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Volumn 6, Issue 7, 2011, Pages 747-761

Aspects of eukaryotic-like signaling in Gram-positive cocci: A focus on virulence

Author keywords

antibiotic resistance; Enterococcus faecalis; serine threonine kinase; Staphylococcus aureus; Streptococcus agalactiae; Streptococcus mutans; Streptococcus pneumoniae; Streptococcus pyogenes; virulence

Indexed keywords

CEFAZOLIN; CEFOTAXIME; CEFTRIAXONE; ERTAPENEM; NAFCILLIN; PROTEIN SERINE THREONINE KINASE;

EID: 79961038710     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.11.62     Document Type: Review
Times cited : (17)

References (151)
  • 1
    • 0002739166 scopus 로고    scopus 로고
    • Posttranslational modifications
    • Angeletti RH (Ed.). Academic Press, CA, USA
    • Krishna RG, Wold F. Posttranslational modifications. In: Protein Analysis and Design. Angeletti RH (Ed.). Academic Press, CA, USA 121-206 (1998).
    • (1998) Protein Analysis and Design , pp. 121-206
    • Krishna, R.G.1    Wold, F.2
  • 2
  • 3
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241(4861), 42-52 (1988).
    • (1988) Science , vol.241 , Issue.4861 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 4
    • 0031764045 scopus 로고    scopus 로고
    • The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait
    • DOI 10.1016/S0168-6445(98)00015-1, PII S0168644598000151
    • Shi L, Potts M, Kennelly PJ. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: a family portrait. FEMS Microbiol. Rev. 22(4), 229-253 (1998). (Pubitemid 28557044)
    • (1998) FEMS Microbiology Reviews , vol.22 , Issue.4 , pp. 229-253
    • Shi, L.1    Potts, M.2    Kennelly, P.J.3
  • 8
    • 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. A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a Gram-negative bacterium. Cell 67(5), 995-1006 (1991). (Pubitemid 121001513)
    • (1991) Cell , vol.67 , Issue.5 , pp. 995-1006
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 9
    • 0031016266 scopus 로고    scopus 로고
    • Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus
    • Hanlon WA, Inouye M, Inouye S. Pkn9, a ser/thr protein kinase involved in the development of Myxococcus xanthus. Mol. Microbiol. 23(3), 459-471 (1997). (Pubitemid 27051376)
    • (1997) Molecular Microbiology , vol.23 , Issue.3 , pp. 459-471
    • Hanlon, W.A.1    Inouye, M.2    Inouye, S.3
  • 10
    • 0033763747 scopus 로고    scopus 로고
    • A large family of eukaryotic-like protein Ser/Thr kinases of Myxococcus xanthus, a developmental bacterium
    • Inouye S, Jain R, Ueki T et al. A large family of eukaryotic-like protein Ser/Thr kinases of Myxococcus xanthus, a developmental bacterium. Microb. Comp. Genomics 5(2), 103-120 (2000).
    • (2000) Microb. Comp. Genomics , vol.5 , Issue.2 , pp. 103-120
    • Inouye, S.1    Jain, R.2    Ueki, T.3
  • 11
    • 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. Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase. Gene 146(1), 47-56 (1994).
    • (1994) Gene , vol.146 , Issue.1 , pp. 47-56
    • Matsumoto, A.1    Hong, S.K.2    Ishizuka, H.3    Horinouchi, S.4
  • 12
    • 0033384565 scopus 로고    scopus 로고
    • Sequences and evolutionary analyses of eukaryotic-type protein kinases from Streptomyces coelicolor A3(2)
    • Ogawara H, Aoyagi N, Watanabe M, Urabe H. Sequences and evolutionary analyses of eukaryotic-type protein kinases from Streptomyces coelicolor A3(2). Microbiology 145, 3343-3352 (1999). (Pubitemid 30018779)
    • (1999) Microbiology , vol.145 , Issue.12 , pp. 3343-3352
    • Ogawara, H.1    Aoyagi, N.2    Watanabe, M.3    Urabe, H.4
  • 13
    • 0027146285 scopus 로고
    • A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120
    • Zhang CC. A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120. Proc. Natl Acad. Sci. USA 90(24), 11840-11844 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , Issue.24 , pp. 11840-11844
    • Zhang, C.C.1
  • 14
    • 0031900923 scopus 로고    scopus 로고
    • Molecular and genetic analysis of two closely linked genes that encode, respectively, a protein phosphatase 1/2A/2B homolog and a protein kinase homolog in the cyanobacterium Anabaena sp. strain PCC 7120
    • Zhang CC, Friry A, Peng L. Molecular and genetic analysis of two closely linked genes that encode, respectively, a protein phosphatase 1/2A/2B homolog and a protein kinase homolog in the cyanobacterium Anabaena sp. strain PCC7120. J. Bacteriol. 180(10), 2616-2622 (1998). (Pubitemid 28213258)
    • (1998) Journal of Bacteriology , vol.180 , Issue.10 , pp. 2616-2622
    • Zhang, C.-C.1    Friry, A.2    Peng, L.3
  • 15
    • 0032529472 scopus 로고    scopus 로고
    • Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome
    • DOI 10.1093/nar/26.16.3619
    • Zhang CC, Gonzalez L, Phalip V. Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome. Nucleic Acids Res. 26(16), 3619-3625 (1998). (Pubitemid 28367964)
    • (1998) Nucleic Acids Research , vol.26 , Issue.16 , pp. 3619-3625
    • Zhang, C.-C.1    Gonzalez, L.2    Phalip, V.3
  • 16
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes
    • DOI 10.1046/j.1365-2958.2002.03178.x
    • 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. 46(2), 571-586 (2002). (Pubitemid 35340965)
    • (2002) Molecular Microbiology , vol.46 , Issue.2 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Seror, S.5
  • 17
    • 73649111360 scopus 로고    scopus 로고
    • Regulatory interactions of a virulence-associated serine/threonine phosphatase-kinase pair in Bacillus anthracis
    • Shakir SM, Bryant KM, Larabee JL et al. Regulatory interactions of a virulence-associated serine/threonine phosphatase-kinase pair in Bacillus anthracis. J. Bacteriol. 192(2), 400-409 (2010).
    • (2010) J. Bacteriol. , vol.192 , Issue.2 , pp. 400-409
    • Shakir, S.M.1    Bryant, K.M.2    Larabee, J.L.3
  • 18
    • 0037853258 scopus 로고    scopus 로고
    • A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence
    • DOI 10.1074/jbc.M212747200
    • Rajagopal L, Clancy A, Rubens CE. A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence. J. Biol. Chem. 278(16), 14429-14441 (2003). (Pubitemid 36799996)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14429-14441
    • Rajagopal, L.1    Clancy, A.2    Rubens, C.E.3
  • 19
    • 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
    • DOI 10.1128/JB.188.4.1628-1632.2006
    • 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. 188(4), 1628-1632 (2006). (Pubitemid 43228697)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1628-1632
    • Hussain, H.1    Branny, P.2    Allan, E.3
  • 20
    • 1842431057 scopus 로고    scopus 로고
    • Protein Serine/Threonine Kinase StkP Positively Controls Virulence and Competence in Streptococcus pneumoniae
    • DOI 10.1128/IAI.72.4.2434-2437.2004
    • Echenique J, Kadioglu A, Romao S, Andrew PW, Trombe MC. Protein serine/threonine kinase StkP positively controls virulence and competence in Streptococcus pneumoniae. Infect. Immun. 72(4), 2434-2437 (2004). (Pubitemid 38419967)
    • (2004) Infection and Immunity , vol.72 , Issue.4 , pp. 2434-2437
    • Echenique, J.1    Kadioglu, A.2    Romao, S.3    Andrew, P.W.4    Trombe, M.-C.5
  • 21
    • 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. 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(5), 1351-1372 (2006).
    • (2006) J. Mol. Biol. , vol.357 , Issue.5 , pp. 1351-1372
    • Jin, H.1    Pancholi, V.2
  • 22
    • 0002452236 scopus 로고    scopus 로고
    • Components of eukaryotic-like protein signaling pathways in Mycobacterium tuberculosis
    • Av-Gay Y, Davies J. Components of eukaryotic-like protein signaling pathways in Mycobacterium tuberculosis. Microb. Comp. Genomics 2, 63-73 (1997).
    • (1997) Microb. Comp. Genomics , vol.2 , pp. 63-73
    • Av-Gay, Y.1    Davies, J.2
  • 23
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • DOI 10.1016/S0966-842X(00)01734-0, PII S0966842X00017340
    • Av-Gay Y, Everett M. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 8(5), 238-244 (2000). (Pubitemid 30236245)
    • (2000) Trends in Microbiology , vol.8 , Issue.5 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 24
    • 0036183002 scopus 로고    scopus 로고
    • Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division
    • DOI 10.1046/j.1432-1033.2002.02778.x
    • Chaba R, Raje M, Chakraborti PK. Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division. Eur. J. Biochem. 269(4), 1078-1085 (2002). (Pubitemid 34175366)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.4 , pp. 1078-1085
    • Chaba, R.1    Raje, M.2    Chakraborti, P.K.3
  • 25
    • 0027535009 scopus 로고
    • A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant
    • DOI 10.1038/361730a0
    • Galyov EE, Hakansson S, Forsberg A, Wolf-Watz H. A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant. Nature 361(6414), 730-732 (1993). (Pubitemid 23070481)
    • (1993) Nature , vol.361 , Issue.6414 , pp. 730-732
    • Galyov, E.E.1    Hakansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 26
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Hakansson S, Galyov EE, Rosqvist R, Wolf-Watz H. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20(3), 593-603 (1996). (Pubitemid 26151900)
    • (1996) Molecular Microbiology , vol.20 , Issue.3 , pp. 593-603
    • Hakansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 27
    • 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
    • DOI 10.1111/j.1365-2958.2005.04551.x
    • Archambaud C, Gouin E, Pizarro-Cerda J, Cossart P, Dussurget O. Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes. Mol. Microbiol. 56(2), 383-396 (2005). (Pubitemid 40516779)
    • (2005) Molecular Microbiology , vol.56 , Issue.2 , pp. 383-396
    • Archambaud, C.1    Gouin, E.2    Pizarro-Cerda, J.3    Cossart, P.4    Dussurget, O.5
  • 28
    • 79961047261 scopus 로고    scopus 로고
    • Serine/threonine protein kinase PrkA of the human pathogen Listeria monocytogenes: Biochemical characterization and identification of interacting partners through proteomic approaches
    • DOI:10.1016/j.jprot.2011.03.005 Epub ahead of print
    • Lima A, Duran R, Schujman GE et al. Serine/threonine protein kinase PrkA of the human pathogen Listeria monocytogenes: biochemical characterization and identification of interacting partners through proteomic approaches. J. Proteomics DOI:10.1016/j.jprot.2011.03.005 (2011) (Epub ahead of print).
    • (2011) J. Proteomics
    • Lima, A.1    Duran, R.2    Schujman, G.E.3
  • 29
    • 0032431404 scopus 로고    scopus 로고
    • A novel serine/threonine protein kinase homologue of Pseudomonas aeruginosa is specifically inducible within the host infection site and is required for full virulence in neutropenic mice
    • Wang J, Li C, Yang H, Mushegian A, Jin S. A novel serine/threonine protein kinase homologue of Pseudomonas aeruginosa is specifically inducible within the host infection site and is required for full virulence in neutropenic mice. J. Bacteriol. 180(24), 6764-6768 (1998). (Pubitemid 29006098)
    • (1998) Journal of Bacteriology , vol.180 , Issue.24 , pp. 6764-6768
    • Wang, J.1    Li, C.2    Yang, H.3    Mushegian, A.4    Jin, S.5
  • 31
    • 63149156264 scopus 로고    scopus 로고
    • Modulation of cell wall structure and antimicrobial susceptibility by a Staphylococcus aureus eukaryote-like serine/threonine kinase and phosphatase
    • Beltramini AM, Mukhopadhyay CD, Pancholi V. Modulation of cell wall structure and antimicrobial susceptibility by a Staphylococcus aureus eukaryote-like serine/threonine kinase and phosphatase. Infect. Immun. 77(4), 1406-1416 (2009).
    • (2009) Infect. Immun. , vol.77 , Issue.4 , pp. 1406-1416
    • Beltramini, A.M.1    Mukhopadhyay, C.D.2    Pancholi, V.3
  • 32
    • 55549098541 scopus 로고    scopus 로고
    • Posttranslational modification influences the effects of MgrA on norA expression in Staphylococcus aureus
    • Truong-Bolduc QC, Ding Y, Hooper DC. Posttranslational modification influences the effects of MgrA on norA expression in Staphylococcus aureus. J. Bacteriol. 190(22), 7375-7381 (2008).
    • (2008) J. Bacteriol. , vol.190 , Issue.22 , pp. 7375-7381
    • Truong-Bolduc, Q.C.1    Ding, Y.2    Hooper, D.C.3
  • 33
    • 0032755508 scopus 로고    scopus 로고
    • Antibiotic resistance as a stress response: Complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin
    • De Lencastre H, Wu SW, Pinho MG et al. Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin. Microb. Drug Resist. 5(3), 163-175 (1999). (Pubitemid 29519892)
    • (1999) Microbial Drug Resistance , vol.5 , Issue.3 , pp. 163-175
    • De Lencastre, H.1    Wu, S.W.2    Pinho, M.G.3    Ludovice, A.M.4    Filipe, S.5    Gardete, S.6    Sobral, R.7    Gill, S.8    Chung, M.9    Tomasz, A.10
  • 35
    • 74049125665 scopus 로고    scopus 로고
    • Molecular mechanisms of cardiovascular toxicity of targeted cancer therapeutics
    • Cheng H, Force T. Molecular mechanisms of cardiovascular toxicity of targeted cancer therapeutics. Circ. Res. 106(1), 21-34 (2010).
    • (2010) Circ. Res. , vol.106 , Issue.1 , pp. 21-34
    • Cheng, H.1    Force, T.2
  • 36
    • 0035743340 scopus 로고    scopus 로고
    • Targeting protein kinases for tumor therapy
    • DOI 10.1159/000055106
    • Sachsenmaier C. Targeting protein kinases for tumor therapy. Onkologie 24(4), 346-355 (2001). (Pubitemid 34701519)
    • (2001) Onkologie , vol.24 , Issue.4 , pp. 346-355
    • Sachsenmaier, C.1
  • 37
    • 0025998844 scopus 로고
    • Classification of protein-serine/threonine phosphatases: Identification and quantitation in cell extracts
    • Cohen P. Classification of protein-serine/threonine phosphatases: identification and quantitation in cell extracts. Methods Enzymol. 201, 389-398 (1991).
    • (1991) Methods Enzymol. , vol.201 , pp. 389-398
    • Cohen, P.1
  • 38
    • 66849115406 scopus 로고    scopus 로고
    • Targeting protein serine/threonine phosphatases for drug development
    • McConnell JL, Wadzinski BE. Targeting protein serine/threonine phosphatases for drug development. Mol. Pharmacol. 75(6), 1249-1261 (2009).
    • (2009) Mol. Pharmacol. , vol.75 , Issue.6 , pp. 1249-1261
    • McConnell, J.L.1    Wadzinski, B.E.2
  • 39
    • 67650860453 scopus 로고    scopus 로고
    • Inhibition of serine/threonine phosphatase PP2A enhances cancer chemotherapy by blocking DNA damage induced defense mechanisms
    • Lu J, Kovach JS, Johnson F et al. Inhibition of serine/threonine phosphatase PP2A enhances cancer chemotherapy by blocking DNA damage induced defense mechanisms. Proc. Natl Acad. Sci. USA 106(28), 11697-11702 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.28 , pp. 11697-11702
    • Lu, J.1    Kovach, J.S.2    Johnson, F.3
  • 40
    • 33747097252 scopus 로고    scopus 로고
    • Protein kinases and phosphatases as therapeutic targets in cancer
    • Ventura JJ, Nebreda AR. Protein kinases and phosphatases as therapeutic targets in cancer. Clin. Transl. Oncol. 8(3), 153-160 (2006).
    • (2006) Clin. Transl. Oncol. , vol.8 , Issue.3 , pp. 153-160
    • Ventura, J.J.1    Nebreda, A.R.2
  • 41
    • 33750444279 scopus 로고    scopus 로고
    • Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: Inside versus outside
    • DOI 10.1128/JB.00800-06
    • Jones G, Dyson P. Evolution of transmembrane protein kinases implicated in coordinating remodeling of Gram-positive peptidoglycan: inside versus outside. J. Bacteriol. 188(21), 7470-7476 (2006). (Pubitemid 44646246)
    • (2006) Journal of Bacteriology , vol.188 , Issue.21 , pp. 7470-7476
    • Jones, G.1    Dyson, P.2
  • 42
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A b-lactam-binding domain
    • Yeats C, Finn RD, Bateman A. The PASTA domain: a b-lactam-binding domain. Trends Biochem. Sci. 27(9), 438-440 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , Issue.9 , pp. 438-440
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 43
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah IM, Laaberki MH, Popham DL, Dworkin J. A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135(3), 486-496 (2008).
    • (2008) Cell , vol.135 , Issue.3 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 44
    • 0029954661 scopus 로고    scopus 로고
    • The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues
    • Bork P, Brown NP, Hegyi H, Schultz J. The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci. 5, 1421-1425 (1996). (Pubitemid 26239449)
    • (1996) Protein Science , vol.5 , Issue.7 , pp. 1421-1425
    • Bork, P.1    Brown, N.P.2    Hegyi, H.3    Schultz, J.4
  • 45
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y. Serine/threonine phosphatases: mechanism through structure. Cell 139(3), 468-484 (2009).
    • (2009) Cell , vol.139 , Issue.3 , pp. 468-484
    • Shi, Y.1
  • 48
    • 0035511679 scopus 로고    scopus 로고
    • Group B streptococcal infections in newborns
    • Mullaney DM. Group B streptococcal infections in newborns. J. Obstet. Gynecol. Neonatal Nurs. 30(6), 649-658 (2001).
    • (2001) J. Obstet. Gynecol. Neonatal Nurs. , vol.30 , Issue.6 , pp. 649-658
    • Mullaney, D.M.1
  • 50
  • 51
    • 24644458797 scopus 로고    scopus 로고
    • Group B streptococcal infections in elderly adults
    • DOI 10.1086/432804
    • Edwards MS, Baker CJ. Group B streptococcal infections in elderly adults. Clin. Infect. Dis. 41(6), 839-847 (2005). (Pubitemid 41266752)
    • (2005) Clinical Infectious Diseases , vol.41 , Issue.6 , pp. 839-847
    • Edwards, M.S.1    Baker, C.J.2
  • 52
    • 0035882422 scopus 로고    scopus 로고
    • Group B streptococcal disease in nonpregnant adults
    • DOI 10.1086/322696
    • Farley MM. Group B streptococcal disease in nonpregnant adults. Clin. Infect. Dis. 33(4), 556-561 (2001). (Pubitemid 32709591)
    • (2001) Clinical Infectious Diseases , vol.33 , Issue.4 , pp. 556-561
    • Farley, M.M.1
  • 55
    • 19944374470 scopus 로고    scopus 로고
    • Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae
    • DOI 10.1111/j.1365-2958.2005.04620.x
    • Rajagopal L, Vo A, Silvestroni A, Rubens CE. Regulation of purine biosynthesis by a eukaryotic-type kinase in Streptococcus agalactiae. Mol. Microbiol. 56(5), 1329-1346 (2005). (Pubitemid 40756014)
    • (2005) Molecular Microbiology , vol.56 , Issue.5 , pp. 1329-1346
    • Rajagopal, L.1    Vo, A.2    Silvestroni, A.3    Rubens, C.E.4
  • 56
    • 33750492300 scopus 로고    scopus 로고
    • Regulation of cytotoxin expression by converging eukaryotic-type and two-component signalling mechanisms in Streptococcus agalactiae
    • DOI 10.1111/j.1365-2958.2006.05431.x
    • Rajagopal L, Vo A, Silvestroni A, Rubens CE. Regulation of cytotoxin expression by converging eukaryotic-type and two-component signalling mechanisms in Streptococcus agalactiae. Mol. Microbiol. 62(4), 941-957 (2006). (Pubitemid 44655310)
    • (2006) Molecular Microbiology , vol.62 , Issue.4 , pp. 941-957
    • Rajagopal, L.1    Vo, A.2    Silvestroni, A.3    Rubens, C.E.4
  • 57
    • 62449179440 scopus 로고    scopus 로고
    • Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR
    • Lin WJ, Walthers D, Connelly JE et al. Threonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR. Mol. Microbiol. 71(6), 1477-1495 (2009).
    • (2009) Mol. Microbiol. , vol.71 , Issue.6 , pp. 1477-1495
    • Lin, W.J.1    Walthers, D.2    Connelly, J.E.3
  • 58
    • 77954372403 scopus 로고    scopus 로고
    • Regulation of CovR expression in Group B Streptococcus impacts blood-brain barrier penetration
    • Lembo A, Gurney MA, Burnside K et al. Regulation of CovR expression in Group B Streptococcus impacts blood-brain barrier penetration. Mol. Microbiol. 77(2), 431-443 (2010).
    • (2010) Mol. Microbiol. , vol.77 , Issue.2 , pp. 431-443
    • Lembo, A.1    Gurney, M.A.2    Burnside, K.3
  • 59
    • 17044377416 scopus 로고    scopus 로고
    • Virulence role of group B Streptococcus b-hemolysin/cytolysin in a neonatal rabbit model of early-onset pulmonary infection
    • Hensler ME, Liu GY, Sobczak S, Benirschke K, Nizet V, Heldt GP. Virulence role of group B Streptococcus b-hemolysin/cytolysin in a neonatal rabbit model of early-onset pulmonary infection. J. Infect. Dis. 191(8), 1287-1291 (2005).
    • (2005) J. Infect. Dis. , vol.191 , Issue.8 , pp. 1287-1291
    • Hensler, M.E.1    Liu, G.Y.2    Sobczak, S.3    Benirschke, K.4    Nizet, V.5    Heldt, G.P.6
  • 60
    • 0033823722 scopus 로고    scopus 로고
    • Severity of group B streptococcal arthritis is correlated with b-hemolysin expression
    • Puliti M, Nizet V, von Hunolstein C et al. Severity of group B streptococcal arthritis is correlated with b-hemolysin expression. J. Infect. Dis. 182(3), 824-832 (2000).
    • (2000) J. Infect. Dis. , vol.182 , Issue.3 , pp. 824-832
    • Puliti, M.1    Nizet, V.2    Von Hunolstein, C.3
  • 61
    • 0033928019 scopus 로고    scopus 로고
    • Group B streptococcal β-hemolysin induces nitric oxide production in murine macrophages
    • DOI 10.1086/315681
    • Ring A, Braun JS, Nizet V, Stremmel W, Shenep JL. Group B streptococcal b-hemolysin induces nitric oxide production in murine macrophages. J. Infect. Dis. 182(1), 150-157 (2000). (Pubitemid 30497799)
    • (2000) Journal of Infectious Diseases , vol.182 , Issue.1 , pp. 150-157
    • Ring, A.1    Braun, J.S.2    Nizet, V.3    Stremmel, W.4    Shenep, J.L.5
  • 62
    • 0029736682 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin expression is associated with injury of lung epithelial cells
    • Nizet V, Gibson RL, Chi EY, Framson PE, Hulse M, Rubens CE. Group B streptococcal b-hemolysin expression is associated with injury of lung epithelial cells. Infect. Immun. 64(9), 3818-3826 (1996). (Pubitemid 26298710)
    • (1996) Infection and Immunity , vol.64 , Issue.9 , pp. 3818-3826
    • Nizet, V.1    Gibson, R.L.2    Chi, E.Y.3    Framson, P.E.4    Hulse, M.5    Rubens, C.E.6
  • 64
    • 0032909112 scopus 로고    scopus 로고
    • Group B streptococcal β-hemolysin promotes injury of lung microvascular endothelial cells
    • Gibson RL, Nizet V, Rubens CE. Group B streptococcal b-hemolysin promotes injury of lung microvascular endothelial cells. Pediatr. Res. 45(5 Pt 1), 626-634 (1999). (Pubitemid 29203591)
    • (1999) Pediatric Research , vol.45 , Issue.5 , pp. 626-634
    • Gibson, R.L.1    Nizet, V.2    Rubens, C.E.3
  • 65
    • 0037080038 scopus 로고    scopus 로고
    • Group B streptococcal β-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8
    • DOI 10.1086/338475
    • Doran KS, Chang JC, Benoit VM, Eckmann L, Nizet V. Group B streptococcal b-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8. J. Infect. Dis. 185(2), 196-203 (2002). (Pubitemid 34056443)
    • (2002) Journal of Infectious Diseases , vol.185 , Issue.2 , pp. 196-203
    • Doran, K.S.1    Chang, J.C.W.2    Benoit, V.M.3    Eckmann, L.4    Nizet, V.5
  • 66
    • 0036966408 scopus 로고    scopus 로고
    • Streptococcal β-hemolysins: Genetics and role in disease pathogenesis
    • DOI 10.1016/S0966-842X(02)02473-3, PII S0966842X02024733
    • Nizet V. Streptococcal b-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 10(12), 575-580 (2002). (Pubitemid 36139879)
    • (2002) Trends in Microbiology , vol.10 , Issue.12 , pp. 575-580
    • Nizet, V.1
  • 67
    • 0141723665 scopus 로고    scopus 로고
    • Group B streptococcal β-hemolysin/cytolysin activates neutrophil signaling pathways in brain endothelium and contributes to development of meningitis
    • DOI 10.1172/JCI200317335
    • Doran KS, Liu GY, Nizet V. Group B streptococcal b-hemolysin/cytolysin activates neutrophil signaling pathways in brain endothelium and contributes to development of meningitis. J. Clin. Invest. 112(5), 736-744 (2003). (Pubitemid 38057714)
    • (2003) Journal of Clinical Investigation , vol.112 , Issue.5 , pp. 736-744
    • Doran, K.S.1    Liu, G.Y.2    Nizet, V.3
  • 68
    • 0037097516 scopus 로고    scopus 로고
    • Group B streptococcal β-hemolysin induces mortality and liver injury in experimental sepsis
    • DOI 10.1086/340818
    • Ring A, Braun JS, Pohl J, Nizet V, Stremmel W, Shenep JL. Group B streptococcal b-hemolysin induces mortality and liver injury in experimental sepsis. J. Infect. Dis. 185(12), 1745-1753 (2002). (Pubitemid 34615468)
    • (2002) Journal of Infectious Diseases , vol.185 , Issue.12 , pp. 1745-1753
    • Ring, A.1    Braun, J.S.2    Pohl, J.3    Nizet, V.4    Stremmel, W.5    Shenep, J.L.6
  • 70
    • 13244268247 scopus 로고    scopus 로고
    • Regulation of virulence by a two-component system in group B Streptococcus
    • DOI 10.1128/JB.187.3.1105-1113.2005
    • Jiang SM, Cieslewicz MJ, Kasper DL, Wessels MR. Regulation of virulence by a two-component system in group B streptococcus. J. Bacteriol. 187(3), 1105-1113 (2005). (Pubitemid 40189783)
    • (2005) Journal of Bacteriology , vol.187 , Issue.3 , pp. 1105-1113
    • Jiang, S.-M.1    Cieslewicz, M.J.2    Kasper, D.L.3    Wessels, M.R.4
  • 72
    • 58149302498 scopus 로고    scopus 로고
    • Phosphorylation of the RitR DNA-binding domain by a Ser-Thr phosphokinase: Implications for global gene regulation in the streptococci
    • Ulijasz AT, Falk SP, Weisblum B. Phosphorylation of the RitR DNA-binding domain by a Ser-Thr phosphokinase: implications for global gene regulation in the streptococci. Mol. Microbiol. 71(2), 382-390 (2009).
    • (2009) Mol. Microbiol. , vol.71 , Issue.2 , pp. 382-390
    • Ulijasz, A.T.1    Falk, S.P.2    Weisblum, B.3
  • 73
    • 77956519362 scopus 로고    scopus 로고
    • Convergence of Ser/Th and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis
    • Chao JD, Papavinasasundaram KG, Zheng X et al. Convergence of Ser/Th and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J. Biol. Chem. 285(38), 29239-29246 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.38 , pp. 29239-29246
    • Chao, J.D.1    Papavinasasundaram, K.G.2    Zheng, X.3
  • 74
    • 66749101235 scopus 로고    scopus 로고
    • Identification of serine/threonine kinase substrates in the human pathogen group B Streptococcus
    • Silvestroni A, Jewell KA, Lin WJ et al. Identification of serine/threonine kinase substrates in the human pathogen group B Streptococcus. J. Proteome Res. 8(5), 2563-2574 (2009).
    • (2009) J. Proteome Res. , vol.8 , Issue.5 , pp. 2563-2574
    • Silvestroni, A.1    Jewell, K.A.2    Lin, W.J.3
  • 75
    • 0023219580 scopus 로고
    • Clinical and bacteriologic observations of a toxic shock-like syndrome due to streptococcus pyogenes
    • Cone LA, Woodard DR, Schlievert PM, Tomory GS. Clinical and bacteriologic observations of a toxic shock-like syndrome due to Streptococcus pyogenes. N. Engl. J. Med. 317(3), 146-149 (1987). (Pubitemid 17092152)
    • (1987) New England Journal of Medicine , vol.317 , Issue.3 , pp. 146-149
    • Cone, L.A.1    Woodard, D.R.2    Schlievert, P.M.3    Tomory, G.S.4
  • 76
    • 27144468026 scopus 로고    scopus 로고
    • The global burden of group A streptococcal diseases
    • DOI 10.1016/S1473-3099(05)70267-X, PII S147330990570267X
    • Carapetis JR, Steer AC, Mulholland EK, Weber M. The global burden of Group A streptococcal diseases. Lancet Infect. Dis. 5(11), 685-694 (2005). (Pubitemid 41505357)
    • (2005) Lancet Infectious Diseases , vol.5 , Issue.11 , pp. 685-694
    • Carapetis, J.R.1    Steer, A.C.2    Mulholland, E.K.3    Weber, M.4
  • 77
    • 0026717164 scopus 로고
    • Epidemiologic analysis of Group A streptococcal serotypes associated with severe systemic infections, rheumatic fever, or uncomplicated pharyngitis
    • Johnson DR, Stevens DL, Kaplan EL. Epidemiologic analysis of Group A streptococcal serotypes associated with severe systemic infections, rheumatic fever, or uncomplicated pharyngitis. J. Infect. Dis. 166(2), 374-382 (1992).
    • (1992) J. Infect. Dis. , vol.166 , Issue.2 , pp. 374-382
    • Johnson, D.R.1    Stevens, D.L.2    Kaplan, E.L.3
  • 78
    • 0029330062 scopus 로고
    • Streptococcal toxic-shock syndrome: Spectrum of disease, pathogenesis, and new concepts in treatment
    • Stevens DL. Streptococcal toxic-shock syndrome: spectrum of disease, pathogenesis, and new concepts in treatment. Emerg. Infect. Dis. 1(3), 69-78 (1995).
    • (1995) Emerg. Infect. Dis. , vol.1 , Issue.3 , pp. 69-78
    • Stevens, D.L.1
  • 80
    • 77957262988 scopus 로고    scopus 로고
    • Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor
    • Pancholi V, Boel G, Jin H. Streptococcus pyogenes Ser/Thr kinase-regulated cell wall hydrolase is a cell division plane-recognizing and chain-forming virulence factor. J. Biol. Chem. 285(40), 30861-30874 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.40 , pp. 30861-30874
    • Pancholi, V.1    Boel, G.2    Jin, H.3
  • 81
    • 0037381650 scopus 로고    scopus 로고
    • Regulation of gene expression by histone-like proteins in bacteria
    • DOI 10.1016/S0959-437X(03)00025-X
    • Dorman CJ, Deighan P. Regulation of gene expression by histone-like proteins in bacteria. Curr. Opin. Genet. Dev. 13(2), 179-184 (2003). (Pubitemid 36369742)
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.2 , pp. 179-184
    • Dorman, C.J.1    Deighan, P.2
  • 82
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • DOI 10.1016/j.mib.2004.02.001, PII S1369527404000141
    • Rimsky S. Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr. Opin. Microbiol. 7(2), 109-114 (2004). (Pubitemid 38447041)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.2 , pp. 109-114
    • Rimsky, S.1
  • 83
    • 6044256118 scopus 로고    scopus 로고
    • Histones and histone modifications
    • Peterson CL, Laniel MA. Histones and histone modifications. Curr. Biol. 14(14), R546-R551 (2004).
    • (2004) Curr. Biol. , vol.14 , Issue.14
    • Peterson, C.L.1    Ma, L.2
  • 84
    • 0030072556 scopus 로고    scopus 로고
    • Histone-like protein HU as a specific transcriptional regulator: Co-factor role in repression of gal transcription by GAL repressor
    • Aki T, Choy HE, Adhya S. Histone-like protein HU as a specific transcriptional regulator: co-factor role in repression of gal transcription by GAL repressor. Genes Cells 1(2), 179-188 (1996). (Pubitemid 126673116)
    • (1996) Genes to Cells , vol.1 , Issue.2 , pp. 179-188
    • Aki, T.1    Choy, H.E.2    Adhya, S.3
  • 85
    • 66449106900 scopus 로고    scopus 로고
    • Histone H3 phosphorylation: Universal code or lineage specific dialects?
    • Cerutti H, Casas-Mollano JA. Histone H3 phosphorylation: universal code or lineage specific dialects? Epigenetics 4(2), 71-75 (2009).
    • (2009) Epigenetics , vol.4 , Issue.2 , pp. 71-75
    • Cerutti, H.1    Casas-Mollano, J.A.2
  • 86
    • 77956199888 scopus 로고    scopus 로고
    • Regulation of hemolysin expression and virulence of Staphylococcus aureus by a serine/threonine kinase and phosphatase
    • Burnside K, Lembo A, de Los Reyes M et al. Regulation of hemolysin expression and virulence of Staphylococcus aureus by a serine/threonine kinase and phosphatase. PLoS ONE 5(6), E11071 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.6
    • Burnside, K.1    Lembo, A.2    De Los Reyes, M.3
  • 87
    • 63149104710 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Epidemiology, risk factors, and strategies for prevention
    • Lynch JP 3rd, Zhanel GG. Streptococcus pneumoniae: epidemiology, risk factors, and strategies for prevention. Semin. Respir. Crit. Care Med. 30(2), 189-209 (2009).
    • (2009) Semin. Respir. Crit. Care Med. , vol.30 , Issue.2 , pp. 189-209
    • Lynch Iii, J.P.1    Zhanel, G.G.2
  • 88
    • 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
    • DOI 10.1111/j.1742-4658.2005.04560.x
    • Novakova L, Saskova L, Pallova P et al. Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates. FEBS J. 272(5), 1243-1254 (2005). (Pubitemid 40314942)
    • (2005) FEBS Journal , vol.272 , Issue.5 , 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
  • 89
    • 34249801777 scopus 로고    scopus 로고
    • Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae
    • DOI 10.1128/JB.01616-06
    • Saskova L, Novakova L, Basler M, Branny P. Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae. J. Bacteriol. 189(11), 4168-4179 (2007). (Pubitemid 46847365)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 4168-4179
    • Saskova, L.1    Novakova, L.2    Basler, M.3    Branny, P.4
  • 91
    • 77953182143 scopus 로고    scopus 로고
    • The pneumococcal eukaryotic-type serine/threonine protein kinase StkP co-localizes with the cell division apparatus and interacts with FtsZ in vitro
    • Giefing C, Jelencsics KE, Gelbmann D, Senn BM, Nagy E. The pneumococcal eukaryotic-type serine/threonine protein kinase StkP co-localizes with the cell division apparatus and interacts with FtsZ in vitro. Microbiology 156(Pt 6), 1697-1707 (2010).
    • (2010) Microbiology , vol.156 , Issue.PART 6 , pp. 1697-1707
    • Giefing, C.1    Jelencsics, K.E.2    Gelbmann, D.3    Senn, B.M.4    Nagy, E.5
  • 93
    • 67650601906 scopus 로고    scopus 로고
    • The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins
    • Dias R, Felix D, Canica M, Trombe MC. The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins. BMC Microbiol. 9, 121 (2009).
    • (2009) BMC Microbiol. , vol.9 , pp. 121
    • Dias, R.1    Felix, D.2    Canica, M.3    Trombe, M.C.4
  • 94
    • 67749116071 scopus 로고    scopus 로고
    • The StkP/PhpP signaling couple in Streptococcus pneumoniae: Cellular organization and physiological characterization
    • Osaki M, Arcondeguy T, Bastide A, Touriol C, Prats H, Trombe MC. The StkP/PhpP signaling couple in Streptococcus pneumoniae: cellular organization and physiological characterization. J. Bacteriol. 191(15), 4943-4950 (2009).
    • (2009) J. Bacteriol. , vol.191 , Issue.15 , pp. 4943-4950
    • Osaki, M.1    Arcondeguy, T.2    Bastide, A.3    Touriol, C.4    Prats, H.5    Trombe, M.C.6
  • 95
    • 64349102078 scopus 로고    scopus 로고
    • Regulation of natural genetic transformation and acquisition of transforming DNA in Streptococcus pneumoniae
    • Johnsborg O, Havarstein LS. Regulation of natural genetic transformation and acquisition of transforming DNA in Streptococcus pneumoniae. FEMS Microbiol. Rev. 33(3), 627-642 (2009).
    • (2009) FEMS Microbiol. Rev. , vol.33 , Issue.3 , pp. 627-642
    • Johnsborg, O.1    Havarstein, L.S.2
  • 96
    • 9244265524 scopus 로고    scopus 로고
    • Regulation of iron transport in Streptococcus pneumoniae by RitR, an orphan response regulator
    • DOI 10.1128/JB.186.23.8123-8136.2004
    • Ulijasz AT, Andes DR, Glasner JD, Weisblum B. Regulation of iron transport in Streptococcus pneumoniae by RitR, an orphan response regulator. J. Bacteriol. 186(23), 8123-8136 (2004). (Pubitemid 39552525)
    • (2004) Journal of Bacteriology , vol.186 , Issue.23 , pp. 8123-8136
    • Ulijasz, A.T.1    Andes, D.R.2    Glasner, J.D.3    Weisblum, B.4
  • 98
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • DOI 10.1006/jmbi.1999.3161
    • Busby S, Ebright RH. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 293(2), 199-213 (1999). (Pubitemid 29516164)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 99
    • 0030032719 scopus 로고    scopus 로고
    • Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli
    • DOI 10.1074/jbc.271.1.32
    • Mengin-Lecreulx D, van Heijenoort J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 271(1), 32-39 (1996). (Pubitemid 26027279)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 32-39
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2
  • 101
    • 0019255349 scopus 로고
    • Biology, immunology, and cariogenicity of Streptococcus mutans
    • Hamada S, Slade HD. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol. Rev. 44(2), 331-384 (1980). (Pubitemid 11128312)
    • (1980) Microbiological Reviews , vol.44 , Issue.2 , pp. 331-384
    • Hamada, S.1    Slade, H.D.2
  • 102
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche WJ. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50(4), 353-380 (1986). (Pubitemid 17202894)
    • (1986) Microbiological Reviews , vol.50 , Issue.4 , pp. 353-380
    • Loesche, W.J.1
  • 103
    • 0027546246 scopus 로고
    • The association of mutans streptococci and non-mutans streptococci capable of acidogenesis at a low pH with dental caries on enamel and root surfaces
    • Sansone C, Van Houte J, Joshipura K, Kent R, Margolis HC. The association of mutans streptococci and non-mutans streptococci capable of acidogenesis at a low pH with dental caries on enamel and root surfaces. J. Dent. Res. 72(2), 508-516 (1993).
    • (1993) J. Dent. Res. , vol.72 , Issue.2 , pp. 508-516
    • Sansone, C.1    Van Houte, J.2    Joshipura, K.3    Kent, R.4    Margolis, H.C.5
  • 104
    • 0027530878 scopus 로고
    • Virulence factors of mutans streptococci: Role of molecular genetics
    • Kuramitsu HK. Virulence factors of mutans streptococci: role of molecular genetics. Crit. Rev. Oral Biol. Med. 4(2), 159-176 (1993). (Pubitemid 23103290)
    • (1993) Critical Reviews in Oral Biology and Medicine , vol.4 , Issue.2 , pp. 159-176
    • Kuramitsu, H.K.1
  • 105
    • 0027501797 scopus 로고
    • Molecular characterization of a Streptococcus mutans mutant altered in environmental stress responses
    • Yamashita Y, Takehara T, Kuramitsu HK. Molecular characterization of a Streptococcus mutans mutant altered in environmental stress responses. J. Bacteriol. 175(19), 6220-6228 (1993). (Pubitemid 23292436)
    • (1993) Journal of Bacteriology , vol.175 , Issue.19 , pp. 6220-6228
    • Yamashita, Y.1    Takehara, T.2    Kuramitsu, H.K.3
  • 106
    • 77951248837 scopus 로고    scopus 로고
    • The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism
    • Banu LD, Conrads G, Rehrauer H, Hussain H, Allan E, van der Ploeg JR. The Streptococcus mutans serine/threonine kinase, PknB, regulates competence development, bacteriocin production, and cell wall metabolism. Infect. Immun. 78(5), 2209-2220 (2010).
    • (2010) Infect. Immun. , vol.78 , Issue.5 , pp. 2209-2220
    • Banu, L.D.1    Conrads, G.2    Rehrauer, H.3    Hussain, H.4    Allan, E.5    Van Der Ploeg, J.R.6
  • 107
    • 77950859836 scopus 로고    scopus 로고
    • Role of Streptococcus mutans eukaryotic-type serine/threonine protein kinase in interspecies interactions with Streptococcus sanguinis
    • Zhu L, Kreth J. Role of Streptococcus mutans eukaryotic-type serine/threonine protein kinase in interspecies interactions with Streptococcus sanguinis. Arch. Oral Biol. 55(5), 385-390 (2010).
    • (2010) Arch. Oral Biol. , vol.55 , Issue.5 , pp. 385-390
    • Zhu, L.1    Kreth, J.2
  • 108
    • 33645897695 scopus 로고    scopus 로고
    • Epidemiology and clinical outcome of enterococcal bacteraemia in an acute care hospital
    • Poh CH, Oh HM, Tan AL. Epidemiology and clinical outcome of enterococcal bacteraemia in an acute care hospital. J. Infect. 52(5), 383-386 (2006).
    • (2006) J. Infect. , vol.52 , Issue.5 , pp. 383-386
    • Poh, C.H.1    Oh, H.M.2    Tan, A.L.3
  • 109
    • 0034630096 scopus 로고    scopus 로고
    • Identification of general stress genes in Enterococcus faecalis
    • DOI 10.1016/S0168-1605(00)00180-X, PII S016816050000180X
    • Rince A, Flahaut S, Auffray Y. Identification of general stress genes in Enterococcus faecalis. Int. J. Food Microbiol. 55(1-3), 87-91 (2000). (Pubitemid 30160810)
    • (2000) International Journal of Food Microbiology , vol.55 , Issue.1-3 , pp. 87-91
    • Rince, A.1    Flahaut, S.2    Auffray, Y.3
  • 111
    • 0001896384 scopus 로고
    • The streptococci
    • Sherman JM. The streptococci. Bacteriol. Rev. 1(1), 3-97 (1937).
    • (1937) Bacteriol. Rev. , vol.1 , Issue.1 , pp. 3-97
    • Sherman, J.M.1
  • 112
    • 0026645135 scopus 로고
    • Emergence of Enterococcus as a significant pathogen
    • Moellering RC Jr. Emergence of Enterococcus as a significant pathogen. Clin. Infect. Dis. 14(6), 1173-1176 (1992).
    • (1992) Clin. Infect. Dis. , vol.14 , Issue.6 , pp. 1173-1176
    • Moellering Jr., R.C.1
  • 114
    • 33644923830 scopus 로고    scopus 로고
    • Laboratory-based surveillance of current antimicrobial resistance patterns and trends among Staphylococcus aureus: 2005 status in the United States
    • Styers D, Sheehan DJ, Hogan P, Sahm DF. Laboratory-based surveillance of current antimicrobial resistance patterns and trends among Staphylococcus aureus: 2005 status in the United States. Ann. Clin. Microbiol. Antimicrob. 5, 2 (2006).
    • (2006) Ann. Clin. Microbiol. Antimicrob. , vol.5 , pp. 2
    • Styers, D.1    Sheehan, D.J.2    Hogan, P.3    Sahm, D.F.4
  • 115
    • 0035033139 scopus 로고    scopus 로고
    • The changing epidemiology of staphylococcus aureus?
    • Chambers HF. The changing epidemiology of Staphylococcus aureus? Emerg. Infect. Dis. 7(2), 178-182 (2001). (Pubitemid 32374323)
    • (2001) Emerging Infectious Diseases , vol.7 , Issue.2 , pp. 178-182
    • Chambers, H.F.1
  • 116
    • 33144454355 scopus 로고    scopus 로고
    • Emergence of community-acquired methicillin-resistant Staphylococcus aureus USA 300 clone as the predominant cause of skin and soft-tissue infections
    • King MD, Humphrey BJ, Wang YF, Kourbatova EV, Ray SM, Blumberg HM. Emergence of community-acquired methicillin-resistant Staphylococcus aureus USA 300 clone as the predominant cause of skin and soft-tissue infections. Ann. Intern. Med. 144(5), 309-317 (2006). (Pubitemid 46768185)
    • (2006) Annals of Internal Medicine , vol.144 , Issue.5 , pp. 309-317
    • King, M.D.1    Humphrey, B.J.2    Wang, Y.F.3    Kourbatova, E.V.4    Ray, S.M.5    Blumberg, H.M.6
  • 118
    • 0035873058 scopus 로고    scopus 로고
    • Survey of infections due to Staphylococcus species: Frequency of occurrence and antimicrobial susceptibility of isolates collected in the United States, Canada, Latin America, Europe, and the Western Pacific region for the SENTRY Antimicrobial Surveillance Program, 1997-1999
    • Diekema DJ, Pfaller MA, Schmitz FJ et al. Survey of infections due to Staphylococcus species: frequency of occurrence and antimicrobial susceptibility of isolates collected in the United States, Canada, Latin America, Europe, and the Western Pacific region for the SENTRY Antimicrobial Surveillance Program, 1997-1999. Clin. Infect. Dis. 32(Suppl. 2), S114-S132 (2001). (Pubitemid 32424266)
    • (2001) Clinical Infectious Diseases , vol.32 , Issue.10 SUPPL. 2
    • Diekema, D.J.1    Pfaller, M.A.2    Schmitz, F.J.3    Smayevsky, J.4    Bell, J.5    Jones, R.N.6    Beach, M.7
  • 119
    • 20144386837 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus disease in three communities
    • Fridkin SK, Hageman JC, Morrison M et al. Methicillin-resistant Staphylococcus aureus disease in three communities. N. Engl. J. Med. 352(14), 1436-1444 (2005).
    • (2005) N. Engl. J. Med. , vol.352 , Issue.14 , pp. 1436-1444
    • Fridkin, S.K.1    Hageman, J.C.2    Morrison, M.3
  • 121
    • 73649088602 scopus 로고    scopus 로고
    • The impact of serine/threonine phosphorylation in Staphylococcus aureus
    • Ohlsen K, Donat S. The impact of serine/threonine phosphorylation in Staphylococcus aureus. Int. J. Med. Microbiol. 300(2-3), 137-141 (2010).
    • (2010) Int. J. Med. Microbiol. , vol.300 , Issue.2-3 , pp. 137-141
    • Ohlsen, K.1    Donat, S.2
  • 122
    • 67649401960 scopus 로고    scopus 로고
    • Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus
    • Donat S, Streker K, Schirmeister T et al. Transcriptome and functional analysis of the eukaryotic-type serine/threonine kinase PknB in Staphylococcus aureus. J. Bacteriol. 191(13), 4056-4069 (2009).
    • (2009) J. Bacteriol. , vol.191 , Issue.13 , pp. 4056-4069
    • Donat, S.1    Streker, K.2    Schirmeister, T.3
  • 123
    • 67649403398 scopus 로고    scopus 로고
    • Characterization of a serine/threonine kinase involved in virulence of Staphylococcus aureus
    • Debarbouille M, Dramsi S, Dussurget O et al. Characterization of a serine/threonine kinase involved in virulence of Staphylococcus aureus. J. Bacteriol. 191(13), 4070-4081 (2009).
    • (2009) J. Bacteriol. , vol.191 , Issue.13 , pp. 4070-4081
    • Debarbouille, M.1    Dramsi, S.2    Dussurget, O.3
  • 124
    • 77955293898 scopus 로고    scopus 로고
    • Role of PknB kinase in antibiotic resistance and virulence in community-acquired methicillin-resistant Staphylococcus aureus strain USA300
    • Tamber S, Schwartzman J, Cheung AL. Role of PknB kinase in antibiotic resistance and virulence in community-acquired methicillin-resistant Staphylococcus aureus strain USA300. Infect. Immun. 78(8), 3637-3646 (2010).
    • (2010) Infect. Immun. , vol.78 , Issue.8 , pp. 3637-3646
    • Tamber, S.1    Schwartzman, J.2    Cheung, A.L.3
  • 125
    • 34250678182 scopus 로고    scopus 로고
    • Several enzymes of the central metabolism are phosphorylated in Staphylococcus aureus
    • DOI 10.1111/j.1574-6968.2007.00742.x
    • Lomas-Lopez R, Paracuellos P, Riberty M, Cozzone AJ, Duclos B. Several enzymes of the central metabolism are phosphorylated in Staphylococcus aureus. FEMS Microbiol. Lett. 272(1), 35-42 (2007). (Pubitemid 46944461)
    • (2007) FEMS Microbiology Letters , vol.272 , Issue.1 , pp. 35-42
    • Lomas-Lopez, R.1    Paracuellos, P.2    Riberty, M.3    Cozzone, A.J.4    Duclos, B.5
  • 126
    • 39549121471 scopus 로고    scopus 로고
    • Vaccine protection against Staphylococcus aureus pneumonia
    • DOI 10.1084/jem.20072208
    • Bubeck Wardenburg J, Schneewind O. Vaccine protection against Staphylococcus aureus pneumonia. J. Exp. Med. 205(2), 287-294 (2008). (Pubitemid 351281594)
    • (2008) Journal of Experimental Medicine , vol.205 , Issue.2 , pp. 287-294
    • Wardenburg, J.B.1    Schneewind, O.2
  • 127
    • 33846814907 scopus 로고    scopus 로고
    • Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia
    • DOI 10.1128/IAI.01313-06
    • Bubeck Wardenburg J, Patel RJ, Schneewind O. Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia. Infect. Immun. 75(2), 1040-1044 (2007). (Pubitemid 46203470)
    • (2007) Infection and Immunity , vol.75 , Issue.2 , pp. 1040-1044
    • Wardenburg, J.B.1    Patel, R.J.2    Schneewind, O.3
  • 128
    • 0034783704 scopus 로고    scopus 로고
    • Diminished virulence of an alpha-toxin mutant of Staphylococcus aureus in experimental brain abscesses
    • DOI 10.1128/IAI.69.11.6902-6911.2001
    • Kielian T, Cheung A, Hickey WF. Diminished virulence of an a-toxin mutant of Staphylococcus aureus in experimental brain abscesses. Infect. Immun. 69(11), 6902-6911 (2001). (Pubitemid 32995450)
    • (2001) Infection and Immunity , vol.69 , Issue.11 , pp. 6902-6911
    • Kielian, T.1    Cheung, A.2    Hickey, W.F.3
  • 129
    • 0033801541 scopus 로고    scopus 로고
    • Immunization with a-toxin toxoid protects the cornea against tissue damage during experimental Staphylococcus aureus keratitis
    • Hume EB, Dajcs JJ, Moreau JM, O'Callaghan RJ. Immunization with a-toxin toxoid protects the cornea against tissue damage during experimental Staphylococcus aureus keratitis. Infect. Immun. 68(10), 6052-6055 (2000).
    • (2000) Infect. Immun. , vol.68 , Issue.10 , pp. 6052-6055
    • Hume, E.B.1    Dajcs, J.J.2    Moreau, J.M.3    O'Callaghan, R.J.4
  • 130
    • 0033053177 scopus 로고    scopus 로고
    • Alpha-toxin and gamma-toxin jointly promote Staphylococcus aureus virulence in murine septic arthritis
    • Nilsson IM, Hartford O, Foster T, Tarkowski A. a-toxin and g-toxin jointly promote Staphylococcus aureus virulence in murine septic arthritis. Infect. Immun. 67(3), 1045-1049 (1999). (Pubitemid 29108475)
    • (1999) Infection and Immunity , vol.67 , Issue.3 , pp. 1045-1049
    • Nilsson, I.-M.1    Hartford, O.2    Foster, T.3    Tarkowski, A.4
  • 131
    • 0028200916 scopus 로고
    • Corneal virulence of Staphylococcus aureus: Roles of alpha-toxin and protein A in pathogenesis
    • Callegan MC, Engel LS, Hill JM, O'Callaghan RJ. Corneal virulence of Staphylococcus aureus: roles of a-toxin and protein A in pathogenesis. Infect. Immun. 62(6), 2478-2482 (1994). (Pubitemid 24157079)
    • (1994) Infection and Immunity , vol.62 , Issue.6 , pp. 2478-2482
    • Callegan, M.C.1    Engel, L.S.2    Hill, J.M.3    O'Callaghan, R.J.4
  • 132
    • 0023518575 scopus 로고
    • Virulence of protein A-deficient and alpha-toxin-deficient mutants of Staphylococcus aureus isolated by allele replacement
    • Patel AH, Nowlan P, Weavers ED, Foster T. Virulence of protein A-deficient and a-toxin-deficient mutants of Staphylococcus aureus isolated by allele replacement. Infect. Immun. 55(12), 3103-3110 (1987). (Pubitemid 18008284)
    • (1987) Infection and Immunity , vol.55 , Issue.12 , pp. 3103-3110
    • Patel, A.H.1    Nowlan, P.2    Weavers, E.D.3    Foster, T.4
  • 133
    • 39549090149 scopus 로고    scopus 로고
    • An antidote for Staphylococcus aureus pneumonia?
    • DOI 10.1084/jem.20080167
    • DeLeo FR, Otto M. An antidote for Staphylococcus aureus pneumonia? J. Exp. Med. 205(2), 271-274 (2008). (Pubitemid 351281592)
    • (2008) Journal of Experimental Medicine , vol.205 , Issue.2 , pp. 271-274
    • DeLeo, F.R.1    Otto, M.2
  • 134
    • 67650079244 scopus 로고    scopus 로고
    • Anti-a-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia
    • Ragle BE, Bubeck Wardenburg J. Anti-a-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia. Infect. Immun. 77(7), 2712-2718 (2009).
    • (2009) Infect. Immun. , vol.77 , Issue.7 , pp. 2712-2718
    • Ragle, B.E.1    Bubeck Wardenburg, J.2
  • 135
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • DOI 10.1016/j.tig.2004.02.007, PII S0168952504000459
    • Nowak SJ, Corces VG. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. 20(4), 214-220 (2004). (Pubitemid 38369193)
    • (2004) Trends in Genetics , vol.20 , Issue.4 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 136
    • 0037376199 scopus 로고    scopus 로고
    • Histone and chromatin cross-talk
    • DOI 10.1016/S0955-0674(03)00013-9
    • Fischle W, Wang Y, Allis CD. Histone and chromatin cross-talk. Curr. Opin. Cell Biol. 15(2), 172-183 (2003). (Pubitemid 36332192)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.2 , pp. 172-183
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 137
    • 33645472239 scopus 로고    scopus 로고
    • Role of two-component systems in the virulence of Streptococcus pneumoniae
    • Paterson GK, Blue CE, Mitchell TJ. Role of two-component systems in the virulence of Streptococcus pneumoniae. J. Med. Microbiol. 55(Pt 4), 355-363 (2006).
    • (2006) J. Med. Microbiol. , vol.55 , Issue.PART 4 , pp. 355-363
    • Paterson, G.K.1    Blue, C.E.2    Mitchell, T.J.3
  • 139
    • 33749642880 scopus 로고    scopus 로고
    • Transcriptional profiling of a Staphylococcus aureus clinical isolate and its isogenic agr and sarA mutants reveals global differences in comparison to the laboratory strain RN6390
    • DOI 10.1099/mic.0.29033-0
    • Cassat J, Dunman PM, Murphy E et al. Transcriptional profiling of a Staphylococcus aureus clinical isolate and its isogenic agr and sarA mutants reveals global differences in comparison to the laboratory strain RN6390. Microbiology 152(Pt 10), 3075-3090 (2006). (Pubitemid 44542387)
    • (2006) Microbiology , vol.152 , Issue.10 , pp. 3075-3090
    • Cassat, J.1    Dunman, P.M.2    Murphy, E.3    Projan, S.J.4    Beenken, K.E.5    Palm, K.J.6    Yang, S.-J.7    Rice, K.C.8    Bayles, K.W.9    Smeltzer, M.S.10
  • 140
    • 77949386274 scopus 로고    scopus 로고
    • Staphylococcal PknB as the first prokaryotic representative of the proline-directed kinases
    • Miller M, Donat S, Rakette S et al. Staphylococcal PknB as the first prokaryotic representative of the proline-directed kinases. PLoS ONE 5(2), E9057 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.2
    • Miller, M.1    Donat, S.2    Rakette, S.3
  • 141
    • 0036842045 scopus 로고    scopus 로고
    • The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells
    • DOI 10.1128/JB.184.22.6109-6114.2002
    • Gaidenko TA, Kim TJ, Price CW. The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J. Bacteriol. 184(22), 6109-6114 (2002). (Pubitemid 35265890)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6109-6114
    • Gaidenko, T.A.1    Kim, T.-J.2    Price, C.W.3
  • 142
    • 0033801870 scopus 로고    scopus 로고
    • Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family
    • Obuchowski M, Madec E, Delattre D et al. Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family. J. Bacteriol. 182(19), 5634-5638 (2000).
    • (2000) J. Bacteriol. , vol.182 , Issue.19 , pp. 5634-5638
    • Obuchowski, M.1    Madec, E.2    Delattre, D.3
  • 143
    • 77950616042 scopus 로고    scopus 로고
    • In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism
    • Pietack N, Becher D, Schmidl SR et al. In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism. J. Mol. Microbiol. Biotechnol. 18(3), 129-140 (2010).
    • (2010) J. Mol. Microbiol. Biotechnol. , vol.18 , Issue.3 , pp. 129-140
    • Pietack, N.1    Becher, D.2    Schmidl, S.R.3
  • 144
    • 77952657885 scopus 로고    scopus 로고
    • The structure of PknB extracellular PASTA domain from Mycobacterium tuberculosis suggests a ligand-dependent kinase activation
    • Barthe P, Mukamolova GV, Roumestand C, Cohen-Gonsaud M. The structure of PknB extracellular PASTA domain from Mycobacterium tuberculosis suggests a ligand-dependent kinase activation. Structure 18(5), 606-615 (2010).
    • (2010) Structure , vol.18 , Issue.5 , pp. 606-615
    • Barthe, P.1    Mukamolova, G.V.2    Roumestand, C.3    Cohen-Gonsaud, M.4
  • 146
    • 23044488472 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape
    • DOI 10.1101/gad.1311105
    • Kang CM, Abbott DW, Park ST, Dascher CC, Cantley LC, Husson RN. The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev. 19(14), 1692-1704 (2005). (Pubitemid 41058365)
    • (2005) Genes and Development , vol.19 , Issue.14 , pp. 1692-1704
    • Kang, C.-M.1    Abbott, D.W.2    Sang, T.P.3    Dascher, C.C.4    Cantley, L.C.5    Husson, R.N.6
  • 147
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Sassetti CM, Boyd DH, Rubin EJ. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48(1), 77-84 (2003). (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 148
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • DOI 10.1074/jbc.M300660200
    • Ortiz-Lombardia M, Pompeo F, Boitel B, Alzari PM. Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J. Biol. Chem. 278(15), 13094-13100 (2003). (Pubitemid 36800077)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompeo, F.2    Boitel, B.3    Alzari, P.M.4
  • 149
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • DOI 10.1038/nsb897
    • Young TA, Delagoutte B, Endrizzi JA, Falick AM, Alber T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10(3), 168-174 (2003). (Pubitemid 36297985)
    • (2003) Nature Structural Biology , 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
  • 150
    • 79952426399 scopus 로고    scopus 로고
    • Eukaryote-like serine/threonine kinases and phosphatases in bacteria
    • Pereira SF, Goss L, Dworkin J. Eukaryote-like serine/threonine kinases and phosphatases in bacteria. Microbiol. Mol. Biol. Rev. 75(1), 192-212 (2011).
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , Issue.1 , pp. 192-212
    • Pereira, S.F.1    Goss, L.2    Dworkin, J.3


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