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Volumn 195, Issue 17, 2013, Pages 3897-3905

Inactivation of cyclic di-GMP binding protein TDE0214 affects the motility, biofilm formation, and virulence of Treponema denticola

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; BIS (3',5') CYCLIC DIMERIC GMP; CYCLIC GMP; TDE0214 PROTEIN; UNCLASSIFIED DRUG;

EID: 84883509129     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00610-13     Document Type: Article
Times cited : (35)

References (78)
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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
  • 5
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U. 2004. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 18:715-727.
    • (2004) Genes Dev. , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 6
    • 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
  • 7
    • 21844451590 scopus 로고    scopus 로고
    • The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains
    • Schmidt AJ, Ryjenkov DA, Gomelsky M. 2005. The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains. J. Bacteriol. 187:4774-4781.
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, A.J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 12
    • 34247213819 scopus 로고    scopus 로고
    • DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus
    • Christen M, Christen B, Allan MG, Folcher M, Jeno P, Grzesiek S, Jenal U. 2007. DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus. Proc. Natl. Acad. Sci. U. S. A. 104:4112-4117.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 4112-4117
    • Christen, M.1    Christen, B.2    Allan, M.G.3    Folcher, M.4    Jeno, P.5    Grzesiek, S.6    Jenal, U.7
  • 13
    • 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
  • 14
    • 79952260048 scopus 로고    scopus 로고
    • Structural basis for c-di-GMPmediated inside-out signaling controlling periplasmic proteolysis
    • doi:10.1371/journal.pbio.1000588
    • Navarro MV, Newell PD, Krasteva PV, Chatterjee D, Madden DR, O'Toole GA, Sondermann H. 2011. Structural basis for c-di-GMPmediated inside-out signaling controlling periplasmic proteolysis. PLoS Biol. 9:e1000588. doi:10.1371/journal.pbio.1000588.
    • (2011) PLoS Biol. , vol.9
    • Navarro, M.V.1    Newell, P.D.2    Krasteva, P.V.3    Chatterjee, D.4    Madden, D.R.5    O'Toole, G.A.6    Sondermann, H.7
  • 15
    • 38749146920 scopus 로고    scopus 로고
    • Get the message out: cyclic-di-GMP regulates multiple levels of flagellum-based motility
    • Wolfe AJ, Visick KL. 2008. Get the message out: cyclic-di-GMP regulates multiple levels of flagellum-based motility. J. Bacteriol. 190:463-475.
    • (2008) J. Bacteriol. , vol.190 , pp. 463-475
    • Wolfe, A.J.1    Visick, K.L.2
  • 16
    • 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
  • 18
    • 76349103493 scopus 로고    scopus 로고
    • Identification and molecular characterization of a cyclic-di-GMP effector protein, PlzA (BB0733): additional evidence for the existence of a functional cyclic-di-GMP regulatory network in the Lyme disease spirochete, Borrelia burgdorferi
    • Freedman JC, Rogers EA, Kostick JL, Zhang H, Iyer R, Schwartz I, Marconi RT. 2010. Identification and molecular characterization of a cyclic-di-GMP effector protein, PlzA (BB0733): additional evidence for the existence of a functional cyclic-di-GMP regulatory network in the Lyme disease spirochete, Borrelia burgdorferi. FEMS Immunol. Med. Microbiol. 58:285-294.
    • (2010) FEMS Immunol. Med. Microbiol. , vol.58 , pp. 285-294
    • Freedman, J.C.1    Rogers, E.A.2    Kostick, J.L.3    Zhang, H.4    Iyer, R.5    Schwartz, I.6    Marconi, R.T.7
  • 19
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman JW, Harwood CS. 2008. Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol. Microbiol. 69:376-389.
    • (2008) Mol. Microbiol. , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 20
    • 70350436270 scopus 로고    scopus 로고
    • Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri.
    • Leduc JL, Roberts GP. 2009. Cyclic di-GMP allosterically inhibits the CRP-like protein (Clp) of Xanthomonas axonopodis pv. citri. J. Bacteriol. 191:7121-7122.
    • (2009) J. Bacteriol. , vol.191 , pp. 7121-7122
    • Leduc, J.L.1    Roberts, G.P.2
  • 21
    • 84863692958 scopus 로고    scopus 로고
    • Cellular levels and binding of c-di-GMP control subcellular localization and activity of the Vibrio cholerae transcriptional regulator VpsT
    • doi:10.1371/journal.ppat.1002719
    • Shikuma NJ, Fong JC, Yildiz FH. 2012. Cellular levels and binding of c-di-GMP control subcellular localization and activity of the Vibrio cholerae transcriptional regulator VpsT. PLoS Pathog. 8:e1002719. doi:10.1371/journal.ppat.1002719.
    • (2012) PLoS Pathog. , vol.8
    • Shikuma, N.J.1    Fong, J.C.2    Yildiz, F.H.3
  • 22
    • 0030734277 scopus 로고    scopus 로고
    • c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum
    • Weinhouse H, Sapir S, Amikam D, Shilo Y, Volman G, Ohana P, Benziman M. 1997. c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. FEBS Lett. 416:207-211.
    • (1997) FEBS Lett. , vol.416 , pp. 207-211
    • Weinhouse, H.1    Sapir, S.2    Amikam, D.3    Shilo, Y.4    Volman, G.5    Ohana, P.6    Benziman, M.7
  • 23
    • 0030042096 scopus 로고    scopus 로고
    • Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa
    • Alm RA, Bodero AJ, Free PD, Mattick JS. 1996. Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa. J. Bacteriol. 178:46-53.
    • (1996) J. Bacteriol. , vol.178 , pp. 46-53
    • Alm, R.A.1    Bodero, A.J.2    Free, P.D.3    Mattick, J.S.4
  • 24
    • 34547682212 scopus 로고    scopus 로고
    • The second messenger bis-(3=-5=)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa
    • Merighi M, Lee VT, Hyodo M, Hayakawa Y, Lory S. 2007. The second messenger bis-(3=-5=)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa. Mol. Microbiol. 65:876-895.
    • (2007) Mol. Microbiol. , vol.65 , pp. 876-895
    • Merighi, M.1    Lee, V.T.2    Hyodo, M.3    Hayakawa, Y.4    Lory, S.5
  • 26
    • 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
  • 27
    • 34250358327 scopus 로고    scopus 로고
    • PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae
    • Pratt JT, Tamayo R, Tischler AD, Camilli A. 2007. PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae. J. Biol. Chem. 282:12860-12870.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12860-12870
    • Pratt, J.T.1    Tamayo, R.2    Tischler, A.D.3    Camilli, A.4
  • 28
    • 79959410913 scopus 로고    scopus 로고
    • Analysis of the Borrelia burgdorferi cyclic-di-GMP-binding protein PlzA reveals a role in motility and virulence
    • Pitzer JE, Sultan SZ, Hayakawa Y, Hobbs G, Miller MR, Motaleb MA. 2011. Analysis of the Borrelia burgdorferi cyclic-di-GMP-binding protein PlzA reveals a role in motility and virulence. Infect. Immun. 79:1815-1825.
    • (2011) Infect. Immun. , vol.79 , pp. 1815-1825
    • Pitzer, J.E.1    Sultan, S.Z.2    Hayakawa, Y.3    Hobbs, G.4    Miller, M.R.5    Motaleb, M.A.6
  • 30
    • 77953616099 scopus 로고    scopus 로고
    • Periodontitis: a polymicrobial disruption of host homeostasis
    • Darveau RP. 2010. Periodontitis: a polymicrobial disruption of host homeostasis. Nat. Rev. Microbiol. 8:481-490.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 481-490
    • Darveau, R.P.1
  • 31
    • 34547477793 scopus 로고    scopus 로고
    • A brief history of national surveillance efforts for periodontal disease in the United States
    • Dye BA, Thornton-Evans G. 2007. A brief history of national surveillance efforts for periodontal disease in the United States. J. Periodontol. 78:1373-1379.
    • (2007) J. Periodontol. , vol.78 , pp. 1373-1379
    • Dye, B.A.1    Thornton-Evans, G.2
  • 35
    • 20444440319 scopus 로고    scopus 로고
    • Spirochetes at the forefront of periodontal infections
    • Ellen RP, Galimanas VB. 2005. Spirochetes at the forefront of periodontal infections. Periodontol. 2000 38:13-32.
    • (2005) Periodontol. 2000 , vol.38 , pp. 13-32
    • Ellen, R.P.1    Galimanas, V.B.2
  • 36
    • 0142060303 scopus 로고    scopus 로고
    • Molecular genetic analysis of the virulence of oral bacterial pathogens: an historical perspective
    • Kuramitsu HK. 2003. Molecular genetic analysis of the virulence of oral bacterial pathogens: an historical perspective. Crit. Rev. Oral Biol. Med. 14:331-344.
    • (2003) Crit. Rev. Oral Biol. Med. , vol.14 , pp. 331-344
    • Kuramitsu, H.K.1
  • 37
    • 84864812761 scopus 로고    scopus 로고
    • Treponema denticola interactions with host proteins
    • 21 February, [Epub ahead of print.] doi:10.3402/jom.v4i0.9929
    • Fenno JC. 21 February 2012. Treponema denticola interactions with host proteins. J. Oral Microbiol. [Epub ahead of print.] doi:10.3402/jom.v4i0.9929.
    • (2012) J. Oral Microbiol.
    • Fenno, J.C.1
  • 38
    • 79952729069 scopus 로고    scopus 로고
    • New insights into the emerging role of oral spirochaetes in periodontal disease
    • Visser MB, Ellen RP. 2011. New insights into the emerging role of oral spirochaetes in periodontal disease. Clin. Microbiol. Infect. 17:502-512.
    • (2011) Clin. Microbiol. Infect. , vol.17 , pp. 502-512
    • Visser, M.B.1    Ellen, R.P.2
  • 39
    • 79952733471 scopus 로고    scopus 로고
    • Virulence factors of the oral spirochete Treponema denticola
    • Dashper SG, Seers CA, Tan KH, Reynolds EC. 2011. Virulence factors of the oral spirochete Treponema denticola. J. Dent. Res. 90:691-703.
    • (2011) J. Dent. Res. , vol.90 , pp. 691-703
    • Dashper, S.G.1    Seers, C.A.2    Tan, K.H.3    Reynolds, E.C.4
  • 41
    • 80052802800 scopus 로고    scopus 로고
    • Molecular signaling mechanisms of the periopathogen, Treponema denticola
    • Frederick JR, Sarkar J, McDowell JV, Marconi RT. 2011. Molecular signaling mechanisms of the periopathogen, Treponema denticola. J. Dent. Res. 90:1155-1163.
    • (2011) J. Dent. Res. , vol.90 , pp. 1155-1163
    • Frederick, J.R.1    Sarkar, J.2    McDowell, J.V.3    Marconi, R.T.4
  • 43
    • 79960389593 scopus 로고    scopus 로고
    • The riboswitch regulates a thiamine pyrophosphate ABC transporter of the oral spirochete Treponema denticola
    • Bian J, Shen H, Tu Y, Yu A, Li C. 2011. The riboswitch regulates a thiamine pyrophosphate ABC transporter of the oral spirochete Treponema denticola. J. Bacteriol. 193:3912-3922.
    • (2011) J. Bacteriol. , vol.193 , pp. 3912-3922
    • Bian, J.1    Shen, H.2    Tu, Y.3    Yu, A.4    Li, C.5
  • 44
    • 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
  • 45
    • 84863233728 scopus 로고    scopus 로고
    • Development of a modified gentamicin resistance cassette for genetic manipulation of the oral spirochete Treponema denticola
    • Bian J, Fenno JC, Li C. 2012. Development of a modified gentamicin resistance cassette for genetic manipulation of the oral spirochete Treponema denticola. Appl. Environ. Microbiol. 78:2059-2062.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 2059-2062
    • Bian, J.1    Fenno, J.C.2    Li, C.3
  • 46
    • 79960085695 scopus 로고    scopus 로고
    • Disruption of a type II endonuclease (TDE0911) enables Treponema denticola ATCC 35405 to accept an unmethylated shuttle vector
    • Bian J, Li C. 2011. Disruption of a type II endonuclease (TDE0911) enables Treponema denticola ATCC 35405 to accept an unmethylated shuttle vector. Appl. Environ. Microbiol. 77:4573-4578.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4573-4578
    • Bian, J.1    Li, C.2
  • 47
    • 4344600506 scopus 로고    scopus 로고
    • Genetic analysis of Treponema denticola ATCC 35405 biofilm formation
    • Vesey PM, Kuramitsu HK. 2004. Genetic analysis of Treponema denticola ATCC 35405 biofilm formation. Microbiology 150:2401-2407.
    • (2004) Microbiology , vol.150 , pp. 2401-2407
    • Vesey, P.M.1    Kuramitsu, H.K.2
  • 48
    • 28644440172 scopus 로고    scopus 로고
    • Biofilm formation by the periodontopathic bacteria Treponema denticola and Porphyromonas gingivalis
    • Kuramitsu HK, Chen W, Ikegami A. 2005. Biofilm formation by the periodontopathic bacteria Treponema denticola and Porphyromonas gingivalis. J. Periodontol. 76:2047-2051.
    • (2005) J. Periodontol. , vol.76 , pp. 2047-2051
    • Kuramitsu, H.K.1    Chen, W.2    Ikegami, A.3
  • 49
    • 0036095062 scopus 로고    scopus 로고
    • Construction and characterization of a cheA mutant of Treponema denticola
    • Lux R, Sim JH, Tsai JP, Shi W. 2002. Construction and characterization of a cheA mutant of Treponema denticola. J. Bacteriol. 184:3130-3134.
    • (2002) J. Bacteriol. , vol.184 , pp. 3130-3134
    • Lux, R.1    Sim, J.H.2    Tsai, J.P.3    Shi, W.4
  • 51
    • 33847235021 scopus 로고    scopus 로고
    • Identification of specific chemoattractants and genetic complementation of a Borrelia burgdorferi chemotaxis mutant: flow cytometry-based capillary tube chemotaxis assay
    • Bakker RG, Li C, Miller MR, Cunningham C, Charon NW. 2007. Identification of specific chemoattractants and genetic complementation of a Borrelia burgdorferi chemotaxis mutant: flow cytometry-based capillary tube chemotaxis assay. Appl. Environ. Microbiol. 73:1180-1188.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1180-1188
    • Bakker, R.G.1    Li, C.2    Miller, M.R.3    Cunningham, C.4    Charon, N.W.5
  • 52
    • 0033014008 scopus 로고    scopus 로고
    • Insertional inactivation of Treponema denticola tap1 results in a nonmotile mutant with elongated flagellar hooks
    • Limberger RJ, Slivienski LL, Izard J, Samsonoff WA. 1999. Insertional inactivation of Treponema denticola tap1 results in a nonmotile mutant with elongated flagellar hooks. J. Bacteriol. 181:3743-3750.
    • (1999) J. Bacteriol. , vol.181 , pp. 3743-3750
    • Limberger, R.J.1    Slivienski, L.L.2    Izard, J.3    Samsonoff, W.A.4
  • 55
    • 84864821396 scopus 로고    scopus 로고
    • Borrelia burgdorferi needs chemotaxis to establish infection in mammals and to accomplish its enzootic cycle
    • Sze CW, Zhang K, Kariu T, Pal U, Li C. 2012. Borrelia burgdorferi needs chemotaxis to establish infection in mammals and to accomplish its enzootic cycle. Infect. Immun. 80:2485-2492.
    • (2012) Infect. Immun. , vol.80 , pp. 2485-2492
    • Sze, C.W.1    Zhang, K.2    Kariu, T.3    Pal, U.4    Li, C.5
  • 57
    • 84873569415 scopus 로고    scopus 로고
    • Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated proteinprotein interaction
    • Steiner S, Lori C, Boehm A, Jenal U. 2013. Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated proteinprotein interaction. EMBO J. 32:354-368.
    • (2013) EMBO J. , vol.32 , pp. 354-368
    • Steiner, S.1    Lori, C.2    Boehm, A.3    Jenal, U.4
  • 58
    • 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
  • 59
    • 84864091339 scopus 로고    scopus 로고
    • A Bacillus subtilis sensor kinase involved in triggering biofilm formation on the roots of tomato plants
    • Chen Y, Cao S, Chai Y, Clardy J, Kolter R, Guo JH, Losick R. 2012. A Bacillus subtilis sensor kinase involved in triggering biofilm formation on the roots of tomato plants. Mol. Microbiol. 85:418-430.
    • (2012) Mol. Microbiol. , vol.85 , pp. 418-430
    • Chen, Y.1    Cao, S.2    Chai, Y.3    Clardy, J.4    Kolter, R.5    Guo, J.H.6    Losick, R.7
  • 60
    • 0034326854 scopus 로고    scopus 로고
    • Cache-a signaling domain common to animal Ca(2+)-channel subunits and a class of prokaryotic chemotaxis receptors
    • Anantharaman V, Aravind L. 2000. Cache-a signaling domain common to animal Ca(2+)-channel subunits and a class of prokaryotic chemotaxis receptors. Trends Biochem. Sci. 25:535-537.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 535-537
    • Anantharaman, V.1    Aravind, L.2
  • 61
    • 34548611290 scopus 로고    scopus 로고
    • PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation
    • Kim C, Cheng CY, Saldanha SA, Taylor SS. 2007. PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation. Cell 130:1032-1043.
    • (2007) Cell , vol.130 , pp. 1032-1043
    • Kim, C.1    Cheng, C.Y.2    Saldanha, S.A.3    Taylor, S.S.4
  • 63
    • 69249241732 scopus 로고    scopus 로고
    • Structural overview on the allosteric activation of cyclic AMP receptor protein
    • Won HS, Lee YS, Lee SH, Lee BJ. 2009. Structural overview on the allosteric activation of cyclic AMP receptor protein. Biochim. Biophys. Acta 1794:1299-1308.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1299-1308
    • Won, H.S.1    Lee, Y.S.2    Lee, S.H.3    Lee, B.J.4
  • 64
    • 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
  • 65
    • 84871784503 scopus 로고    scopus 로고
    • Structural mechanism of GAF-regulated sigma(54) activators from Aquifex aeolicus
    • Batchelor JD, Lee PS, Wang AC, Doucleff M, Wemmer DE. 2013. Structural mechanism of GAF-regulated sigma(54) activators from Aquifex aeolicus. J. Mol. Biol. 425:156-170.
    • (2013) J. Mol. Biol. , vol.425 , pp. 156-170
    • Batchelor, J.D.1    Lee, P.S.2    Wang, A.C.3    Doucleff, M.4    Wemmer, D.E.5
  • 68
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox
    • Zhulin IB, Taylor BL, Dixon R. 1997. PAS domain S-boxes in archaea, bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22:331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3
  • 69
    • 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
  • 70
    • 0034721950 scopus 로고    scopus 로고
    • Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli
    • Ko M, Park C. 2000. Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli. J. Mol. Biol. 303:371-382.
    • (2000) J. Mol. Biol. , vol.303 , pp. 371-382
    • Ko, M.1    Park, C.2
  • 71
    • 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
  • 73
    • 79959551165 scopus 로고    scopus 로고
    • The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes
    • Kostick JL, Szkotnicki LT, Rogers EA, Bocci P, Raffaelli N, Marconi RT. 2011. The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes. Mol. Microbiol. 81:219-231.
    • (2011) Mol. Microbiol. , vol.81 , pp. 219-231
    • Kostick, J.L.1    Szkotnicki, L.T.2    Rogers, E.A.3    Bocci, P.4    Raffaelli, N.5    Marconi, R.T.6
  • 74
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: a common cause of persistent infections
    • Costerton JW, Stewart PS, Greenberg EP. 1999. Bacterial biofilms: a common cause of persistent infections. Science 284:1318-1322.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 75
    • 0031724115 scopus 로고    scopus 로고
    • Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development
    • O'Toole GA, Kolter R. 1998. Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Mol. Microbiol. 30:295-304.
    • (1998) Mol. Microbiol. , vol.30 , pp. 295-304
    • O'Toole, G.A.1    Kolter, R.2
  • 76
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: roles of flagella, motility, chemotaxis and type I pili
    • Pratt LA, Kolter R. 1998. Genetic analysis of Escherichia coli biofilm formation: roles of flagella, motility, chemotaxis and type I pili. Mol. Microbiol. 30:285-293.
    • (1998) Mol. Microbiol. , vol.30 , pp. 285-293
    • Pratt, L.A.1    Kolter, R.2
  • 77
    • 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
  • 78
    • 0034819849 scopus 로고    scopus 로고
    • Motility and chemotaxis in tissue penetration of oral epithelial cell layers by Treponema denticola
    • Lux R, Miller JN, Park NH, Shi W. 2001. Motility and chemotaxis in tissue penetration of oral epithelial cell layers by Treponema denticola. Infect. Immun. 69:6276-6283.
    • (2001) Infect. Immun. , vol.69 , pp. 6276-6283
    • Lux, R.1    Miller, J.N.2    Park, N.H.3    Shi, W.4


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