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Volumn 33, Issue 1, 2015, Pages 124-141

Bacterial diguanylate cyclases: Structure, function and mechanism in exopolysaccharide biofilm development

Author keywords

Aerobic granules; Bacterial diguanylates cyclase; Biofilm; Biosynthesis; Cyclic di guanosine monophosphate; Exopolysaccharides; Structure

Indexed keywords

ANTIMICROBIAL AGENTS; BACTERIA; BIOCHEMISTRY; BIOLOGICAL WATER TREATMENT; BIOREMEDIATION; BIOSYNTHESIS; ENZYMES; GRANULAR MATERIALS; GRANULATION; METABOLITES; NUCLEOTIDES; STRUCTURE (COMPOSITION); WASTEWATER TREATMENT;

EID: 84922947346     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2014.11.010     Document Type: Review
Times cited : (89)

References (162)
  • 1
    • 43049125438 scopus 로고    scopus 로고
    • Extraction of extracellular polymeric substances from aerobic granule with compact interior structure
    • Adav S.S., Lee D.-J. Extraction of extracellular polymeric substances from aerobic granule with compact interior structure. J Hazard Mater 2008, 154:1120-1126.
    • (2008) J Hazard Mater , vol.154 , pp. 1120-1126
    • Adav, S.S.1    Lee, D.-J.2
  • 2
    • 41049092063 scopus 로고    scopus 로고
    • Physiological characterization and interactions of isolates in phenol-degrading aerobic granules
    • Adav S.S., Lee D.-J. Physiological characterization and interactions of isolates in phenol-degrading aerobic granules. Appl Microbiol Biotechnol 2008, 78:899-905.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 899-905
    • Adav, S.S.1    Lee, D.-J.2
  • 3
    • 33947584104 scopus 로고    scopus 로고
    • Degradation of phenol by aerobic granules and isolated yeast Candida tropicalis
    • Adav S.S., Chen M.Y., Lee D.-J., Ren N.Q. Degradation of phenol by aerobic granules and isolated yeast Candida tropicalis. Biotechnol Bioeng 2007, 96:844-852.
    • (2007) Biotechnol Bioeng , vol.96 , pp. 844-852
    • Adav, S.S.1    Chen, M.Y.2    Lee, D.-J.3    Ren, N.Q.4
  • 4
    • 34249933045 scopus 로고    scopus 로고
    • Biodegradation of pyridine using aerobic granules in the presence of phenol
    • Adav S.S., Lee D.-J., Ren N.Q. Biodegradation of pyridine using aerobic granules in the presence of phenol. Water Res 2007, 41:2903-2910.
    • (2007) Water Res , vol.41 , pp. 2903-2910
    • Adav, S.S.1    Lee, D.-J.2    Ren, N.Q.3
  • 5
    • 36949002768 scopus 로고    scopus 로고
    • Activity and structure of stored aerobic granules
    • Adav S.S., Lee D.-J., Tay J.H. Activity and structure of stored aerobic granules. Environ Technol 2007, 28:1227-1235.
    • (2007) Environ Technol , vol.28 , pp. 1227-1235
    • Adav, S.S.1    Lee, D.-J.2    Tay, J.H.3
  • 6
    • 44649151626 scopus 로고    scopus 로고
    • Intergeneric coaggregation of strains isolated from phenol-degrading aerobic granules
    • Adav S.S., Lee D.-J., Lai J.Y. Intergeneric coaggregation of strains isolated from phenol-degrading aerobic granules. Appl Microbiol Biotechnol 2008, 79:657-661.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 657-661
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 8
    • 40749120924 scopus 로고    scopus 로고
    • Extracellular polymeric substances and structural stability of aerobic granule
    • Adav S.S., Lee D.-J., Tay J.H. Extracellular polymeric substances and structural stability of aerobic granule. Water Res 2008, 42:1644-1650.
    • (2008) Water Res , vol.42 , pp. 1644-1650
    • Adav, S.S.1    Lee, D.-J.2    Tay, J.H.3
  • 9
    • 67650251229 scopus 로고    scopus 로고
    • Aerobic granulation in sequencing batch reactor at different settling times
    • Adav S.S., Lee D.-J., Lai J.Y. Aerobic granulation in sequencing batch reactor at different settling times. Bioresour Technol 2009, 100:5359-5361.
    • (2009) Bioresour Technol , vol.100 , pp. 5359-5361
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 10
    • 64849105927 scopus 로고    scopus 로고
    • Functional consortium from aerobic granules under high organic loading rates
    • Adav S.S., Lee D.-J., Lai J.Y. Functional consortium from aerobic granules under high organic loading rates. Bioresour Technol 2009, 100:3465-3470.
    • (2009) Bioresour Technol , vol.100 , pp. 3465-3470
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 11
    • 51349088515 scopus 로고    scopus 로고
    • Proteolytic activity in stored aerobic granular sludge and structural integrity
    • Adav S.S., Lee D.J., Lai J.Y. Proteolytic activity in stored aerobic granular sludge and structural integrity. Bioresour Technol 2009, 100:68-73.
    • (2009) Bioresour Technol , vol.100 , pp. 68-73
    • Adav, S.S.1    Lee, D.J.2    Lai, J.Y.3
  • 12
    • 67349087731 scopus 로고    scopus 로고
    • Treating chemical industries influent using aerobic granular sludge: recent development
    • Adav S.S., Lee D.-J., Lai J.Y. Treating chemical industries influent using aerobic granular sludge: recent development. J Taiwan Inst Chem Eng 2009, 40:333-336.
    • (2009) J Taiwan Inst Chem Eng , vol.40 , pp. 333-336
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 13
    • 74149091664 scopus 로고    scopus 로고
    • Enhanced biological denitrification of high concentration of nitrite with supplementary carbon sources
    • Adav S.S., Lee D.-J., Lai J.Y. Enhanced biological denitrification of high concentration of nitrite with supplementary carbon sources. Appl Microbiol Biotechnol 2010, 85:773-778.
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 773-778
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 14
    • 74149093863 scopus 로고    scopus 로고
    • Microbial community of acetate utilizing denitrifiers in aerobic granules
    • Adav S.S., Lee D.-J., Lai J.Y. Microbial community of acetate utilizing denitrifiers in aerobic granules. Appl Microbiol Biotechnol 2010, 85:753-762.
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 753-762
    • Adav, S.S.1    Lee, D.-J.2    Lai, J.Y.3
  • 15
    • 74449083629 scopus 로고    scopus 로고
    • Stereological assessment of extracellular polymeric substances, exo-enzymes, and specific bacterial strains in bioaggregates using fluorescence experiments
    • Adav S.S., Lin J.C.T., Yang Z., Whiteley C.G., Lee D.-J., Peng X.-F., et al. Stereological assessment of extracellular polymeric substances, exo-enzymes, and specific bacterial strains in bioaggregates using fluorescence experiments. Biotechnol Adv 2010, 28:255-280.
    • (2010) Biotechnol Adv , vol.28 , pp. 255-280
    • Adav, S.S.1    Lin, J.C.T.2    Yang, Z.3    Whiteley, C.G.4    Lee, D.-J.5    Peng, X.-F.6
  • 16
    • 34248220350 scopus 로고    scopus 로고
    • Effect of protein, polysaccharide, and oxygen concentration profiles on biofilm cohesiveness
    • Ahimou F., Semmens M.J., Haugstad G., Novak P.J. Effect of protein, polysaccharide, and oxygen concentration profiles on biofilm cohesiveness. Appl Environ Microbiol 2007, 73(9):2905-2910.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.9 , pp. 2905-2910
    • Ahimou, F.1    Semmens, M.J.2    Haugstad, G.3    Novak, P.J.4
  • 17
    • 84874106350 scopus 로고    scopus 로고
    • Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signalling
    • Airola M.V., Huh D., Sukomon N., Widom J., Sircar R., Borbat P.P., et al. Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signalling. J Mol Biol 2013, 425:886-901.
    • (2013) J Mol Biol , vol.425 , pp. 886-901
    • Airola, M.V.1    Huh, D.2    Sukomon, N.3    Widom, J.4    Sircar, R.5    Borbat, P.P.6
  • 18
    • 84874674749 scopus 로고    scopus 로고
    • Exposure of Salmonella enterica serovar typhimurium to a protective monoclonal IgA triggers exopolysaccharide production via a diguanylate cyclase-dependent pathway
    • Amarasinghe J.J., D'Hondt R.E., Waters C.M., Mantis N.J. Exposure of Salmonella enterica serovar typhimurium to a protective monoclonal IgA triggers exopolysaccharide production via a diguanylate cyclase-dependent pathway. Infect Immun 2013, 81(3):653-664.
    • (2013) Infect Immun , vol.81 , Issue.3 , pp. 653-664
    • Amarasinghe, J.J.1    D'Hondt, R.E.2    Waters, C.M.3    Mantis, N.J.4
  • 19
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam D., Galperin M.Y. PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 2006, 22(1):3-6.
    • (2006) Bioinformatics , vol.22 , Issue.1 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 20
    • 84884292053 scopus 로고    scopus 로고
    • A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis
    • An S.Q., Chin K.H., Febrer M., McCarthy Y., Yang Y., Liu C.L., et al. A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis. EMBO 2013, 32(18):2430-2438.
    • (2013) EMBO , vol.32 , Issue.18 , pp. 2430-2438
    • An, S.Q.1    Chin, K.H.2    Febrer, M.3    McCarthy, Y.4    Yang, Y.5    Liu, C.L.6
  • 21
    • 76649134086 scopus 로고    scopus 로고
    • Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors
    • Antoniani D., Bocci P., Maciag A., Raffaelli N., Landini P. Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors. Appl Microbiol Biotechnol 2010, 85(4):1095-1104.
    • (2010) Appl Microbiol Biotechnol , vol.85 , Issue.4 , pp. 1095-1104
    • Antoniani, D.1    Bocci, P.2    Maciag, A.3    Raffaelli, N.4    Landini, P.5
  • 22
    • 0035899964 scopus 로고    scopus 로고
    • Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
    • [16]
    • Ausmees N., Mayer R., Weinhouse H., Volman G., Amikam D., Benziman M., et al. Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. FEMS Microbiol Lett 2001, 204(1):163-167. [16].
    • (2001) FEMS Microbiol Lett , vol.204 , Issue.1 , pp. 163-167
    • Ausmees, N.1    Mayer, R.2    Weinhouse, H.3    Volman, G.4    Amikam, D.5    Benziman, M.6
  • 24
    • 84857169052 scopus 로고    scopus 로고
    • Poly-N-acetyl-α-(1-6)-glucosamine is a target for protective immunity against Acinetobacter baumannii infections
    • Bentancor L.V., O'Malley J.M., Bozkurt-Guzel C., Pier G.B., Maira-Litran T. Poly-N-acetyl-α-(1-6)-glucosamine is a target for protective immunity against Acinetobacter baumannii infections. Infect Immun 2012, 80:651-656.
    • (2012) Infect Immun , vol.80 , pp. 651-656
    • Bentancor, L.V.1    O'Malley, J.M.2    Bozkurt-Guzel, C.3    Pier, G.B.4    Maira-Litran, T.5
  • 25
    • 66949141781 scopus 로고    scopus 로고
    • Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress
    • Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D., et al. Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress. Mol Microbiol 2009, 72:1500-1516.
    • (2009) Mol Microbiol , vol.72 , pp. 1500-1516
    • Boehm, A.1    Steiner, S.2    Zaehringer, F.3    Casanova, A.4    Hamburger, F.5    Ritz, D.6
  • 26
    • 0036837981 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus scrABC, a novel operon affecting swarming and capsular polysaccharide regulation
    • Boles B.R., McCarter L.L. Vibrio parahaemolyticus scrABC, a novel operon affecting swarming and capsular polysaccharide regulation. J Bacteriol 2002, 184(21):5946-5954.
    • (2002) J Bacteriol , vol.184 , Issue.21 , pp. 5946-5954
    • Boles, B.R.1    McCarter, L.L.2
  • 27
    • 0037312852 scopus 로고    scopus 로고
    • Identification and characterization of a Vibrio cholerae gene, mbaA, involved in maintenance of biofilm architecture
    • Bomchil N., Watnick P., Kolter R. Identification and characterization of a Vibrio cholerae gene, mbaA, involved in maintenance of biofilm architecture. J Bacteriol 2003, 185:1384-1390.
    • (2003) J Bacteriol , vol.185 , pp. 1384-1390
    • Bomchil, N.1    Watnick, P.2    Kolter, R.3
  • 28
    • 84864358273 scopus 로고    scopus 로고
    • Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor
    • Bonomi H.R., Posadas D.M., Paris G., Carrica M del C., Frederickson M., Pietrasanta L.I., et al. Light regulates attachment, exopolysaccharide production, and nodulation in Rhizobium leguminosarum through a LOV-histidine kinase photoreceptor. Proc Natl Acad Sci U S A 2012, 109(30):12135-12140.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.30 , pp. 12135-12140
    • Bonomi, H.R.1    Posadas, D.M.2    Paris, G.3    Carrica M del, C.4    Frederickson, M.5    Pietrasanta, L.I.6
  • 29
    • 70350144293 scopus 로고    scopus 로고
    • Genetic and biochemical analyses of the Pseudomonas aeruginosa Psl exopolysaccharide reveal overlapping roles for polysaccharide synthesis enzymes in Psl and LPS production
    • Byrd M.S., Sadovskaya I., Vinogradov E., Lu H., Sprinle A.B., Richardson S.H., et al. Genetic and biochemical analyses of the Pseudomonas aeruginosa Psl exopolysaccharide reveal overlapping roles for polysaccharide synthesis enzymes in Psl and LPS production. Mol Microbiol 2009, 73(4):622-638.
    • (2009) Mol Microbiol , vol.73 , Issue.4 , pp. 622-638
    • Byrd, M.S.1    Sadovskaya, I.2    Vinogradov, E.3    Lu, H.4    Sprinle, A.B.5    Richardson, S.H.6
  • 30
    • 77951862766 scopus 로고    scopus 로고
    • A blue light-inducible phosphodiesterase activity in the cyanobacterium Synechococcus elongatus
    • Cao Z., Livoti E., Losi A., Gartner W. A blue light-inducible phosphodiesterase activity in the cyanobacterium Synechococcus elongatus. Photochem Photobiol 2010, 86:606-611.
    • (2010) Photochem Photobiol , vol.86 , pp. 606-611
    • Cao, Z.1    Livoti, E.2    Losi, A.3    Gartner, W.4
  • 31
    • 77949566572 scopus 로고    scopus 로고
    • A direct comparison amongst different technologies (aerobic granular sludge, SBR and MBR) for the treatment of wastewater contaminated by 4-chlorophenol
    • Carucci A., Millia S., Cappai G., Muntoni A. A direct comparison amongst different technologies (aerobic granular sludge, SBR and MBR) for the treatment of wastewater contaminated by 4-chlorophenol. J Hazard Mater 2010, 177:1119-1125.
    • (2010) J Hazard Mater , vol.177 , pp. 1119-1125
    • Carucci, A.1    Millia, S.2    Cappai, G.3    Muntoni, A.4
  • 32
    • 0014478832 scopus 로고
    • Two compounds implicated in the function of the RC gene of Escherichia coli
    • Cashel M., Gallant J. Two compounds implicated in the function of the RC gene of Escherichia coli. Nature 1969, 221:838-841.
    • (1969) Nature , vol.221 , pp. 838-841
    • Cashel, M.1    Gallant, J.2
  • 33
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • Chan C., Paul R., Samoray D., Amiot N.C., Giese B., Jenal U., et al. Structural basis of activity and allosteric control of diguanylate cyclase. Proc Natl Acad Sci U S A 2004, 101:17084-17089.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17084-17089
    • Chan, C.1    Paul, R.2    Samoray, D.3    Amiot, N.C.4    Giese, B.5    Jenal, U.6
  • 34
    • 84864379470 scopus 로고    scopus 로고
    • The Pel and Psl polysaccharides provide Pseudomonas aeruginosa structural redundancy within the biofilm matrix
    • Colvin K.M., Irie Y., Tart C.S., Urbano R., Whitney J.C., Ryder C., et al. The Pel and Psl polysaccharides provide Pseudomonas aeruginosa structural redundancy within the biofilm matrix. Environ Microbiol 2012, 14(8):1913-1928.
    • (2012) Environ Microbiol , vol.14 , Issue.8 , pp. 1913-1928
    • Colvin, K.M.1    Irie, Y.2    Tart, C.S.3    Urbano, R.4    Whitney, J.C.5    Ryder, C.6
  • 36
    • 84863515120 scopus 로고    scopus 로고
    • Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae
    • Cruz D.P., Huertas M.G., Lozano M., Zárate L., Zambrano M.M. Comparative analysis of diguanylate cyclase and phosphodiesterase genes in Klebsiella pneumoniae. BMC Microbiol 2012, 12(139). 10.1186/1471-2180-12-139.
    • (2012) BMC Microbiol , vol.12 , Issue.139
    • Cruz, D.P.1    Huertas, M.G.2    Lozano, M.3    Zárate, L.4    Zambrano, M.M.5
  • 38
    • 70349783823 scopus 로고    scopus 로고
    • Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
    • De N., Navarro M.V., Raghavan R.V., Sondermann H. Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR. J Mol Biol 2009, 393:619-633.
    • (2009) J Mol Biol , vol.393 , pp. 619-633
    • De, N.1    Navarro, M.V.2    Raghavan, R.V.3    Sondermann, H.4
  • 39
    • 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., et al. Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 2009, 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
  • 40
    • 84885465370 scopus 로고    scopus 로고
    • Cyclic Di-GMP modulates the disease progression of Erwinia amylovora
    • Edmunds A.C., Castiblanco L.F., Sundin G.W., Waters C.M. Cyclic Di-GMP modulates the disease progression of Erwinia amylovora. J Bacteriol 2013, 195(10):2155-2165.
    • (2013) J Bacteriol , vol.195 , Issue.10 , pp. 2155-2165
    • Edmunds, A.C.1    Castiblanco, L.F.2    Sundin, G.W.3    Waters, C.M.4
  • 41
    • 1242297814 scopus 로고    scopus 로고
    • Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms
    • Friedman L., Kolter R. Genes involved in matrix formation in Pseudomonas aeruginosa PA14 biofilms. Mol Microbiol 2004, 51(3):675-690.
    • (2004) Mol Microbiol , vol.51 , Issue.3 , pp. 675-690
    • Friedman, L.1    Kolter, R.2
  • 42
    • 3042735895 scopus 로고    scopus 로고
    • Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix
    • Friedman L., Kolter R. Two genetic loci produce distinct carbohydrate-rich structural components of the Pseudomonas aeruginosa biofilm matrix. J Bacteriol 2004, 186(14):4457-4465.
    • (2004) J Bacteriol , vol.186 , Issue.14 , pp. 4457-4465
    • Friedman, L.1    Kolter, R.2
  • 43
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin M.Y., Nikolskaya A.N., Koonin E.V. Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 2001, 203:11-21.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 44
    • 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., Lasa I. Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation. Mol Microbiol 2004, 54(1):264-277.
    • (2004) Mol Microbiol , vol.54 , Issue.1 , pp. 264-277
    • Garcia, B.1    Latasa, C.2    Solano, C.3    Garcia-del Portillo, F.4    Gamazo, C.5    Lasa, I.6
  • 45
    • 79961042398 scopus 로고    scopus 로고
    • Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture
    • Ghafoor A., Hay I.D., Rehm B.H.A. Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture. Appl Environ Microbiol 2011, 77(15):5238-5246.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.15 , pp. 5238-5246
    • Ghafoor, A.1    Hay, I.D.2    Rehm, B.H.A.3
  • 46
    • 84896718101 scopus 로고    scopus 로고
    • Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: Clues from the structure of the catalytic domain
    • Giardina G., Paiardini A., Fernicola S., Franceschini S., Rinaldo S., Stelitano V., et al. Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: Clues from the structure of the catalytic domain. PLoS One 2013, 8(11). 10.1371/journal.pone.0081324.
    • (2013) PLoS One , vol.8 , Issue.11
    • Giardina, G.1    Paiardini, A.2    Fernicola, S.3    Franceschini, S.4    Rinaldo, S.5    Stelitano, V.6
  • 48
    • 59949088230 scopus 로고    scopus 로고
    • MucR, a novel membrane associated regulator of alginate biosynthesis in Pseudomonas aeruginosa
    • Hay I.D., Remminghorst U., Rehm B.H. MucR, a novel membrane associated regulator of alginate biosynthesis in Pseudomonas aeruginosa. Appl Environ Microbiol 2009, 75:1110-1120.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1110-1120
    • Hay, I.D.1    Remminghorst, U.2    Rehm, B.H.3
  • 49
    • 0028844985 scopus 로고
    • Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus
    • Hecht G.B., Newton A. Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. J Bacteriol 1995, 177:6223-6229.
    • (1995) J Bacteriol , vol.177 , pp. 6223-6229
    • Hecht, G.B.1    Newton, A.2
  • 50
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman J.W., Harwood C.S. Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol Microbiol 2008, 69:376-389.
    • (2008) Mol Microbiol , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 51
    • 26444582915 scopus 로고    scopus 로고
    • A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels
    • Hickman J.W., Tifrea D.F., Harwood C.S. A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc Natl Acad Sci U S A 2005, 102:14422-14427.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14422-14427
    • Hickman, J.W.1    Tifrea, D.F.2    Harwood, C.S.3
  • 52
    • 0042065283 scopus 로고    scopus 로고
    • Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein
    • Hinsa S.M., Espinosa-Urgel M., Ramos J.L., O'Toole G.A. Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol Microbiol 2003, 49:905-918.
    • (2003) Mol Microbiol , vol.49 , pp. 905-918
    • Hinsa, S.M.1    Espinosa-Urgel, M.2    Ramos, J.L.3    O'Toole, G.A.4
  • 53
    • 84860905515 scopus 로고    scopus 로고
    • Discrete cyclic di-GMP-dependent control of bacterial predation versus axenic growth in Bdellovibrio bacteriovorus
    • Hobley L., Fung R.K., Lambert C., Harris M.A., Dabhi J.M., King S.S., et al. Discrete cyclic di-GMP-dependent control of bacterial predation versus axenic growth in Bdellovibrio bacteriovorus. PLoS Pathog 2012, 8(2):e1002493.
    • (2012) PLoS Pathog , vol.8 , Issue.2 , pp. e1002493
    • Hobley, L.1    Fung, R.K.2    Lambert, C.3    Harris, M.A.4    Dabhi, J.M.5    King, S.S.6
  • 54
    • 78149257816 scopus 로고    scopus 로고
    • Structure of bacterial cellulose synthase subunit D octamer with four inner passageways
    • Hu S.Q., Gao Y.G., Tajima K., Sunagawa N., Zhou Y., Kawano S., et al. Structure of bacterial cellulose synthase subunit D octamer with four inner passageways. Proc Natl Acad Sci U S A 2010, 107:17957-17961.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17957-17961
    • Hu, S.Q.1    Gao, Y.G.2    Tajima, K.3    Sunagawa, N.4    Zhou, Y.5    Kawano, S.6
  • 55
    • 0036428671 scopus 로고    scopus 로고
    • Genetic analysis of functions involved in the late stages of biofilm development in Burkholderia cepacia H111
    • Huber B., Riedel K., Köthe M., Givskov M., Molin S., Eberl L. Genetic analysis of functions involved in the late stages of biofilm development in Burkholderia cepacia H111. Mol Microbiol 2002, 46(2):411-426.
    • (2002) Mol Microbiol , vol.46 , Issue.2 , pp. 411-426
    • Huber, B.1    Riedel, K.2    Köthe, M.3    Givskov, M.4    Molin, S.5    Eberl, L.6
  • 56
    • 84893203213 scopus 로고    scopus 로고
    • The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP
    • Hunter J.L., Severin G.B., Koestler B.J., Waters C.M. The Vibrio cholerae diguanylate cyclase VCA0965 has an AGDEF active site and synthesizes cyclic di-GMP. BMC Microbiol 2014, 14:22. 10.1186/1471-2180-14-22.
    • (2014) BMC Microbiol , vol.14 , pp. 22
    • Hunter, J.L.1    Severin, G.B.2    Koestler, B.J.3    Waters, C.M.4
  • 57
    • 11144330206 scopus 로고    scopus 로고
    • Depolymerization of beta-1,6-N-acetyl-d-glucosamine disrupts the integrity of diverse bacterial biofilms
    • Itoh Y., Wang X., Hinnebusch B.J., Preston J.F., Romeo T. Depolymerization of beta-1,6-N-acetyl-d-glucosamine disrupts the integrity of diverse bacterial biofilms. J Bacteriol 2005, 187:382-387.
    • (2005) J Bacteriol , vol.187 , pp. 382-387
    • Itoh, Y.1    Wang, X.2    Hinnebusch, B.J.3    Preston, J.F.4    Romeo, T.5
  • 58
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria?
    • Jenal U. Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria?. Curr Opin Microbiol 2004, 7:185-191.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 185-191
    • Jenal, U.1
  • 59
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal U., Malone J. Mechanisms of cyclic-di-GMP signaling in bacteria. Annu Rev Genet 2006, 40:385-407.
    • (2006) Annu Rev Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 60
    • 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., Römling U. Hierarchical involvement of various GGDEF domain proteins in rdar morphotype development of Salmonella enterica serovar Typhimurium. Mol Microbiol 2006, 60:602-616.
    • (2006) Mol Microbiol , vol.60 , pp. 602-616
    • Kader, A.1    Simm, R.2    Gerstel, U.3    Morr, M.4    Römling, U.5
  • 61
    • 13844262033 scopus 로고    scopus 로고
    • C-di-GMP (3'-5'-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation
    • Karaolis D.K.R., Rashid M.H., Chythanya R., Luo W., Hyodo M., Hayakawa Y. c-di-GMP (3'-5'-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation. Antimicrob Agents Chemother 2005, 49(3):1029-1038.
    • (2005) Antimicrob Agents Chemother , vol.49 , Issue.3 , pp. 1029-1038
    • Karaolis, D.K.R.1    Rashid, M.H.2    Chythanya, R.3    Luo, W.4    Hyodo, M.5    Hayakawa, Y.6
  • 62
    • 4744337730 scopus 로고    scopus 로고
    • HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis
    • Kirillina O., Fetherston J.D., Bobrov A.G., Abney J., Perry R.D. HmsP, a putative phosphodiesterase, and HmsT, a putative diguanylate cyclase, control Hms-dependent biofilm formation in Yersinia pestis. Mol Microbiol 2004, 54:75-88.
    • (2004) Mol Microbiol , vol.54 , pp. 75-88
    • Kirillina, O.1    Fetherston, J.D.2    Bobrov, A.G.3    Abney, J.4    Perry, R.D.5
  • 63
    • 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., et al. Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins. J Mol Biol 2010, 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
  • 64
    • 79959551165 scopus 로고    scopus 로고
    • The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes
    • Kostick J.L., Szkotnick L.T., Rogers E.A., Bocci P., Raffaelli N., Marconi R.T. The diguanylate cyclase, Rrp1, regulates critical steps in the enzootic cycle of the Lyme disease spirochetes. Mol Microbiol 2011, 81(1):219-231.
    • (2011) Mol Microbiol , vol.81 , Issue.1 , pp. 219-231
    • Kostick, J.L.1    Szkotnick, L.T.2    Rogers, E.A.3    Bocci, P.4    Raffaelli, N.5    Marconi, R.T.6
  • 65
    • 36549021125 scopus 로고    scopus 로고
    • BifA, a cyclic-di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
    • Kuchma S.L., Brothers K.M., Merritt J.H., Liberati N.T., Ausubel F.M., O'Toole G.A. BifA, a cyclic-di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J Bacteriol 2007, 189:8165-8178.
    • (2007) J Bacteriol , vol.189 , pp. 8165-8178
    • Kuchma, S.L.1    Brothers, K.M.2    Merritt, J.H.3    Liberati, N.T.4    Ausubel, F.M.5    O'Toole, G.A.6
  • 66
    • 63449138218 scopus 로고    scopus 로고
    • The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection
    • Lai T.H., Kumagai Y., Hyodo M., Hayakawa Y., Rikihisa Y. The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection. J Bacteriol 2009, 191(3):693-700.
    • (2009) J Bacteriol , vol.191 , Issue.3 , pp. 693-700
    • Lai, T.H.1    Kumagai, Y.2    Hyodo, M.3    Hayakawa, Y.4    Rikihisa, Y.5
  • 67
    • 65349090694 scopus 로고    scopus 로고
    • BcsQ is an essential component of the Escherichia coli cellulose biosynthesis apparatus that localizes at the bacterial cell pole
    • Le Quere B., Ghigo J.M. BcsQ is an essential component of the Escherichia coli cellulose biosynthesis apparatus that localizes at the bacterial cell pole. Mol Microbiol 2009, 72:724-740.
    • (2009) Mol Microbiol , vol.72 , pp. 724-740
    • Le Quere, B.1    Ghigo, J.M.2
  • 68
    • 80455173988 scopus 로고    scopus 로고
    • Alginate: properties and biomedical applications
    • Lee K.-Y., Mooney D.J. Alginate: properties and biomedical applications. Prog Polym Sci 2012, 37:106-126.
    • (2012) Prog Polym Sci , vol.37 , pp. 106-126
    • Lee, K.-Y.1    Mooney, D.J.2
  • 69
    • 0035844214 scopus 로고    scopus 로고
    • Crystal structure of activated CheY. Comparison with other activated receiver domains
    • Lee S.Y., Cho H.S., Pelton J.G., Yan D., Berry E.A., Wemmer D.E. Crystal structure of activated CheY. Comparison with other activated receiver domains. J Biol Chem 2001, 276(19):16425-16431.
    • (2001) J Biol Chem , vol.276 , Issue.19 , pp. 16425-16431
    • Lee, S.Y.1    Cho, H.S.2    Pelton, J.G.3    Yan, D.4    Berry, E.A.5    Wemmer, D.E.6
  • 71
    • 58149144742 scopus 로고    scopus 로고
    • Amylase activity in substrate deficiency aerobic granules
    • Lee C.-C., Lee D.-J., Lai J.Y. Amylase activity in substrate deficiency aerobic granules. Appl Microbiol Biotechnol 2009, 81:961-967.
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 961-967
    • Lee, C.-C.1    Lee, D.-J.2    Lai, J.Y.3
  • 72
    • 79954716359 scopus 로고    scopus 로고
    • Mucoid Pseudomonas aeruginosa isolates maintain the biofilm formation capacity and the gene expression profiles during the chronic lung infection of CF patients
    • Lee B., Schjerling C.K., Kirkby N., Hoffmann N., Borup R., Molin S., et al. Mucoid Pseudomonas aeruginosa isolates maintain the biofilm formation capacity and the gene expression profiles during the chronic lung infection of CF patients. APMIS 2011, 119:263-274.
    • (2011) APMIS , vol.119 , pp. 263-274
    • Lee, B.1    Schjerling, C.K.2    Kirkby, N.3    Hoffmann, N.4    Borup, R.5    Molin, S.6
  • 73
    • 84896835151 scopus 로고    scopus 로고
    • Structure analysis of aerobic granule from a sequencing batch reactor for organic matter and ammonia nitrogen removal
    • Li J., Cai A., Wang D., Chen C., Ni Y. Structure analysis of aerobic granule from a sequencing batch reactor for organic matter and ammonia nitrogen removal. Int J Environ Res Public Health 2014, 11(3):2427-2436.
    • (2014) Int J Environ Res Public Health , vol.11 , Issue.3 , pp. 2427-2436
    • Li, J.1    Cai, A.2    Wang, D.3    Chen, C.4    Ni, Y.5
  • 74
    • 84887358084 scopus 로고    scopus 로고
    • Production of bacterial cellulose by Gluconacetobacter hansenii CGMCC 3917 using only waste beer yeast as nutrient source
    • Lin D., Lopez-Sanchez P., Li R., Li Z. Production of bacterial cellulose by Gluconacetobacter hansenii CGMCC 3917 using only waste beer yeast as nutrient source. Bioresour Technol 2014, 151:113-119.
    • (2014) Bioresour Technol , vol.151 , pp. 113-119
    • Lin, D.1    Lopez-Sanchez, P.2    Li, R.3    Li, Z.4
  • 75
    • 0026317733 scopus 로고
    • Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli
    • Liu J.D., Parkinson J.S. Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli. J Bacteriol 1991, 173:4941-4951.
    • (1991) J Bacteriol , vol.173 , pp. 4941-4951
    • Liu, J.D.1    Parkinson, J.S.2
  • 76
    • 11144233381 scopus 로고    scopus 로고
    • State of the art of biogranulation technology for wastewater treatment
    • Liu Y., Tay J.H. State of the art of biogranulation technology for wastewater treatment. Biotechnol Adv 2004, 22:533-563.
    • (2004) Biotechnol Adv , vol.22 , pp. 533-563
    • Liu, Y.1    Tay, J.H.2
  • 77
    • 79952010744 scopus 로고    scopus 로고
    • Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities
    • Liu N., Pak T., Boon E.M. Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities. Mol Biosyst 2010, 6(9):1561-1564.
    • (2010) Mol Biosyst , vol.6 , Issue.9 , pp. 1561-1564
    • Liu, N.1    Pak, T.2    Boon, E.M.3
  • 78
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah T.F., O'Toole G.A. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol 2001, 9(1):34-39.
    • (2001) Trends Microbiol , vol.9 , Issue.1 , pp. 34-39
    • Mah, T.F.1    O'Toole, G.A.2
  • 79
    • 0344011974 scopus 로고    scopus 로고
    • A genetic basis for Pseudomonas aeruginosa biofilm antibiotic resistance
    • Mah T.F., Pitts B., Pellock B., Walker G.C., Stewart P.S., O'Toole G.A. A genetic basis for Pseudomonas aeruginosa biofilm antibiotic resistance. Nature 2003, 426(6964):306-310.
    • (2003) Nature , vol.426 , Issue.6964 , pp. 306-310
    • Mah, T.F.1    Pitts, B.2    Pellock, B.3    Walker, G.C.4    Stewart, P.S.5    O'Toole, G.A.6
  • 80
    • 34247202706 scopus 로고    scopus 로고
    • The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain
    • Malone J.G., Williams R., Christen M., Jenal U., Spiers A.J., Rainey P.B. The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain. Microbiology 2007, 153:980-994.
    • (2007) Microbiology , vol.153 , pp. 980-994
    • Malone, J.G.1    Williams, R.2    Christen, M.3    Jenal, U.4    Spiers, A.J.5    Rainey, P.B.6
  • 81
    • 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., et al. YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa. PLoS Pathog 2010, 6:e1000804. 10.1371/journal.ppat.1000804.
    • (2010) PLoS Pathog , vol.6 , pp. e1000804
    • Malone, J.G.1    Jaeger, T.2    Spangler, C.3    Ritz, D.4    Spang, A.5    Arrieumerlou, C.6
  • 83
    • 83855165110 scopus 로고    scopus 로고
    • Should we stay or should we go: mechanisms and ecological consequences for biofilm dispersal
    • McDougald D., Rice S.A., Barraud N., Steinberg P.D., Kjelleberg S. Should we stay or should we go: mechanisms and ecological consequences for biofilm dispersal. Nat Rev Microbiol 2012, 10:39-50.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 39-50
    • McDougald, D.1    Rice, S.A.2    Barraud, N.3    Steinberg, P.D.4    Kjelleberg, S.5
  • 84
    • 34548428704 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa cupA encoded fimbriae expression is regulated by a GGDEF and EAL domaindependent modulation of the intracellular level of cyclic diguanylate
    • Meissner A., Wild V., Simm R., Rohde M., Erck C., Bredenbruch F., et al. Pseudomonas aeruginosa cupA encoded fimbriae expression is regulated by a GGDEF and EAL domaindependent modulation of the intracellular level of cyclic diguanylate. Environ Microbiol 2007, 9:2475-2485.
    • (2007) Environ Microbiol , vol.9 , pp. 2475-2485
    • Meissner, A.1    Wild, V.2    Simm, R.3    Rohde, M.4    Erck, C.5    Bredenbruch, F.6
  • 85
    • 33646346867 scopus 로고    scopus 로고
    • Genome wide transcriptional profile of Escherichia coli in response to high levels of the second messenger c-di-GMP
    • Mendez-Ortiz M.M., Hyodo M., Hayakawa Y., Membrillo-Hernandez J. Genome wide transcriptional profile of Escherichia coli in response to high levels of the second messenger c-di-GMP. J Biol Chem 2006, 281:8090-8099.
    • (2006) J Biol Chem , vol.281 , pp. 8090-8099
    • Mendez-Ortiz, M.M.1    Hyodo, M.2    Hayakawa, Y.3    Membrillo-Hernandez, J.4
  • 86
    • 36549037688 scopus 로고    scopus 로고
    • SadC reciprocally influences biofilm formation and swarming motility via modulation of exopolysaccharide production and flagellar function
    • Merritt J.H., Brothers K.M., Kuchma S.L., O'Toole A.G. SadC reciprocally influences biofilm formation and swarming motility via modulation of exopolysaccharide production and flagellar function. J Bacteriol 2007, 189:8154-8164.
    • (2007) J Bacteriol , vol.189 , pp. 8154-8164
    • Merritt, J.H.1    Brothers, K.M.2    Kuchma, S.L.3    O'Toole, A.G.4
  • 87
    • 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., et al. Specific control of Pseudomonas aeruginosa surface-associated behaviors by two c-di-GMP diguanylate cyclases. mBio 2010, 1(4):1-9.
    • (2010) mBio , vol.1 , Issue.4 , pp. 1-9
    • Merritt, J.H.1    Ha, D.G.2    Cowles, K.N.3    Lu, W.4    Morales, D.K.5    Rabinowitz, J.6
  • 88
    • 79960431250 scopus 로고    scopus 로고
    • The bacterial second messenger c-di-GMP: mechanisms of signalling
    • Mills E., Pultz I.S., Kulasekara H.D., Miller S.I. The bacterial second messenger c-di-GMP: mechanisms of signalling. Cell Microbiol 2011, 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
  • 89
    • 84922854198 scopus 로고    scopus 로고
    • Investigation of bacterial cellulose biosynthesis mechanism in Gluconoacetobacter hansenii
    • Mohite B.V., Patil S.V. Investigation of bacterial cellulose biosynthesis mechanism in Gluconoacetobacter hansenii. ISRN Microbiol 2014, 10.1155/2014/836083.
    • (2014) ISRN Microbiol
    • Mohite, B.V.1    Patil, S.V.2
  • 90
    • 84872141928 scopus 로고    scopus 로고
    • Crystallographic snapshot of cellulose synthesis and membrane translocation
    • Morgan J.L.W., Strumillo J., Zimmer J. Crystallographic snapshot of cellulose synthesis and membrane translocation. Nature 2013, 493:181-186.
    • (2013) Nature , vol.493 , pp. 181-186
    • Morgan, J.L.W.1    Strumillo, J.2    Zimmer, J.3
  • 91
    • 84902080356 scopus 로고    scopus 로고
    • Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP
    • Morgan J.L.W., McNamara J.T., Zimmer J. Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP. Nat Struct Mol Biol 2014, 21:489-496.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 489-496
    • Morgan, J.L.W.1    McNamara, J.T.2    Zimmer, J.3
  • 92
    • 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 D.A. Cyclic-di-GMP regulates extracellular polysaccharide production, biofilm formation, and rugose colony development by Vibrio vulnificus. Appl Environ Microbiol 2008, 74:4199-4209.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 4199-4209
    • Nakhamchik, A.1    Wilde, C.2    Rowe-Magnus, D.A.3
  • 93
    • 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., Sondermann H. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure 2009, 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
  • 94
    • 79952260048 scopus 로고    scopus 로고
    • Structural basis for c-di-GMP mediated inside-out signaling controlling periplasmic proteolysis
    • (e1000588-e1000588)
    • Navarro M.V., Newell P.D., Krasteva P.V., Chatterjee D., Madden D.R., O'Toole G.A., et al. Structural basis for c-di-GMP mediated inside-out signaling controlling periplasmic proteolysis. PLoS Biol 2011, 9. (e1000588-e1000588).
    • (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
  • 95
    • 53849116782 scopus 로고    scopus 로고
    • The Anabaena sp. strain PCC 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions
    • Neunuebel M.R., Golden J.W. The Anabaena sp. strain PCC 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions. J Bacteriol 2008, 190(20):6829-6836.
    • (2008) J Bacteriol , vol.190 , Issue.20 , pp. 6829-6836
    • Neunuebel, M.R.1    Golden, J.W.2
  • 96
    • 62549150834 scopus 로고    scopus 로고
    • LapD is a bis-(3,5)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens p f0-1
    • Newell P.D., Monds R.D., O'Toole G.A. LapD is a bis-(3,5)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens p f0-1. Proc Natl Acad Sci U S A 2009, 106:3461-3466.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'Toole, G.A.3
  • 97
    • 80052519940 scopus 로고    scopus 로고
    • Systematic analysis of diguanylate cyclases that promote biofilm formation
    • Newell P.D., Yoshioka S., Hvorecny K.L., Mondes R.D., Toole G.A. Systematic analysis of diguanylate cyclases that promote biofilm formation. J Bacteriol 2011, 193:4685-4698.
    • (2011) J Bacteriol , vol.193 , pp. 4685-4698
    • Newell, P.D.1    Yoshioka, S.2    Hvorecny, K.L.3    Mondes, R.D.4    Toole, G.A.5
  • 98
    • 33751378939 scopus 로고    scopus 로고
    • Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri
    • O'Shea T.M., Klein A.H., Geszvain K., Wolfe A.J., Visick K.L. Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri. J Bacteriol 2006, 188(23):8196-8205.
    • (2006) J Bacteriol , vol.188 , Issue.23 , pp. 8196-8205
    • O'Shea, T.M.1    Klein, A.H.2    Geszvain, K.3    Wolfe, A.J.4    Visick, K.L.5
  • 99
    • 48449097813 scopus 로고    scopus 로고
    • Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization
    • Oglesby L.L., Jain S., Ohman D.E. Membrane topology and roles of Pseudomonas aeruginosa Alg8 and Alg44 in alginate polymerization. Microbiology 2008, 154:1605-1615.
    • (2008) Microbiology , vol.154 , pp. 1605-1615
    • Oglesby, L.L.1    Jain, S.2    Ohman, D.E.3
  • 100
    • 84887086438 scopus 로고    scopus 로고
    • BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis
    • Omadjela O., Narahari A., Strumillo J., Mélida H., Mazur O., Bulone V., et al. BcsA and BcsB form the catalytically active core of bacterial cellulose synthase sufficient for in vitro cellulose synthesis. Proc Natl Acad Sci U S A 2013, 110(44):17856-17861.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.44 , pp. 17856-17861
    • Omadjela, O.1    Narahari, A.2    Strumillo, J.3    Mélida, H.4    Mazur, O.5    Bulone, V.6
  • 102
    • 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 N.C., Chan C., Schirmer T., Giese B., et al. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev 2004, 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
  • 103
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization
    • Paul R., Abel S., Wassmann P., Beck A., Heerklotz H., Jenal U. Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J Biol Chem 2007, 282(40):29170-29177.
    • (2007) J Biol Chem , vol.282 , Issue.40 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 104
    • 84856615725 scopus 로고    scopus 로고
    • Alginate derivatization: a review of chemistry, properties and applications
    • Pawar S.N., Edgar K.J. Alginate derivatization: a review of chemistry, properties and applications. Biomaterials 2012, 33(11):3279-3305.
    • (2012) Biomaterials , vol.33 , Issue.11 , pp. 3279-3305
    • Pawar, S.N.1    Edgar, K.J.2
  • 105
    • 82555181640 scopus 로고    scopus 로고
    • N-Acetyl-glucosamine-dependent biofilm formation in Pectobacterium atrosepticum is cryptic and activated by elevated c-di-GMP levels
    • Perez-Mendoza D., Coulthurst S.J., Sanjuan J., Salmond G.P. N-Acetyl-glucosamine-dependent biofilm formation in Pectobacterium atrosepticum is cryptic and activated by elevated c-di-GMP levels. Microbiology 2011, 157:3340-3348.
    • (2011) Microbiology , vol.157 , pp. 3340-3348
    • Perez-Mendoza, D.1    Coulthurst, S.J.2    Sanjuan, J.3    Salmond, G.P.4
  • 106
    • 80054835780 scopus 로고    scopus 로고
    • A multi-repeat adhesin of the phytopathogen, Pectobacterium atrosepticum, is secreted by a Type I pathway and is subject to complex regulation involving a non-canonical diguanylate cyclase
    • Perez-Mendoza D., Coulthurst S.J., Humphris S., Campbell E., Welch M., Toth I.K., et al. A multi-repeat adhesin of the phytopathogen, Pectobacterium atrosepticum, is secreted by a Type I pathway and is subject to complex regulation involving a non-canonical diguanylate cyclase. Mol Microbiol 2011, 82(3):719-733.
    • (2011) Mol Microbiol , vol.82 , Issue.3 , pp. 719-733
    • Perez-Mendoza, D.1    Coulthurst, S.J.2    Humphris, S.3    Campbell, E.4    Welch, M.5    Toth, I.K.6
  • 107
    • 0031262875 scopus 로고    scopus 로고
    • PAS: a multifunctional domain family comes to light
    • Ponting C.P., Aravind L. PAS: a multifunctional domain family comes to light. Curr Biol 1997, 7:R674-R677.
    • (1997) Curr Biol , vol.7 , pp. R674-R677
    • Ponting, C.P.1    Aravind, L.2
  • 108
    • 84864023989 scopus 로고    scopus 로고
    • Cyclic diguanylate inversely regulates motility and aggregation in clostridium difficile
    • Purcell E.B., McKee R.W., McBride S.M., Waters C.M., Tamayo R. Cyclic diguanylate inversely regulates motility and aggregation in clostridium difficile. J Bacteriol 2012, 194(13):3307-3316.
    • (2012) J Bacteriol , vol.194 , Issue.13 , pp. 3307-3316
    • Purcell, E.B.1    McKee, R.W.2    McBride, S.M.3    Waters, C.M.4    Tamayo, R.5
  • 109
    • 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 Z.X. A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum. Biochemistry 2009, 48:10275-10285.
    • (2009) Biochemistry , vol.48 , pp. 10275-10285
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.X.4
  • 111
    • 67349108043 scopus 로고    scopus 로고
    • Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase
    • Rao F., Pasunooti S., Ng Y., Zhuo W., Lim L., Liu A.W., et al. Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase. Anal Biochem 2009, 389(2):138-142.
    • (2009) Anal Biochem , vol.389 , Issue.2 , pp. 138-142
    • Rao, F.1    Pasunooti, S.2    Ng, Y.3    Zhuo, W.4    Lim, L.5    Liu, A.W.6
  • 112
    • 0345946329 scopus 로고    scopus 로고
    • Identification of genes involved in the switch between the smooth and rugose phenotypes of Vibrio cholerae
    • Rashid M.H., Rajanna C., Ali A., Karaolis D.K. Identification of genes involved in the switch between the smooth and rugose phenotypes of Vibrio cholerae. FEMS Microbiol Lett 2003, 227:113-119.
    • (2003) FEMS Microbiol Lett , vol.227 , pp. 113-119
    • Rashid, M.H.1    Rajanna, C.2    Ali, A.3    Karaolis, D.K.4
  • 113
    • 0345861987 scopus 로고    scopus 로고
    • Role of exopolysaccharide, the rugose phenotype and VpsR in the pathogenesis of epidemic Vibrio cholerae
    • Rashid M.H., Rajanna C., Zhang D., Pasquale V., Magder L.S., Ali A., et al. Role of exopolysaccharide, the rugose phenotype and VpsR in the pathogenesis of epidemic Vibrio cholerae. FEMS Microbiol Lett 2004, 230(1):105-113.
    • (2004) FEMS Microbiol Lett , vol.230 , Issue.1 , pp. 105-113
    • Rashid, M.H.1    Rajanna, C.2    Zhang, D.3    Pasquale, V.4    Magder, L.S.5    Ali, A.6
  • 114
    • 33749025232 scopus 로고    scopus 로고
    • Bacterial alginates: from biosynthesis to applications
    • Remminghorst U., Rehm B.H. Bacterial alginates: from biosynthesis to applications. Biotechnol Lett 2006, 28(21):1701-1712.
    • (2006) Biotechnol Lett , vol.28 , Issue.21 , pp. 1701-1712
    • Remminghorst, U.1    Rehm, B.H.2
  • 115
    • 84898056538 scopus 로고    scopus 로고
    • HmsC, a periplasmic protein controls biofilm formation via repression of HmsD, a diguanylate cyclase in Yersinia pestis
    • Ren G.X., Yan H.Q., Zhu H., Guo X.P., Sun Y.C. HmsC, a periplasmic protein controls biofilm formation via repression of HmsD, a diguanylate cyclase in Yersinia pestis. Environ Microbiol 2014, 16(4):1202-1216.
    • (2014) Environ Microbiol , vol.16 , Issue.4 , pp. 1202-1216
    • Ren, G.X.1    Yan, H.Q.2    Zhu, H.3    Guo, X.P.4    Sun, Y.C.5
  • 116
    • 22644438480 scopus 로고    scopus 로고
    • C-di-GMP: the dawning of a novel bacterial signalling system
    • Römling U., Gomelsky M., Galperin M.Y. C-di-GMP: the dawning of a novel bacterial signalling system. Mol Microbiol 2005, 57:629-639.
    • (2005) Mol Microbiol , vol.57 , pp. 629-639
    • Römling, U.1    Gomelsky, M.2    Galperin, M.Y.3
  • 117
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: the first 25years of a universal bacterial second messenger
    • Römling U., Galperin M.Y., Gomelsky M. Cyclic di-GMP: the first 25years of a universal bacterial second messenger. Microbiol Mol Biol Rev 2013, 77(1):1-52.
    • (2013) Microbiol Mol Biol Rev , vol.77 , Issue.1 , pp. 1-52
    • Römling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 118
    • 0023090935 scopus 로고
    • Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid
    • Ross P., Weinhouse H., Aloni Y., Michaeli D., Weinberger-Ohana P., Mayer R., et al. Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid. Nature 1987, 325:279-281.
    • (1987) Nature , vol.325 , pp. 279-281
    • Ross, P.1    Weinhouse, H.2    Aloni, Y.3    Michaeli, D.4    Weinberger-Ohana, P.5    Mayer, R.6
  • 119
    • 0026093011 scopus 로고
    • Cellulose biosynthesis and function in bacteria
    • Ross P., Mayer R., Benziman M. Cellulose biosynthesis and function in bacteria. Microbiol Mol Biol Rev 1991, 55(1):35-58.
    • (1991) Microbiol Mol Biol Rev , vol.55 , Issue.1 , pp. 35-58
    • Ross, P.1    Mayer, R.2    Benziman, M.3
  • 120
    • 33646249963 scopus 로고    scopus 로고
    • Cell-cell signalling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover
    • Ryan R.P., Fouhy Y., Lucey J.F., Crossman L.C., Spiro S., He Y.W., et al. Cell-cell signalling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover. Proc Natl Acad Sci U S A 2006, 103:6712-6717.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6712-6717
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3    Crossman, L.C.4    Spiro, S.5    He, Y.W.6
  • 121
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain
    • Ryjenkov D.A., Tarutina M., Moskvin O.V., Gomelsky M. Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J Bacteriol 2005, 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
  • 122
    • 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., Römling U., Gomelsky M. 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 2006, 281(41):30310-30314.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Römling, U.3    Gomelsky, M.4
  • 124
    • 84891741030 scopus 로고    scopus 로고
    • Identification of small molecules inhibiting diguanylate cyclases to control bacterial biofilm development
    • Sambanthamoorthy K., Luo C., Pattabiraman N., Feng X., Koestler B., Waters C.M., et al. Identification of small molecules inhibiting diguanylate cyclases to control bacterial biofilm development. Biofouling 2014, 30(1):17-28.
    • (2014) Biofouling , vol.30 , Issue.1 , pp. 17-28
    • Sambanthamoorthy, K.1    Luo, C.2    Pattabiraman, N.3    Feng, X.4    Koestler, B.5    Waters, C.M.6
  • 125
    • 84863578309 scopus 로고    scopus 로고
    • Light-induced alteration of c-di-GMP level controls motility of Synechocystis sp. PCC 6803
    • Savakis P., De Causmaecker S., Angerer V., Ruppert U., Anders K., Essen L.O., et al. Light-induced alteration of c-di-GMP level controls motility of Synechocystis sp. PCC 6803. Mol Microbiol 2012, 85:239-251.
    • (2012) Mol Microbiol , vol.85 , pp. 239-251
    • Savakis, P.1    De Causmaecker, S.2    Angerer, V.3    Ruppert, U.4    Anders, K.5    Essen, L.O.6
  • 126
    • 71649089775 scopus 로고    scopus 로고
    • Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP
    • Sawai H., Yoshioka S., Uchida T., Hyodo M., Hayakawa Y., Ishimori K., et al. Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP. Biochim Biophys Acta 2010, 1804(1):166-172.
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.1 , pp. 166-172
    • Sawai, H.1    Yoshioka, S.2    Uchida, T.3    Hyodo, M.4    Hayakawa, Y.5    Ishimori, K.6
  • 127
    • 84862203439 scopus 로고    scopus 로고
    • Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa
    • Sawai H., Sugimoto H., Shiro Y., Ishikawa H., Mizutani Y., Aono S. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa. Chem Commun 2012, 48:6523-6525.
    • (2012) Chem Commun , vol.48 , pp. 6523-6525
    • Sawai, H.1    Sugimoto, H.2    Shiro, Y.3    Ishikawa, H.4    Mizutani, Y.5    Aono, S.6
  • 128
    • 0029148367 scopus 로고
    • Identification of a second cellulose synthase gene (acsAII) in Acetobacter xylinum
    • Saxena I.M., Brown R.M. Identification of a second cellulose synthase gene (acsAII) in Acetobacter xylinum. J Bacteriol 1995, 177:5276-5283.
    • (1995) J Bacteriol , vol.177 , pp. 5276-5283
    • Saxena, I.M.1    Brown, R.M.2
  • 129
    • 77957017458 scopus 로고    scopus 로고
    • Extracellular polymeric substances (EPS) of microbial aggregates in biological wastewater treatment systems: a review
    • Sheng G.P., Yu H.Q., Li X.Y. Extracellular polymeric substances (EPS) of microbial aggregates in biological wastewater treatment systems: a review. Biotechnol Adv 2010, 28(6):882-894.
    • (2010) Biotechnol Adv , vol.28 , Issue.6 , pp. 882-894
    • Sheng, G.P.1    Yu, H.Q.2    Li, X.Y.3
  • 130
    • 75949088945 scopus 로고    scopus 로고
    • Proteomic analysis of Acinetobacter baumannii in biofilm and planktonic growth mode
    • Shin J.H., Lee H.W., Kim S.M., Kim J. Proteomic analysis of Acinetobacter baumannii in biofilm and planktonic growth mode. J Microbiol 2009, 47(6):728-735.
    • (2009) J Microbiol , vol.47 , Issue.6 , pp. 728-735
    • Shin, J.H.1    Lee, H.W.2    Kim, S.M.3    Kim, J.4
  • 131
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • Simm R., Morr M., Kader A., Nimtz M., Römling U. GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol Microbiol 2004, 53:1123-1134.
    • (2004) Mol Microbiol , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Römling, U.5
  • 132
    • 25144497412 scopus 로고    scopus 로고
    • Phenotypic convergence mediated by GGDEF-domain-containing proteins
    • Simm R., Fetherston J.D., Kader A., Römling U., Perry R.D. Phenotypic convergence mediated by GGDEF-domain-containing proteins. J Bacteriol 2005, 187(19):6816-6823.
    • (2005) J Bacteriol , vol.187 , Issue.19 , pp. 6816-6823
    • Simm, R.1    Fetherston, J.D.2    Kader, A.3    Römling, U.4    Perry, R.D.5
  • 133
    • 78650787467 scopus 로고    scopus 로고
    • Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2', (3')-substituted purine and pyrimidine nucleotides
    • Spangler C., Kaever V., Seifert R. Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2', (3')-substituted purine and pyrimidine nucleotides. J Pharmacol Exp Ther 2011, 336(1):234-241.
    • (2011) J Pharmacol Exp Ther , vol.336 , Issue.1 , pp. 234-241
    • Spangler, C.1    Kaever, V.2    Seifert, R.3
  • 134
    • 84868372310 scopus 로고    scopus 로고
    • Enzymatically active and inactive phosphodiesterases and diguanylate cyclases are involved in regulation of motility or sessility in Escherichia coli CFT073
    • Spurbeck R.R., Tarrien R.J., Mobley H.L. Enzymatically active and inactive phosphodiesterases and diguanylate cyclases are involved in regulation of motility or sessility in Escherichia coli CFT073. mBio 2012, 3:e00307-e00312.
    • (2012) mBio , vol.3 , pp. e00307-e00312
    • Spurbeck, R.R.1    Tarrien, R.J.2    Mobley, H.L.3
  • 135
    • 66149084428 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa rugose small colony variants have adaptations likely to promote persistence in the cystic fibrosis lung
    • Starkey M., Hickman J.H., Ma L., Zhang N., De Long S., Hinz A., et al. Pseudomonas aeruginosa rugose small colony variants have adaptations likely to promote persistence in the cystic fibrosis lung. J Bacteriol 2009, 191:3492-3503.
    • (2009) J Bacteriol , vol.191 , pp. 3492-3503
    • Starkey, M.1    Hickman, J.H.2    Ma, L.3    Zhang, N.4    De Long, S.5    Hinz, A.6
  • 137
    • 79955774904 scopus 로고    scopus 로고
    • Differential control of Yersinia pestis biofilm formation in vitro and in the flea vector by two c-di-GMP diguanylate cyclases
    • Sun Y.C., Koumoutsi A., Jarrett C., Lawrence K., Gherardini F.C., Darby C., et al. Differential control of Yersinia pestis biofilm formation in vitro and in the flea vector by two c-di-GMP diguanylate cyclases. PLoS One 2011, 6(4):e19267.
    • (2011) PLoS One , vol.6 , Issue.4 , pp. e19267
    • Sun, Y.C.1    Koumoutsi, A.2    Jarrett, C.3    Lawrence, K.4    Gherardini, F.C.5    Darby, C.6
  • 138
    • 0035152224 scopus 로고    scopus 로고
    • Biofilm exopolysaccharides: a strong and sticky framework
    • Sutherland I.W. Biofilm exopolysaccharides: a strong and sticky framework. Microbiology 2001, 147:3-9.
    • (2001) Microbiology , vol.147 , pp. 3-9
    • Sutherland, I.W.1
  • 139
    • 77957862775 scopus 로고    scopus 로고
    • The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon
    • Tagliabue L., Antoniani D., Maciag A., Bocci P., Raffaelli N., Landini P. The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon. Microbiology 2010, 156(10):2901-2911.
    • (2010) Microbiology , vol.156 , Issue.10 , pp. 2901-2911
    • Tagliabue, L.1    Antoniani, D.2    Maciag, A.3    Bocci, P.4    Raffaelli, N.5    Landini, P.6
  • 140
    • 0031783181 scopus 로고    scopus 로고
    • Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes
    • Tal R., Wong H.C., Calhoon R., Gelfand D., Fear A.L., Volman G., et al. Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: genetic organization and occurrence of conserved domains in isoenzymes. J Bacteriol 1998, 180:4416-4425.
    • (1998) J Bacteriol , vol.180 , pp. 4416-4425
    • Tal, R.1    Wong, H.C.2    Calhoon, R.3    Gelfand, D.4    Fear, A.L.5    Volman, G.6
  • 141
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • Tamayo R., Pratt J.T., Camilli A. Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu Rev Microbiol 2007, 61:131-148.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 142
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP
    • Tarutina M., Ryjenkov D.A., Gomelsky M. An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the second messenger c-di-GMP. J Biol Chem 2006, 281:34751-34758.
    • (2006) J Biol Chem , vol.281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 143
    • 77956921553 scopus 로고    scopus 로고
    • Structural insight into the mechanism of c-di-GMP hydrolysis by EAL domain phosphodiesterases
    • Tchigvintsev A., Xu X., Singer A., Chang C., Brown G., Proudfoot M., et al. Structural insight into the mechanism of c-di-GMP hydrolysis by EAL domain phosphodiesterases. J Mol Biol 2010, 402:524-538.
    • (2010) J Mol Biol , vol.402 , pp. 524-538
    • Tchigvintsev, A.1    Xu, X.2    Singer, A.3    Chang, C.4    Brown, G.5    Proudfoot, M.6
  • 144
    • 33645213032 scopus 로고    scopus 로고
    • Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP
    • Thormann K.M., Duttler S., Saville R.M., Hyodo M., Shukla S., Hayakawa Y., et al. Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP. J Bacteriol 2006, 188:2681-2691.
    • (2006) J Bacteriol , vol.188 , pp. 2681-2691
    • Thormann, K.M.1    Duttler, S.2    Saville, R.M.3    Hyodo, M.4    Shukla, S.5    Hayakawa, Y.6
  • 145
    • 79958062471 scopus 로고    scopus 로고
    • Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor
    • Tran N.T., Den Hengst C.D., Gomez-Escribano J.P., Buttner M.J. Identification and characterization of CdgB, a diguanylate cyclase involved in developmental processes in Streptomyces coelicolor. J Bacteriol 2011, 193(12):3100-3108.
    • (2011) J Bacteriol , vol.193 , Issue.12 , pp. 3100-3108
    • Tran, N.T.1    Den Hengst, C.D.2    Gomez-Escribano, J.P.3    Buttner, M.J.4
  • 146
    • 70350047301 scopus 로고    scopus 로고
    • An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
    • Tuckerman J.R., Gonzalez G., Sousa E.H., Wan X., Saito J.A., Alam M., et al. An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 2009, 48:9764-9774.
    • (2009) Biochemistry , vol.48 , pp. 9764-9774
    • Tuckerman, J.R.1    Gonzalez, G.2    Sousa, E.H.3    Wan, X.4    Saito, J.A.5    Alam, M.6
  • 147
    • 33749405542 scopus 로고    scopus 로고
    • Biofilm formation and cellulose expression among diverse environmental Pseudomonas isolates
    • Ude S., Arnold D.L., Moon C.D., Timms-Wilson T., Spiers A. Biofilm formation and cellulose expression among diverse environmental Pseudomonas isolates. Environ Microbiol 2006, 8(11):1997-2011.
    • (2006) Environ Microbiol , vol.8 , Issue.11 , pp. 1997-2011
    • Ude, S.1    Arnold, D.L.2    Moon, C.D.3    Timms-Wilson, T.4    Spiers, A.5
  • 148
    • 67650863623 scopus 로고    scopus 로고
    • Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885)
    • Ueda A., Wood T.K. Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885). PLoS Pathog 2009, 5:e1000483. 10.1371/journal.ppat.1000483.
    • (2009) PLoS Pathog , vol.5 , pp. e1000483
    • Ueda, A.1    Wood, T.K.2
  • 149
    • 84865519312 scopus 로고    scopus 로고
    • Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product
    • Vorobiev S.M., Neely H., Yu B., Seetharaman J., Xiao R., Acton T.B., et al. Crystal structure of a catalytically active GG(D/E)EF diguanylate cyclase domain from Marinobacter aquaeolei with bound c-di-GMP product. J Struct Funct Genomics 2012, 13(3):177-183.
    • (2012) J Struct Funct Genomics , vol.13 , Issue.3 , pp. 177-183
    • Vorobiev, S.M.1    Neely, H.2    Yu, B.3    Seetharaman, J.4    Xiao, R.5    Acton, T.B.6
  • 150
    • 84882616755 scopus 로고    scopus 로고
    • Disintegration of aerobic granules: role of second messenger cyclic di-GMP
    • Wan C.L., Zhang P., Lee D.-J., Yang X., Liu X., Sun S.P., et al. Disintegration of aerobic granules: role of second messenger cyclic di-GMP. Bioresour Technol 2013, 146:330-335.
    • (2013) Bioresour Technol , vol.146 , pp. 330-335
    • Wan, C.L.1    Zhang, P.2    Lee, D.-J.3    Yang, X.4    Liu, X.5    Sun, S.P.6
  • 151
    • 84891151101 scopus 로고    scopus 로고
    • Aerobic granulation of aggregating consortium X9 isolated from aerobic granules and role of cyclic di-GMP
    • Wan C.L., Yang X., Lee D.-J., Wang X.-Y., Yang Q., Pan X.-L. Aerobic granulation of aggregating consortium X9 isolated from aerobic granules and role of cyclic di-GMP. Bioresour Technol 2014, 152:557-561.
    • (2014) Bioresour Technol , vol.152 , pp. 557-561
    • Wan, C.L.1    Yang, X.2    Lee, D.-J.3    Wang, X.-Y.4    Yang, Q.5    Pan, X.-L.6
  • 152
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann P., Chan C., Paul R., Beck A., Heerklotz H., Jenal U., et al. Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 2007, 15:915-927.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 153
    • 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., Hengge R. Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia coli. Mol Microbiol 2006, 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
  • 154
    • 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., Howell P.L. Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa. J Biol Chem 2012, 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
  • 156
    • 83255188008 scopus 로고    scopus 로고
    • Characterization of the poly-_-1,6-Nacetylglucosamine polysaccharide component of Burkholderia biofilms
    • Yakandawala N., Gawande P.V., Lovetri K., Cardona S.T., Romeo T., Nitz M., et al. Characterization of the poly-_-1,6-Nacetylglucosamine polysaccharide component of Burkholderia biofilms. Appl Environ Microbiol 2011, 77:8303-8309.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 8303-8309
    • Yakandawala, N.1    Gawande, P.V.2    Lovetri, K.3    Cardona, S.T.4    Romeo, T.5    Nitz, M.6
  • 158
    • 79251615811 scopus 로고    scopus 로고
    • Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli
    • Zähringer F., Massa C., Schirmer T. Efficient enzymatic production of the bacterial second messenger c-di-GMP by the diguanylate cyclase YdeH from E. coli. Appl Biochem Biotechnol 2011, 163(1):71-79.
    • (2011) Appl Biochem Biotechnol , vol.163 , Issue.1 , pp. 71-79
    • Zähringer, F.1    Massa, C.2    Schirmer, T.3
  • 159
    • 84879826686 scopus 로고    scopus 로고
    • Structure and signaling mechanism of a zinc-sensory diguanylate cyclase
    • Zähringer F., Lacanna E., Jenal U., Schirmer T., Boehm A. Structure and signaling mechanism of a zinc-sensory diguanylate cyclase. Structure 2013, 21:1149-1157.
    • (2013) Structure , vol.21 , pp. 1149-1157
    • Zähringer, F.1    Lacanna, E.2    Jenal, U.3    Schirmer, T.4    Boehm, A.5
  • 160
    • 77954384425 scopus 로고    scopus 로고
    • Structural characterization of the predominant family of histidine kinase sensor domains
    • Zhang Z., Hendrickson W.A. Structural characterization of the predominant family of histidine kinase sensor domains. J Mol Biol 2010, 400:335-353.
    • (2010) J Mol Biol , vol.400 , pp. 335-353
    • Zhang, Z.1    Hendrickson, W.A.2
  • 161
    • 0031804060 scopus 로고    scopus 로고
    • Measurement of polysaccharides and proteins in biofilm extracellular polymers
    • Zhang X.Q., Bishop P.L., Kupferie M.J. Measurement of polysaccharides and proteins in biofilm extracellular polymers. Water Sci Technol 1998, 37:345-348.
    • (1998) Water Sci Technol , vol.37 , pp. 345-348
    • Zhang, X.Q.1    Bishop, P.L.2    Kupferie, M.J.3
  • 162
    • 84884876659 scopus 로고    scopus 로고
    • Recovery of stored aerobic granular sludge and its contaminants removal deficiency under different operation conditions
    • Zhao Z., Wang S., Shi W., Li J. Recovery of stored aerobic granular sludge and its contaminants removal deficiency under different operation conditions. Biomed Res Int 2013, 2013:168581. 10.1155/2013/168581.
    • (2013) Biomed Res Int , vol.2013 , pp. 168581
    • Zhao, Z.1    Wang, S.2    Shi, W.3    Li, J.4


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