메뉴 건너뛰기




Volumn 53, Issue 4, 2004, Pages 1135-1146

Structure of the Pseudomonas aeruginosa acyl-homoserilactone synthase LasI

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; CARRIER PROTEIN; HOMOSERINE; HOMOSERINELACTONE SYNTHASE LASL; S ADENOSYLMETHIONINE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 4344612832     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04211.x     Document Type: Article
Times cited : (148)

References (56)
  • 1
    • 0032560537 scopus 로고    scopus 로고
    • A negative regulator mediates quorum-sensing control of exopolysaccharide production in Pantoea stewartii subsp. stewartii
    • Beck von Bodman, S., Majerczak, D.R., and Coplin, D.L. (1998) A negative regulator mediates quorum-sensing control of exopolysaccharide production in Pantoea stewartii subsp. stewartii. Proc Natl Acad Sci USA 95: 7687-7692.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7687-7692
    • Beck Von Bodman, S.1    Majerczak, D.R.2    Coplin, D.L.3
  • 4
    • 0035318081 scopus 로고    scopus 로고
    • Quorum-sensing genes in Pseudomonas aeruginosa biofilms: Their role and expression patterns
    • De Kievit, T.R., Gillis, R., Marx, S., Brown, C., and Iglewski, B.H. (2001) Quorum-sensing genes in Pseudomonas aeruginosa biofilms: their role and expression patterns. Appl Environ Microbiol 67: 1865-1873.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1865-1873
    • De Kievit, T.R.1    Gillis, R.2    Marx, S.3    Brown, C.4    Iglewski, B.H.5
  • 5
    • 0033862847 scopus 로고    scopus 로고
    • Bacterial quorum sensing in pathogenic relationships
    • De Kievit, T.R., and Iglewski, B.H. (2000) Bacterial quorum sensing in pathogenic relationships. Infect Immun 68: 4839-4849.
    • (2000) Infect Immun , vol.68 , pp. 4839-4849
    • De Kievit, T.R.1    Iglewski, B.H.2
  • 6
    • 0037129841 scopus 로고    scopus 로고
    • Role of the Pseudomonas aeruginosa las and rhI quorum-sensing systems in rhII regulation
    • De Kievit, T.R., Kakai, Y., Register, J.K., Pesci, E.C., and Iglewski, B.H. (2002) Role of the Pseudomonas aeruginosa las and rhI quorum-sensing systems in rhII regulation. FEMS Microbiol Lett 212: 101-106.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 101-106
    • De Kievit, T.R.1    Kakai, Y.2    Register, J.K.3    Pesci, E.C.4    Iglewski, B.H.5
  • 7
    • 0035859128 scopus 로고    scopus 로고
    • Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase
    • Dong, Y.-H., Wang, L.-H., Xu, J.-L., Zhang, H.-B., Zhang, X.-F., and Zhang, L.-H. (2001) Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 411: 813-817.
    • (2001) Nature , vol.411 , pp. 813-817
    • Dong, Y.-H.1    Wang, L.-H.2    Xu, J.-L.3    Zhang, H.-B.4    Zhang, X.-F.5    Zhang, L.-H.6
  • 9
    • 0001890923 scopus 로고    scopus 로고
    • Signal generation in autoinduction systems: Synthesis of acylated homoserine lactones by LuxI-type proteins
    • Dunny, G., and Winans, S.C. (eds). Washington: AMS Press
    • Fuqua, C., and Eberhard, A. (1999) Signal generation in autoinduction systems: synthesis of acylated homoserine lactones by LuxI-type proteins. In Cell-Cell Communication in Bacteria. Dunny, G., and Winans, S.C. (eds). Washington: AMS Press, pp. 211-230.
    • (1999) Cell-Cell Communication in Bacteria , pp. 211-230
    • Fuqua, C.1    Eberhard, A.2
  • 10
    • 0036731699 scopus 로고    scopus 로고
    • Listening in on bacteria: Acyl-homoserine lactone signalling
    • Fuqua, C., and Greenberg, E.P. (2002) Listening in on bacteria: acyl-homoserine lactone signalling. Nature Rev 3: 685-695.
    • (2002) Nature Rev , vol.3 , pp. 685-695
    • Fuqua, C.1    Greenberg, E.P.2
  • 11
    • 0027121375 scopus 로고
    • Experimental conditions may affect reproducibility of the beta-galactosidase assay
    • Giacomini, A., Corich, V., Ollero, F.J., Squartini, A., and Nuti, M.P. (1992) Experimental conditions may affect reproducibility of the beta-galactosidase assay. FEMS Microbiol Lett 79: 87-90.
    • (1992) FEMS Microbiol Lett , vol.79 , pp. 87-90
    • Giacomini, A.1    Corich, V.2    Ollero, F.J.3    Squartini, A.4    Nuti, M.P.5
  • 12
    • 4344572524 scopus 로고    scopus 로고
    • Crystallization of Pseudomonas aeruginosa AHL synthase LasI using beta-turn crystal engineering
    • Gould, T.A., Watson, W.T., Choi, S.H., Schweizer, H.P., and Churchill, M.E.A. (2004) Crystallization of Pseudomonas aeruginosa AHL synthase LasI using beta-turn crystal engineering. Acta Crystallogr D D60: 5118-5120.
    • (2004) Acta Crystallogr D , vol.D60 , pp. 5118-5120
    • Gould, T.A.1    Watson, W.T.2    Choi, S.H.3    Schweizer, H.P.4    Churchill, M.E.A.5
  • 13
    • 0030762454 scopus 로고    scopus 로고
    • Mutational analysis of the Vibrio fischeri LuxI polypeptide: Critical regions of an auto-inducer synthase
    • Hanzelka, B.L., Stevens, A.M., Parsek, M.R., Crone, T.J., and Greenberg, E.P. (1997) Mutational analysis of the Vibrio fischeri LuxI polypeptide: critical regions of an auto-inducer synthase. J Bacteriol 179: 4882-4887.
    • (1997) J Bacteriol , vol.179 , pp. 4882-4887
    • Hanzelka, B.L.1    Stevens, A.M.2    Parsek, M.R.3    Crone, T.J.4    Greenberg, E.P.5
  • 14
    • 0041989633 scopus 로고    scopus 로고
    • Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors
    • Hentzer, M., Wu, H., Andersen, J.B., Riedel, K., Rasmussen, T.B., Bagge, N., et al. (2003) Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors. EMBO J 22: 3803-3815.
    • (2003) EMBO J , vol.22 , pp. 3803-3815
    • Hentzer, M.1    Wu, H.2    Andersen, J.B.3    Riedel, K.4    Rasmussen, T.B.5    Bagge, N.6
  • 15
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 Å resolution with a bisubstrate analog
    • Hickman, A.B., Namboodiri, M.A., Klein, D.C., and Dyda, F. (1999) The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97: 361-369.
    • (1999) Cell , vol.97 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.2    Klein, D.C.3    Dyda, F.4
  • 16
    • 0032882026 scopus 로고    scopus 로고
    • Construction and use of low-copy number T7 expression vectors for purification of problem proteins: Purification of Mycobacterium tuberculosis RmID and Pseudomonas aeruginosa LasI and RhII proteins, and functional analysis of purified RhII
    • Hoang, T.T., Ma, Y., Stern, R.J., McNeil, M.R., and Schweizer, H.P. (1999) Construction and use of low-copy number T7 expression vectors for purification of problem proteins: purification of Mycobacterium tuberculosis RmID and Pseudomonas aeruginosa LasI and RhII proteins, and functional analysis of purified RhII. Gene 237: 361-371.
    • (1999) Gene , vol.237 , pp. 361-371
    • Hoang, T.T.1    Ma, Y.2    Stern, R.J.3    McNeil, M.R.4    Schweizer, H.P.5
  • 17
    • 0036952586 scopus 로고    scopus 로고
    • Beta-ketoacyl acyl carrier protein reductase (FabG) activity of the fatty acid biosynthetic pathway is a determining factor of 3-oxo-homoserine lactone acyl chain lengths
    • Hoang, T.T., Sullivan, S.A., Cusick, J.K., and Schweizer, H.P. (2002) Beta-ketoacyl acyl carrier protein reductase (FabG) activity of the fatty acid biosynthetic pathway is a determining factor of 3-oxo-homoserine lactone acyl chain lengths. Microbiology 148: 3849-3856.
    • (2002) Microbiology , vol.148 , pp. 3849-3856
    • Hoang, T.T.1    Sullivan, S.A.2    Cusick, J.K.3    Schweizer, H.P.4
  • 18
    • 0037192859 scopus 로고    scopus 로고
    • Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis
    • Huang, C.C., Smith, C.V., Glickman, M.S., Jacobs, W.R., Jr, and Sacchettini, J.C. (2002) Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis. J Biol Chem 277: 11559-11569.
    • (2002) J Biol Chem , vol.277 , pp. 11559-11569
    • Huang, C.C.1    Smith, C.V.2    Glickman, M.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjelgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47: 110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0028148276 scopus 로고
    • Multiple N-acyl-L-homoserine lactone autoinducers of luminescence in the marine symbiotic bacterium Vibrio fischeri
    • Kuo, A., Blough, N.V., and Dunlap, P.V. (1994) Multiple N-acyl-L-homoserine lactone autoinducers of luminescence in the marine symbiotic bacterium Vibrio fischeri. J Bacteriol 176: 7558-7565.
    • (1994) J Bacteriol , vol.176 , pp. 7558-7565
    • Kuo, A.1    Blough, N.V.2    Dunlap, P.V.3
  • 22
    • 0034460299 scopus 로고    scopus 로고
    • Metabolism of acyl-homoserine lactone quorum-sensing signals by Variovorax paradoxus
    • Leadbetter, J.R., and Greenberg, E.P. (2000) Metabolism of acyl-homoserine lactone quorum-sensing signals by Variovorax paradoxus. J Bacteriol 182: 6921-6926.
    • (2000) J Bacteriol , vol.182 , pp. 6921-6926
    • Leadbetter, J.R.1    Greenberg, E.P.2
  • 24
    • 0036786039 scopus 로고    scopus 로고
    • Characterization of the Sinorhizobium meliloti sinR/sinI locus and the production of novel N-acyl homoserine lactones
    • Marketon, M.M., Gronquist, M.R., Eberhard, A., and Gonzalez, J.E. (2002) Characterization of the Sinorhizobium meliloti sinR/sinI locus and the production of novel N-acyl homoserine lactones. J Bacteriol 184: 5686-5695.
    • (2002) J Bacteriol , vol.184 , pp. 5686-5695
    • Marketon, M.M.1    Gronquist, M.R.2    Eberhard, A.3    Gonzalez, J.E.4
  • 25
    • 0035313803 scopus 로고    scopus 로고
    • Histone acetyltransferases: Function, structure, and catalysis
    • Marmorstein, R., and Roth, S.Y. (2001) Histone acetyltransferases: function, structure, and catalysis. Curr Opin Genet Dev 11: 155-161.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 155-161
    • Marmorstein, R.1    Roth, S.Y.2
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 28
    • 0029980095 scopus 로고    scopus 로고
    • Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates
    • Moré, M.I., Finger, L.D., Stryker, J.L., Fuqua, C., Eberhard, A., and Winans, S.C. (1996) Enzymatic synthesis of a quorum-sensing autoinducer through use of defined substrates. Science 272: 1655-1658.
    • (1996) Science , vol.272 , pp. 1655-1658
    • Moré, M.I.1    Finger, L.D.2    Stryker, J.L.3    Fuqua, C.4    Eberhard, A.5    Winans, S.C.6
  • 29
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta: Serotonin N-acetyltransferase complex - Role for scaffolding in enzyme regulation
    • Obsil, T., Ghirlando, R., Klein, D.C., Ganguly, S., and Dyda, F. (2001) Crystal structure of the 14-3-3zeta: serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation. Cell 105: 257-267.
    • (2001) Cell , vol.105 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris, K.D., Lin, L., Tam, A., Mathew, R., Hixon, J., Stahl, M., et al. (2000) Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure Fold Des 15: 883-895.
    • (2000) Structure Fold des , vol.15 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6
  • 32
    • 0034254922 scopus 로고    scopus 로고
    • Acyl-homoserine lactone quorum sensing in Gram-negative bacteria: A signaling mechanism involved in the association with higher organisms
    • Parsek, M.R., and Greenberg, E.P. (2000) Acyl-homoserine lactone quorum sensing in Gram-negative bacteria: a signaling mechanism involved in the association with higher organisms. Proc Natl Acad Sci USA 97: 8789-8793.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8789-8793
    • Parsek, M.R.1    Greenberg, E.P.2
  • 33
    • 0030732985 scopus 로고    scopus 로고
    • Analysis of random and site-directed mutations in rhII, a Pseudomonas aeruginosa gene encoding an acyl homoserine lactone synthase
    • Parsek, M.R., Schaefer, A.L., and Greenberg, E.P. (1997) Analysis of random and site-directed mutations in rhII, a Pseudomonas aeruginosa gene encoding an acyl homoserine lactone synthase. Mol Microbiol 26: 301-310.
    • (1997) Mol Microbiol , vol.26 , pp. 301-310
    • Parsek, M.R.1    Schaefer, A.L.2    Greenberg, E.P.3
  • 36
    • 0037156349 scopus 로고    scopus 로고
    • New synthetic analogues of N-acyl homoserine lactones as agonists or antagonists of transcriptional regulators involved in bacterial quorum sensing
    • Reverchon, S., Chantegrel, B., Deshayes, C., Doutheau, A., and Cotte-Pattat, N. (2002) New synthetic analogues of N-acyl homoserine lactones as agonists or antagonists of transcriptional regulators involved in bacterial quorum sensing. Bioorg Med Chem Lett 12: 1153-1157.
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 1153-1157
    • Reverchon, S.1    Chantegrel, B.2    Deshayes, C.3    Doutheau, A.4    Cotte-Pattat, N.5
  • 37
    • 0032755655 scopus 로고    scopus 로고
    • Contribution of quorum sensing to the virulence of Pseudomonas aeruginosa in burn wound infections
    • Rumbaugh, K.P., Griswold, J.A., Iglewski, B.H., and Hamood, A.N. (1999) Contribution of quorum sensing to the virulence of Pseudomonas aeruginosa in burn wound infections. Infect Immun 67: 5853-5862.
    • (1999) Infect Immun , vol.67 , pp. 5853-5862
    • Rumbaugh, K.P.1    Griswold, J.A.2    Iglewski, B.H.3    Hamood, A.N.4
  • 38
    • 0348236990 scopus 로고    scopus 로고
    • Bacterial communication and possible application in control and therapy of bacterial diseases
    • Rychlik, I., Volf, J., and Sevcik, M. (2000) Bacterial communication and possible application in control and therapy of bacterial diseases. Vet Med 45: 181-188.
    • (2000) Vet Med , vol.45 , pp. 181-188
    • Rychlik, I.1    Volf, J.2    Sevcik, M.3
  • 39
    • 0033931441 scopus 로고    scopus 로고
    • Detection, purification, and structural elucidation of the acylhomoserine lactone inducer of Vibrio fischeri luminescence and other related molecules
    • Schaefer, A.L., Hanzelka, B.L., Parsek, M.R., and Greenberg, E.P. (2000) Detection, purification, and structural elucidation of the acylhomoserine lactone inducer of Vibrio fischeri luminescence and other related molecules. Methods Enzymol 305: 288-301.
    • (2000) Methods Enzymol , vol.305 , pp. 288-301
    • Schaefer, A.L.1    Hanzelka, B.L.2    Parsek, M.R.3    Greenberg, E.P.4
  • 40
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert, H.L., Blumenthal, R.M., and Cheng, X. (2003) Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 28: 329-335.
    • (2003) Trends Biochem Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 41
    • 0037378570 scopus 로고    scopus 로고
    • Identification, timing, and signal specificity of Pseudomonas aeruginosa quorum-controlled genes: A transcriptome analysis
    • Schuster, M., Lostroh, C.P., Ogi, T., and Greenberg, E.P. (2003) Identification, timing, and signal specificity of Pseudomonas aeruginosa quorum-controlled genes: a transcriptome analysis. J Bacteriol 185: 2066-2079.
    • (2003) J Bacteriol , vol.185 , pp. 2066-2079
    • Schuster, M.1    Lostroh, C.P.2    Ogi, T.3    Greenberg, E.P.4
  • 42
    • 0028967496 scopus 로고
    • Activation of the Pseudomonas aeruginosa lasI gene by LasR and the Pseudomonas autoinducer PAI: An autoinduction regulatory hierarchy
    • Seed, C.P., Passador, L., and Iglewski, B.H. (1995) Activation of the Pseudomonas aeruginosa lasI gene by LasR and the Pseudomonas autoinducer PAI: an autoinduction regulatory hierarchy. J Bacteriol 177: 654-659.
    • (1995) J Bacteriol , vol.177 , pp. 654-659
    • Seed, C.P.1    Passador, L.2    Iglewski, B.H.3
  • 43
    • 0036174583 scopus 로고    scopus 로고
    • Effects of quorum-sensing deficiency on Pseudomonas aeruginosa biofilm formation and antibiotic resistance
    • Shih, P.C., and Huang, C.T. (2002) Effects of quorum-sensing deficiency on Pseudomonas aeruginosa biofilm formation and antibiotic resistance. J Antimicrob Chemother 49: 309-314.
    • (2002) J Antimicrob Chemother , vol.49 , pp. 309-314
    • Shih, P.C.1    Huang, C.T.2
  • 44
    • 0037256665 scopus 로고    scopus 로고
    • Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthetic autoinducer analogs
    • Smith, K.M., Bu, Y., and Suga, H. (2003) Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthetic autoinducer analogs. Chem Biol 10: 81-89.
    • (2003) Chem Biol , vol.10 , pp. 81-89
    • Smith, K.M.1    Bu, Y.2    Suga, H.3
  • 45
    • 0346969987 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa quorum sensing as a potential antimicrobial target
    • Smith, R.S., and Iglewski, B.H. (2003) Pseudomonas aeruginosa quorum sensing as a potential antimicrobial target. J Clin Invest 112: 1460-1465.
    • (2003) J Clin Invest , vol.112 , pp. 1460-1465
    • Smith, R.S.1    Iglewski, B.H.2
  • 46
    • 0002794364 scopus 로고    scopus 로고
    • N-acylhomoserine lactones and quorum sensing in Proteobacteria
    • Dunny, G., and Winans, S.C. (eds). Washington: ASM Press
    • Swift, S., Williams, P., and Stewart, G.S.A.B. (1999) N-acylhomoserine lactones and quorum sensing in Proteobacteria. In Cell-Cell Communication in Bacteria. Dunny, G., and Winans, S.C. (eds). Washington: ASM Press, pp. 291-313.
    • (1999) Cell-Cell Communication in Bacteria , pp. 291-313
    • Swift, S.1    Williams, P.2    Stewart, G.S.A.B.3
  • 47
    • 0030045365 scopus 로고    scopus 로고
    • Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection
    • Tang, H.B., DiMango, E., Bryan, R., Gambello, M., Iglewski, B.H., Goldberg, J.B., and Prince, A. (1996) Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection. Infect Immun 64: 37-43.
    • (1996) Infect Immun , vol.64 , pp. 37-43
    • Tang, H.B.1    DiMango, E.2    Bryan, R.3    Gambello, M.4    Iglewski, B.H.5    Goldberg, J.B.6    Prince, A.7
  • 48
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • Tanner, K.G., Trievel, R.C., Huo, M.-H., Howard, R.M., Berger, S.L., Allis, C.D., et al. (1999) Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. J Biol Chem 274: 18157-18160.
    • (1999) J Biol Chem , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Huo, M.-H.3    Howard, R.M.4    Berger, S.L.5    Allis, C.D.6
  • 49
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T.C. (2000) Maximum-likelihood density modification. Acta Crystallogr D56: 965-972.
    • (2000) Acta Crystallogr , vol.D56 , pp. 965-972
    • Terwilliger, T.C.1
  • 50
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T.C., and Berendzen, J. (1999) Automated structure solution for MIR and MAD. Acta Crystallogr D55: 849-861.
    • (1999) Acta Crystallogr , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 51
    • 0031923690 scopus 로고    scopus 로고
    • In vivo evidence that S-adenosylmethionine and fatty acid synthesis intermediates are the substrates for the LuxI family of autoinducer synthases
    • Val, D.L., and Cronan, J.E.J. (1998) In vivo evidence that S-adenosylmethionine and fatty acid synthesis intermediates are the substrates for the LuxI family of autoinducer synthases. J Bacteriol 180: 2644-2651.
    • (1998) J Bacteriol , vol.180 , pp. 2644-2651
    • Val, D.L.1    Cronan, J.E.J.2
  • 52
    • 0037377827 scopus 로고    scopus 로고
    • Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: Effects of growth phase and environment
    • Wagner, V.E., Bushnell, D., Passador, L., Brooks, A.I., and Iglewski, B.H. (2003) Microarray analysis of Pseudomonas aeruginosa quorum-sensing regulons: effects of growth phase and environment. J Bacteriol 185: 2080-2095.
    • (2003) J Bacteriol , vol.185 , pp. 2080-2095
    • Wagner, V.E.1    Bushnell, D.2    Passador, L.3    Brooks, A.I.4    Iglewski, B.H.5
  • 53
    • 0036204586 scopus 로고    scopus 로고
    • Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing
    • Watson, W.T., Minogue, T.D., Val, D.L., Beck von Bodman, S., and Churchill, M.E.A. (2002) Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing. Mol Cell 9: 685-694.
    • (2002) Mol Cell , vol.9 , pp. 685-694
    • Watson, W.T.1    Minogue, T.D.2    Val, D.L.3    Beck Von Bodman, S.4    Churchill, M.E.A.5
  • 55
    • 0035070998 scopus 로고    scopus 로고
    • Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria
    • Withers, H., Swift, S., and Williams, P. (2001) Quorum sensing as an integral component of gene regulatory networks in Gram-negative bacteria. Curr Opin Microbiol 4: 186-193.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 186-193
    • Withers, H.1    Swift, S.2    Williams, P.3
  • 56
    • 0036830560 scopus 로고    scopus 로고
    • The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate
    • Yan, Y., Harper, S., Speicher, D.W., and Marmorstein, R. (2002) The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nature Struct Biol 9: 862-869.
    • (2002) Nature Struct Biol , vol.9 , pp. 862-869
    • Yan, Y.1    Harper, S.2    Speicher, D.W.3    Marmorstein, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.