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Volumn 288, Issue 6, 2013, Pages 3739-3752

Oxidation-sensing regulator AbfR regulates oxidative stress responses, bacterial aggregation, and biofilm formation in staphylococcus epidermidis

Author keywords

[No Author keywords available]

Indexed keywords

BIOFILM FORMATION; CRITICAL COMPONENT; CUMENE HYDROPEROXIDE; DE-REPRESSION; DISULFIDE BONDS; EPIDERMIDIS; FUNCTIONAL RESIDUES; HUMAN PATHOGENS; IMPLANTED MEDICAL DEVICES; IN-VITRO ANALYSIS; IN-VIVO; OXIDATIVE STRESS RESPONSE; PSEUDOMONAS AERUGINOSA; REACTIVE OXYGEN SPECIES; REDOX REGULATION; STAPHYLOCOCCUS EPIDERMIDIS;

EID: 84873668524     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.426205     Document Type: Article
Times cited : (25)

References (67)
  • 1
  • 2
    • 0036271350 scopus 로고    scopus 로고
    • Staphylococcus and biofilms
    • Götz, F. (2002) Staphylococcus and biofilms. Mol. Microbiol. 43, 1367-1378
    • (2002) Mol. Microbiol. , vol.43 , pp. 1367-1378
    • Götz, F.1
  • 3
    • 84897975929 scopus 로고    scopus 로고
    • Staphylococcal infections. Mechanisms of biofilm maturation and detachment as critical determinants of pathogenicity
    • Otto, M. (2013) Staphylococcal infections. Mechanisms of biofilm maturation and detachment as critical determinants of pathogenicity. Annu. Aev. Afe. 64, 1-14
    • (2013) Annu. Aev. Afe. , vol.64 , pp. 1-14
    • Otto, M.1
  • 4
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. (2008) Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77, 755-776
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 6
    • 65249105971 scopus 로고    scopus 로고
    • Hydrogen peroxide induced repression of icaADBC transcription and biofilm development in Staphylococcus epi-dermidis
    • Glynn, A. A., O'Donnell, S. T., Molony, D. C., Sheehan, E., McCormack, D. J., and O'Gara, J. P. (2009) Hydrogen peroxide induced repression of icaADBC transcription and biofilm development in Staphylococcus epi-dermidis. J. Orthop. Res. 27, 627-630
    • (2009) J. Orthop. Res. , vol.27 , pp. 627-630
    • Glynn, A.A.1    O'Donnell, S.T.2    Molony, D.C.3    Sheehan, E.4    McCormack, D.J.5    O'Gara, J.P.6
  • 7
    • 79951906200 scopus 로고    scopus 로고
    • Thiol-based redox switches and gene regulation
    • Antelmann, H., and Helmann, J. D. (2011) Thiol-based redox switches and gene regulation. Antioxid. Redox Signal. 14, 1049-1063
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1049-1063
    • Antelmann, H.1    Helmann, J.D.2
  • 8
    • 70349547204 scopus 로고    scopus 로고
    • Management of oxidative stress in Bacillus
    • Zuber, P. (2009) Management of oxidative stress in Bacillus. Annu. Rev. Microbiol. 63, 575-597
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 575-597
    • Zuber, P.1
  • 9
    • 75749157723 scopus 로고    scopus 로고
    • PerR vs OhrR. Selective peroxide sensing in Bacillus subtilis
    • Duarte, V., and Latour, J. M. (2010) PerR vs OhrR. Selective peroxide sensing in Bacillus subtilis. Mol. Biosyst. 6, 316-323
    • (2010) Mol. Biosyst. , vol.6 , pp. 316-323
    • Duarte, V.1    Latour, J.M.2
  • 10
    • 84868603203 scopus 로고    scopus 로고
    • Peroxide-sensing transcriptional regulators in bacteria
    • Dubbs, J. M., and Mongkolsuk, S. (2012) Peroxide-sensing transcriptional regulators in bacteria. Bacteriol. 194, 5495-5503
    • (2012) Bacteriol. , vol.194 , pp. 5495-5503
    • Dubbs, J.M.1    Mongkolsuk, S.2
  • 11
    • 79951505770 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand-me-diated attenuation of DNA binding by MarR family transcriptional regulators
    • Perera, I. C., and Grove, A. (2010) Molecular mechanisms of ligand-me-diated attenuation of DNA binding by MarR family transcriptional regulators. Mol. Cell Biol. 2, 243-254
    • (2010) Mol. Cell Biol. , vol.2 , pp. 243-254
    • Perera, I.C.1    Grove, A.2
  • 12
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., and Helmann, J. D. (2002) The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sei. U.S.A. 99, 6690-6695
    • (2002) Proc. Natl. Acad. Sei. U.S.A. , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 13
    • 34547399134 scopus 로고    scopus 로고
    • A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
    • Lee, J. W., Soonsanga, S., and Helmann, J. D. (2007) A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc. Natl. Acad. Sei. U.S.A. 104, 8743-8748
    • (2007) Proc. Natl. Acad. Sei. U.S.A. , vol.104 , pp. 8743-8748
    • Lee, J.W.1    Soonsanga, S.2    Helmann, J.D.3
  • 14
    • 0034944405 scopus 로고    scopus 로고
    • Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-induc-ible negative regulator, and posttranscriptional modifications
    • Sukchawalit, R., Loprasert, S., Atichartpongkul, S., and Mongkolsuk, S. (2001) Complex regulation of the organic hydroperoxide resistance gene (ohr) from Xanthomonas involves OhrR, a novel organic peroxide-induc-ible negative regulator, and posttranscriptional modifications. Bacteriol. 183, 4405-4412
    • (2001) Bacteriol. , vol.183 , pp. 4405-4412
    • Sukchawalit, R.1    Loprasert, S.2    Atichartpongkul, S.3    Mongkolsuk, S.4
  • 15
    • 77950682314 scopus 로고    scopus 로고
    • Analyses of the regulatory mechanism and physiological roles of Pseudomonas aeruginosa OhrR, a transcription regulator and a sensor of organic hydroperoxides
    • Atichartpongkul, S., Fuangthong, M., Vattanaviboon, P., and Mongkolsuk, S. (2010) Analyses of the regulatory mechanism and physiological roles of Pseudomonas aeruginosa OhrR, a transcription regulator and a sensor of organic hydroperoxides. Bacteriol. 192, 2093-2101
    • (2010) Bacteriol. , vol.192 , pp. 2093-2101
    • Atichartpongkul, S.1    Fuangthong, M.2    Vattanaviboon, P.3    Mongkolsuk, S.4
  • 16
    • 25844514282 scopus 로고    scopus 로고
    • Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family
    • Hong, M., Fuangthong, M., Helmann, J. D., and Brennan, R. G. (2005) Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol. Cell 20, 131-141
    • (2005) Mol. Cell , vol.20 , pp. 131-141
    • Hong, M.1    Fuangthong, M.2    Helmann, J.D.3    Brennan, R.G.4
  • 17
    • 36248933266 scopus 로고    scopus 로고
    • Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR
    • Newberry, K. J., Fuangthong, M., Panmanee, W., Mongkolsuk, S., and Brennan, R. G. (2007) Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR. Mol. Cell 28, 652-664
    • (2007) Mol. Cell , vol.28 , pp. 652-664
    • Newberry, K.J.1    Fuangthong, M.2    Panmanee, W.3    Mongkolsuk, S.4    Brennan, R.G.5
  • 18
    • 31344443334 scopus 로고    scopus 로고
    • Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins
    • Wilkinson, S. P., and Grove, A. (2006) Ligand-responsive transcriptional regulation by members of the MarR family of winged helix proteins. Curr. IssuesMol. Biol. 8, 51-62
    • (2006) Curr. IssuesMol. Biol. , vol.8 , pp. 51-62
    • Wilkinson, S.P.1    Grove, A.2
  • 19
    • 33750230997 scopus 로고    scopus 로고
    • An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus
    • Chen, P. R., Bae, T., Williams, W. A., Duguid, E. M., Rice, P. A., Schneewind, O., and He, C. (2006) An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus. Nat. Chem. Biol. 2, 591-595
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 591-595
    • Chen, P.R.1    Bae, T.2    Williams, W.A.3    Duguid, E.M.4    Rice, P.A.5    Schneewind, O.6    He, C.7
  • 20
    • 51649131425 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa multidrug efflux regulator MexR uses an oxidation-sensing mechanism
    • Chen, H, Hu, J., Chen, P. R., Lan, L., Li, Z., Hicks, L. M., Dinner, A. R., and He, C. (2008) The Pseudomonas aeruginosa multidrug efflux regulator MexR uses an oxidation-sensing mechanism. Proc. Natl. Acad. Sei. U.S.A. 105, 13586-13591
    • (2008) Proc. Natl. Acad. Sei. U.S.A. , vol.105 , pp. 13586-13591
    • Chen, H.1    Hu, J.2    Chen, P.R.3    Lan, L.4    Li, Z.5    Hicks, L.M.6    Dinner, A.R.7    He, C.8
  • 21
    • 72949110182 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection
    • Lan, L., Murray, T. S., Kazmierczak, B. I., and He, C. (2010) Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection. Mol. Microbiol. 75, 76-91
    • (2010) Mol. Microbiol. , vol.75 , pp. 76-91
    • Lan, L.1    Murray, T.S.2    Kazmierczak, B.I.3    He, C.4
  • 23
    • 84859773974 scopus 로고    scopus 로고
    • MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria
    • Aoki, R., Takeda, T., Omata, T., Ihara, IC, and Fujita, Y. (2012) MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria. Biol. Chem. 287, 13500-13507
    • (2012) Biol. Chem. , vol.287 , pp. 13500-13507
    • Aoki, R.1    Takeda, T.2    Omata, T.3    Ihara, I.C.4    Fujita, Y.5
  • 24
    • 0038715856 scopus 로고    scopus 로고
    • Mgr, a novel global regulator in Staphylococcus aureus
    • Luong, T. T., Newell, S. W., and Lee, C. Y. (2003) Mgr, a novel global regulator in Staphylococcus aureus. J. Bacteriol. 185, 3703-3710
    • (2003) J. Bacteriol. , vol.185 , pp. 3703-3710
    • Luong, T.T.1    Newell, S.W.2    Lee, C.Y.3
  • 25
    • 73849088337 scopus 로고    scopus 로고
    • Control of thioredoxin reductase gene (trxB) transcription by SarA in Staphylococcus aureus
    • Ballal, A., and Manna, A. C. (2010) Control of thioredoxin reductase gene (trxB) transcription by SarA in Staphylococcus aureus. J. Bacteriol. 192, 336-345
    • (2010) J. Bacteriol. , vol.192 , pp. 336-345
    • Ballal, A.1    Manna, A.C.2
  • 26
    • 84865648246 scopus 로고    scopus 로고
    • Redox active thiol sensors of oxidative and nitrosative stress
    • Vazquez-Torres, A. (2012) Redox active thiol sensors of oxidative and nitrosative stress. Antioxid. Redox Signal. 17, 1201-1214
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1201-1214
    • Vazquez-Torres, A.1
  • 27
    • 29144482705 scopus 로고    scopus 로고
    • Allelic replacement in Staphylococcus aureus with inducible counter-selection
    • Bae, T., and Schneewind, O. (2006) Allelic replacement in Staphylococcus aureus with inducible counter-selection. Plasmid 55, 58-63
    • (2006) Plasmid , vol.55 , pp. 58-63
    • Bae, T.1    Schneewind, O.2
  • 29
    • 0032728823 scopus 로고    scopus 로고
    • Regulated anti-sense RNA eliminates alpha-toxin virulence in Staphylococcus aureus infection
    • Ji, Y., Marra, A., Rosenberg, M., and Woodnutt, G. (1999) Regulated anti-sense RNA eliminates alpha-toxin virulence in Staphylococcus aureus infection, Bacteriol. 181, 6585-6590
    • (1999) Bacteriol. , vol.181 , pp. 6585-6590
    • Ji, Y.1    Marra, A.2    Rosenberg, M.3    Woodnutt, G.4
  • 31
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié, S. (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 32
    • 33745875402 scopus 로고    scopus 로고
    • Identification of the DNA bases of a DNase i footprint by the use of dye primer sequencing on an automated capillary DNA analysis instrument
    • Zianni, M., Tessanne, IC, Merighi, M., Laguna, R., and Tabita, F. R. (2006) Identification of the DNA bases of a DNase I footprint by the use of dye primer sequencing on an automated capillary DNA analysis instrument. J. Biomol. Tech. 17, 103-113
    • (2006) J. Biomol. Tech. , vol.17 , pp. 103-113
    • Zianni, M.1    Tessanne, I.C.2    Merighi, M.3    Laguna, R.4    Tabita, F.R.5
  • 34
    • 0028103275 scopus 로고
    • The CCP4 suite. Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite. Programs for protein crystallography. Acte Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acte Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 35
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 36
  • 41
    • 33845955265 scopus 로고    scopus 로고
    • Formation and properties of in vitro biofilms of ica-negative Staphylococcus epidermidis clinical isolates
    • Qin, Z., Yang, X., Yang, L., Jiang, J., Ou, Y., Molin, S., and Qu, D. (2007) Formation and properties of in vitro biofilms of ica-negative Staphylococcus epidermidis clinical isolates. Med. Microbiol. 56, 83-93
    • (2007) Med. Microbiol. , vol.56 , pp. 83-93
    • Qin, Z.1    Yang, X.2    Yang, L.3    Jiang, J.4    Ou, Y.5    Molin, S.6    Qu, D.7
  • 42
    • 84863235693 scopus 로고    scopus 로고
    • Thiazolidione derivatives targeting the histidine kinase YycG are effective against both planktonic and biofilm-associated Staphylococcus epidermidis
    • Huang, R. Z., Zheng, L. IC, Liu, H. Y., Pan, B., Hu, J., Zhu, T., Wang, W., Jiang, D. B., Wu, Y., Wu, Y. C, Han, S. Q., and Qu, D. (2012) Thiazolidione derivatives targeting the histidine kinase YycG are effective against both planktonic and biofilm-associated Staphylococcus epidermidis. Acta Pharmacol. Sin. 33, 418-425
    • (2012) Acta Pharmacol. Sin. , vol.33 , pp. 418-425
    • Huang, R.Z.1    Zheng, L.I.C.2    Liu, H.Y.3    Pan, B.4    Hu, J.5    Zhu, T.6    Wang, W.7    Jiang, D.B.8    Wu, Y.9    Wu, Y.C.10    Han, S.Q.11    Qu, D.12
  • 43
    • 33745252231 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase. A target and generator of oxidative stress
    • Tretter, L., and Adam-Vizi, V. (2005) Alpha-ketoglutarate dehydrogenase. A target and generator of oxidative stress. Philos. Trans. R. Soc. Lond B Biol. Sei. 360, 2335-2345
    • (2005) Philos. Trans. R. Soc. Lond B Biol. Sei. , vol.360 , pp. 2335-2345
    • Tretter, L.1    Adam-Vizi, V.2
  • 44
    • 8944258926 scopus 로고    scopus 로고
    • Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat
    • Moore, T. D., and Sparling, P. F. (1996) Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat. Bacteriol. 178, 4301-4305
    • (1996) Bacteriol. , vol.178 , pp. 4301-4305
    • Moore, T.D.1    Sparling, P.F.2
  • 45
    • 0034887133 scopus 로고    scopus 로고
    • The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution
    • Alekshun, M. N., Levy, S. B., Mealy, T. R., Seaton, B. A., and Head, J. F. (2001) The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Wat Struct. Biol. 8, 710-714
    • (2001) Wat Struct. Biol. , vol.8 , pp. 710-714
    • Alekshun, M.N.1    Levy, S.B.2    Mealy, T.R.3    Seaton, B.A.4    Head, J.F.5
  • 46
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • Poor, C. B., Chen, P. R., Duguid, E., Rice, P. A., and He, C (2009) Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus. J. Biol. Chem. 284, 23517-23524
    • (2009) J. Biol. Chem. , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 47
    • 79959326641 scopus 로고    scopus 로고
    • Crystal structures of SlyA protein, a master virulence regulator of Salmonella, in free and DNA-bound states
    • Dolan, K. T., Duguid, E. M., and He, C. (2011) Crystal structures of SlyA protein, a master virulence regulator of Salmonella, in free and DNA-bound states. Biol. Chem. 286, 22178-22185
    • (2011) Biol. Chem. , vol.286 , pp. 22178-22185
    • Dolan, K.T.1    Duguid, E.M.2    He, C.3
  • 50
    • 77956229209 scopus 로고    scopus 로고
    • Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR
    • Chen, H, Yi, C, Zhang, J., Zhang, W., Ge, Z., Yang, C. G., and He, C. (2010) Structural insight into the oxidation-sensing mechanism of the antibiotic resistance of regulator MexR. EMBORep. 11, 685-690
    • (2010) EMBORep. , vol.11 , pp. 685-690
    • Chen, H.1    Yi, C.2    Zhang, J.3    Zhang, W.4    Ge, Z.5    Yang, C.G.6    He, C.7
  • 53
    • 15544372331 scopus 로고    scopus 로고
    • Rat/MgrA, a regulator of autolysis, is a regulator of virulence genes in Staphylococcus aureus
    • Ingavale, S., van Wamel, W., Luong, T. T., Lee, C Y., and Cheung, A. L. (2005) Rat/MgrA, a regulator of autolysis, is a regulator of virulence genes in Staphylococcus aureus. Infect. Immun. 73, 1423-1431
    • (2005) Infect. Immun. , vol.73 , pp. 1423-1431
    • Ingavale, S.1    Van Wamel, W.2    Luong, T.T.3    Lee, C.Y.4    Cheung, A.L.5
  • 54
    • 84862285306 scopus 로고    scopus 로고
    • Staphylococcus aureus CymR is a new thiol-based oxidation-sensing regulator of stress resistance and oxidative response
    • Ji, Q., Zhang, L., Sun, F., Deng, X., Liang, H, Bae, T., and He, C. (2012) Staphylococcus aureus CymR is a new thiol-based oxidation-sensing regulator of stress resistance and oxidative response. J. Biol. Chem. 287, 21102-21109
    • (2012) J. Biol. Chem. , vol.287 , pp. 21102-21109
    • Ji, Q.1    Zhang, L.2    Sun, F.3    Deng, X.4    Liang, H.5    Bae, T.6    He, C.7
  • 56
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P. J., Bennik, M. H., and Demple, B. (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. Bacteriol. 183, 3890-3902
    • (2001) Bacteriol. , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 57
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi, H., Kim, S., Mukhopadhyay, P., Cho, S., Woo, J., Storz, G., and Ryu, S. E. (2001) Structural basis of the redox switch in the OxyR transcription factor. Cell 105, 103-113
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.E.7
  • 58
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F., and Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 62
    • 70349816733 scopus 로고    scopus 로고
    • Role of reactive oxygen species in antibiotic action and resistance
    • Dwyer, D. J., Kohanski, M. A., and Collins, J. J. (2009) Role of reactive oxygen species in antibiotic action and resistance. Curr. Opin. Microbiol. 12, 482-489
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 482-489
    • Dwyer, D.J.1    Kohanski, M.A.2    Collins, J.J.3
  • 63
    • 42949109357 scopus 로고    scopus 로고
    • Wall teichoic acids are dispensable for anchoring the PNAG exopolysaccharide to the Staphylococcus aureus cell surface
    • Vergara-Irigaray, M., Maira-Litrân, T., Merino, N., Pier, G. B., Penadés, J. R., and Lasa, I. (2008) Wall teichoic acids are dispensable for anchoring the PNAG exopolysaccharide to the Staphylococcus aureus cell surface. Microbiology 154, 865-877
    • (2008) Microbiology , vol.154 , pp. 865-877
    • Vergara-Irigaray, M.1    Maira-Litrân, T.2    Merino, N.3    Pier, G.B.4    Penadés, J.R.5    Lasa, I.6
  • 64
    • 79951498487 scopus 로고    scopus 로고
    • Mutation of tagO reveals an essential role for wall teichoic acids in Staphylococcus epider-midis biofilm development
    • Holland, L. M., Conlon, B., and O'Gara, J. P. (2011) Mutation of tagO reveals an essential role for wall teichoic acids in Staphylococcus epider-midis biofilm development. Microbiology 157, 408-418
    • (2011) Microbiology , vol.157 , pp. 408-418
    • Holland, L.M.1    Conlon, B.2    O'Gara, J.P.3
  • 65
    • 77953236848 scopus 로고    scopus 로고
    • Current concepts in biofilm formation of Staphylococcus epidermidis
    • Fey, P. D., and Olson, M. E. (2010) Current concepts in biofilm formation of Staphylococcus epidermidis. Future Microbiol. 5, 917-933
    • (2010) Future Microbiol. , vol.5 , pp. 917-933
    • Fey, P.D.1    Olson, M.E.2
  • 66
    • 84863760498 scopus 로고    scopus 로고
    • In vitro oxidant effects of D-glucosamine reduce adhesion and biofilm formation of Staphylococcus epidermidis
    • Aiassa, V., Barnes, A. I., and Albesa, I. (2012) In vitro oxidant effects of D-glucosamine reduce adhesion and biofilm formation of Staphylococcus epidermidis. Rev. Argent Microbiol. 44, 16-20
    • (2012) Rev. Argent Microbiol. , vol.44 , pp. 16-20
    • Aiassa, V.1    Barnes, A.I.2    Albesa, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.