메뉴 건너뛰기




Volumn 195, Issue 21, 2013, Pages 4782-4792

Functional characterization of core components of the bacillus: Subtilis cyclic-Di-GMP signaling pathway

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYBIS (3' 5') CYCLIC DIMERIC GUANOSINE PHOSPHATE; CYCLIC GMP PHOSPHODIESTERASE; DGCK PROTEIN; DGCP PROTEIN; DGCW PROTEIN; PDEH PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84886035253     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00373-13     Document Type: Article
Times cited : (66)

References (63)
  • 1
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge R. 2009. Principles of c-di-GMP signalling in bacteria. Nat. Rev. Microbiol. 7:263-273.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 263-273
    • Hengge, R.1
  • 2
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal U, Malone J. 2006. Mechanisms of cyclic-di-GMP signaling in bacteria. Annu. Rev. Genet. 40:385-407.
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 3
    • 77954933973 scopus 로고    scopus 로고
    • 3',5'-Cyclic diguanylic acid: a small nucleotide that makes big impacts
    • Yan HB, Chen WX. 2010. 3=,5=-Cyclic diguanylic acid: a small nucleotide that makes big impacts. Chem. Soc. Rev. 39:2914-2924.
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 2914-2924
    • Yan, H.B.1    Chen, W.X.2
  • 7
    • 77950629120 scopus 로고    scopus 로고
    • Molecular mechanisms of compounds affecting bacterial biofilm formation and dispersal
    • Landini P, Antoniani D, Burgess JG, Nijland R. 2010. Molecular mechanisms of compounds affecting bacterial biofilm formation and dispersal. Appl. Microbiol. Biotechnol. 86:813-823.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 813-823
    • Landini, P.1    Antoniani, D.2    Burgess, J.G.3    Nijland, R.4
  • 9
    • 33846847846 scopus 로고    scopus 로고
    • c-di-GMP-mediated regulation of virulence and biofilm formation
    • Cotter PA, Stibitz S. 2007. c-di-GMP-mediated regulation of virulence and biofilm formation. Curr. Opin. Microbiol. 10:17-23.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 17-23
    • Cotter, P.A.1    Stibitz, S.2
  • 10
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo R, Pratt JT, Camilli A. 2007. Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu. Rev. Microbiol. 61:131-148.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 11
    • 82555185619 scopus 로고    scopus 로고
    • Complex c-di-GMP signaling networks mediate transition between virulence properties and biofilm formation in Salmonella enterica serovar Typhimurium
    • Ahmad I, Lamprokostopoulou A, Le Guyon S, Streck E, Barthel M, Peters V, Hardt WD, Romling U. 2011. Complex c-di-GMP signaling networks mediate transition between virulence properties and biofilm formation in Salmonella enterica serovar Typhimurium. PLoS One 6:e28351.
    • (2011) PLoS One , vol.6
    • Ahmad, I.1    Lamprokostopoulou, A.2    Le Guyon, S.3    Streck, E.4    Barthel, M.5    Peters, V.6    Hardt, W.D.7    Romling, U.8
  • 12
    • 79953038793 scopus 로고    scopus 로고
    • Quorum sensing and c-di-GMP-dependent alterations in gene transcripts and virulenceassociated phenotypes in a clinical isolate of Aeromonas hydrophila
    • Kozlova EV, Khajanchi BK, Sha J, Chopra AK. 2011. Quorum sensing and c-di-GMP-dependent alterations in gene transcripts and virulenceassociated phenotypes in a clinical isolate of Aeromonas hydrophila. Microb. Pathog. 50:213-223.
    • (2011) Microb. Pathog. , vol.50 , pp. 213-223
    • Kozlova, E.V.1    Khajanchi, B.K.2    Sha, J.3    Chopra, A.K.4
  • 13
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin MY, Nikolskaya AN, Koonin EV. 2001. Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol. Lett. 203:11-21.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 14
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer T, Jenal U. 2009. Structural and mechanistic determinants of c-di-GMP signalling. Nat. Rev. Microbiol. 7:724-735.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 16
    • 77955630859 scopus 로고    scopus 로고
    • An allosteric self-splicing ribozyme triggered by a bacterial second messenger
    • Lee ER, Baker JL, Weinberg Z, Sudarsan N, Breaker RR. 2010. An allosteric self-splicing ribozyme triggered by a bacterial second messenger. Science 329:845-848.
    • (2010) Science , vol.329 , pp. 845-848
    • Lee, E.R.1    Baker, J.L.2    Weinberg, Z.3    Sudarsan, N.4    Breaker, R.R.5
  • 17
    • 55549144752 scopus 로고    scopus 로고
    • Cyclic di-GMP: a second messenger required for long-term survival, but not for biofilm formation, in Mycobacterium smegmatis
    • Kumar M, Chatterji D. 2008. Cyclic di-GMP: a second messenger required for long-term survival, but not for biofilm formation, in Mycobacterium smegmatis. Microbiology 154:2942-2955.
    • (2008) Microbiology , vol.154 , pp. 2942-2955
    • Kumar, M.1    Chatterji, D.2
  • 18
    • 84861918212 scopus 로고    scopus 로고
    • A full-length bifunctional protein involved in c-di-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis
    • Bharati BK, Sharma IM, Kasetty S, Kumar M, Mukherjee R, Chatterji D. 2012. A full-length bifunctional protein involved in c-di-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis. Microbiology 158:1415-1427.
    • (2012) Microbiology , vol.158 , pp. 1415-1427
    • Bharati, B.K.1    Sharma, I.M.2    Kasetty, S.3    Kumar, M.4    Mukherjee, R.5    Chatterji, D.6
  • 19
    • 84871200600 scopus 로고    scopus 로고
    • LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis
    • Li W, He ZG. 2012. LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis. Nucleic Acids Res. 40:11292-11307.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11292-11307
    • Li, W.1    He, Z.G.2
  • 20
    • 78649800745 scopus 로고    scopus 로고
    • Identification, activity and disulfide connectivity of c-di-GMP regulating proteins in Mycobacterium tuberculosis
    • Gupta K, Kumar P, Chatterji D. 2010. Identification, activity and disulfide connectivity of c-di-GMP regulating proteins in Mycobacterium tuberculosis. PLoS One 5:e15072.
    • (2010) PLoS One , vol.5
    • Gupta, K.1    Kumar, P.2    Chatterji, D.3
  • 21
    • 78649368524 scopus 로고    scopus 로고
    • Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth
    • den Hengst CD, Tran NT, Bibb MJ, Chandra G, Leskiw BK, Buttner MJ. 2010. Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth. Mol. Microbiol. 78:361-379.
    • (2010) Mol. Microbiol. , vol.78 , pp. 361-379
    • Den Hengst, C.D.1    Tran, N.T.2    Bibb, M.J.3    Chandra, G.4    Leskiw, B.K.5    Buttner, M.J.6
  • 22
    • 79958062471 scopus 로고    scopus 로고
    • Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor
    • Tran NT, Den Hengst CD, Gomez-Escribano JP, Buttner MJ. 2011. Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor. J. Bacteriol. 193:3100-3108.
    • (2011) J. Bacteriol. , vol.193 , pp. 3100-3108
    • Tran, N.T.1    Den Hengst, C.D.2    Gomez-Escribano, J.P.3    Buttner, M.J.4
  • 23
    • 84866330705 scopus 로고    scopus 로고
    • Cyclic di-GMP phosphodiesterases RmdA and RmdB are involved in regulating colony morphology and development in Streptomyces coelicolor
    • Hull TD, Ryu MH, Sullivan MJ, Johnson RC, Klena NT, Geiger RM, Gomelsky M, Bennett JA. 2012. Cyclic di-GMP phosphodiesterases RmdA and RmdB are involved in regulating colony morphology and development in Streptomyces coelicolor. J. Bacteriol. 194:4642-4651.
    • (2012) J. Bacteriol. , vol.194 , pp. 4642-4651
    • Hull, T.D.1    Ryu, M.H.2    Sullivan, M.J.3    Johnson, R.C.4    Klena, N.T.5    Geiger, R.M.6    Gomelsky, M.7    Bennett, J.A.8
  • 24
    • 79953733174 scopus 로고    scopus 로고
    • c-di-GMP turnover in Clostridium difficile is controlled by a plethora of diguanylate cyclases and phosphodiesterases
    • Bordeleau E, Fortier LC, Malouin F, Burrus V. 2011. c-di-GMP turnover in Clostridium difficile is controlled by a plethora of diguanylate cyclases and phosphodiesterases. PLoS Genet. 7:e1002039.
    • (2011) PLoS Genet , vol.7
    • Bordeleau, E.1    Fortier, L.C.2    Malouin, F.3    Burrus, V.4
  • 25
    • 84864023989 scopus 로고    scopus 로고
    • Cyclic diguanylate inversely regulates motility and aggregation in Clostridium difficile
    • Purcell EB, McKee RW, McBride SM, Waters CM, Tamayo R. 2012. Cyclic diguanylate inversely regulates motility and aggregation in Clostridium difficile. J. Bacteriol. 194:3307-3316.
    • (2012) J. Bacteriol. , vol.194 , pp. 3307-3316
    • Purcell, E.B.1    McKee, R.W.2    McBride, S.M.3    Waters, C.M.4    Tamayo, R.5
  • 26
    • 84866397780 scopus 로고    scopus 로고
    • Evidence for cyclic di-GMPmediated signaling in Bacillus subtilis
    • Chen Y, Chai Y, Guo JH, Losick R. 2012. Evidence for cyclic di-GMPmediated signaling in Bacillus subtilis. J. Bacteriol. 194:5080-5090.
    • (2012) J. Bacteriol. , vol.194 , pp. 5080-5090
    • Chen, Y.1    Chai, Y.2    Guo, J.H.3    Losick, R.4
  • 27
    • 77952580705 scopus 로고    scopus 로고
    • A liquid chromatography- coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate
    • Spangler C, Bohm A, Jenal U, Seifert R, Kaever V. 2010. A liquid chromatography- coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate. J. Microbiol. Methods 81:226-231.
    • (2010) J. Microbiol. Methods , vol.81 , pp. 226-231
    • Spangler, C.1    Bohm, A.2    Jenal, U.3    Seifert, R.4    Kaever, V.5
  • 28
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to the cell poles
    • Ben-Yehuda S, Rudner DZ, Losick R. 2003. RacA, a bacterial protein that anchors chromosomes to the cell poles. Science 299:532-536.
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 29
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtilis
    • Guerout-Fleury AM, Frandsen N, Stragier P. 1996. Plasmids for ectopic integration in Bacillus subtilis. Gene 180:57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guerout-Fleury, A.M.1    Frandsen, N.2    Stragier, P.3
  • 30
    • 55349109965 scopus 로고    scopus 로고
    • MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis
    • Patrick JE, Kearns DB. 2008. MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis. Mol. Microbiol. 70:1166-1179.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1166-1179
    • Patrick, J.E.1    Kearns, D.B.2
  • 32
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S
    • Wach A. 1996. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12:259-265.
    • (1996) cerevisiae. Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 34
    • 0016352815 scopus 로고
    • Transduction in Bacillus subtilis by bacteriophage SPP1
    • Yasbin RE, Young FE. 1974. Transduction in Bacillus subtilis by bacteriophage SPP1. J. Virol. 14:1343-1348.
    • (1974) J. Virol. , vol.14 , pp. 1343-1348
    • Yasbin, R.E.1    Young, F.E.2
  • 36
    • 69949095254 scopus 로고    scopus 로고
    • Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity
    • Chen R, Guttenplan SB, Blair KM, Kearns DB. 2009. Role of the sigmaD-dependent autolysins in Bacillus subtilis population heterogeneity. J. Bacteriol. 191:5775-5784.
    • (2009) J. Bacteriol. , vol.191 , pp. 5775-5784
    • Chen, R.1    Guttenplan, S.B.2    Blair, K.M.3    Kearns, D.B.4
  • 37
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield P, Garrard S, Derewenda Z. 1999. Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr. Purif. 15:34-39.
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 38
    • 0041664046 scopus 로고    scopus 로고
    • Swarming motility in undomesticated Bacillus subtilis
    • Kearns DB, Losick R. 2003. Swarming motility in undomesticated Bacillus subtilis. Mol. Microbiol. 49:581-590.
    • (2003) Mol. Microbiol. , vol.49 , pp. 581-590
    • Kearns, D.B.1    Losick, R.2
  • 39
    • 73649086209 scopus 로고    scopus 로고
    • YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity
    • Rao F, See RY, Zhang D, Toh DC, Ji Q, Liang ZX. 2010. YybT is a signaling protein that contains a cyclic dinucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity. J. Biol. Chem. 285:473-482.
    • (2010) J. Biol. Chem. , vol.285 , pp. 473-482
    • Rao, F.1    See, R.Y.2    Zhang, D.3    Toh, D.C.4    Ji, Q.5    Liang, Z.X.6
  • 40
    • 79952812426 scopus 로고    scopus 로고
    • Unusual heme-binding PAS domain from YybT family proteins
    • Rao F, Ji Q, Soehano I, Liang ZX. 2011. Unusual heme-binding PAS domain from YybT family proteins. J. Bacteriol. 193:1543-1551.
    • (2011) J. Bacteriol. , vol.193 , pp. 1543-1551
    • Rao, F.1    Ji, Q.2    Soehano, I.3    Liang, Z.X.4
  • 42
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
    • Ryjenkov DA, Tarutina M, Moskvin OV, Gomelsky M. 2005. Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187:1792-1798.
    • (2005) J. Bacteriol. , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 44
    • 40849096004 scopus 로고    scopus 로고
    • The GAF domain of the cGMP-binding, cGMP-specific phosphodiesterase (PDE5) is a sensor and a sink for cGMP
    • Biswas KH, Sopory S, Visweswariah SS. 2008. The GAF domain of the cGMP-binding, cGMP-specific phosphodiesterase (PDE5) is a sensor and a sink for cGMP. Biochemistry 47:3534-3543.
    • (2008) Biochemistry , vol.47 , pp. 3534-3543
    • Biswas, K.H.1    Sopory, S.2    Visweswariah, S.S.3
  • 45
    • 0037174858 scopus 로고    scopus 로고
    • Binding of cGMP to GAF domains in amphibian rod photoreceptor cGMP phosphodiesterase (PDE). Identification of GAF domains in PDE alphabeta subunits and distinct domains in the PDE gamma subunit involved in stimulation of cGMP binding to GAF domains
    • Yamazaki M, Li N, Bondarenko VA, Yamazaki RK, Baehr W, Yamazaki A.Binding of cGMP to GAF domains in amphibian rod photoreceptor cGMP phosphodiesterase (PDE). Identification of GAF domains in PDE alphabeta subunits and distinct domains in the PDE gamma subunit involved in stimulation of cGMP binding to GAF domains. J. Biol. Chem. 277:40675- 40686.
    • J. Biol. Chem , vol.277 , pp. 40675-40686
    • Yamazaki, M.1    Li, N.2    Bondarenko, V.A.3    Yamazaki, R.K.4    Baehr, W.5    Yamazaki, A.6
  • 46
    • 33646379135 scopus 로고    scopus 로고
    • cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11
    • Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE. 2006. cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J. Biol. Chem. 281:2841-2846.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2841-2846
    • Gross-Langenhoff, M.1    Hofbauer, K.2    Weber, J.3    Schultz, A.4    Schultz, J.E.5
  • 47
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 48
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • Delgado-Nixon VM, Gonzalez G, Gilles-Gonzalez MA. 2000. Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39:2685-2691.
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 49
    • 67649586805 scopus 로고    scopus 로고
    • Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis
    • Cho HY, Cho HJ, Kim YM, Oh JI, Kang BS. 2009. Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis. J. Biol. Chem. 284:13057-13067.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13057-13067
    • Cho, H.Y.1    Cho, H.J.2    Kim, Y.M.3    Oh, J.I.4    Kang, B.S.5
  • 50
    • 70350501347 scopus 로고    scopus 로고
    • A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum
    • Qi Y, Rao F, Luo Z, Liang ZX. 2009. A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum. Biochemistry 48:10275-10285.
    • (2009) Biochemistry , vol.48 , pp. 10275-10285
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.X.4
  • 51
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • Henry JT, Crosson S. 2011. Ligand-binding PAS domains in a genomic, cellular, and structural context. Annu. Rev. Microbiol. 65:261-286.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 52
    • 84857032024 scopus 로고    scopus 로고
    • The sensor region of the ubiquitous cytosolic sensor kinase, PdtaS, contains PAS and GAF domain sensing modules
    • Preu J, Panjikar S, Morth P, Jaiswal R, Karunakar P, Tucker PA. 2012. The sensor region of the ubiquitous cytosolic sensor kinase, PdtaS, contains PAS and GAF domain sensing modules. J. Struct. Biol. 177:498-505.
    • (2012) J. Struct. Biol. , vol.177 , pp. 498-505
    • Preu, J.1    Panjikar, S.2    Morth, P.3    Jaiswal, R.4    Karunakar, P.5    Tucker, P.A.6
  • 53
    • 47049115663 scopus 로고    scopus 로고
    • Catalytic mechanism of cyclic di- GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa
    • Rao F, Yang Y, Qi Y, Liang ZX. 2008. Catalytic mechanism of cyclic di- GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa. J. Bacteriol. 190:3622-3631.
    • (2008) J. Bacteriol. , vol.190 , pp. 3622-3631
    • Rao, F.1    Yang, Y.2    Qi, Y.3    Liang, Z.X.4
  • 56
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam D, Galperin MY. 2006. PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22:3-6.
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 57
    • 33750044865 scopus 로고    scopus 로고
    • The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria
    • Ryjenkov DA, Simm R, Romling U, Gomelsky M. 2006. The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria. J. Biol. Chem. 281:30310-30314.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Romling, U.3    Gomelsky, M.4
  • 58
    • 77950370030 scopus 로고    scopus 로고
    • The c-di- GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism
    • Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM. 2010. The c-di- GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol. Cell 38:128-139.
    • (2010) Mol. Cell , vol.38 , pp. 128-139
    • Paul, K.1    Nieto, V.2    Carlquist, W.C.3    Blair, D.F.4    Harshey, R.M.5
  • 59
    • 77952813357 scopus 로고    scopus 로고
    • A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility
    • Fang X, Gomelsky M. 2010. A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility. Mol. Microbiol. 76:1295-1305.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1295-1305
    • Fang, X.1    Gomelsky, M.2
  • 61
    • 46949102189 scopus 로고    scopus 로고
    • Cyclic-di-GMP regulates extracellular polysaccharide production, biofilm formation, and rugose colony development by Vibrio vulnificus
    • Nakhamchik A, Wilde C, Rowe-Magnus DA. 2008. Cyclic-di-GMP regulates extracellular polysaccharide production, biofilm formation, and rugose colony development by Vibrio vulnificus. Appl. Environ. Microbiol. 74:4199-4209.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 4199-4209
    • Nakhamchik, A.1    Wilde, C.2    Rowe-Magnus, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.