메뉴 건너뛰기




Volumn 86, Issue 6, 2012, Pages 1424-1440

The response threshold of Salmonella PilZ domain proteins is determined by their binding affinities for c-di-GMP

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BCSA PROTEIN; CELLULOSE; CYCLIC GMP; FUNGAL ENZYME; PILZ DOMAIN PROTEIN; UNCLASSIFIED DRUG; YCGR PROTEIN; YHJH ENZYME;

EID: 84870985711     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12066     Document Type: Article
Times cited : (79)

References (67)
  • 1
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam, D., and Galperin, M.Y. (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
  • 3
    • 0019308328 scopus 로고
    • Positive selection for loss of tetracycline resistance
    • Bochner, B.R., Huang, H.C., Schieven, G.L., and Ames, B.N. (1980) Positive selection for loss of tetracycline resistance. J Bacteriol 143: 926-933.
    • (1980) J Bacteriol , vol.143 , pp. 926-933
    • Bochner, B.R.1    Huang, H.C.2    Schieven, G.L.3    Ames, B.N.4
  • 4
    • 77950928649 scopus 로고    scopus 로고
    • Second messenger-mediated adjustment of bacterial swimming velocity
    • Boehm, A., Kaiser, M., Li, H., Spangler, C., Kasper, C.A., Ackermann, M., etal. (2010) Second messenger-mediated adjustment of bacterial swimming velocity. Cell 141: 107-116.
    • (2010) Cell , vol.141 , pp. 107-116
    • Boehm, A.1    Kaiser, M.2    Li, H.3    Spangler, C.4    Kasper, C.A.5    Ackermann, M.6
  • 6
    • 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, M.G., Folcher, M., Jeno, P., Grzesiek, S., and 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 USA 104: 4112-4117.
    • (2007) Proc Natl Acad Sci USA , 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
  • 7
    • 77953244382 scopus 로고    scopus 로고
    • Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division
    • Christen, M., Kulasekara, H.D., Christen, B., Kulasekara, B.R., Hoffman, L.R., and Miller, S.I. (2010) Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division. Science 328: 1295-1297.
    • (2010) Science , vol.328 , pp. 1295-1297
    • Christen, M.1    Kulasekara, H.D.2    Christen, B.3    Kulasekara, B.R.4    Hoffman, L.R.5    Miller, S.I.6
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig, A., Abel, S., Folcher, M., Nicollier, M., Schwede, T., Amiot, N., etal. (2009) Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 23: 93-104.
    • (2009) Genes Dev , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6
  • 10
    • 84856405959 scopus 로고    scopus 로고
    • A chemical proteomics approach to identify c-di-GMP binding proteins in Pseudomonas aeruginosa
    • Duvel, J., Bertinetti, D., Moller, S., Schwede, F., Morr, M., Wissing, J., etal. (2012) A chemical proteomics approach to identify c-di-GMP binding proteins in Pseudomonas aeruginosa. J Microbiol Methods 88: 229-236.
    • (2012) J Microbiol Methods , vol.88 , pp. 229-236
    • Duvel, J.1    Bertinetti, D.2    Moller, S.3    Schwede, F.4    Morr, M.5    Wissing, J.6
  • 11
    • 77952813357 scopus 로고    scopus 로고
    • A post-translational, c-di-GMP-dependent mechanism regulating flagellar motility
    • Fang, X., and 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
  • 12
    • 0021866912 scopus 로고
    • Omega mutagenesis in gram-negative bacteria: a selectable interposon which is strongly polar in a wide range of bacterial species
    • Frey, J., and Krisch, H.M. (1985) Omega mutagenesis in gram-negative bacteria: a selectable interposon which is strongly polar in a wide range of bacterial species. Gene 36: 143-150.
    • (1985) Gene , vol.36 , pp. 143-150
    • Frey, J.1    Krisch, H.M.2
  • 14
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Furste, J.P., Pansegrau, W., Frank, R., Blocker, H., Scholz, P., Bagdasarian, M., and Lanka, E. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48: 119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Furste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 15
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin, M.Y., Nikolskaya, A.N., and Koonin, E.V. (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
  • 16
    • 4744349524 scopus 로고    scopus 로고
    • Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
    • Garcia, B., Latasa, C., Solano, C., Garcia-del Portillo, F., Gamazo, C., and Lasa, I. (2004) Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation. Mol Microbiol 54: 264-277.
    • (2004) Mol Microbiol , vol.54 , pp. 264-277
    • Garcia, B.1    Latasa, C.2    Solano, C.3    Garcia-del Portillo, F.4    Gamazo, C.5    Lasa, I.6
  • 17
    • 51149124278 scopus 로고    scopus 로고
    • Cellulose modulates biofilm formation by counteracting curli-mediated colonization of solid surfaces in Escherichia coli
    • Gualdi, L., Tagliabue, L., Bertagnoli, S., Ierano, T., De, C., and Landini, P. (2008) Cellulose modulates biofilm formation by counteracting curli-mediated colonization of solid surfaces in Escherichia coli. Microbiology 154: 2017-2024.
    • (2008) Microbiology , vol.154 , pp. 2017-2024
    • Gualdi, L.1    Tagliabue, L.2    Bertagnoli, S.3    Ierano, T.4    De, C.5    Landini, P.6
  • 18
    • 36549080792 scopus 로고    scopus 로고
    • Subcellular location characteristics of the Pseudomonas aeruginosa GGDEF protein, WspR, indicate that it produces cyclic-di-GMP in response to growth on surfaces
    • Guvener, Z.T., and Harwood, C.S. (2007) Subcellular location characteristics of the Pseudomonas aeruginosa GGDEF protein, WspR, indicate that it produces cyclic-di-GMP in response to growth on surfaces. Mol Microbiol 66: 1459-1473.
    • (2007) Mol Microbiol , vol.66 , pp. 1459-1473
    • Guvener, Z.T.1    Harwood, C.S.2
  • 19
    • 84855362209 scopus 로고    scopus 로고
    • 2-Heptyl-4-quinolone, a precursor of the Pseudomonas quinolone signal molecule, modulates swarming motility in Pseudomonas aeruginosa
    • Ha, D.G., Merritt, J.H., Hampton, T.H., Hodgkinson, J.T., Janecek, M., Spring, D.R., etal. (2011) 2-Heptyl-4-quinolone, a precursor of the Pseudomonas quinolone signal molecule, modulates swarming motility in Pseudomonas aeruginosa. J Bacteriol 193: 6770-6780.
    • (2011) J Bacteriol , vol.193 , pp. 6770-6780
    • Ha, D.G.1    Merritt, J.H.2    Hampton, T.H.3    Hodgkinson, J.T.4    Janecek, M.5    Spring, D.R.6
  • 20
    • 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
  • 21
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman, J.W., and Harwood, C.S. (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
  • 24
    • 33645819810 scopus 로고    scopus 로고
    • Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium
    • Kader, A., Simm, R., Gerstel, U., Morr, M., and Romling, U. (2006) Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium. Mol Microbiol 60: 602-616.
    • (2006) Mol Microbiol , vol.60 , pp. 602-616
    • Kader, A.1    Simm, R.2    Gerstel, U.3    Morr, M.4    Romling, U.5
  • 25
    • 77950859347 scopus 로고    scopus 로고
    • Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins
    • Ko, J., Ryu, K.S., Kim, H., Shin, J.S., Lee, J.O., Cheong, C., and Choi, B.S. (2010) Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins. J Mol Biol 398: 97-110.
    • (2010) J Mol Biol , vol.398 , pp. 97-110
    • Ko, J.1    Ryu, K.S.2    Kim, H.3    Shin, J.S.4    Lee, J.O.5    Cheong, C.6    Choi, B.S.7
  • 26
    • 0034721950 scopus 로고    scopus 로고
    • Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli
    • Ko, M., and 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
  • 27
    • 76749083886 scopus 로고    scopus 로고
    • Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP
    • Krasteva, P.V., Fong, J.C., Shikuma, N.J., Beyhan, S., Navarro, M.V., Yildiz, F.H., and Sondermann, H. (2010) Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science 327: 866-868.
    • (2010) Science , vol.327 , pp. 866-868
    • Krasteva, P.V.1    Fong, J.C.2    Shikuma, N.J.3    Beyhan, S.4    Navarro, M.V.5    Yildiz, F.H.6    Sondermann, H.7
  • 28
    • 33644516891 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence
    • Kulasakara, H., Lee, V., Brencic, A., Liberati, N., Urbach, J., Miyata, S., etal. (2006) Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence. Proc Natl Acad Sci USA 103: 2839-2844.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2839-2844
    • Kulasakara, H.1    Lee, V.2    Brencic, A.3    Liberati, N.4    Urbach, J.5    Miyata, S.6
  • 29
    • 77950405367 scopus 로고    scopus 로고
    • YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa
    • Malone, J.G., Jaeger, T., Spangler, C., Ritz, D., Spang, A., Arrieumerlou, C., etal. (2010) YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa. PLoS Pathog 6: e1000804.
    • (2010) PLoS Pathog , vol.6
    • Malone, J.G.1    Jaeger, T.2    Spangler, C.3    Ritz, D.4    Spang, A.5    Arrieumerlou, C.6
  • 31
    • 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, V.T., Hyodo, M., Hayakawa, Y., and 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
  • 32
    • 79952168685 scopus 로고    scopus 로고
    • Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases
    • Merritt, J.H., Ha, D.G., Cowles, K.N., Lu, W., Morales, D.K., Rabinowitz, J., etal. (2010) Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases. mBio 1: 00183-10.
    • (2010) mBio , vol.1 , pp. 00183-00110
    • Merritt, J.H.1    Ha, D.G.2    Cowles, K.N.3    Lu, W.4    Morales, D.K.5    Rabinowitz, J.6
  • 33
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: mechanisms of signalling
    • Mills, E., Pultz, I.S., Kulasekara, H.D., and Miller, S.I. (2011) The bacterial second messenger c-di-GMP: mechanisms of signalling. Cell Microbiol 13: 1122-1129.
    • (2011) Cell Microbiol , vol.13 , pp. 1122-1129
    • Mills, E.1    Pultz, I.S.2    Kulasekara, H.D.3    Miller, S.I.4
  • 35
    • 68149172669 scopus 로고    scopus 로고
    • Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX
    • Navarro, M.V., De, N., Bae, N., Wang, Q., and Sondermann, H. (2009) Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure 17: 1104-1116.
    • (2009) Structure , vol.17 , pp. 1104-1116
    • Navarro, M.V.1    De, N.2    Bae, N.3    Wang, Q.4    Sondermann, H.5
  • 36
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A.W., and Daugherty, P.S. (2005) Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat Biotechnol 23: 355-360.
    • (2005) Nat Biotechnol , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 37
    • 31344471740 scopus 로고    scopus 로고
    • Fluorescent sensors for rapid monitoring of intracellular cGMP
    • Nikolaev, V.O., Gambaryan, S., and Lohse, M.J. (2006) Fluorescent sensors for rapid monitoring of intracellular cGMP. Nat Methods 3: 23-25.
    • (2006) Nat Methods , vol.3 , pp. 23-25
    • Nikolaev, V.O.1    Gambaryan, S.2    Lohse, M.J.3
  • 38
    • 79956134862 scopus 로고    scopus 로고
    • Role of the biofilm master regulator CsgD in cross-regulation between biofilm formation and flagellar synthesis
    • Ogasawara, H., Yamamoto, K., and Ishihama, A. (2011) Role of the biofilm master regulator CsgD in cross-regulation between biofilm formation and flagellar synthesis. J Bacteriol 193: 2587-2597.
    • (2011) J Bacteriol , vol.193 , pp. 2587-2597
    • Ogasawara, H.1    Yamamoto, K.2    Ishihama, A.3
  • 39
    • 34250885891 scopus 로고    scopus 로고
    • An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins
    • Ohashi, T., Galiacy, S.D., Briscoe, G., and Erickson, H. (2007) An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins. Protein Sci 16: 1429-1438.
    • (2007) Protein Sci , vol.16 , pp. 1429-1438
    • Ohashi, T.1    Galiacy, S.D.2    Briscoe, G.3    Erickson, H.4
  • 40
    • 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, W.C., Blair, D.F., and Harshey, R.M. (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
  • 41
    • 51149098349 scopus 로고    scopus 로고
    • Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli
    • Pesavento, C., Becker, G., Sommerfeldt, N., Possling, A., Tschowri, N., Mehlis, A., and Hengge, R. (2008) Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli. Genes Dev 22: 2434-2446.
    • (2008) Genes Dev , vol.22 , pp. 2434-2446
    • Pesavento, C.1    Becker, G.2    Sommerfeldt, N.3    Possling, A.4    Tschowri, N.5    Mehlis, A.6    Hengge, R.7
  • 42
    • 34250358327 scopus 로고    scopus 로고
    • PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae
    • Pratt, J.T., Tamayo, R., Tischler, A.D., and 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
  • 43
    • 33846006935 scopus 로고    scopus 로고
    • NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein
    • Ramelot, T.A., Yee, A., Cort, J.R., Semesi, A., Arrowsmith, C.H., and Kennedy, M.A. (2007) NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Proteins 66: 266-271.
    • (2007) Proteins , vol.66 , pp. 266-271
    • Ramelot, T.A.1    Yee, A.2    Cort, J.R.3    Semesi, A.4    Arrowsmith, C.H.5    Kennedy, M.A.6
  • 45
    • 21144439731 scopus 로고    scopus 로고
    • Characterization of the rdar morphotype, a multicellular behaviour in Enterobacteriaceae
    • Romling, U. (2005) Characterization of the rdar morphotype, a multicellular behaviour in Enterobacteriaceae. Cell Mol Life Sci 62: 1234-1246.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1234-1246
    • Romling, U.1
  • 46
    • 0031932327 scopus 로고    scopus 로고
    • Curli fibers are highly conserved between Salmonella Typhimurium and Escherichia coli with respect to operon structure and regulation
    • Romling, U., Bian, Z., Hammar, M., Sierralta, W.D., and Normark, S. (1998a) Curli fibers are highly conserved between Salmonella Typhimurium and Escherichia coli with respect to operon structure and regulation. J Bacteriol 180: 722-731.
    • (1998) J Bacteriol , vol.180 , pp. 722-731
    • Romling, U.1    Bian, Z.2    Hammar, M.3    Sierralta, W.D.4    Normark, S.5
  • 47
    • 0031896213 scopus 로고    scopus 로고
    • Multicellular and aggregative behaviour of Salmonella Typhimurium strains is controlled by mutations in the agfD promoter
    • Romling, U., Sierralta, W.D., Eriksson, K., and Normark, S. (1998b) Multicellular and aggregative behaviour of Salmonella Typhimurium strains is controlled by mutations in the agfD promoter. Mol Microbiol 28: 249-264.
    • (1998) Mol Microbiol , vol.28 , pp. 249-264
    • Romling, U.1    Sierralta, W.D.2    Eriksson, K.3    Normark, S.4
  • 48
    • 0034128490 scopus 로고    scopus 로고
    • AgfD, the checkpoint of multicellular and aggregative behaviour in Salmonella Typhimurium regulates at least two independent pathways
    • Romling, U., Rohde, M., Olsen, A., Normark, S., and Reinkoster, J. (2000) AgfD, the checkpoint of multicellular and aggregative behaviour in Salmonella Typhimurium regulates at least two independent pathways. Mol Microbiol 36: 10-23.
    • (2000) Mol Microbiol , vol.36 , pp. 10-23
    • Romling, U.1    Rohde, M.2    Olsen, A.3    Normark, S.4    Reinkoster, J.5
  • 49
    • 84864003643 scopus 로고    scopus 로고
    • The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion
    • Roy, A.B., Petrova, O.E., and Sauer, K. (2012) The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion. J Bacteriol 194: 2904-2915.
    • (2012) J Bacteriol , vol.194 , pp. 2904-2915
    • Roy, A.B.1    Petrova, O.E.2    Sauer, K.3
  • 50
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy, R., Hohng, S., and Ha, T. (2008) A practical guide to single-molecule FRET. Nat Methods 5: 507-516.
    • (2008) Nat Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 51
    • 35148812231 scopus 로고    scopus 로고
    • Design of fluorescence resonance energy transfer (FRET)-based cGMP indicators: a systematic approach
    • Russwurm, M., Mullershausen, F., Friebe, A., Jager, R., Russwurm, C., and Koesling, D. (2007) Design of fluorescence resonance energy transfer (FRET)-based cGMP indicators: a systematic approach. Biochem J 407: 69-77.
    • (2007) Biochem J , vol.407 , pp. 69-77
    • Russwurm, M.1    Mullershausen, F.2    Friebe, A.3    Jager, R.4    Russwurm, C.5    Koesling, D.6
  • 52
    • 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, D.A., Simm, R., Romling, U., and 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
  • 53
    • 79954699584 scopus 로고    scopus 로고
    • GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and swimming motility in Escherichia coli
    • Sanchez-Torres, V., Hu, H., and Wood, T.K. (2011) GGDEF proteins YeaI, YedQ, and YfiN reduce early biofilm formation and swimming motility in Escherichia coli. Appl Microbiol Biotechnol 90: 651-658.
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 651-658
    • Sanchez-Torres, V.1    Hu, H.2    Wood, T.K.3
  • 54
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer, T., and 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
  • 55
    • 79251540863 scopus 로고    scopus 로고
    • Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate
    • Shin, J.S., Ryu, K.S., Ko, J., Lee, A., and Choi, B.S. (2011) Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate. Protein Sci 20: 270-277.
    • (2011) Protein Sci , vol.20 , pp. 270-277
    • Shin, J.S.1    Ryu, K.S.2    Ko, J.3    Lee, A.4    Choi, B.S.5
  • 56
    • 34247566143 scopus 로고    scopus 로고
    • Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium
    • Simm, R., Lusch, A., Kader, A., Andersson, M., and Romling, U. (2007) Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium. J Bacteriol 189: 3613-3623.
    • (2007) J Bacteriol , vol.189 , pp. 3613-3623
    • Simm, R.1    Lusch, A.2    Kader, A.3    Andersson, M.4    Romling, U.5
  • 57
    • 0036270804 scopus 로고    scopus 로고
    • Genetic analysis of Salmonella enteritidis biofilm formation: critical role of cellulose
    • Solano, C., Garcia, B., Valle, J., Berasain, C., Ghigo, J.M., Gamazo, C., and Lasa, I. (2002) Genetic analysis of Salmonella enteritidis biofilm formation: critical role of cellulose. Mol Microbiol 43: 793-808.
    • (2002) Mol Microbiol , vol.43 , pp. 793-808
    • Solano, C.1    Garcia, B.2    Valle, J.3    Berasain, C.4    Ghigo, J.M.5    Gamazo, C.6    Lasa, I.7
  • 58
    • 66049142620 scopus 로고    scopus 로고
    • Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonella
    • Solano, C., Garcia, B., Latasa, C., Toledo-Arana, A., Zorraquino, V., Valle, J., etal. (2009) Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonella. Proc Natl Acad Sci USA 106: 7997-8002.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7997-8002
    • Solano, C.1    Garcia, B.2    Latasa, C.3    Toledo-Arana, A.4    Zorraquino, V.5    Valle, J.6
  • 59
    • 80655125443 scopus 로고    scopus 로고
    • Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae
    • Srivastava, D., Harris, R.C., and Waters, C.M. (2011) Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae. J Bacteriol 193: 6331-6341.
    • (2011) J Bacteriol , vol.193 , pp. 6331-6341
    • Srivastava, D.1    Harris, R.C.2    Waters, C.M.3
  • 61
    • 0034094370 scopus 로고    scopus 로고
    • Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer
    • Vanderklish, P.W., Krushel, L.A., Holst, B.H., Gally, J.A., Crossin, K.L., and Edelman, G.M. (2000) Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc Natl Acad Sci USA 97: 2253-2258.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2253-2258
    • Vanderklish, P.W.1    Krushel, L.A.2    Holst, B.H.3    Gally, J.A.4    Crossin, K.L.5    Edelman, G.M.6
  • 62
    • 29144451307 scopus 로고    scopus 로고
    • Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription
    • Wang, S., Fleming, R.T., Westbrook, E.M., Matsumura, P., and McKay, D.B. (2006) Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription. J Mol Biol 355: 798-808.
    • (2006) J Mol Biol , vol.355 , pp. 798-808
    • Wang, S.1    Fleming, R.T.2    Westbrook, E.M.3    Matsumura, P.4    McKay, D.B.5
  • 63
    • 33750432511 scopus 로고    scopus 로고
    • Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli
    • Weber, H., Pesavento, C., Possling, A., Tischendorf, G., and Hengge, R. (2006) Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli. Mol Microbiol 62: 1014-1034.
    • (2006) Mol Microbiol , vol.62 , pp. 1014-1034
    • Weber, H.1    Pesavento, C.2    Possling, A.3    Tischendorf, G.4    Hengge, R.5
  • 64
    • 84863611012 scopus 로고    scopus 로고
    • Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa
    • Whitney, J.C., Colvin, K.M., Marmont, L.S., Robinson, H., Parsek, M.R., and Howell, P.L. (2012) Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa. J Biol Chem 287: 23582-23593.
    • (2012) J Biol Chem , vol.287 , pp. 23582-23593
    • Whitney, J.C.1    Colvin, K.M.2    Marmont, L.S.3    Robinson, H.4    Parsek, M.R.5    Howell, P.L.6
  • 65
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z., and Liu, Y. (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys J 81: 2395-2402.
    • (2001) Biophys J , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 66
    • 77954855585 scopus 로고    scopus 로고
    • Unphosphorylated CsgD controls biofilm formation in Salmonella enterica serovar Typhimurium
    • Zakikhany, K., Harrington, C.R., Nimtz, M., Hinton, J.C., and Romling, U. (2010) Unphosphorylated CsgD controls biofilm formation in Salmonella enterica serovar Typhimurium. Mol Microbiol 77: 771-786.
    • (2010) Mol Microbiol , vol.77 , pp. 771-786
    • Zakikhany, K.1    Harrington, C.R.2    Nimtz, M.3    Hinton, J.C.4    Romling, U.5
  • 67
    • 0035065254 scopus 로고    scopus 로고
    • The multicellular morphotypes of Salmonella Typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
    • Zogaj, X., Nimtz, M., Rohde, M., Bokranz, W., and Romling, U. (2001) The multicellular morphotypes of Salmonella Typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix. Mol Microbiol 39: 1452-1463.
    • (2001) Mol Microbiol , vol.39 , pp. 1452-1463
    • Zogaj, X.1    Nimtz, M.2    Rohde, M.3    Bokranz, W.4    Romling, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.