메뉴 건너뛰기




Volumn 51, Issue 10, 2012, Pages 2087-2099

Nitric oxide regulation of cyclic di-GMP synthesis and hydrolysis in Shewanella woodyi

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PARTNERS; BIOFILM FORMATION; BIOFILM GROWTH; CYCLASES; HEMOPROTEINS; MOLECULAR BASIS; MOLECULAR LEVELS; MOLECULAR MECHANISM; MUTANT STRAIN; NANOMOLAR; NANOMOLAR LEVELS; NO SENSOR; PHOSPHODIESTERASE ACTIVITY; PURIFIED PROTEIN; SHEWANELLA; SIGNALING MOLECULES; WILD TYPES;

EID: 84863229664     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201753f     Document Type: Article
Times cited : (135)

References (70)
  • 1
    • 0034443286 scopus 로고    scopus 로고
    • Microbial biofilms: From ecology to molecular genetics
    • DOI 10.1128/MMBR.64.4.847-867.2000
    • Davey, M. E. and O'Toole, G. A. (2000) Microbial biofilms: From ecology to molecular genetics Microbiol. Mol. Biol. Rev. 64, 847-867 (Pubitemid 32475933)
    • (2000) Microbiology and Molecular Biology Reviews , vol.64 , Issue.4 , pp. 847-867
    • Davey, M.E.1    O'Toole, G.A.2
  • 2
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. (1992) Nitric oxide as a secretory product of mammalian cells FASEB J. 6, 3051-3064
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 3
    • 1942475411 scopus 로고    scopus 로고
    • Physiologic and Proteomic Evidence for a Role of Nitric Oxide in Biofilm Formation by Nitrosomonas europaea and Other Ammonia Oxidizers
    • DOI 10.1128/JB.186.9.2781-2788.2004
    • Schmidt, I., Steenbakkers, P., op den Camp, H., Schmidt, K., and Jetten, M. (2004) Physiologic and proteomic evidence for a role of nitric oxide in biofilm formation by Nitrosomonas europaea and other ammonia oxidizers J. Bacteriol. 186, 2781-2788 (Pubitemid 38525933)
    • (2004) Journal of Bacteriology , vol.186 , Issue.9 , pp. 2781-2788
    • Schmidt, I.1    Steenbakkers, P.J.M.2    Op Den Camp, H.J.M.3    Schmidt, K.4    Jetten, M.S.M.5
  • 4
    • 33750479893 scopus 로고    scopus 로고
    • Involvement of nitric oxide in biofilm dispersal of Pseudomonas aeruginosa
    • DOI 10.1128/JB.00779-06
    • Barraud, N., Hassett, D. J., Hwang, S.-H., Rice, S. A., Kjelleberg, S., and Webb, J. S. (2006) Involvement of Nitric Oxide in Biofilm Dispersal of Pseudomonas aeruginosa J. Bacteriol. 188, 7344-7353 (Pubitemid 44646233)
    • (2006) Journal of Bacteriology , vol.188 , Issue.21 , pp. 7344-7353
    • Barraud, N.1    Hassett, D.J.2    Hwang, S.-H.3    Rice, S.A.4    Kjelleberg, S.5    Webb, J.S.6
  • 5
    • 0035802331 scopus 로고    scopus 로고
    • Sol-gel derived nitric-oxide releasing materials that reduce bacterial adhesion [20]
    • DOI 10.1021/ja0165077
    • Nablo, B. J., Chen, T. Y., and Schoenfisch, M. H. (2001) Sol-gel derived nitric-oxide releasing materials that reduce bacterial adhesion J. Am. Chem. Soc. 123, 9712-9713 (Pubitemid 32937759)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.39 , pp. 9712-9713
    • Nablo, B.J.1    Chen, T.-Y.2    Schoenfisch, M.H.3
  • 6
    • 61549143059 scopus 로고    scopus 로고
    • Anti-biofilm efficacy of nitric oxide-releasing silica nanoparticles
    • Hetrick, E. M., Shin, J. H., Paul, H. S., and Schoenfisch, M. H. (2009) Anti-biofilm efficacy of nitric oxide-releasing silica nanoparticles Biomaterials 30, 2782-2789
    • (2009) Biomaterials , vol.30 , pp. 2782-2789
    • Hetrick, E.M.1    Shin, J.H.2    Paul, H.S.3    Schoenfisch, M.H.4
  • 7
    • 79952477593 scopus 로고    scopus 로고
    • Efficacy of surface-generated nitric oxide against Candida albicans adhesion and biofilm formation
    • Privett, B. J., Nutz, S. T., and Schoenfisch, M. H. (2010) Efficacy of surface-generated nitric oxide against Candida albicans adhesion and biofilm formation Biofouling 26, 973-983
    • (2010) Biofouling , vol.26 , pp. 973-983
    • Privett, B.J.1    Nutz, S.T.2    Schoenfisch, M.H.3
  • 8
    • 60349108749 scopus 로고    scopus 로고
    • The developmental model of microbial biofilms: Ten years of a paradigm up for review
    • Monds, R. D. and O'Toole, G. A. (2009) The developmental model of microbial biofilms: Ten years of a paradigm up for review Trends Microbiol. 17, 73-87
    • (2009) Trends Microbiol. , vol.17 , pp. 73-87
    • Monds, R.D.1    O'Toole, G.A.2
  • 9
    • 84864389119 scopus 로고    scopus 로고
    • Cyclic di-GMP, an established secondary messenger still speeding up
    • 10.1111/j.1462-2920.2011.02617.x
    • Romling, U. (2011) Cyclic di-GMP, an established secondary messenger still speeding up Environ. Microbiol. 10.1111/j.1462-2920.2011.02617.x
    • (2011) Environ. Microbiol.
    • Romling, U.1
  • 10
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria?
    • DOI 10.1016/j.mib.2004.02.007, PII S1369527404000207
    • Jenal, U. (2004) Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria? Curr. Opin. Microbiol. 7, 185-191 (Pubitemid 38447053)
    • (2004) Current Opinion in Microbiology , vol.7 , Issue.2 , pp. 185-191
    • Jenal, U.1
  • 11
    • 4444250897 scopus 로고    scopus 로고
    • Cyclic di-GMP as a bacterial second messenger
    • D'Argenio, D. A. and Miller, S. I. (2004) Cyclic di-GMP as a bacterial second messenger Microbiology 150, 2497-2502 (Pubitemid 39173255)
    • (2004) Microbiology , vol.150 , Issue.8 , pp. 2497-2502
    • D'Argenio, D.A.1    Miller, S.I.2
  • 12
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • DOI 10.1111/j.1365-2958.2004.04155.x
    • Tischler, A. D. and Camilli, A. (2004) Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation Mol. Microbiol. 53, 857-869 (Pubitemid 39036965)
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 13
    • 0035899964 scopus 로고    scopus 로고
    • Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
    • DOI 10.1016/S0378-1097(01)00394-9, PII S0378109701003949
    • Ausmees, N., Mayer, R., Weinhouse, H., Volman, G., Amikam, D., Benziman, M., and Lindberg, M. (2001) Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity FEMS Microbiol. Lett. 204, 163-167 (Pubitemid 33000051)
    • (2001) FEMS Microbiology Letters , 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    Lindberg, M.7
  • 15
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessibility to motility
    • DOI 10.1111/j.1365-2958.2004.04206.x
    • Simm, R., Morr, M., Kader, A., Nimtz, M., and Romling, U. (2004) GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility Mol. Microbiol. 53, 1123-1134 (Pubitemid 39120434)
    • (2004) Molecular Microbiology , vol.53 , Issue.4 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 16
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • DOI 10.1016/S0378-1097(01)00326-3, PII S0378109701003263
    • 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 (Pubitemid 32830987)
    • (2001) FEMS Microbiology Letters , vol.203 , Issue.1 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 17
    • 12944308816 scopus 로고    scopus 로고
    • Purification and initial characterization of a putative blue light-regulated phosphodiesterase from Escherichia coli
    • DOI 10.1562/2004-06-16-RA-203.1
    • Rajagopal, S., Key, J. M., Purcell, E. B., Boerema, D. J., and Moffat, K. (2004) Purification and initial characterization of a putative blue light-regulated phosphodiesterase from Escherichia coli Photochem. Photobiol. 80, 542-547 (Pubitemid 40174483)
    • (2004) Photochemistry and Photobiology , vol.80 , Issue.3 , pp. 542-547
    • Rajagopal, S.1    Key, J.M.2    Purcell, E.B.3    Boerema, D.J.4    Moffat, K.5
  • 18
    • 27144544090 scopus 로고    scopus 로고
    • NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine
    • DOI 10.1128/JB.187.21.7434-7443.2005
    • Karatan, E., Duncan, T. R., and Watnick, P. I. (2005) NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine J. Bacteriol. 187, 7434-7443 (Pubitemid 41507800)
    • (2005) Journal of Bacteriology , vol.187 , Issue.21 , pp. 7434-7443
    • Karatan, E.1    Duncan, T.R.2    Watnick, P.I.3
  • 20
    • 72249092095 scopus 로고    scopus 로고
    • Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic diguanosine-5′-monophosphate levels and enhanced dispersal
    • Barraud, N., Schleheck, D., Klebensberger, J., Webb, J. S., Hassett, D. J., Rice, S. A., and Kjelleberg, S. (2009) Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic diguanosine-5′-monophosphate levels and enhanced dispersal J. Bacteriol. 191, 7333-7342
    • (2009) J. Bacteriol. , vol.191 , pp. 7333-7342
    • Barraud, N.1    Schleheck, D.2    Klebensberger, J.3    Webb, J.S.4    Hassett, D.J.5    Rice, S.A.6    Kjelleberg, S.7
  • 21
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • DOI 10.1016/j.cbpa.2005.08.015, PII S1367593105001122, Mechanisms / Analytical Techniques
    • Boon, E. M. and Marletta, M. A. (2005) Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins Curr. Opin. Chem. Biol. 9, 441-446 (Pubitemid 41338195)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.5 , pp. 441-446
    • Boon, E.M.1    Marletta, M.A.2
  • 23
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005) A molecular basis for NO selectivity in soluble guanylate cyclase Nat. Chem. Biol. 1, 53-59
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 24
    • 16244376841 scopus 로고    scopus 로고
    • Ligand specificity of H-NOX domains: From sGC to bacterial NO sensors
    • DOI 10.1016/j.jinorgbio.2004.12.016, Heme-Diatomic Interactions, Part 2
    • Boon, E. M. and Marletta, M. A. (2005) Ligand specificity of H-NOX domains: from sGC to bacterial NO sensors J. Inorg. Biochem. 99, 892-902 (Pubitemid 40461919)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.4 , pp. 892-902
    • Boon, E.M.1    Marletta, M.A.2
  • 25
    • 33746890867 scopus 로고    scopus 로고
    • Sensitive and selective detection of nitric oxide using an H-NOX domain
    • DOI 10.1021/ja0632714
    • Boon, E. M. and Marletta, M. A. (2006) Sensitive and selective detection of nitric oxide using an H-NOX domain J. Am. Chem. Soc. 128, 10022-10023 (Pubitemid 44201079)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.31 , pp. 10022-10023
    • Boon, E.M.1    Marletta, M.A.2
  • 26
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer, L. M., Anantharaman, V., and Aravind, L. (2003) Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins BMC Genomics 4, 5-12
    • (2003) BMC Genomics , vol.4 , pp. 5-12
    • Iyer, L.M.1    Anantharaman, V.2    Aravind, L.3
  • 27
    • 77955401388 scopus 로고    scopus 로고
    • H-NOX regulation of c-di-GMP metabolism and biofilm formation in Legionella pneumophila
    • Carlson, H. K., Vance, R. E., and Marletta, M. A. (2010) H-NOX regulation of c-di-GMP metabolism and biofilm formation in Legionella pneumophila Mol. Microbiol. 77, 930-942
    • (2010) Mol. Microbiol. , vol.77 , pp. 930-942
    • Carlson, H.K.1    Vance, R.E.2    Marletta, M.A.3
  • 28
    • 36849072336 scopus 로고    scopus 로고
    • Shewanella oneidensis MR-1 H-NOX regulation of a histidine kinase by nitric oxide
    • DOI 10.1021/bi7019035
    • Price, M. S., Chao, L. Y., and Marletta, M. A. (2007) Shewanella oneidensis MR-1 H-NOX regulation of a histidine kinase by nitric oxide Biochemistry 46, 13677-13683 (Pubitemid 350223895)
    • (2007) Biochemistry , vol.46 , Issue.48 , pp. 13677-13683
    • Price, M.S.1    Chao, L.Y.2    Marletta, M.A.3
  • 30
    • 79952010744 scopus 로고    scopus 로고
    • Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities
    • Liu, N., Pak, T., and Boon, E. M. (2010) Characterization of a diguanylate cyclase from Shewanella woodyi with cyclase and phosphodiesterase activities Mol. BioSyst. 6, 1561-1564
    • (2010) Mol. BioSyst. , vol.6 , pp. 1561-1564
    • Liu, N.1    Pak, T.2    Boon, E.M.3
  • 32
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., Elzer, P. H., Hill, D. S., Robertson, G. T., Farris, M. A., Roop, R. M., II, and Peterson, K. M. (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes Gene 166, 175-176
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop, R.M.I.I.6    Peterson, K.M.7
  • 33
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: Roles of flagella, motility, chemotaxis and type I pili
    • DOI 10.1046/j.1365-2958.1998.01061.x
    • Pratt, L. A. and Kolter, R. (1998) Genetic analysis of Escherichia coli biofilm formation: Roles of flagella, motility, chemotaxis and type I pili Mol. Microbiol. 30, 285-293 (Pubitemid 28480180)
    • (1998) Molecular Microbiology , vol.30 , Issue.2 , pp. 285-293
    • Pratt, L.A.1    Kolter, R.2
  • 34
    • 41549091882 scopus 로고    scopus 로고
    • Quorum sensing controls biofilm formation in Vibrio cholerae through modulation of cyclic Di-GMP levels and repression of vpsT
    • DOI 10.1128/JB.01756-07
    • Waters, C. M., Lu, W., Rabinowitz, J. D., and Bassler, B. L. (2008) Quorum sensing controls biofilm formation in Vibrio cholerae through modulation of cyclic di-GMP levels and repression of vpsT J. Bacteriol. 190, 2527-2536 (Pubitemid 351466348)
    • (2008) Journal of Bacteriology , vol.190 , Issue.7 , pp. 2527-2536
    • Waters, C.M.1    Lu, W.2    Rabinowitz, J.D.3    Bassler, B.L.4
  • 35
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • DOI 10.1021/bi970201o
    • Kharitonov, V. G., Sharma, V. S., Magde, D., and Koesling, D. (1997) Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase Biochemistry 36, 6814-6818 (Pubitemid 27242342)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 36
    • 0017112413 scopus 로고
    • Cooperativity in the dissociation of nitric oxide from hemoglobin
    • Moore, E. G. and Gibson, Q. H. (1976) Cooperativity in the dissociation of nitric oxide from hemoglobin J. Biol. Chem. 251, 2788-2794
    • (1976) J. Biol. Chem. , vol.251 , pp. 2788-2794
    • Moore, E.G.1    Gibson, Q.H.2
  • 38
    • 0027408207 scopus 로고
    • Nitric oxide/nucleophile complexes inhibit the in vitro proliferation of A375 melanoma cells via nitric oxide release
    • Maragos, C. M., Wang, J. M., Hrabie, J. A., Oppenheim, J. J., and Keefer, L. K. (1993) Nitric oxide/nucleophile complexes inhibit the in vitro proliferation of A375 melanoma cells via nitric oxide release Cancer Res. 53, 564-568 (Pubitemid 23059437)
    • (1993) Cancer Research , vol.53 , Issue.3 , pp. 564-568
    • Maragos, C.M.1    Ji Ming Wang2    Hrabie, J.A.3    Oppenheim, J.J.4    Keefer, L.K.5
  • 39
    • 0029821342 scopus 로고    scopus 로고
    • 'NONOates' (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: Convenient nitric oxide dosage forms
    • Keefer, L. K., Nims, R. W., Davies, K. M., and Wink, D. A. (1996) "NONOates" (1-substituted diazen-1-ium-1,2-diolates) as nitric oxide donors: Convenient nitric oxide dosage forms Methods Enzymol. 268, 281-293 (Pubitemid 26286370)
    • (1996) Methods in Enzymology , vol.268 , pp. 281-293
    • Keefer, L.K.1    Nims, R.W.2    Davies, K.M.3    Wink, D.A.4
  • 41
    • 0035853035 scopus 로고    scopus 로고
    • Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1
    • DOI 10.1073/pnas.041603998
    • Pervin, S., Singh, R., and Chaudhuri, G. (2001) Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1 Proc. Natl. Acad. Sci. U.S.A. 98, 3583-3588 (Pubitemid 32220888)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.6 , pp. 3583-3588
    • Pervin, S.1    Singh, R.2    Chaudhuri, G.3
  • 42
    • 33749344234 scopus 로고    scopus 로고
    • Urinary excretion of darbepoetin after intravenous vs subcutaneous administration to preterm neonates
    • DOI 10.1038/sj.jp.7211596, PII 7211596
    • Warwood, T. L., Ohls, R. K., Lambert, D. K., Leve, E. A., Veng-Pedersen, P., and Christensen, R. D. (2006) Urinary excretion of darbepoetin after intravenous vs subcutaneous administration to preterm neonates J. Perinatol. 26, 636-639 (Pubitemid 44489569)
    • (2006) Journal of Perinatology , vol.26 , Issue.10 , pp. 636-639
    • Warwood, T.L.1    Ohls, R.K.2    Lambert, D.K.3    Leve, E.A.4    Veng-Pedersen, P.5    Christensen, R.D.6
  • 43
    • 70349783823 scopus 로고    scopus 로고
    • Determinants for the Activation and Autoinhibition of the Diguanylate Cyclase Response Regulator WspR
    • De, N., Navarro, M. V. A. S., Raghavan, R. V., and Sondermann, H. (2009) Determinants for the Activation and Autoinhibition of the Diguanylate Cyclase Response Regulator WspR J. Mol. Biol. 393, 619-633
    • (2009) J. Mol. Biol. , vol.393 , pp. 619-633
    • De, N.1    Navarro, M.V.A.S.2    Raghavan, R.V.3    Sondermann, H.4
  • 44
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
    • DOI 10.1074/jbc.M504429200
    • Christen, M., Christen, B., Folcher, M., Schauerte, A., and Jenal, U. (2005) Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP J. Biol. Chem. 280, 30829-30837 (Pubitemid 41291813)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 45
    • 5844284193 scopus 로고    scopus 로고
    • Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide
    • DOI 10.1021/bi9519718
    • Stone, J. R. and Marletta, M. A. (1996) Spectral and kinetic studies on the activation of soluble guanylate cyclase by nitric oxide Biochemistry 35, 1093-1099 (Pubitemid 26050770)
    • (1996) Biochemistry , vol.35 , Issue.4 , pp. 1093-1099
    • Stone, J.R.1    Marletta, M.A.2
  • 48
    • 36549038207 scopus 로고    scopus 로고
    • Biofilms 2007: Broadened horizons and new emphases
    • DOI 10.1128/JB.00787-07
    • Palmer, R. J., Jr. and Stoodley, P. (2007) Biofilms 2007: Broadened horizons and new emphases J. Bacteriol. 189, 7948-7960 (Pubitemid 350178904)
    • (2007) Journal of Bacteriology , vol.189 , Issue.22 , pp. 7948-7960
    • Palmer Jr., R.J.1    Stoodley, P.2
  • 49
    • 4744349524 scopus 로고    scopus 로고
    • Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
    • DOI 10.1111/j.1365-2958.2004.04269.x
    • 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 (Pubitemid 39315174)
    • (2004) Molecular Microbiology , 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
  • 50
    • 72249093590 scopus 로고    scopus 로고
    • Nitric oxide-mediated dispersal in single- and multi-species biofilms of clinically and industrially relevant microorganisms
    • Barraud, N., Storey, M. V., Moore, Z. P., Webb, J. S., Rice, S. A., and Kjelleberg, S. (2009) Nitric oxide-mediated dispersal in single- and multi-species biofilms of clinically and industrially relevant microorganisms Microb. Biotechnol. 2, 370-378
    • (2009) Microb. Biotechnol. , vol.2 , pp. 370-378
    • Barraud, N.1    Storey, M.V.2    Moore, Z.P.3    Webb, J.S.4    Rice, S.A.5    Kjelleberg, S.6
  • 51
    • 72249092095 scopus 로고    scopus 로고
    • Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic di-GMP levels, and enhanced dispersal
    • Barraud, N., Schleheck, D., Klebensberger, J., Webb, J. S., Hassett, D. J., Rice, S. A., and Kjelleberg, S. (2009) Nitric oxide signaling in Pseudomonas aeruginosa biofilms mediates phosphodiesterase activity, decreased cyclic di-GMP levels, and enhanced dispersal J. Bacteriol. 191, 7333-7342
    • (2009) J. Bacteriol. , vol.191 , pp. 7333-7342
    • Barraud, N.1    Schleheck, D.2    Klebensberger, J.3    Webb, J.S.4    Hassett, D.J.5    Rice, S.A.6    Kjelleberg, S.7
  • 52
    • 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., and Spormann, A. M. (2006) Control of formation and cellular detachment from Shewanella oneidensis MR-1 biofilms by cyclic di-GMP J. Bacteriol. 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    Spormann, A.M.7
  • 55
    • 4744349524 scopus 로고    scopus 로고
    • Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
    • DOI 10.1111/j.1365-2958.2004.04269.x
    • 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 (Pubitemid 39315174)
    • (2004) Molecular Microbiology , 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
  • 57
    • 33645296297 scopus 로고    scopus 로고
    • Cyclic-diGMP signal transduction systems in Vibrio cholerae: Modulation of rugosity and biofilm formation
    • Lim, B., Beyhan, S., Meir, J., and Yildiz, F. H. (2006) Cyclic-diGMP signal transduction systems in Vibrio cholerae: Modulation of rugosity and biofilm formation Mol. Microbiol. 60, 331-348
    • (2006) Mol. Microbiol. , vol.60 , pp. 331-348
    • Lim, B.1    Beyhan, S.2    Meir, J.3    Yildiz, F.H.4
  • 58
    • 34247566143 scopus 로고    scopus 로고
    • Role of EAL-containing proteins in multicellular behavior of Salmonella enterica serovar typhimurium
    • DOI 10.1128/JB.01719-06
    • 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 (Pubitemid 46668826)
    • (2007) Journal of Bacteriology , vol.189 , Issue.9 , pp. 3613-3623
    • Simm, R.1    Lusch, A.2    Kader, A.3    Andersson, M.4    Romling, U.5
  • 59
    • 61449200221 scopus 로고    scopus 로고
    • Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli
    • Sommerfeldt, N., Possling, A., Becker, G., Pesavento, C., Tschowri, N., and Hengge, R. (2009) Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli Microbiology 155, 1318-1331
    • (2009) Microbiology , vol.155 , pp. 1318-1331
    • Sommerfeldt, N.1    Possling, A.2    Becker, G.3    Pesavento, C.4    Tschowri, N.5    Hengge, R.6
  • 61
    • 33745726455 scopus 로고    scopus 로고
    • Dynamics of development and dispersal in sessile microbial communities: Examples from Pseudomonas aeruginosa and Pseudomonas putida model biofilms
    • DOI 10.1111/j.1574-6968.2006.00280.x
    • Klausen, M., Gjermansen, M., Kreft, J. U., and Tolker-Nielsen, T. (2006) Dynamics of development and dispersal in sessile microbial communities: Examples from Pseudomonas aeruginosa and Pseudomonas putida model biofilms FEMS Microbiol. Lett. 261, 1-11 (Pubitemid 43999693)
    • (2006) FEMS Microbiology Letters , vol.261 , Issue.1 , pp. 1-11
    • Klausen, M.1    Gjermansen, M.2    Kreft, J.-U.3    Tolker-Nielsen, T.4
  • 62
    • 0037255736 scopus 로고    scopus 로고
    • Are there biofilm-specific physiological pathways beyond a reasonable doubt?
    • Ghigo, J. M. (2003) Are there biofilm-specific physiological pathways beyond a reasonable doubt? Res. Microbiol. 154, 1-8
    • (2003) Res. Microbiol. , vol.154 , pp. 1-8
    • Ghigo, J.M.1
  • 64
    • 0036200207 scopus 로고    scopus 로고
    • Nitric oxide signaling and NO dependent transcriptional control in bacterial denitrification by members of the FNR-CRP regulator family
    • Zumft, W. G. (2002) Nitric oxide signaling and NO dependent transcriptional control in bacterial denitrification by members of the FNR-CRP regulator family J. Mol. Microbiol. Biotechnol. 4, 277-286 (Pubitemid 34256703)
    • (2002) Journal of Molecular Microbiology and Biotechnology , vol.4 , Issue.3 , pp. 277-286
    • Zumft, W.G.1
  • 65
    • 0024243882 scopus 로고
    • Reduction of nitrite to nitric oxide by enteric bacteria
    • DOI 10.1016/S0006-291X(88)80018-4
    • Ji, X. B. and Hollocher, T. C. (1988) Reduction of nitrite to nitric oxide by enteric bacteria Biochem. Biophys. Res. Commun. 157, 106-108 (Pubitemid 19004831)
    • (1988) Biochemical and Biophysical Research Communications , vol.157 , Issue.1 , pp. 106-108
    • Ji, X.B.1    Hollocher, T.C.2
  • 66
    • 39149100341 scopus 로고    scopus 로고
    • Physiological heterogeneity in biofilms
    • DOI 10.1038/nrmicro1838, PII NRMICRO1838
    • Stewart, P. S. and Franklin, M. J. (2008) Physiological heterogeneity in biofilms Nat. Rev. Microbiol. 6, 199-210 (Pubitemid 351256315)
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.3 , pp. 199-210
    • Stewart, P.S.1    Franklin, M.J.2
  • 67
    • 79956225765 scopus 로고    scopus 로고
    • The role of nitric-oxide-synthase-derived nitric oxide in multicellular traits of Bacillus subtilis 3610: Biofilm formation, swarming, and dispersal
    • Schreiber, F., Beutler, M., Enning, D., Lamprecht-Grandio, M., Zafra, O., Gonzalez-Pastor, J., and de Beer, D. (2011) The role of nitric-oxide-synthase- derived nitric oxide in multicellular traits of Bacillus subtilis 3610: Biofilm formation, swarming, and dispersal BMC Microbiol. 11, 111
    • (2011) BMC Microbiol. , vol.11 , pp. 111
    • Schreiber, F.1    Beutler, M.2    Enning, D.3    Lamprecht-Grandio, M.4    Zafra, O.5    Gonzalez-Pastor, J.6    De Beer, D.7
  • 68
    • 77952172681 scopus 로고    scopus 로고
    • Bioluminescence in the Ocean: Origins of Biological, Chemical, and Ecological Diversity
    • Widder, E. A. (2010) Bioluminescence in the Ocean: Origins of Biological, Chemical, and Ecological Diversity Science 328, 704-708
    • (2010) Science , vol.328 , pp. 704-708
    • Widder, E.A.1
  • 69
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • DOI 10.1021/bi00184a036
    • Stone, J. R. and Marletta, M. A. (1994) Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states Biochemistry 33, 5636-5640 (Pubitemid 24163003)
    • (1994) Biochemistry , vol.33 , Issue.18 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 70
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • DOI 10.1021/bi049374l
    • Karow, D. S., Pan, D., Tran, R., Pellicena, P., Presley, A., Mathies, R. A., and Marletta, M. A. (2004) Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis Biochemistry 43, 10203-10211 (Pubitemid 39030911)
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10203-10211
    • Karow, D.S.1    Pan, D.2    Tran, R.3    Pellicena, P.4    Presley, A.5    Mathies, R.A.6    Marletta, M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.