 로고    scopus 로고
    • The Ser/Thr kinase activity of the Yersinia protein kinase A (YpkA) is necessary for full virulence in the mouse, mollifying phagocytes, and disrupting the eukaryotic cytoskeleton
    • Wiley DJ, Nordfeldth R, Rosenzweig J, DaFonseca CJ, Gustin R, et al. (2006) The Ser/Thr kinase activity of the Yersinia protein kinase A (YpkA) is necessary for full virulence in the mouse, mollifying phagocytes, and disrupting the eukaryotic cytoskeleton. Microb Pathog 40: 234-243.
    • (2006) Microb Pathog , vol.40 , pp. 234-243
    • Wiley, D.J.1    Nordfeldth, R.2    Rosenzweig, J.3    Dafonseca, C.J.4    Gustin, R.5
  • 41
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • Ortiz-Lombardia M, Pompeo F, Boitel B, Alzari PM (2003) Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J Biol Chem 278: 13094-13100.
    • (2003) J Biol Chem , vol.278 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompeo, F.2    Boitel, B.3    Alzari, P.M.4
  • 42
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young TA, Delagoutte B, Endrizzi JA, Falick AM, 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
  • 43
    • 33846987910 scopus 로고    scopus 로고
    • Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway
    • Zheng J, He C, Singh VK, Martin NL, Jia Z (2007) Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway. Mol Microbiol 63: 1360-1371.
    • (2007) Mol Microbiol , vol.63 , pp. 1360-1371
    • Zheng, J.1    He, C.2    Singh, V.K.3    Martin, N.L.4    Jia, Z.5
  • 44
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM, Hunter T (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 46
    • 0033954149 scopus 로고    scopus 로고
    • SENTRA, a database of signal transduction proteins
    • D'Souza M, Romine MF, Maltsev N (2000) SENTRA, a database of signal transduction proteins. Nucleic Acids Res 28: 335-336.
    • (2000) Nucleic Acids Res , vol.28 , pp. 335-336
    • D'souza, M.1    Romine, M.F.2    Maltsev, N.3
  • 47
    • 33846039022 scopus 로고    scopus 로고
    • Sentra: A database of signal transduction proteins for comparative genome analysis
    • D'Souza M, Glass EM, Syed MH, Zhang Y, Rodriguez A, et al. (2007) Sentra: a database of signal transduction proteins for comparative genome analysis. Nucleic Acids Res 35: D271-273.
    • (2007) Nucleic Acids Res , vol.35
    • D'souza, M.1    Glass, E.M.2    Syed, M.H.3    Zhang, Y.4    Rodriguez, A.5
  • 48
    • 0023720656 scopus 로고
    • Proteobacteria classis nov., a Name for the Phylogenetic Taxon That Includes the ''Purple Bacteria and Their Relatives''
    • Stackebrandt RGEMaHGT E (1988) Proteobacteria classis nov., a Name for the Phylogenetic Taxon That Includes the ''Purple Bacteria and Their Relatives''. Int J Syst Bacteriol 38: 321-325.
    • (1988) Int J Syst Bacteriol , vol.38 , pp. 321-325
    • Stackebrandt, R.E.1
  • 49
    • 0026640799 scopus 로고
    • Identification of a putative eukaryotic- like protein kinase family in the developmental bacterium Myxococcus xanthus
    • Zhang W, Munoz-Dorado J, Inouye M, Inouye S (1992) Identification of a putative eukaryotic- like protein kinase family in the developmental bacterium Myxococcus xanthus. J Bacteriol 174: 5450-5453.
    • (1992) J Bacteriol , vol.174 , pp. 5450-5453
    • Zhang, W.1    Munoz-Dorado, J.2    Inouye, M.3    Inouye, S.4
  • 50
    • 0025790172 scopus 로고
    • A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium
    • Munoz-Dorado J, Inouye S, Inouye M (1991) A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium. Cell 67: 995-1006.
    • (1991) Cell , vol.67 , pp. 995-1006
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 51
    • 0029971544 scopus 로고    scopus 로고
    • Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases
    • Zhang W, Inouye M, Inouye S (1996) Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases. Mol Microbiol 20: 435-447.
    • (1996) Mol Microbiol , vol.20 , pp. 435-447
    • Zhang, W.1    Inouye, M.2    Inouye, S.3
  • 52
    • 0036886520 scopus 로고    scopus 로고
    • MglA, a small GTPase, interacts with a tyrosine kinase to control type IV pilimediated motility and development of Myxococcus xanthus
    • Thomasson B, Link J, Stassinopoulos AG, Burke N, Plamann L, et al. (2002) MglA, a small GTPase, interacts with a tyrosine kinase to control type IV pilimediated motility and development of Myxococcus xanthus. Mol Microbiol 46: 1399-1413.
    • (2002) Mol Microbiol , vol.46 , pp. 1399-1413
    • Thomasson, B.1    Link, J.2    Stassinopoulos, A.G.3    Burke, N.4    Plamann, L.5
  • 53
    • 5444227627 scopus 로고    scopus 로고
    • A proposal for further integration of the cyanobacteria under the bacteriological code
    • Oren A (2004) A proposal for further integration of the cyanobacteria under the Bacteriological Code Int J Syst Evol Microbiol 54: 1895-1902.
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 1895-1902
    • Oren, A.1
  • 54
    • 0035116854 scopus 로고    scopus 로고
    • A eukaryotic-type protein kinase, SpkA, is required for normal motility of the unicellular Cyanobacterium synechocystis sp. strain PCC 6803
    • Kamei A, Yuasa T, Orikawa K, Geng XX, Ikeuchi M (2001) A eukaryotic-type protein kinase, SpkA, is required for normal motility of the unicellular Cyanobacterium synechocystis sp. strain PCC 6803. J Bacteriol 183: 1505-1510.
    • (2001) J Bacteriol , vol.183 , pp. 1505-1510
    • Kamei, A.1    Yuasa, T.2    Orikawa, K.3    Geng, X.X.4    Ikeuchi, M.5
  • 55
    • 0038481516 scopus 로고    scopus 로고
    • Biochemical and functional characterization of a eukaryotic-type protein kinase, SpkB, in the cyanobacterium, Synechocystis sp. PCC 6803
    • Kamei A, Yoshihara S, Yuasa T, Geng X, Ikeuchi M (2003) Biochemical and functional characterization of a eukaryotic-type protein kinase, SpkB, in the cyanobacterium, Synechocystis sp. PCC 6803. Curr Microbiol 46: 296-301.
    • (2003) Curr Microbiol , vol.46 , pp. 296-301
    • Kamei, A.1    Yoshihara, S.2    Yuasa, T.3    Geng, X.4    Ikeuchi, M.5
  • 56
    • 0036923542 scopus 로고    scopus 로고
    • Biochemical examination of the potential eukaryotic-type protein kinase genes in the complete genome of the unicellular Cyanobacterium synechocystis sp. PCC 6803
    • Kamei A, Yuasa T, Geng X, Ikeuchi M (2002) Biochemical examination of the potential eukaryotic-type protein kinase genes in the complete genome of the unicellular Cyanobacterium synechocystis sp. PCC 6803. DNA Res 9: 71-78.
    • (2002) DNA Res , vol.9 , pp. 71-78
    • Kamei, A.1    Yuasa, T.2    Geng, X.3    Ikeuchi, M.4
  • 57
    • 0027146285 scopus 로고
    • A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120
    • Zhang CC (1993) A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120. Proc Natl Acad Sci U S A 90: 11840-11844.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11840-11844
    • Zhang, C.C.1
  • 59
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese CR, Kandler O, Wheelis ML (1990) Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci U S A 87: 4576-4579.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 61
    • 39349090644 scopus 로고    scopus 로고
    • Pathogenic diversity among Chlamydia trachomatis ocular strains in nonhuman primates is affected by subtle genomic variations
    • Kari L, Whitmire WM, Carlson JH, Crane DD, Reveneau N, et al. (2008) Pathogenic diversity among Chlamydia trachomatis ocular strains in nonhuman primates is affected by subtle genomic variations. J Infect Dis 197: 449-456.
    • (2008) J Infect Dis , vol.197 , pp. 449-456
    • Kari, L.1    Whitmire, W.M.2    Carlson, J.H.3    Crane, D.D.4    Reveneau, N.5
  • 62
    • 25444493846 scopus 로고    scopus 로고
    • Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains
    • Carlson JH, Porcella SF, McClarty G, Caldwell HD (2005) Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains. Infect Immun 73: 6407-6418.
    • (2005) Infect Immun , vol.73 , pp. 6407-6418
    • Carlson, J.H.1    Porcella, S.F.2    McClarty, G.3    Caldwell, H.D.4
  • 63
    • 38049046557 scopus 로고    scopus 로고
    • Chlamydia trachomatis: Genome sequence analysis of lymphogranuloma venereum isolates
    • Thomson NR, Holden MT, Carder C, Lennard N, Lockey SJ, et al. (2008) Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates. Genome Res 18: 161-171.
    • (2008) Genome Res , vol.18 , pp. 161-171
    • Thomson, N.R.1    Holden, M.T.2    Carder, C.3    Lennard, N.4    Lockey, S.J.5
  • 64
    • 0032953228 scopus 로고    scopus 로고
    • Comparative genomes of Chlamydia pneumoniae and C. trachomatis
    • Kalman S, Mitchell W, Marathe R, Lammel C, Fan J, et al. (1999) Comparative genomes of Chlamydia pneumoniae and C. trachomatis. Nat Genet 21: 385-389.
    • (1999) Nat Genet , vol.21 , pp. 385-389
    • Kalman, S.1    Mitchell, W.2    Marathe, R.3    Lammel, C.4    Fan, J.5
  • 65
    • 0141557667 scopus 로고    scopus 로고
    • Identification of two eukaryote-like serine/ threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1
    • Verma A, Maurelli AT (2003) Identification of two eukaryote-like serine/ threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1. Infect Immun 71: 5772-5784.
    • (2003) Infect Immun , vol.71 , pp. 5772-5784
    • Verma, A.1    Maurelli, A.T.2
  • 66
    • 33846016960 scopus 로고    scopus 로고
    • Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1
    • Mongodin EF, Shapir N, Daugherty SC, DeBoy RT, Emerson JB, et al. (2006) Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1. PLoS Genet 2: e214.
    • (2006) PLoS Genet , pp. 2
    • Mongodin, E.F.1    Shapir, N.2    Daugherty, S.C.3    Deboy, R.T.4    Emerson, J.B.5
  • 68
    • 45249116205 scopus 로고    scopus 로고
    • The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing
    • Tauch A, Trost E, Tilker A, Ludewig U, Schneiker S, et al. (2008) The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing. J Biotechnol 136: 11-21.
    • (2008) J Biotechnol , vol.136 , pp. 11-21
    • Tauch, A.1    Trost, E.2    Tilker, A.3    Ludewig, U.4    Schneiker, S.5
  • 69
    • 21144440616 scopus 로고    scopus 로고
    • Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora
    • Tauch A, Kaiser O, Hain T, Goesmann A, Weisshaar B, et al. (2005) Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora. J Bacteriol 187: 4671-4682.
    • (2005) J Bacteriol , vol.187 , pp. 4671-4682
    • Tauch, A.1    Kaiser, O.2    Hain, T.3    Goesmann, A.4    Weisshaar, B.5
  • 70
    • 0036781756 scopus 로고    scopus 로고
    • Clinical and taxonomic status of pathogenic nonpigmented or late-pigmenting rapidly growing mycobacteria
    • Brown-Elliott BA, Wallace RJ, Jr. (2002) Clinical and taxonomic status of pathogenic nonpigmented or late-pigmenting rapidly growing mycobacteria. Clin Microbiol Rev 15: 716-746.
    • (2002) Clin Microbiol Rev , vol.15 , pp. 716-746
    • Brown-Elliott, B.A.1    Wallace Jr., R.J.2
  • 71
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5
  • 72
    • 70549103951 scopus 로고    scopus 로고
    • Comparative genomic and phylogeographic analysis of Mycobacterium leprae
    • Monot M, Honore N, Garnier T, Zidane N, Sherafi D, et al. (2009) Comparative genomic and phylogeographic analysis of Mycobacterium leprae. Nat Genet 41: 1282-1289.
    • (2009) Nat Genet , vol.41 , pp. 1282-1289
    • Monot, M.1    Honore, N.2    Garnier, T.3    Zidane, N.4    Sherafi, D.5
  • 73
  • 74
    • 0029986352 scopus 로고    scopus 로고
    • The aerial myceliumdefective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2)
    • Ueda K, Umeyama T, Beppu T, Horinouchi S (1996) The aerial myceliumdefective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2). Gene 169: 91-95.
    • (1996) Gene , vol.169 , pp. 91-95
    • Ueda, K.1    Umeyama, T.2    Beppu, T.3    Horinouchi, S.4
  • 75
    • 3042660151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo
    • Cowley S, Ko M, Pick N, Chow R, Downing KJ, et al. (2004) The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo. Mol Microbiol 52: 1691-1702.
    • (2004) Mol Microbiol , vol.52 , pp. 1691-1702
    • Cowley, S.1    Ko, M.2    Pick, N.3    Chow, R.4    Downing, K.J.5
  • 76
    • 2942718724 scopus 로고    scopus 로고
    • Protein kinase G from pathogenic mycobacteria promotes survival within macrophages
    • Walburger A, Koul A, Ferrari G, Nguyen L, Prescianotto-Baschong C, et al. (2004) Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 304: 1800-1804.
    • (2004) Science , vol.304 , pp. 1800-1804
    • Walburger, A.1    Koul, A.2    Ferrari, G.3    Nguyen, L.4    Prescianotto-Baschong, C.5
  • 77
    • 0022379813 scopus 로고
    • Production, isolation, physico-chemical and biological properties of angiolam A, a new antibiotic from Angiococcus disciformis (Myxobacterales)
    • (Tokyo)
    • Kunze B, Kohl W, Hofle G, Reichenbach H (1985) Production, isolation, physico-chemical and biological properties of angiolam A, a new antibiotic from Angiococcus disciformis (Myxobacterales). J Antibiot (Tokyo) 38: 1649-1654.
    • (1985) J Antibiot , vol.38 , pp. 1649-1654
    • Kunze, B.1    Kohl, W.2    Hofle, G.3    Reichenbach, H.4
  • 78
    • 0021273146 scopus 로고
    • Stigmatellin, a new antibiotic from Stigmatella aurantiaca (Myxobacterales). I. Production, physico-chemical and biological properties
    • (Tokyo)
    • Kunze B, Kemmer T, Hofle G, Reichenbach H (1984) Stigmatellin, a new antibiotic from Stigmatella aurantiaca (Myxobacterales). I. Production, physico-chemical and biological properties. J Antibiot (Tokyo) 37: 454-461.
    • (1984) J Antibiot , vol.37 , pp. 454-461
    • Kunze, B.1    Kemmer, T.2    Hofle, G.3    Reichenbach, H.4
  • 79
    • 0031851364 scopus 로고    scopus 로고
    • Shewanella amazonensis sp. nov., a novel metal-reducing facultative anaerobe from Amazonian shelf muds
    • Venkateswaran K, Dollhopf ME, Aller R, Stackebrandt E, Nealson KH (1998) Shewanella amazonensis sp. nov., a novel metal-reducing facultative anaerobe from Amazonian shelf muds. Int J Syst Bacteriol 48 Pt 3: 965-972.
    • (1998) Int J Syst Bacteriol , vol.48 , Issue.3 , pp. 965-972
    • Venkateswaran, K.1    Dollhopf, M.E.2    Aller, R.3    Stackebrandt, E.4    Nealson, K.H.5
  • 80
    • 0036867531 scopus 로고    scopus 로고
    • Shewanella denitrificans sp. nov., a vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea
    • Brettar I, Christen R, Hofle MG (2002) Shewanella denitrificans sp. nov., a vigorously denitrifying bacterium isolated from the oxic-anoxic interface of the Gotland Deep in the central Baltic Sea. Int J Syst Evol Microbiol 52: 2211-2217.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 2211-2217
    • Brettar, I.1    Christen, R.2    Hofle, M.G.3
  • 81
    • 0030871068 scopus 로고    scopus 로고
    • Shewanella woodyi sp. nov., an exclusively respiratory luminous bacterium isolated from the Alboran Sea
    • Makemson JC, Fulayfil NR, Landry W, Van Ert LM, Wimpee CF, et al. (1997) Shewanella woodyi sp. nov., an exclusively respiratory luminous bacterium isolated from the Alboran Sea. Int J Syst Bacteriol 47: 1034-1039.
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 1034-1039
    • Makemson, J.C.1    Fulayfil, N.R.2    Landry, W.3    van Ert, L.M.4    Wimpee, C.F.5
  • 82
    • 21844477811 scopus 로고    scopus 로고
    • The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota
    • Chen L, Brugger K, Skovgaard M, Redder P, She Q, et al. (2005) The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota. J Bacteriol 187: 4992-4999.
    • (2005) J Bacteriol , vol.187 , pp. 4992-4999
    • Chen, L.1    Brugger, K.2    Skovgaard, M.3    Redder, P.4    She, Q.5
  • 84
    • 0346655237 scopus 로고    scopus 로고
    • A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity
    • Lower BH, Potters MB, Kennelly PJ (2004) A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity. J Bacteriol 186: 463-472.
    • (2004) J Bacteriol , vol.186 , pp. 463-472
    • Lower, B.H.1    Potters, M.B.2    Kennelly, P.J.3
  • 85
    • 0001960079 scopus 로고
    • Metallosphaera sedula gen. nov. and sp. nov. represents a new genus of aerobic, metalmobilizing, thermoacidophilic archaebacteria
    • Huber G, Spinnler C, Gambacorta A, Stetter KO (1989) Metallosphaera sedula gen. nov. and sp. nov. represents a new genus of aerobic, metalmobilizing, thermoacidophilic archaebacteria. Syst Appl Microbio 12: 38-47.
    • (1989) Syst Appl Microbio , vol.12 , pp. 38-47
    • Huber, G.1    Spinnler, C.2    Gambacorta, A.3    Stetter, K.O.4
  • 86
    • 84879795980 scopus 로고    scopus 로고
    • Regulatory Interactions of a Virulence-Associated Serine/Threonine Phosphatase- Kinase Pair in Bacillus anthracis
    • Shakir SM, Bryant KM, Larabee JL, Hamm EE, Lovchik J, et al. (2009) Regulatory Interactions of a Virulence-Associated Serine/Threonine Phosphatase- Kinase Pair in Bacillus anthracis. J Bacteriol.
    • (2009) J Bacteriol
    • Shakir, S.M.1    Bryant, K.M.2    Larabee, J.L.3    Hamm, E.E.4    Lovchik, J.5
  • 87
    • 0025790172 scopus 로고
    • A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium
    • Munoz-Dorado J, Inouye S, Inouye M (1991) A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium. Cell 67: 995-1006.
    • (1991) Cell , vol.67 , pp. 995-1006
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 88
    • 2342578723 scopus 로고    scopus 로고
    • Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller
    • Good MC, Greenstein AE, Young TA, Ng HL, 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
  • 90
    • 34247588355 scopus 로고    scopus 로고
    • M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog
    • Greenstein AE, MacGurn JA, Baer CE, Falick AM, Cox JS, et al. (2007) M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. PLoS Pathog 3: e49.
    • (2007) PLoS Pathog , pp. 3
    • Greenstein, A.E.1    Macgurn, J.A.2    Baer, C.E.3    Falick, A.M.4    Cox, J.S.5
  • 91
    • 23344450436 scopus 로고    scopus 로고
    • An ABC transporter containing a forkhead-associated domain interacts with a serinethreonine protein kinase and is required for growth of Mycobacterium tuberculosis in mice
    • Curry JM, Whalan R, Hunt DM, Gohil K, Strom M, et al. (2005) An ABC transporter containing a forkhead-associated domain interacts with a serinethreonine protein kinase and is required for growth of Mycobacterium tuberculosis in mice. Infect Immun 73: 4471-4477.
    • (2005) Infect Immun , vol.73 , pp. 4471-4477
    • Curry, J.M.1    Whalan, R.2    Hunt, D.M.3    Gohil, K.4    Strom, M.5
  • 92
    • 22244486672 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis serine/ threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains
    • Grundner C, Gay LM, Alber T (2005) Mycobacterium tuberculosis serine/ threonine kinases PknB, PknD, PknE, and PknF phosphorylate multiple FHA domains. Protein Sci 14: 1918-1921.
    • (2005) Protein Sci , vol.14 , pp. 1918-1921
    • Grundner, C.1    Gay, L.M.2    Alber, T.3
  • 93
    • 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 GS, Cozzone AJ, et al. (2003) 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
  • 94
    • 23644451812 scopus 로고    scopus 로고
    • Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice
    • Papavinasasundaram KG, Chan B, Chung JH, Colston MJ, Davis EO, et al. (2005) Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice. J Bacteriol 187: 5751-5760.
    • (2005) J Bacteriol , vol.187 , pp. 5751-5760
    • Papavinasasundaram, K.G.1    Chan, B.2    Chung, J.H.3    Colston, M.J.4    Davis, E.O.5
  • 95
    • 32244443761 scopus 로고    scopus 로고
    • The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillinbinding 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 penicillinbinding 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
  • 96
    • 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 MJ, Zanella-Cleon I, Becchi M, Cozzone AJ, et al. (2008) 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 283: 18099-18112.
    • (2008) J Biol Chem , vol.283 , pp. 18099-18112
    • Fiuza, M.1    Canova, M.J.2    Zanella-Cleon, I.3    Becchi, M.4    Cozzone, A.J.5
  • 97
    • 0028986249 scopus 로고
    • Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation
    • Udo H, Munoz-Dorado J, Inouye M, Inouye S (1995) Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation. Genes Dev 9: 972-983.
    • (1995) Genes Dev , vol.9 , pp. 972-983
    • Udo, H.1    Munoz-Dorado, J.2    Inouye, M.3    Inouye, S.4
  • 98
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea LD, Regan L (2003) TPR proteins: the versatile helix. Trends Biochem Sci 28: 655-662.
    • (2003) Trends Biochem Sci , vol.28 , pp. 655-662
    • D'andrea, L.D.1    Regan, L.2
  • 99
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (1994) The ancient regulatory-protein family of WD-repeat proteins. Nature 371: 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 101
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A beta-lactambinding domain
    • Yeats C, Finn RD, Bateman A (2002) The PASTA domain: a beta-lactambinding domain. Trends Biochem Sci 27: 438.
    • (2002) Trends Biochem Sci , vol.27 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 102
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • Aravind L, Ponting CP (1997) The GAF domain: an evolutionary link between diverse phototransducing proteins. Trends Biochem Sci 22: 458-459.
    • (1997) Trends Biochem Sci , vol.22 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 103
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe DM, Grossman AR (1996) Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 273: 1409-1412.
    • (1996) Science , vol.273 , pp. 1409-1412
    • Kehoe, D.M.1    Grossman, A.R.2
  • 104
    • 2942620419 scopus 로고    scopus 로고
    • Identification and analysis of novel tandem repeats in the cell surface proteins of archaeal and bacterial genomes using computational tools
    • Adindla S, Inampudi KK, Guruprasad K, Guruprasad L (2004) Identification and analysis of novel tandem repeats in the cell surface proteins of archaeal and bacterial genomes using computational tools. Comp Funct Genomics 5: 2-16.
    • (2004) Comp Funct Genomics , vol.5 , pp. 2-16
    • Adindla, S.1    Inampudi, K.K.2    Guruprasad, K.3    Guruprasad, L.4
  • 105
    • 0032614298 scopus 로고    scopus 로고
    • Aminoglycoside phosphotransferases: Proteins, structure, and mechanism
    • Wright GD, Thompson PR (1999) Aminoglycoside phosphotransferases: proteins, structure, and mechanism. Front Biosci 4: D9-21.
    • (1999) Front Biosci , vol.4 , pp. 9-21
    • Wright, G.D.1    Thompson, P.R.2
  • 106
    • 2542542070 scopus 로고    scopus 로고
    • The emergence of catalytic and structural diversity within the beta- clip fold
    • Iyer LM, Aravind L (2004) The emergence of catalytic and structural diversity within the beta- clip fold. Proteins 55: 977-991.
    • (2004) Proteins , vol.55 , pp. 977-991
    • Iyer, L.M.1    Aravind, L.2
  • 107
    • 0028225734 scopus 로고
    • Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest
    • Nystrom T, Neidhardt FC (1994) Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Mol Microbiol 11: 537-544.
    • (1994) Mol Microbiol , vol.11 , pp. 537-544
    • Nystrom, T.1    Neidhardt, F.C.2
  • 108
    • 0031778594 scopus 로고    scopus 로고
    • Structure and distribution of pentapeptide repeats in bacteria
    • Bateman A, Murzin AG, Teichmann SA (1998) Structure and distribution of pentapeptide repeats in bacteria. Protein Sci 7: 1477-1480.
    • (1998) Protein Sci , vol.7 , pp. 1477-1480
    • Bateman, A.1    Murzin, A.G.2    Teichmann, S.A.3
  • 109
    • 0037215715 scopus 로고    scopus 로고
    • Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea
    • Zhulin IB, Nikolskaya AN, Galperin MY (2003) Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in bacteria and archaea. J Bacteriol 185: 285-294.
    • (2003) J Bacteriol , vol.185 , pp. 285-294
    • Zhulin, I.B.1    Nikolskaya, A.N.2    Galperin, M.Y.3
  • 110
    • 0037102138 scopus 로고    scopus 로고
    • Diverse recognition of non- PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p
    • Kami K, Takeya R, Sumimoto H, Kohda D (2002) Diverse recognition of non- PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p. Embo J 21: 4268-4276.
    • (2002) Embo J , vol.21 , pp. 4268-4276
    • Kami, K.1    Takeya, R.2    Sumimoto, H.3    Kohda, D.4
  • 111
    • 0033197541 scopus 로고    scopus 로고
    • The FHA domain is a modular phosphopeptide recognition motif
    • Durocher D, Henckel J, Fersht AR, Jackson SP (1999) The FHA domain is a modular phosphopeptide recognition motif. Mol Cell 4: 387-394.
    • (1999) Mol Cell , vol.4 , pp. 387-394
    • Durocher, D.1    Henckel, J.2    Fersht, A.R.3    Jackson, S.P.4
  • 113
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI- BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI- BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 115
    • 33644878163 scopus 로고    scopus 로고
    • MulPSSM: A database of multiple position-specific scoring matrices of protein domain families
    • Gowri VS, Krishnadev O, Swamy CS, Srinivasan N (2006) MulPSSM: a database of multiple position-specific scoring matrices of protein domain families. Nucleic Acids Res 34: D243-246.
    • (2006) Nucleic Acids Res , vol.34 , pp. 243-246
    • Gowri, V.S.1    Krishnadev, O.2    Swamy, C.S.3    Srinivasan, N.4
  • 116
    • 34248574685 scopus 로고    scopus 로고
    • Strategies for the effective identification of remotely related sequences in multiple PSSM search approach
    • Gowri VS, Tina KG, Krishnadev O, Srinivasan N (2007) Strategies for the effective identification of remotely related sequences in multiple PSSM search approach. Proteins 67: 789-794.
    • (2007) Proteins , vol.67 , pp. 789-794
    • Gowri, V.S.1    Tina, K.G.2    Krishnadev, O.3    Srinivasan, N.4
  • 117
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR (1998) Profile hidden Markov models. Bioinformatics 14: 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 118
    • 10844221661 scopus 로고    scopus 로고
    • A genomic perspective of protein kinases in Plasmodium falciparum
    • Anamika K, Srinivasan N, Krupa A (2005) A genomic perspective of protein kinases in Plasmodium falciparum. Proteins 58: 180-189.
    • (2005) Proteins , vol.58 , pp. 180-189
    • Anamika, K.1    Srinivasan, N.2    Krupa, A.3
  • 119
    • 34447273585 scopus 로고    scopus 로고
    • Comparative kinomics of Plasmodium organisms: Unity in diversity
    • Anamika K, Srinivasan N (2007) Comparative kinomics of Plasmodium organisms: unity in diversity. Protein Pept Lett 14: 509-517.
    • (2007) Protein Pept Lett , vol.14 , pp. 509-517
    • Anamika, K.1    Srinivasan, N.2
  • 120
    • 41149097700 scopus 로고    scopus 로고
    • Analysis of the protein kinome of Entamoeba histolytica
    • Anamika K, Bhattacharya A, Srinivasan N (2008) Analysis of the protein kinome of Entamoeba histolytica. Proteins 71: 995-1006.
    • (2008) Proteins , vol.71 , pp. 995-1006
    • Anamika, K.1    Bhattacharya, A.2    Srinivasan, N.3
  • 121
    • 61949375711 scopus 로고    scopus 로고
    • Comparative kinomics of human and chimpanzee reveal unique kinship and functional diversity generated by new domain combinations
    • Anamika K, Martin J, Srinivasan N (2008) Comparative kinomics of human and chimpanzee reveal unique kinship and functional diversity generated by new domain combinations. BMC Genomics 9: 625.
    • (2008) BMC Genomics , vol.9 , pp. 625
    • Anamika, K.1    Martin, J.2    Srinivasan, N.3
  • 123
    • 0035072551 scopus 로고    scopus 로고
    • Clustering of highly homologous sequences to reduce the size of large protein databases
    • Li W, Jaroszewski L, Godzik A (2001) Clustering of highly homologous sequences to reduce the size of large protein databases. Bioinformatics 17: 282-283.
    • (2001) Bioinformatics , vol.17 , pp. 282-283
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 125
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 126
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4


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