Show simple item record

Initial characterization of the Streptococcus gordonii htpX gene

dc.contributor.authorVickerman, M. M.en_US
dc.contributor.authorMather, N. M.en_US
dc.contributor.authorMinick, P. E.en_US
dc.contributor.authorEdwards, C. A.en_US
dc.date.accessioned2010-06-01T20:46:19Z
dc.date.available2010-06-01T20:46:19Z
dc.date.issued2002-02en_US
dc.identifier.citationVickerman, M. M . ; Mather, N. M . ; Minick, P. E . ; Edwards, C. A . (2002). "Initial characterization of the Streptococcus gordonii htpX gene." Oral Microbiology and Immunology 17(1): 22-31. <http://hdl.handle.net/2027.42/73872>en_US
dc.identifier.issn0902-0055en_US
dc.identifier.issn1399-302Xen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/73872
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=11860552&dopt=citationen_US
dc.format.extent305411 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Science, Ltden_US
dc.rights© Munksgaard 2002en_US
dc.subject.otherOral Streptococcien_US
dc.subject.otherGlucansen_US
dc.subject.otherBacterial Adhesionen_US
dc.subject.otherHeat Shocken_US
dc.titleInitial characterization of the Streptococcus gordonii htpX geneen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelDentistryen_US
dc.subject.hlbsecondlevelMicrobiology and Immunologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Cell Biology and Anatomy, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Oral Surgery and Hospital Dentistry, School of Dentistry, anden_US
dc.contributor.affiliationotherDepartment of Microbiology and Immunology, School of Medicine, Indiana University, Indianapolis, IN, USA anden_US
dc.contributor.affiliationotherDepartment of Microbiology and Immunolgy anden_US
dc.identifier.pmid11860552en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/73872/1/j.0902-0055.2001.00000.x.pdf
dc.identifier.doi10.1046/j.0902-0055.2001.00000.xen_US
dc.identifier.sourceOral Microbiology and Immunologyen_US
dc.identifier.citedreferenceAltschul SG, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990: 215: 403 – 410.en_US
dc.identifier.citedreferenceArnau J, Sorensen KI, Appel KF, Vogensen FK, Hammer K. Analysis of the heat shock gene expression in Lactococcus lactis MG1363. Microbiology 1996: 142: 1685 – 1691.en_US
dc.identifier.citedreferenceAusubel FM, Brent B, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K. Current Protocols in Molecular Biology. New York: John Wiley & Sons, 1987.en_US
dc.identifier.citedreferenceBateman A, Birney E, Durbin R, Eddy SR, Howe KL, Sonnhammer EL. The Pfam protein families database. Nucl Acids Res 2000: 28: 263 – 266.en_US
dc.identifier.citedreferenceBlattner FR, Plunkett G, Bloch CA, Perna NT, Burland V, Riley M et al. The complete genome sequence of Escherichia coli K-12. Science 1997: 277: 1453 – 1474.en_US
dc.identifier.citedreferenceBray DF, Bagu J, Koegler P. A comparison of HMDS, Peldri II, and critical point drying methods for SEM of biological specimens. Microsc Res Tech 1993: 26: 489 – 495.en_US
dc.identifier.citedreferenceFrandsen EVG, Pedrazzoli V, Kilian M. Ecology of viridans streptococci in the oral cavity and pharynx. Oral Microbiol Immunol 1991: 6: 129 – 133.en_US
dc.identifier.citedreferenceFranklin CD. The aetiology, epidemiology, pathogenesis and changing pattern of infective endocarditis, with a note on prophylaxis. Br Dent J 1992: 172: 369 – 373.en_US
dc.identifier.citedreferenceGeorgopoulos C, Welch WJ. Role of the major heat shock proteins as molecular chaperones. Ann Rev Cell Biol 1993: 9: 601 – 634.en_US
dc.identifier.citedreferenceGrahame DA, Mayer RM. The origin and composition of multiple forms of dextransucrase from Streptococcus sanguis. Biochim Biophys Acta 1984: 786: 42 – 48.en_US
dc.identifier.citedreferenceGribskov M, Burgess RR. Sigma factors from E. coli, B. subtilis, phage SP01 and phage T4 are homologous proteins. Nucleic Acids Research 1986: 14: 6745 – 6763.en_US
dc.identifier.citedreferenceHaisman RJ, Jenkinson HF. Mutantsof Streptococcus gordonii Challis over-producing glucosyltransferase. J Gen Microbiol 1991: 137: 483 – 489.en_US
dc.identifier.citedreferenceHecker M, Schumann W, Volker U. Heat-shock and general stress response in Bacillus subtilis. Mol Microbiol 1996: 19: 417 – 428.en_US
dc.identifier.citedreferenceHofmann K, Stoffel W. TMbase – A database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 1993: 374: 166.en_US
dc.identifier.citedreferenceJayaraman GC, Penders JE, Burne RA. Transcriptional analysis of the Streptococcus mutans hrcA, grpE and dnaK genes and regulation of expression in response to heat shock and environmental acidification. Mol Microbiol 1997: 25: 329 – 341.en_US
dc.identifier.citedreferenceJenkinson HF.Cell-surface proteins of Streptococcus sanguis associated with cell hydrophobicity and coaggregation properties. J General Microbiol 1986: 132: 1575 – 1589.en_US
dc.identifier.citedreferenceJones GW, Clewell DB, Charles L, Vickerman MM. Multiple phase variation in haemolytic, adhesive and antigenic properties of Streptococcus gordonii. Microbiology 1996: 142: 181 – 189.en_US
dc.identifier.citedreferenceJuranka P, Zhang F, Kulpa J, Endicott JA, Blight M, Holland IB, Ling B. Characterization of the hemolysin transporter, HlyB, using an epitope insertion. J Biol Chem 1992: 267: 3764 – 3770.en_US
dc.identifier.citedreferenceKornitzer D, Teff D, Altuvia S, Oppenheim AB. Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX. J Bacteriol 1991: 173: 2944 – 2953.en_US
dc.identifier.citedreferenceLawson J, Gooder H. Growth and development of competence in the group H streptococci. J Bacteriol 1970: 102: 820 – 825.en_US
dc.identifier.citedreferenceLenz LL, Dere B, Bevan MJ. Identification of an H2–M3- restricted Listeria epitope: implications for antigen presentation by M3. Immunity 1996: 5: 63 – 72.en_US
dc.identifier.citedreferenceMechold U, Cashel M, Steiner K, Gentry D, Malke H. Functional analysis of a relA/spoT gene homolog from Streptococcus equisimilis. J Bacteriol 1996: 178: 1401 – 1411.en_US
dc.identifier.citedreferenceNeedleman SB, Wunsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970: 48: 443 – 453.en_US
dc.identifier.citedreferenceNielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Engineering 1997: 10: 1 – 6.en_US
dc.identifier.citedreferenceSegal G, Ron EZ. Regulation of heat-shock response in bacteria. Ann NY Acad Sci 1998: 851: 147 – 151.en_US
dc.identifier.citedreferenceSmyth CJ, Jonsson P, Olsson E, Soderlind O, Rosengren J, Hjerten S, Wadstrom T. Differences in hydrophobic surface characteristics of porcine enteropathogenic Escherichia coli with or without K88 antigen as revealed by hydrophobic interaction chromatography. Infect Immun 1978: 22: 462 – 472.en_US
dc.identifier.citedreferenceSulavik MC, Clewell DB. Rgg is a positive transcriptional regulator of the Streptococcus gordonii gtfG gene. J Bacteriol 1996: 178: 5826 – 2830.en_US
dc.identifier.citedreferenceSulavik MC, Tardif G, Clewell DB. Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J Bacteriol 1992: 174: 3577 – 3586.en_US
dc.identifier.citedreferenceSvensater G, Sjogreen B, Hamilton IR. Multiple stress responses in Streptococcus mutans and the induction of general and stress-specific proteins. Microbiology 2000: 146: 107 – 117.en_US
dc.identifier.citedreferenceTardif G, Sulavik M, Jones GW, Clewell DB. Spontaneous switching of the sucrose-promoted colony phenotype in Streptococcus sanguis. Infect Immun 1989: 57: 3945 – 3948.en_US
dc.identifier.citedreferenceTerleckyj B, Willett NP, Shockman GD. Growth of several cariogenic strains of oral streptococci in a chemically defined medium. Infect Immun 1975: 11: 649 – 655.en_US
dc.identifier.citedreferenceVickerman MM, Clewell DB. Deletions in the carboxyl-terminal region of Streptococcus gordonii glucosyltransferase affect cell-associated enzyme activity and sucrose-associated accumulation of growing cells. Appl Environ Microbiol 1997: 63: 1667 – 1673.en_US
dc.identifier.citedreferenceVickerman MM, Jones GW. Sucrose-dependent accumulation of oral streptococci and their adhesion-defective mutants on saliva-coated hydroxyapatite. Oral Microbiol Immunol 1995: 10: 175 – 182.en_US
dc.identifier.citedreferenceVickerman MM, Clewell DB, Jones GW. Sucrose-promoted accumulation of growing glucosyltransferase variants of Streptococcus gordonii on hydroxyapatite surfaces. Infect Immun 1991: 59: 3523 – 3530.en_US
dc.identifier.citedreferenceVickerman MM, Jones GW, Clewell DB. Molecular analysis of representative Streptococcus gordonii Spp phase variants reveals no differences in the glucosyltransferase structural gene, gtfG. Oral Microbiol Immunol 1997: 12: 82 – 90.en_US
dc.identifier.citedreferenceVickerman MM, Sulavik MC, Minick PE, Clewell DB. Changes in the carboxyl terminal repeat region affect extracellular activity and glucan products of Streptococcus gordonii glucosyltransferase. Infect Immun 1996: 64: 5117 – 5128.en_US
dc.identifier.citedreferenceVickerman MM, Sulavik MC, Nowak JD, Gardner NM, Jones GW, Clewell DB. Nucleotide sequence analysis of the Streptococcus gordonii glucosyltransferase gene, gtfG. DNA Sequence 1997: 7: 83 – 95.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.