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Volumn 65, Issue , 2014, Pages 257-335

Physiological Adaptations of Key Oral Bacteria

Author keywords

Adhesins; Biofilm; Caries; Endodontic disease; Glycans; Glycosidases; Periodontitis; Proteolysis; Saliva

Indexed keywords

ADHESIN; GLYCAN; GLYCOSIDASE; SIALIC ACID;

EID: 84919489710     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ampbs.2014.08.005     Document Type: Chapter
Times cited : (16)

References (388)
  • 1
    • 84896759900 scopus 로고    scopus 로고
    • Major membrane protein TDE2508 regulates adhesive potency in Treponema denticola
    • Abiko Y., Nagano K., Yoshida Y., Yoshimura F. Major membrane protein TDE2508 regulates adhesive potency in Treponema denticola. PLoS One 2014, 9:e89051.
    • (2014) PLoS One , vol.9 , pp. e89051
    • Abiko, Y.1    Nagano, K.2    Yoshida, Y.3    Yoshimura, F.4
  • 2
    • 84876842615 scopus 로고    scopus 로고
    • The subgingival microbiome in health and periodontitis and its relationship with community biomass and inflammation
    • Abusleme L., Dupuy A.K., Dutzan N., Silva N., Burleson J.A., Strausbaugh L.D., et al. The subgingival microbiome in health and periodontitis and its relationship with community biomass and inflammation. The ISME Journal 2013, 7:1016-1025.
    • (2013) The ISME Journal , vol.7 , pp. 1016-1025
    • Abusleme, L.1    Dupuy, A.K.2    Dutzan, N.3    Silva, N.4    Burleson, J.A.5    Strausbaugh, L.D.6
  • 6
    • 1842851984 scopus 로고    scopus 로고
    • Variations of Porphyromonas gingivalis fimbriae in relation to microbial pathogenesis
    • Amano A., Nakagawa I., Okahashi N., Hamada N. Variations of Porphyromonas gingivalis fimbriae in relation to microbial pathogenesis. Journal of Periodontal Research 2004, 39(2):136-142.
    • (2004) Journal of Periodontal Research , vol.39 , Issue.2 , pp. 136-142
    • Amano, A.1    Nakagawa, I.2    Okahashi, N.3    Hamada, N.4
  • 7
    • 80855141275 scopus 로고    scopus 로고
    • Filifactor alocis has virulence attributes that can enhance its persistence under oxidative stress conditions and mediate invasion of epithelial cells by Porphyromonas gingivalis
    • Aruni A.W., Roy F., Fletcher H.M. Filifactor alocis has virulence attributes that can enhance its persistence under oxidative stress conditions and mediate invasion of epithelial cells by Porphyromonas gingivalis. Infection and Immunity 2011, 79:3872-3886.
    • (2011) Infection and Immunity , vol.79 , pp. 3872-3886
    • Aruni, A.W.1    Roy, F.2    Fletcher, H.M.3
  • 8
    • 79959404064 scopus 로고    scopus 로고
    • Sialidase and sialoglycoproteases can modulate virulence in Porphyromonas gingivalis
    • Aruni W., Vanterpool E., Osbourne D., Roy F., Muthiah A., Dou Y., et al. Sialidase and sialoglycoproteases can modulate virulence in Porphyromonas gingivalis. Infection and Immunity 2011, 79:2779-2791.
    • (2011) Infection and Immunity , vol.79 , pp. 2779-2791
    • Aruni, W.1    Vanterpool, E.2    Osbourne, D.3    Roy, F.4    Muthiah, A.5    Dou, Y.6
  • 9
    • 84883514036 scopus 로고    scopus 로고
    • The effects of stress on periodontal treatment: A longitudinal investigation using clinical and biological markers
    • Bakri I., Douglas C.W.I., Rawlinson A. The effects of stress on periodontal treatment: A longitudinal investigation using clinical and biological markers. Journal of Clinical Periodontology 2013, 40:955-961.
    • (2013) Journal of Clinical Periodontology , vol.40 , pp. 955-961
    • Bakri, I.1    Douglas, C.W.I.2    Rawlinson, A.3
  • 10
    • 84856597549 scopus 로고    scopus 로고
    • Novel protein identification methods for biomarker discovery via a proteomic analysis of periodontally healthy and diseased gingival crevicular fluid samples
    • Baliban R.C., Sakellari D., Li Z., DiMaggio P.A., Garcia B.A., Floudas C.A. Novel protein identification methods for biomarker discovery via a proteomic analysis of periodontally healthy and diseased gingival crevicular fluid samples. Journal of Clinical Periodontology 2012, 39:203-212.
    • (2012) Journal of Clinical Periodontology , vol.39 , pp. 203-212
    • Baliban, R.C.1    Sakellari, D.2    Li, Z.3    DiMaggio, P.A.4    Garcia, B.A.5    Floudas, C.A.6
  • 11
    • 34548502272 scopus 로고    scopus 로고
    • The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation
    • Bamford C.V., Fenno J.C., Jenkinson H.F., Dymock D. The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation. Infection and Immunity 2007, 75:4364-4372.
    • (2007) Infection and Immunity , vol.75 , pp. 4364-4372
    • Bamford, C.V.1    Fenno, J.C.2    Jenkinson, H.F.3    Dymock, D.4
  • 12
    • 84895873020 scopus 로고    scopus 로고
    • Single cell genomics of uncultured, health-associated Tannerella BU063 (Oral Taxon 286) and comparison to the closely related pathogen Tannerella forsythia
    • Beall C.J., Campbell A.G., Dayeh D.M., Griffen A.L., Podar M., Leys E.J. Single cell genomics of uncultured, health-associated Tannerella BU063 (Oral Taxon 286) and comparison to the closely related pathogen Tannerella forsythia. PLoS One 2014, 9:e89398.
    • (2014) PLoS One , vol.9 , pp. e89398
    • Beall, C.J.1    Campbell, A.G.2    Dayeh, D.M.3    Griffen, A.L.4    Podar, M.5    Leys, E.J.6
  • 13
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker D.J., Lowe J.B. Fucose: Biosynthesis and biological function in mammals. Glycobiology 2003, 13:41R-53R.
    • (2003) Glycobiology , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 15
    • 23944512875 scopus 로고    scopus 로고
    • The complex oral microflora of high-risk individuals and groups and its role in the caries process
    • Beighton D. The complex oral microflora of high-risk individuals and groups and its role in the caries process. Community Dentistry and Oral Epidemiology 2005, 33:248-255.
    • (2005) Community Dentistry and Oral Epidemiology , vol.33 , pp. 248-255
    • Beighton, D.1
  • 16
    • 0026437156 scopus 로고
    • Glycosidase activities in gingival crevicular fluid in subjects with adult periodontitis or gingivitis
    • Beighton D., Radford J.R., Naylor M.N. Glycosidase activities in gingival crevicular fluid in subjects with adult periodontitis or gingivitis. Archives of Oral Biology 1992, 37:343-348.
    • (1992) Archives of Oral Biology , vol.37 , pp. 343-348
    • Beighton, D.1    Radford, J.R.2    Naylor, M.N.3
  • 17
    • 0035115568 scopus 로고    scopus 로고
    • Genetic loci of Streptococcus mitis that mediate binding to human platelets
    • Bensing B.A., Rubens C.E., Sullam P.M. Genetic loci of Streptococcus mitis that mediate binding to human platelets. Infection and Immunity 2001, 69:1373-1380.
    • (2001) Infection and Immunity , vol.69 , pp. 1373-1380
    • Bensing, B.A.1    Rubens, C.E.2    Sullam, P.M.3
  • 18
    • 0036091006 scopus 로고    scopus 로고
    • An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets
    • Bensing B.A., Sullam P.M. An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets. Molecular Microbiology 2002, 44:1081-1094.
    • (2002) Molecular Microbiology , vol.44 , pp. 1081-1094
    • Bensing, B.A.1    Sullam, P.M.2
  • 19
    • 0021905838 scopus 로고
    • The pH of human crevicular fluid measured by a new microanalytical technique
    • Bickel M., Cimasoni G. The pH of human crevicular fluid measured by a new microanalytical technique. Journal of Periodontal Research 1985, 20:35-40.
    • (1985) Journal of Periodontal Research , vol.20 , pp. 35-40
    • Bickel, M.1    Cimasoni, G.2
  • 20
    • 79958856251 scopus 로고    scopus 로고
    • Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans
    • Bitoun J.P., Nguyen A.H., Fan Y., Burne R.A., Wen Z.T. Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans. FEMS Microbiology Letters 2011, 320:110-117.
    • (2011) FEMS Microbiology Letters , vol.320 , pp. 110-117
    • Bitoun, J.P.1    Nguyen, A.H.2    Fan, Y.3    Burne, R.A.4    Wen, Z.T.5
  • 22
    • 35048903505 scopus 로고    scopus 로고
    • Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens
    • Boraston A.B., Ficko-Blean E., Healey M. Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens. Biochemistry 2007, 46:11352-11360.
    • (2007) Biochemistry , vol.46 , pp. 11352-11360
    • Boraston, A.B.1    Ficko-Blean, E.2    Healey, M.3
  • 23
    • 84904415406 scopus 로고    scopus 로고
    • Effect of periodontal disease on diabetes: systematic review of epidemiologic observational evidence
    • Borgnakke W.S., Ylöstalo P.V., Taylor G.W., Genco R.J. Effect of periodontal disease on diabetes: systematic review of epidemiologic observational evidence. Journal of Clinical Periodontology 2013, 40(Suppl. 1):S135-S152.
    • (2013) Journal of Clinical Periodontology , vol.40 , pp. S135-S152
    • Borgnakke, W.S.1    Ylöstalo, P.V.2    Taylor, G.W.3    Genco, R.J.4
  • 24
    • 79951854037 scopus 로고    scopus 로고
    • Biology of Streptococcus mutans-derived glucosyltransferases: Role in extracellular matrix formation of cariogenic biofilms
    • Bowen W.H., Koo H. Biology of Streptococcus mutans-derived glucosyltransferases: Role in extracellular matrix formation of cariogenic biofilms. Caries Research 2011, 45:69-86.
    • (2011) Caries Research , vol.45 , pp. 69-86
    • Bowen, W.H.1    Koo, H.2
  • 25
    • 0031610167 scopus 로고    scopus 로고
    • Analysis of pH-driven disruption of oral microbial communities in vitro
    • Bradshaw D.J., Marsh P.D. Analysis of pH-driven disruption of oral microbial communities in vitro. Caries Research 1998, 32:456-462.
    • (1998) Caries Research , vol.32 , pp. 456-462
    • Bradshaw, D.J.1    Marsh, P.D.2
  • 26
    • 0026601301 scopus 로고
    • Rapid presumptive identification and further characterization of Bacteroides forsythus
    • Braham P.H., Moncla B.J. Rapid presumptive identification and further characterization of Bacteroides forsythus. Journal of Clinical Microbiology 1992, 30:649-654.
    • (1992) Journal of Clinical Microbiology , vol.30 , pp. 649-654
    • Braham, P.H.1    Moncla, B.J.2
  • 27
    • 77956054494 scopus 로고    scopus 로고
    • O-GalNAc glycans
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY), A. Varki, R. Cummings, J. Esko (Eds.)
    • Brockhausen I., Schachter H., Stanley P. O-GalNAc glycans. Essentials in glycobiology 2009, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY). 2nd ed. A. Varki, R. Cummings, J. Esko (Eds.).
    • (2009) Essentials in glycobiology
    • Brockhausen, I.1    Schachter, H.2    Stanley, P.3
  • 28
    • 0030954705 scopus 로고    scopus 로고
    • Identification of a Streptococcus gordonii SspB domain that mediates adhesion to Porphyromonas gingivalis
    • Brooks W., Demuth D.R., Gil S., Lamont R.J. Identification of a Streptococcus gordonii SspB domain that mediates adhesion to Porphyromonas gingivalis. Infection and Immunity 1997, 65:3753-3758.
    • (1997) Infection and Immunity , vol.65 , pp. 3753-3758
    • Brooks, W.1    Demuth, D.R.2    Gil, S.3    Lamont, R.J.4
  • 29
    • 0036044319 scopus 로고    scopus 로고
    • The economics of periodontal
    • Brown L.J., Johns A.B., Wall T.P. The economics of periodontal. Periodontology 2002, 2000(29):223-234.
    • (2002) Periodontology , vol.2000 , Issue.29 , pp. 223-234
    • Brown, L.J.1    Johns, A.B.2    Wall, T.P.3
  • 34
    • 0032967175 scopus 로고    scopus 로고
    • Sequential deglycosylation and utilization of the N-linked, complex-type glycans of human alpha1-acid glycoprotein mediates growth of Streptococcus oralis
    • Byers H.L., Tarelli E., Homer K.A., Beighton D. Sequential deglycosylation and utilization of the N-linked, complex-type glycans of human alpha1-acid glycoprotein mediates growth of Streptococcus oralis. Glycobiology 1999, 9:469-479.
    • (1999) Glycobiology , vol.9 , pp. 469-479
    • Byers, H.L.1    Tarelli, E.2    Homer, K.A.3    Beighton, D.4
  • 35
    • 0034009184 scopus 로고    scopus 로고
    • Isolation and characterisation of sialidase from a strain of Streptococcus oralis
    • Byers H.L., Tarelli E., Homer K.A., Beighton D. Isolation and characterisation of sialidase from a strain of Streptococcus oralis. Journal of Medical Microbiology 2000, 49:235-244.
    • (2000) Journal of Medical Microbiology , vol.49 , pp. 235-244
    • Byers, H.L.1    Tarelli, E.2    Homer, K.A.3    Beighton, D.4
  • 37
    • 84876197055 scopus 로고    scopus 로고
    • Evidence of mutualism between two periodontal pathogens: Co-operative haem acquisition by the HmuY haemophore of Porphyromonas gingivalis and the cysteine protease interpain A (InpA) of Prevotella intermedia
    • Byrne D.P., Potempa J., Olczak T., Smalley J.W. Evidence of mutualism between two periodontal pathogens: Co-operative haem acquisition by the HmuY haemophore of Porphyromonas gingivalis and the cysteine protease interpain A (InpA) of Prevotella intermedia. Molecular Oral Microbiology 2013, 28:219-229.
    • (2013) Molecular Oral Microbiology , vol.28 , pp. 219-229
    • Byrne, D.P.1    Potempa, J.2    Olczak, T.3    Smalley, J.W.4
  • 38
    • 72449195888 scopus 로고    scopus 로고
    • Role of the cysteine protease interpain A of Prevotella intermedia in breakdown and release of haem from haemoglobin
    • Byrne D.P., Wawrzonek K., Jaworska A., Birss A.J., Potempa J., Smalley J.W. Role of the cysteine protease interpain A of Prevotella intermedia in breakdown and release of haem from haemoglobin. The Biochemical Journal 2010, 425:257-264.
    • (2010) The Biochemical Journal , vol.425 , pp. 257-264
    • Byrne, D.P.1    Wawrzonek, K.2    Jaworska, A.3    Birss, A.J.4    Potempa, J.5    Smalley, J.W.6
  • 40
    • 84857456592 scopus 로고    scopus 로고
    • Proteome data set of human gingival crevicular fluid from healthy periodontium sites by multidimensional protein separation and mass spectrometry
    • Carneiro L.G., Venuleo C., Oppenheim F.G., Salih E. Proteome data set of human gingival crevicular fluid from healthy periodontium sites by multidimensional protein separation and mass spectrometry. Journal of Periodontal Research 2012, 47:248-262.
    • (2012) Journal of Periodontal Research , vol.47 , pp. 248-262
    • Carneiro, L.G.1    Venuleo, C.2    Oppenheim, F.G.3    Salih, E.4
  • 41
    • 84863289353 scopus 로고    scopus 로고
    • Leukocyte inflammatory responses provoked by pneumococcal sialidase
    • Chang Y., Uchiyama S., Varki A., Nizet V. Leukocyte inflammatory responses provoked by pneumococcal sialidase. mBio 2012, 3:e00220. 10.1128/mBio.00220-11.
    • (2012) mBio , vol.3 , pp. e00220
    • Chang, Y.1    Uchiyama, S.2    Varki, A.3    Nizet, V.4
  • 42
    • 77749254858 scopus 로고    scopus 로고
    • ClpP of Streptococcus mutans differentially regulates expression of genomic islands, mutacin production, and antibiotic tolerance
    • Chattoraj P., Banerjee A., Biswas S., Biswas I. ClpP of Streptococcus mutans differentially regulates expression of genomic islands, mutacin production, and antibiotic tolerance. Journal of Bacteriology 2010, 192:1312-1323.
    • (2010) Journal of Bacteriology , vol.192 , pp. 1312-1323
    • Chattoraj, P.1    Banerjee, A.2    Biswas, S.3    Biswas, I.4
  • 43
    • 0035061098 scopus 로고    scopus 로고
    • Porphyromonas gingivalis gingipains and adhesion to epithelial cells
    • Chen T., Nakayama K., Belliveau L., Duncan M.J. Porphyromonas gingivalis gingipains and adhesion to epithelial cells. Infection and Immunity 2001, 69:3048-3056.
    • (2001) Infection and Immunity , vol.69 , pp. 3048-3056
    • Chen, T.1    Nakayama, K.2    Belliveau, L.3    Duncan, M.J.4
  • 44
    • 79951811721 scopus 로고    scopus 로고
    • The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis
    • Chen Y.-Y., Peng B., Yang Q., Glew M.D., Veith P.D., Cross K.J., et al. The outer membrane protein LptO is essential for the O-deacylation of LPS and the co-ordinated secretion and attachment of A-LPS and CTD proteins in Porphyromonas gingivalis. Molecular Microbiology 2011, 79:1380-1401.
    • (2011) Molecular Microbiology , vol.79 , pp. 1380-1401
    • Chen, Y.-Y.1    Peng, B.2    Yang, Q.3    Glew, M.D.4    Veith, P.D.5    Cross, K.J.6
  • 45
    • 0028784174 scopus 로고
    • Lectin recognition of host-like saccharide motifs in streptococcal cell wall polysaccharides
    • Cisar J.O., Sandberg A.L., Abeygunawardana C., Reddy G.P., Bush C.A. Lectin recognition of host-like saccharide motifs in streptococcal cell wall polysaccharides. Glycobiology 1995, 5:655-662.
    • (1995) Glycobiology , vol.5 , pp. 655-662
    • Cisar, J.O.1    Sandberg, A.L.2    Abeygunawardana, C.3    Reddy, G.P.4    Bush, C.A.5
  • 46
    • 84899573335 scopus 로고    scopus 로고
    • Importance of biofilm formation and dipeptidyl peptidase IV for the pathogenicity of clinical Porphyromonas gingivalis isolates
    • Clais S., Boulet G., Kerstens M., Horemans T., Teughels W., Quirynen M., et al. Importance of biofilm formation and dipeptidyl peptidase IV for the pathogenicity of clinical Porphyromonas gingivalis isolates. Pathogens and Disease 2014, 70:408-413.
    • (2014) Pathogens and Disease , vol.70 , pp. 408-413
    • Clais, S.1    Boulet, G.2    Kerstens, M.3    Horemans, T.4    Teughels, W.5    Quirynen, M.6
  • 48
    • 38649126553 scopus 로고    scopus 로고
    • Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans
    • Clock S.A., Planet P.J., Perez B.A., Figurski D.H. Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans. Journal of Bacteriology 2008, 190:980-990.
    • (2008) Journal of Bacteriology , vol.190 , pp. 980-990
    • Clock, S.A.1    Planet, P.J.2    Perez, B.A.3    Figurski, D.H.4
  • 51
  • 52
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • Crennell S., Garman E., Laver G., Vimr E., Taylor G. Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain. Structure (London, England: 1993) 1994, 2:535-544.
    • (1994) Structure (London, England: 1993) , vol.2 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 53
    • 33845881184 scopus 로고    scopus 로고
    • TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans
    • Crosby J.A., Kachlany S.C. TdeA, a TolC-like protein required for toxin and drug export in Aggregatibacter (Actinobacillus) actinomycetemcomitans. Gene 2007, 388:83-92.
    • (2007) Gene , vol.388 , pp. 83-92
    • Crosby, J.A.1    Kachlany, S.C.2
  • 54
    • 84866546211 scopus 로고    scopus 로고
    • Mind-altering microorganisms: The impact of the gut microbiota on brain and behaviour
    • Cryan J.F., Dinan T.G. Mind-altering microorganisms: The impact of the gut microbiota on brain and behaviour. Nature Reviews. Neuroscience 2012, 13:701-712.
    • (2012) Nature Reviews. Neuroscience , vol.13 , pp. 701-712
    • Cryan, J.F.1    Dinan, T.G.2
  • 55
    • 0036892852 scopus 로고    scopus 로고
    • Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor
    • Curtis M.A., Aduse Opoku J., Rangarajan M., Gallagher A., Sterne J.A.C., Reid C.R., et al. Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor. Infection and Immunity 2002, 70:6968-6975.
    • (2002) Infection and Immunity , vol.70 , pp. 6968-6975
    • Curtis, M.A.1    Aduse Opoku, J.2    Rangarajan, M.3    Gallagher, A.4    Sterne, J.A.C.5    Reid, C.R.6
  • 57
    • 0032769105 scopus 로고    scopus 로고
    • Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50
    • Curtis M.A., Thickett A., Slaney J.M., Rangarajan M., Aduse-Opoku J., Shepherd P., et al. Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50. Infection and Immunity 1999, 67:3816-3823.
    • (1999) Infection and Immunity , vol.67 , pp. 3816-3823
    • Curtis, M.A.1    Thickett, A.2    Slaney, J.M.3    Rangarajan, M.4    Aduse-Opoku, J.5    Shepherd, P.6
  • 58
    • 80054921127 scopus 로고    scopus 로고
    • The relationship of the oral microbiotia to periodontal health and disease
    • Curtis M.A., Zenobia C., Darveau R.P. The relationship of the oral microbiotia to periodontal health and disease. Cell Host & Microbe 2011, 10:302-306.
    • (2011) Cell Host & Microbe , vol.10 , pp. 302-306
    • Curtis, M.A.1    Zenobia, C.2    Darveau, R.P.3
  • 59
    • 0029054845 scopus 로고
    • Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system
    • Cvitkovitch D.G., Boyd D.A., Thevenot T., Hamilton I.R. Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system. Journal of Bacteriology 1995, 177:2251-2258.
    • (1995) Journal of Bacteriology , vol.177 , pp. 2251-2258
    • Cvitkovitch, D.G.1    Boyd, D.A.2    Thevenot, T.3    Hamilton, I.R.4
  • 60
    • 33645596055 scopus 로고    scopus 로고
    • Antimicrobial peptides in the oral environment: Expression and function in health and disease
    • Horizon Bioscience, Wymondham, United Kingdom, R.L. Gallo (Ed.)
    • Dale B.D., Page Fredericks L. Antimicrobial peptides in the oral environment: Expression and function in health and disease. Antimicrobial peptides in human health and disease 2004, 223-251. Horizon Bioscience, Wymondham, United Kingdom. R.L. Gallo (Ed.).
    • (2004) Antimicrobial peptides in human health and disease , pp. 223-251
    • Dale, B.D.1    Page Fredericks, L.2
  • 61
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David S.S., O'Shea V.L., Kundu S. Base-excision repair of oxidative DNA damage. Nature 2007, 447:941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 67
    • 34347399868 scopus 로고    scopus 로고
    • Association of a high-molecular weight arginine-binding protein of Fusobacterium nucleatum ATCC 10953 with adhesion to secretory immunoglobulin A and coaggregation with Streptococcus cristatus
    • Edwards A.M., Grossman T.J., Rudney J.D. Association of a high-molecular weight arginine-binding protein of Fusobacterium nucleatum ATCC 10953 with adhesion to secretory immunoglobulin A and coaggregation with Streptococcus cristatus. Oral Microbiology and Immunology 2007, 22:217-224.
    • (2007) Oral Microbiology and Immunology , vol.22 , pp. 217-224
    • Edwards, A.M.1    Grossman, T.J.2    Rudney, J.D.3
  • 68
    • 17644380678 scopus 로고    scopus 로고
    • Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405
    • Edwards A.M., Jenkinson H.F., Woodward M.J., Dymock D. Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405. Infection and Immunity 2005, 73:2891-2898.
    • (2005) Infection and Immunity , vol.73 , pp. 2891-2898
    • Edwards, A.M.1    Jenkinson, H.F.2    Woodward, M.J.3    Dymock, D.4
  • 71
    • 84899734976 scopus 로고    scopus 로고
    • Preferential packing of acidic glycosidases and proteases into Bacteroides outer membrane vesicles
    • Elhenawy W., Debelyy M.O., Feldman M.F. Preferential packing of acidic glycosidases and proteases into Bacteroides outer membrane vesicles. mBio 2014, 5:e00909-e00914. 10.1128/mBio.00909-14.
    • (2014) mBio , vol.5 , pp. e00909-e00914
    • Elhenawy, W.1    Debelyy, M.O.2    Feldman, M.F.3
  • 72
    • 77951032403 scopus 로고    scopus 로고
    • Plaque plague
    • El-Kheshen M. Plaque plague. The Dentist 2008, 2008:48-50.
    • (2008) The Dentist , vol.2008 , pp. 48-50
    • El-Kheshen, M.1
  • 73
    • 78650170511 scopus 로고    scopus 로고
    • Streptococcus mutans antigen I/II binds to α5β1 integrins via its A-domain and increases β1 integrins expression on periodontal ligament fibroblast cells
    • Engels-Deutsch M., Rizk S., Haïkel Y. Streptococcus mutans antigen I/II binds to α5β1 integrins via its A-domain and increases β1 integrins expression on periodontal ligament fibroblast cells. Archives of Oral Biology 2011, 56:22-28.
    • (2011) Archives of Oral Biology , vol.56 , pp. 22-28
    • Engels-Deutsch, M.1    Rizk, S.2    Haïkel, Y.3
  • 75
    • 83355166277 scopus 로고    scopus 로고
    • Fusobacterium nucleatum adhesin FadA binds vascular endothelial cadherin and alters endothelial integrity
    • Fardini Y., Wang X., Témoin S., Nithianantham S., Lee D., Shoham M., et al. Fusobacterium nucleatum adhesin FadA binds vascular endothelial cadherin and alters endothelial integrity. Molecular Microbiology 2011, 82:1468-1480.
    • (2011) Molecular Microbiology , vol.82 , pp. 1468-1480
    • Fardini, Y.1    Wang, X.2    Témoin, S.3    Nithianantham, S.4    Lee, D.5    Shoham, M.6
  • 76
    • 0026437024 scopus 로고
    • Temperature differences at periodontal sites in health and disease
    • Fedi P.F., Killoy W.J. Temperature differences at periodontal sites in health and disease. Journal of Periodontology 1992, 63:24-27.
    • (1992) Journal of Periodontology , vol.63 , pp. 24-27
    • Fedi, P.F.1    Killoy, W.J.2
  • 77
    • 84859496090 scopus 로고    scopus 로고
    • Sialyl residues modulate LPS-mediated signaling through the Toll-like receptor 4 complex
    • Feng C., Stamatos N.M., Dragan A.I., Medvedev A., Whitford M., Zhang L., et al. Sialyl residues modulate LPS-mediated signaling through the Toll-like receptor 4 complex. PLoS One 2012, 7:e32359.
    • (2012) PLoS One , vol.7 , pp. e32359
    • Feng, C.1    Stamatos, N.M.2    Dragan, A.I.3    Medvedev, A.4    Whitford, M.5    Zhang, L.6
  • 79
    • 78049496429 scopus 로고    scopus 로고
    • Mapping the epithelial-cell-binding domain of the Aggregatibacter actinomycetemcomitans autotransporter adhesin Aae
    • Fine D.H., Kaplan J.B., Furgang D., Karched M., Velliyagounder K., Yue G. Mapping the epithelial-cell-binding domain of the Aggregatibacter actinomycetemcomitans autotransporter adhesin Aae. Microbiology (Reading, England) 2010, 156:3412-3420.
    • (2010) Microbiology (Reading, England) , vol.156 , pp. 3412-3420
    • Fine, D.H.1    Kaplan, J.B.2    Furgang, D.3    Karched, M.4    Velliyagounder, K.5    Yue, G.6
  • 80
    • 16244374885 scopus 로고    scopus 로고
    • The Actinobacillus actinomycetemcomitans autotransporter adhesin Aae exhibits specificity for buccal epithelial cells from humans and old world primates
    • Fine D.H., Velliyagounder K., Furgang D., Kaplan J.B. The Actinobacillus actinomycetemcomitans autotransporter adhesin Aae exhibits specificity for buccal epithelial cells from humans and old world primates. Infection and Immunity 2005, 73:1947-1953.
    • (2005) Infection and Immunity , vol.73 , pp. 1947-1953
    • Fine, D.H.1    Velliyagounder, K.2    Furgang, D.3    Kaplan, J.B.4
  • 81
    • 66949139751 scopus 로고    scopus 로고
    • The gingipains: Scissors and glue of the periodontal pathogen, Porphyromonas gingivalis
    • Fitzpatrick R.E., Wijeyewickrema L.C., Pike R.N. The gingipains: Scissors and glue of the periodontal pathogen, Porphyromonas gingivalis. Future Microbiology 2009, 4:471-487.
    • (2009) Future Microbiology , vol.4 , pp. 471-487
    • Fitzpatrick, R.E.1    Wijeyewickrema, L.C.2    Pike, R.N.3
  • 83
    • 79960095377 scopus 로고    scopus 로고
    • Aggregatibacter actinomycetemcomitans leukotoxin is post-translationally modified by addition of either saturated or hydroxylated fatty acyl chains
    • Fong K.P., Tang H.-Y., Brown A.C., Kieba I.R., Speicher D.W., Boesze-Battaglia K., et al. Aggregatibacter actinomycetemcomitans leukotoxin is post-translationally modified by addition of either saturated or hydroxylated fatty acyl chains. Molecular Oral Microbiology 2011, 26:262-276.
    • (2011) Molecular Oral Microbiology , vol.26 , pp. 262-276
    • Fong, K.P.1    Tang, H.-Y.2    Brown, A.C.3    Kieba, I.R.4    Speicher, D.W.5    Boesze-Battaglia, K.6
  • 85
    • 77649340032 scopus 로고    scopus 로고
    • Two intramolecular isopeptide bonds are identified in the crystal structure of the Streptococcus gordonii SspB C-terminal domain
    • Forsgren N., Lamont R.J., Persson K. Two intramolecular isopeptide bonds are identified in the crystal structure of the Streptococcus gordonii SspB C-terminal domain. Journal of Molecular Biology 2010, 397:740-751.
    • (2010) Journal of Molecular Biology , vol.397 , pp. 740-751
    • Forsgren, N.1    Lamont, R.J.2    Persson, K.3
  • 86
    • 0028675972 scopus 로고
    • Carbohydrate depletion of immunoglobulin A1 by oral species of gram-positive rods
    • Frandsen E.V. Carbohydrate depletion of immunoglobulin A1 by oral species of gram-positive rods. Oral Microbiology and Immunology 1994, 9:352-358.
    • (1994) Oral Microbiology and Immunology , vol.9 , pp. 352-358
    • Frandsen, E.V.1
  • 87
    • 0037469594 scopus 로고    scopus 로고
    • Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens
    • Fujimura S., Ueda O., Shibata Y., Hirai K. Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens. FEMS Microbiology Letters 2003, 219:305-309.
    • (2003) FEMS Microbiology Letters , vol.219 , pp. 305-309
    • Fujimura, S.1    Ueda, O.2    Shibata, Y.3    Hirai, K.4
  • 88
    • 84874739008 scopus 로고    scopus 로고
    • Dpr and sod in Streptococcus mutans are involved in coexistence with S. sanguinis, and PerR is associated with resistance to H2O2
    • Fujishima K., Kawada-Matsuo M., Oogai Y., Tokuda M., Torii M., Komatsuzawa H. dpr and sod in Streptococcus mutans are involved in coexistence with S. sanguinis, and PerR is associated with resistance to H2O2. Applied and Environmental Microbiology 2013, 79:1436-1443.
    • (2013) Applied and Environmental Microbiology , vol.79 , pp. 1436-1443
    • Fujishima, K.1    Kawada-Matsuo, M.2    Oogai, Y.3    Tokuda, M.4    Torii, M.5    Komatsuzawa, H.6
  • 89
    • 0036484444 scopus 로고    scopus 로고
    • Differential and quantitative analyses of mRNA expression of glucosyltransferases from Streptococcus mutans MT8148
    • Fujiwara T., Hoshino T., Ooshima T., Hamada S. Differential and quantitative analyses of mRNA expression of glucosyltransferases from Streptococcus mutans MT8148. Journal of Dental Research 2002, 81:109-113.
    • (2002) Journal of Dental Research , vol.81 , pp. 109-113
    • Fujiwara, T.1    Hoshino, T.2    Ooshima, T.3    Hamada, S.4
  • 90
    • 0037137491 scopus 로고    scopus 로고
    • Roles of mucin-type O-glycans in cell adhesion
    • Fukuda M. Roles of mucin-type O-glycans in cell adhesion. Biochimica et Biophysica Acta 2002, 1573:394-405.
    • (2002) Biochimica et Biophysica Acta , vol.1573 , pp. 394-405
    • Fukuda, M.1
  • 92
    • 0017070551 scopus 로고
    • Scanning electron microscopic investigation of human dentinal tubules
    • Garberoglio R., Brännström M. Scanning electron microscopic investigation of human dentinal tubules. Archives of Oral Biology 1976, 21:355-362.
    • (1976) Archives of Oral Biology , vol.21 , pp. 355-362
    • Garberoglio, R.1    Brännström, M.2
  • 93
    • 0023757544 scopus 로고
    • Adsorbed salivary proline-rich protein 1 and statherin: Receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces
    • Gibbons R.J., Hay D.I., Cisar J.O., Clark W.B. Adsorbed salivary proline-rich protein 1 and statherin: Receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces. Infection and Immunity 1988, 56:2990-2993.
    • (1988) Infection and Immunity , vol.56 , pp. 2990-2993
    • Gibbons, R.J.1    Hay, D.I.2    Cisar, J.O.3    Clark, W.B.4
  • 94
  • 95
    • 84876182331 scopus 로고    scopus 로고
    • Conservation and revised annotation of the Treponema denticola prcB-prcA-prtP locus encoding the dentilisin (CTLP) protease complex
    • Goetting-Minesky M.P., Godovikova V., Li J.J., Seshadrinathan S., Timm J.C., Kamodia S.S., et al. Conservation and revised annotation of the Treponema denticola prcB-prcA-prtP locus encoding the dentilisin (CTLP) protease complex. Molecular Oral Microbiology 2013, 28:181-191.
    • (2013) Molecular Oral Microbiology , vol.28 , pp. 181-191
    • Goetting-Minesky, M.P.1    Godovikova, V.2    Li, J.J.3    Seshadrinathan, S.4    Timm, J.C.5    Kamodia, S.S.6
  • 96
    • 84863590936 scopus 로고    scopus 로고
    • Role of DNA base excision repair in the mutability and virulence of Streptococcus mutans
    • Gonzalez K., Faustoferri R.C., Quivey R.G. Role of DNA base excision repair in the mutability and virulence of Streptococcus mutans. Molecular Microbiology 2012, 85:361-377.
    • (2012) Molecular Microbiology , vol.85 , pp. 361-377
    • Gonzalez, K.1    Faustoferri, R.C.2    Quivey, R.G.3
  • 98
    • 84919467730 scopus 로고    scopus 로고
    • Binding properties of Treponema denticola lipooligosaccharide
    • Grenier D. Binding properties of Treponema denticola lipooligosaccharide. Journal of Oral Microbiology 2013, 5:3-7.
    • (2013) Journal of Oral Microbiology , vol.5 , pp. 3-7
    • Grenier, D.1
  • 99
    • 84861342868 scopus 로고    scopus 로고
    • Distinct and complex bacterial profiles in human periodontitis and health revealed by 16S pyrosequencing
    • Griffen A.L., Beall C.J., Campbell J.H., Firestone N.D., Kumar P.S., Yang Z.K., et al. Distinct and complex bacterial profiles in human periodontitis and health revealed by 16S pyrosequencing. The ISME Journal 2012, 6:1176-1185.
    • (2012) The ISME Journal , vol.6 , pp. 1176-1185
    • Griffen, A.L.1    Beall, C.J.2    Campbell, J.H.3    Firestone, N.D.4    Kumar, P.S.5    Yang, Z.K.6
  • 100
    • 1542286881 scopus 로고    scopus 로고
    • Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159
    • Griswold A.R., Chen Y.-Y.M., Burne R.A. Analysis of an agmatine deiminase gene cluster in Streptococcus mutans UA159. Journal of Bacteriology 2004, 186:1902-1904.
    • (2004) Journal of Bacteriology , vol.186 , pp. 1902-1904
    • Griswold, A.R.1    Chen, Y.-Y.M.2    Burne, R.A.3
  • 102
    • 77955760680 scopus 로고    scopus 로고
    • Dichotomy of gingipains action as virulence factors: From cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins
    • Guo Y., Nguyen K.-A., Potempa J. Dichotomy of gingipains action as virulence factors: From cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins. Periodontology 2010, 2000(54):15-44.
    • (2010) Periodontology , vol.2000 , Issue.54 , pp. 15-44
    • Guo, Y.1    Nguyen, K.-A.2    Potempa, J.3
  • 104
    • 84869006781 scopus 로고    scopus 로고
    • Beyond the red complex and into more complexity: The polymicrobial synergy and dysbiosis (PSD) model of periodontal disease etiology
    • Hajishengallis G., Lamont R.J. Beyond the red complex and into more complexity: The polymicrobial synergy and dysbiosis (PSD) model of periodontal disease etiology. Molecular Oral Microbiology 2012, 27:409-419.
    • (2012) Molecular Oral Microbiology , vol.27 , pp. 409-419
    • Hajishengallis, G.1    Lamont, R.J.2
  • 105
    • 81755166205 scopus 로고    scopus 로고
    • Low-abundance biofilm species orchestrates inflammatory periodontal disease through the commensal microbiota and complement
    • Hajishengallis G., Liang S., Payne M.A., Hashim A., Jotwani R., Eskan M.A., et al. Low-abundance biofilm species orchestrates inflammatory periodontal disease through the commensal microbiota and complement. Cell Host & Microbe 2011, 10:497-506.
    • (2011) Cell Host & Microbe , vol.10 , pp. 497-506
    • Hajishengallis, G.1    Liang, S.2    Payne, M.A.3    Hashim, A.4    Jotwani, R.5    Eskan, M.A.6
  • 106
    • 84897868561 scopus 로고    scopus 로고
    • Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes
    • Hall M., Nylander Å., Jenkinson H.F., Persson K. Structure of the C-terminal domain of AspA (antigen I/II-family) protein from Streptococcus pyogenes. FEBS Open Bio 2014, 4:283-289.
    • (2014) FEBS Open Bio , vol.4 , pp. 283-289
    • Hall, M.1    Nylander, Å.2    Jenkinson, H.F.3    Persson, K.4
  • 107
    • 0032488979 scopus 로고    scopus 로고
    • Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
    • Haltiwanger R.S., Grove K., Philipsberg G.A. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate. The Journal of Biological Chemistry 1998, 273:3611-3617.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 3611-3617
    • Haltiwanger, R.S.1    Grove, K.2    Philipsberg, G.A.3
  • 108
    • 22544468802 scopus 로고    scopus 로고
    • Identification and characterization of a novel adhesin unique to oral fusobacteria
    • Han Y.W., Ikegami A., Rajanna C., Kawsar H.I., Zhou Y., Li M., et al. Identification and characterization of a novel adhesin unique to oral fusobacteria. Journal of Bacteriology 2005, 187:5330-5340.
    • (2005) Journal of Bacteriology , vol.187 , pp. 5330-5340
    • Han, Y.W.1    Ikegami, A.2    Rajanna, C.3    Kawsar, H.I.4    Zhou, Y.5    Li, M.6
  • 109
    • 33645926032 scopus 로고    scopus 로고
    • Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: a possible implication in dental root caries and endocarditis
    • Han T.K., Zhang C., Dao M.L. Identification and characterization of collagen-binding activity in Streptococcus mutans wall-associated protein: a possible implication in dental root caries and endocarditis. Biochemical and Biophysical Research Communications 2006, 343(3):787-792.
    • (2006) Biochemical and Biophysical Research Communications , vol.343 , Issue.3 , pp. 787-792
    • Han, T.K.1    Zhang, C.2    Dao, M.L.3
  • 110
    • 71049192315 scopus 로고    scopus 로고
    • Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2
    • Hasegawa Y., Iwami J., Sato K., Park Y., Nishikawa K., Atsumi T., et al. Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2. Microbiology (Reading, England) 2009, 155:3333-3347.
    • (2009) Microbiology (Reading, England) , vol.155 , pp. 3333-3347
    • Hasegawa, Y.1    Iwami, J.2    Sato, K.3    Park, Y.4    Nishikawa, K.5    Atsumi, T.6
  • 111
    • 84886313084 scopus 로고    scopus 로고
    • Localization and function of the accessory protein Mfa3 in Porphyromonas gingivalis Mfa1 fimbriae
    • Hasegawa Y., Nagano K., Ikai R., Izumigawa M., Yoshida Y., Kitai N., et al. Localization and function of the accessory protein Mfa3 in Porphyromonas gingivalis Mfa1 fimbriae. Molecular Oral Microbiology 2013, 28:467-480.
    • (2013) Molecular Oral Microbiology , vol.28 , pp. 467-480
    • Hasegawa, Y.1    Nagano, K.2    Ikai, R.3    Izumigawa, M.4    Yoshida, Y.5    Kitai, N.6
  • 112
    • 0642377572 scopus 로고    scopus 로고
    • Binding of Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin
    • Hashimoto M., Ogawa S., Asai Y., Takai Y., Ogawa T. Binding of Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin. FEMS Microbiology Letters 2003, 226:267-271.
    • (2003) FEMS Microbiology Letters , vol.226 , pp. 267-271
    • Hashimoto, M.1    Ogawa, S.2    Asai, Y.3    Takai, Y.4    Ogawa, T.5
  • 113
    • 0026949210 scopus 로고
    • The relationship between clinical symptoms and anaerobic bacteria from infected root canals
    • Hashioka K., Yamasaki M., Nakane A., Horiba N., Nakamura H. The relationship between clinical symptoms and anaerobic bacteria from infected root canals. Journal of Endodontics 1992, 18:558-561.
    • (1992) Journal of Endodontics , vol.18 , pp. 558-561
    • Hashioka, K.1    Yamasaki, M.2    Nakane, A.3    Horiba, N.4    Nakamura, H.5
  • 114
    • 0017031234 scopus 로고
    • Neuraminic acid derivatives newly discovered in humans: N-acetyl-9-O-L-lactoylneuraminic acid, N,9-O-Diacetylneuraminic acid and N-acetyl-2,3-dehydro-2-deoxyneuraminic acid
    • Haverkamp J., Schauer R., Wember M. Neuraminic acid derivatives newly discovered in humans: N-acetyl-9-O-L-lactoylneuraminic acid, N,9-O-Diacetylneuraminic acid and N-acetyl-2,3-dehydro-2-deoxyneuraminic acid. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 1976, 357:1699-1705.
    • (1976) Hoppe-Seyler's Zeitschrift für Physiologische Chemie , vol.357 , pp. 1699-1705
    • Haverkamp, J.1    Schauer, R.2    Wember, M.3
  • 115
    • 0020688591 scopus 로고
    • The acidogenic microbial composition of dental plaque from caries-free and caries-prone people
    • Hayes M.L., Carter E.C., Griffiths S.J. The acidogenic microbial composition of dental plaque from caries-free and caries-prone people. Archives of Oral Biology 1983, 28:381-386.
    • (1983) Archives of Oral Biology , vol.28 , pp. 381-386
    • Hayes, M.L.1    Carter, E.C.2    Griffiths, S.J.3
  • 116
    • 0030868761 scopus 로고    scopus 로고
    • The human complement regulatory factor-H-like protein 1, which represents a truncated form of factor H, displays cell-attachment activity
    • Hellwage J., Ku S., Zipfel P.F. The human complement regulatory factor-H-like protein 1, which represents a truncated form of factor H, displays cell-attachment activity. The Biochemical Journal 1997, 326:321-327.
    • (1997) The Biochemical Journal , vol.326 , pp. 321-327
    • Hellwage, J.1    Ku, S.2    Zipfel, P.F.3
  • 120
    • 84899043538 scopus 로고    scopus 로고
    • Protective role of the PG1036-PG1037-PG1038 operon in oxidative stress in Porphyromonas gingivalis W83
    • Henry L.G., Aruni W., Sandberg L., Fletcher H.M. Protective role of the PG1036-PG1037-PG1038 operon in oxidative stress in Porphyromonas gingivalis W83. PLoS One 2013, 8:e69645.
    • (2013) PLoS One , vol.8 , pp. e69645
    • Henry, L.G.1    Aruni, W.2    Sandberg, L.3    Fletcher, H.M.4
  • 122
    • 57349085080 scopus 로고    scopus 로고
    • DNA repair of 8-oxo-7,8-dihydroguanine lesions in Porphyromonas gingivalis
    • Henry L.G., Sandberg L., Zhang K., Fletcher H.M. DNA repair of 8-oxo-7,8-dihydroguanine lesions in Porphyromonas gingivalis. Journal of Bacteriology 2008, 190:7985-7993.
    • (2008) Journal of Bacteriology , vol.190 , pp. 7985-7993
    • Henry, L.G.1    Sandberg, L.2    Zhang, K.3    Fletcher, H.M.4
  • 124
    • 0029909058 scopus 로고    scopus 로고
    • Candida albicans binding to the oral bacterium Streptococcus gordonii involves multiple adhesin-receptor interactions
    • Holmes A.R., McNab R., Jenkinson H.F. Candida albicans binding to the oral bacterium Streptococcus gordonii involves multiple adhesin-receptor interactions. Infection and Immunity 1996, 64:4680-4685.
    • (1996) Infection and Immunity , vol.64 , pp. 4680-4685
    • Holmes, A.R.1    McNab, R.2    Jenkinson, H.F.3
  • 125
    • 67650744786 scopus 로고    scopus 로고
    • The OxyR homologue in Tannerella forsythia regulates expression of oxidative stress responses and biofilm formation
    • Honma K., Mishima E., Inagaki S., Sharma A. The OxyR homologue in Tannerella forsythia regulates expression of oxidative stress responses and biofilm formation. Microbiology 2009, 155:1912-1922.
    • (2009) Microbiology , vol.155 , pp. 1912-1922
    • Honma, K.1    Mishima, E.2    Inagaki, S.3    Sharma, A.4
  • 126
    • 78650912796 scopus 로고    scopus 로고
    • Role of Tannerella forsythia NanH sialidase in epithelial cell attachment
    • Honma K., Mishima E., Sharma A. Role of Tannerella forsythia NanH sialidase in epithelial cell attachment. Infection and Immunity 2011, 79:393-401.
    • (2011) Infection and Immunity , vol.79 , pp. 393-401
    • Honma, K.1    Mishima, E.2    Sharma, A.3
  • 128
  • 129
    • 0042236733 scopus 로고    scopus 로고
    • Cloning and expression of alpha-D-glucosidase and N-acetyl-beta-glucosaminidase from the periodontal pathogen, Tannerella forsythensis (Bacteroides forsythus)
    • Hughes C.V., Malki G., Loo C.Y., Tanner A.C.R., Ganeshkumar N. Cloning and expression of alpha-D-glucosidase and N-acetyl-beta-glucosaminidase from the periodontal pathogen, Tannerella forsythensis (Bacteroides forsythus). Oral Microbiology and Immunology 2003, 18:309-312.
    • (2003) Oral Microbiology and Immunology , vol.18 , pp. 309-312
    • Hughes, C.V.1    Malki, G.2    Loo, C.Y.3    Tanner, A.C.R.4    Ganeshkumar, N.5
  • 131
    • 67650079271 scopus 로고    scopus 로고
    • Complementation of the fadA mutation in Fusobacterium nucleatum demonstrates that the surface-exposed adhesin promotes cellular invasion and placental colonization
    • Ikegami A., Chung P., Han Y.W. Complementation of the fadA mutation in Fusobacterium nucleatum demonstrates that the surface-exposed adhesin promotes cellular invasion and placental colonization. Infection and Immunity 2009, 77:3075-3079.
    • (2009) Infection and Immunity , vol.77 , pp. 3075-3079
    • Ikegami, A.1    Chung, P.2    Han, Y.W.3
  • 132
    • 3342927588 scopus 로고    scopus 로고
    • Multiple functions of the leucine-rich repeat protein LrrA of Treponema denticola
    • Ikegami A., Honma K., Sharma A., Kuramitsu H.K. Multiple functions of the leucine-rich repeat protein LrrA of Treponema denticola. Infection and Immunity 2004, 72:4619-4627.
    • (2004) Infection and Immunity , vol.72 , pp. 4619-4627
    • Ikegami, A.1    Honma, K.2    Sharma, A.3    Kuramitsu, H.K.4
  • 133
    • 33748038463 scopus 로고    scopus 로고
    • Porphyromonas gingivalis vesicles enhance attachment, and the leucine-rich repeat BspA protein is required for invasion of epithelial cells by "Tannerella forsythia"
    • Inagaki S., Onishi S., Kuramitsu H.K., Sharma A. Porphyromonas gingivalis vesicles enhance attachment, and the leucine-rich repeat BspA protein is required for invasion of epithelial cells by "Tannerella forsythia". Infection and Immunity 2006, 74(9):5023-5028.
    • (2006) Infection and Immunity , vol.74 , Issue.9 , pp. 5023-5028
    • Inagaki, S.1    Onishi, S.2    Kuramitsu, H.K.3    Sharma, A.4
  • 134
    • 0031968738 scopus 로고    scopus 로고
    • Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae
    • Inoue T., Tanimoto I., Ohta H., Kato K., Murayama Y., Fukui K. Molecular characterization of low-molecular-weight component protein, Flp, in Actinobacillus actinomycetemcomitans fimbriae. Microbiology and Immunology 1998, 42:253-258.
    • (1998) Microbiology and Immunology , vol.42 , pp. 253-258
    • Inoue, T.1    Tanimoto, I.2    Ohta, H.3    Kato, K.4    Murayama, Y.5    Fukui, K.6
  • 135
    • 48849093368 scopus 로고    scopus 로고
    • Screen for leukotoxin mutants in Aggregatibacter actinomycetemcomitans: Genes of the phosphotransferase system are required for leukotoxin biosynthesis
    • Isaza M.P., Duncan M.S., Kaplan J.B., Kachlany S.C. Screen for leukotoxin mutants in Aggregatibacter actinomycetemcomitans: Genes of the phosphotransferase system are required for leukotoxin biosynthesis. Infection and Immunity 2008, 76:3561-3568.
    • (2008) Infection and Immunity , vol.76 , pp. 3561-3568
    • Isaza, M.P.1    Duncan, M.S.2    Kaplan, J.B.3    Kachlany, S.C.4
  • 136
    • 76149138468 scopus 로고    scopus 로고
    • Talk of the town: Interspecies communication in oral biofilms
    • Jakubovics N.S. Talk of the town: Interspecies communication in oral biofilms. Molecular Oral Microbiology 2010, 25:4-14.
    • (2010) Molecular Oral Microbiology , vol.25 , pp. 4-14
    • Jakubovics, N.S.1
  • 137
    • 70450260429 scopus 로고    scopus 로고
    • Multiple adhesin proteins on the cell surface of Streptococcus gordonii are involved in adhesion to human fibronectin
    • Jakubovics N.S., Brittan J.L., Dutton L.C., Jenkinson H.F. Multiple adhesin proteins on the cell surface of Streptococcus gordonii are involved in adhesion to human fibronectin. Microbiology (Reading, England) 2009, 155:3572-3580.
    • (2009) Microbiology (Reading, England) , vol.155 , pp. 3572-3580
    • Jakubovics, N.S.1    Brittan, J.L.2    Dutton, L.C.3    Jenkinson, H.F.4
  • 138
    • 25444481307 scopus 로고    scopus 로고
    • Functions of cell surface-anchored antigen I/II family and hsa polypeptides in interactions of Streptococcus gordonii with host receptors
    • Jakubovics N.S., Kerrigan S.W., Nobbs A.H., Stro N., Van Dolleweerd C.J., Cox D.M., et al. Functions of cell surface-anchored antigen I/II family and hsa polypeptides in interactions of Streptococcus gordonii with host receptors. Infection and Immunity 2005, 73:6629-6638.
    • (2005) Infection and Immunity , vol.73 , pp. 6629-6638
    • Jakubovics, N.S.1    Kerrigan, S.W.2    Nobbs, A.H.3    Stro, N.4    Van Dolleweerd, C.J.5    Cox, D.M.6
  • 140
    • 14844307064 scopus 로고    scopus 로고
    • Differential binding specificities of oral streptococcal antigen I/II family adhesins for human or bacterial ligands
    • Jakubovics N.S., Strömberg N., van Dolleweerd C.J., Kelly C.G., Jenkinson H.F. Differential binding specificities of oral streptococcal antigen I/II family adhesins for human or bacterial ligands. Molecular Microbiology 2005, 55:1591-1605.
    • (2005) Molecular Microbiology , vol.55 , pp. 1591-1605
    • Jakubovics, N.S.1    Strömberg, N.2    van Dolleweerd, C.J.3    Kelly, C.G.4    Jenkinson, H.F.5
  • 141
    • 84870458537 scopus 로고    scopus 로고
    • Autoinducer 2 of Fusobacterium nucleatum as a target molecule to inhibit biofilm formation of periodontopathogens
    • Jang Y.-J., Choi Y.-J., Lee S.-H., Jun H.-K., Choi B.-K. Autoinducer 2 of Fusobacterium nucleatum as a target molecule to inhibit biofilm formation of periodontopathogens. Archives of Oral Biology 2013, 58:17-27.
    • (2013) Archives of Oral Biology , vol.58 , pp. 17-27
    • Jang, Y.-J.1    Choi, Y.-J.2    Lee, S.-H.3    Jun, H.-K.4    Choi, B.-K.5
  • 142
    • 84885209646 scopus 로고    scopus 로고
    • The effects of stress hormones on growth of selected periodontitis related bacteria
    • Jentsch H.F.R., März D., Krüger M. The effects of stress hormones on growth of selected periodontitis related bacteria. Anaerobe 2013, 24:49-54.
    • (2013) Anaerobe , vol.24 , pp. 49-54
    • Jentsch, H.F.R.1    März, D.2    Krüger, M.3
  • 143
    • 78049284441 scopus 로고    scopus 로고
    • Mechanistic studies of agmatine deiminase from multiple bacterial species
    • Jones J.E., Dreyton C.J., Flick H., Causey C.P., Thompson P.R. Mechanistic studies of agmatine deiminase from multiple bacterial species. Biochemistry 2010, 49:9413-9423.
    • (2010) Biochemistry , vol.49 , pp. 9413-9423
    • Jones, J.E.1    Dreyton, C.J.2    Flick, H.3    Causey, C.P.4    Thompson, P.R.5
  • 145
    • 84857463226 scopus 로고    scopus 로고
    • A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system
    • Jusko M., Potempa J., Karim A.Y., Ksiazek M., Riesbeck K., Garred P., et al. A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system. Journal of Immunology (Baltimore, Md.: 1950) 2012, 188:2338-2349.
    • (2012) Journal of Immunology (Baltimore, Md.: 1950) , vol.188 , pp. 2338-2349
    • Jusko, M.1    Potempa, J.2    Karim, A.Y.3    Ksiazek, M.4    Riesbeck, K.5    Garred, P.6
  • 146
    • 0033758854 scopus 로고    scopus 로고
    • Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea
    • Kachlany S.C., Planet P.J., Bhattacharjee M.K., Kollia E., Desalle R., Fine D.H., et al. Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in bacteria and archaea. Journal of Bacteriology 2000, 182:6169-6176.
    • (2000) Journal of Bacteriology , vol.182 , pp. 6169-6176
    • Kachlany, S.C.1    Planet, P.J.2    Bhattacharjee, M.K.3    Kollia, E.4    Desalle, R.5    Fine, D.H.6
  • 149
    • 58149114833 scopus 로고    scopus 로고
    • The Fusobacterium nucleatum outer membrane protein RadD is an arginine-inhibitable adhesin required for inter-species adherence and the structured architecture of multispecies biofilm
    • Kaplan C.W., Lux R., Haake S.K., Shi W. The Fusobacterium nucleatum outer membrane protein RadD is an arginine-inhibitable adhesin required for inter-species adherence and the structured architecture of multispecies biofilm. Molecular Microbiology 2009, 71:35-47.
    • (2009) Molecular Microbiology , vol.71 , pp. 35-47
    • Kaplan, C.W.1    Lux, R.2    Haake, S.K.3    Shi, W.4
  • 151
    • 84876399347 scopus 로고    scopus 로고
    • Periodontal disease and rheumatoid arthritis: A systematic review
    • Kaur S., White S., Bartold P.M. Periodontal disease and rheumatoid arthritis: A systematic review. Journal of Dental Research 2013, 92:399-408.
    • (2013) Journal of Dental Research , vol.92 , pp. 399-408
    • Kaur, S.1    White, S.2    Bartold, P.M.3
  • 153
    • 47749149187 scopus 로고    scopus 로고
    • Detection of bone loss with different X-ray techniques in periodontal patients
    • Kim T.-S., Obst C., Zehaczek S., Geenen C. Detection of bone loss with different X-ray techniques in periodontal patients. Journal of Periodontology 2008, 79:1141-1149.
    • (2008) Journal of Periodontology , vol.79 , pp. 1141-1149
    • Kim, T.-S.1    Obst, C.2    Zehaczek, S.3    Geenen, C.4
  • 154
    • 84862516820 scopus 로고    scopus 로고
    • Porphyromonas gingivalis influences actin degradation within epithelial cells during invasion and apoptosis
    • Kinane J.A., Benakanakere M.R., Zhao J., Hosur K.B., Kinane D.F. Porphyromonas gingivalis influences actin degradation within epithelial cells during invasion and apoptosis. Cellular Microbiology 2012, 14:1085-1096.
    • (2012) Cellular Microbiology , vol.14 , pp. 1085-1096
    • Kinane, J.A.1    Benakanakere, M.R.2    Zhao, J.3    Hosur, K.B.4    Kinane, D.F.5
  • 155
    • 0027499315 scopus 로고
    • Localization of the Fusobacterium nucleatum T18 adhesin activity mediating coaggregation with Porphyromonas gingivalis T22
    • Kinder S.A., Holt S.C. Localization of the Fusobacterium nucleatum T18 adhesin activity mediating coaggregation with Porphyromonas gingivalis T22. Journal of Bacteriology 1993, 175:840-850.
    • (1993) Journal of Bacteriology , vol.175 , pp. 840-850
    • Kinder, S.A.1    Holt, S.C.2
  • 156
    • 22544485354 scopus 로고    scopus 로고
    • NanA, a neuraminidase from Streptococcus pneumoniae, shows high levels of sequence diversity, at least in part through recombination with Streptococcus oralis
    • King S.J., Whatmore A.M., Dowson C.G. NanA, a neuraminidase from Streptococcus pneumoniae, shows high levels of sequence diversity, at least in part through recombination with Streptococcus oralis. Journal of Bacteriology 2005, 187:5376-5386.
    • (2005) Journal of Bacteriology , vol.187 , pp. 5376-5386
    • King, S.J.1    Whatmore, A.M.2    Dowson, C.G.3
  • 157
    • 84869074022 scopus 로고    scopus 로고
    • Identification and characterization of novel glycoproteins involved in growth and biofilm formation by Porphyromonas gingivalis
    • Kishi M., Hasegawa Y., Nagano K., Nakamura H., Murakami Y., Yoshimura F. Identification and characterization of novel glycoproteins involved in growth and biofilm formation by Porphyromonas gingivalis. Molecular Oral Microbiology 2012, 27:458-470.
    • (2012) Molecular Oral Microbiology , vol.27 , pp. 458-470
    • Kishi, M.1    Hasegawa, Y.2    Nagano, K.3    Nakamura, H.4    Murakami, Y.5    Yoshimura, F.6
  • 158
    • 84881534314 scopus 로고    scopus 로고
    • Bacterial community development in experimental gingivitis
    • Kistler J.O., Booth V., Bradshaw D.J., Wade W.G. Bacterial community development in experimental gingivitis. PLoS One 2013, 8:e71227.
    • (2013) PLoS One , vol.8 , pp. e71227
    • Kistler, J.O.1    Booth, V.2    Bradshaw, D.J.3    Wade, W.G.4
  • 160
    • 0028384718 scopus 로고
    • Determination of plasma proteins in dentinal fluid from cavities prepared in healthy young human teeth
    • Knutsson G., Jontell M., Bergenholtz G. Determination of plasma proteins in dentinal fluid from cavities prepared in healthy young human teeth. Archives of Oral Biology 1994, 39:185-190.
    • (1994) Archives of Oral Biology , vol.39 , pp. 185-190
    • Knutsson, G.1    Jontell, M.2    Bergenholtz, G.3
  • 161
    • 0024448776 scopus 로고
    • Inhibition of coaggregation between Fusobacterium nucleatum and Porphyromonas (Bacteroides) gingivalis by lactose and related sugars
    • Kolenbrander P.E., Andersen R.N. Inhibition of coaggregation between Fusobacterium nucleatum and Porphyromonas (Bacteroides) gingivalis by lactose and related sugars. Infection and Immunity 1989, 57:3204-3209.
    • (1989) Infection and Immunity , vol.57 , pp. 3204-3209
    • Kolenbrander, P.E.1    Andersen, R.N.2
  • 164
    • 0034819577 scopus 로고    scopus 로고
    • Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: Insights into the reaction mechanism
    • Krüger D., Schauer R., Traving C. Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: Insights into the reaction mechanism. European Journal of Biochemistry/FEBS 2001, 268:3831-3839.
    • (2001) European Journal of Biochemistry/FEBS , vol.268 , pp. 3831-3839
    • Krüger, D.1    Schauer, R.2    Traving, C.3
  • 165
    • 67650590872 scopus 로고    scopus 로고
    • Distinct roles of long/short fimbriae and gingipains in homotypic biofilm development by Porphyromonas gingivalis
    • Kuboniwa M., Amano A., Hashino E., Yamamoto Y., Inaba H., Hamada N., et al. Distinct roles of long/short fimbriae and gingipains in homotypic biofilm development by Porphyromonas gingivalis. BMC Microbiology 2009, 9:105.
    • (2009) BMC Microbiology , vol.9 , pp. 105
    • Kuboniwa, M.1    Amano, A.2    Hashino, E.3    Yamamoto, Y.4    Inaba, H.5    Hamada, N.6
  • 167
    • 84883204508 scopus 로고    scopus 로고
    • A surface-exposed neuraminidase affects complement resistance and virulence of the oral spirochaete Treponema denticola
    • Kurniyati K., Zhang W., Zhang K., Li C. A surface-exposed neuraminidase affects complement resistance and virulence of the oral spirochaete Treponema denticola. Molecular Microbiology 2013, 89:842-856.
    • (2013) Molecular Microbiology , vol.89 , pp. 842-856
    • Kurniyati, K.1    Zhang, W.2    Zhang, K.3    Li, C.4
  • 168
    • 0035987235 scopus 로고    scopus 로고
    • Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates
    • Lamont R.J., El-Sabaeny A., Park Y., Cook G.S., Costerton J.W., Demuth D.R. Role of the Streptococcus gordonii SspB protein in the development of Porphyromonas gingivalis biofilms on streptococcal substrates. Microbiology (Reading, England) 2002, 148:1627-1636.
    • (2002) Microbiology (Reading, England) , vol.148 , pp. 1627-1636
    • Lamont, R.J.1    El-Sabaeny, A.2    Park, Y.3    Cook, G.S.4    Costerton, J.W.5    Demuth, D.R.6
  • 169
    • 39649089147 scopus 로고    scopus 로고
    • Structure of N-acetyl-beta-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline
    • Langley D.B., Harty D.W.S., Jacques N.A., Hunter N., Guss J.M., Collyer C.A. Structure of N-acetyl-beta-D-glucosaminidase (GcnA) from the endocarditis pathogen Streptococcus gordonii and its complex with the mechanism-based inhibitor NAG-thiazoline. Journal of Molecular Biology 2008, 377:104-116.
    • (2008) Journal of Molecular Biology , vol.377 , pp. 104-116
    • Langley, D.B.1    Harty, D.W.S.2    Jacques, N.A.3    Hunter, N.4    Guss, J.M.5    Collyer, C.A.6
  • 170
    • 79958742851 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains
    • Larson M.R., Rajashankar K.R., Crowley P.J., Kelly C., Mitchell T.J., Brady L.J., et al. Crystal structure of the C-terminal region of Streptococcus mutans antigen I/II and characterization of salivary agglutinin adherence domains. The Journal of Biological Chemistry 2011, 286:21657-21666.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 21657-21666
    • Larson, M.R.1    Rajashankar, K.R.2    Crowley, P.J.3    Kelly, C.4    Mitchell, T.J.5    Brady, L.J.6
  • 173
    • 0031260603 scopus 로고    scopus 로고
    • Evaluation of root canal bacteria and their antimicrobial susceptibility in teeth with necrotic pulp
    • Le Goff A., Bunetel L., Mouton C., Bonnaure-Mallet M. Evaluation of root canal bacteria and their antimicrobial susceptibility in teeth with necrotic pulp. Oral Microbiology and Immunology 1997, 12:318-322.
    • (1997) Oral Microbiology and Immunology , vol.12 , pp. 318-322
    • Le Goff, A.1    Bunetel, L.2    Mouton, C.3    Bonnaure-Mallet, M.4
  • 174
    • 33645210489 scopus 로고    scopus 로고
    • Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia
    • Lee S.-W., Sabet M., Um H.-S., Yang J., Kim H.C., Zhu W. Identification and characterization of the genes encoding a unique surface (S-) layer of Tannerella forsythia. Gene 2006, 371:102-111.
    • (2006) Gene , vol.371 , pp. 102-111
    • Lee, S.-W.1    Sabet, M.2    Um, H.-S.3    Yang, J.4    Kim, H.C.5    Zhu, W.6
  • 176
    • 57349140742 scopus 로고    scopus 로고
    • A model of efficiency: Stress tolerance by Streptococcus mutans
    • Lemos J.A., Burne R.A. A model of efficiency: Stress tolerance by Streptococcus mutans. Microbiology (Reading, England) 2008, 154:3247-3255.
    • (2008) Microbiology (Reading, England) , vol.154 , pp. 3247-3255
    • Lemos, J.A.1    Burne, R.A.2
  • 177
    • 2942593979 scopus 로고    scopus 로고
    • Proteome analysis of Streptococcus mutans metabolic phenotype during acid tolerance
    • Len A.C.L., Harty D.W.S., Jacques N.A. Proteome analysis of Streptococcus mutans metabolic phenotype during acid tolerance. Microbiology (Reading, England) 2004, 150:1353-1366.
    • (2004) Microbiology (Reading, England) , vol.150 , pp. 1353-1366
    • Len, A.C.L.1    Harty, D.W.S.2    Jacques, N.A.3
  • 178
    • 2942625671 scopus 로고    scopus 로고
    • Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance
    • Len A.C.L., Harty D.W.S., Jacques N.A. Stress-responsive proteins are upregulated in Streptococcus mutans during acid tolerance. Microbiology (Reading, England) 2004, 150:1339-1351.
    • (2004) Microbiology (Reading, England) , vol.150 , pp. 1339-1351
    • Len, A.C.L.1    Harty, D.W.S.2    Jacques, N.A.3
  • 180
    • 72249113435 scopus 로고    scopus 로고
    • Metal uptake in host-pathogen interactions: Role of iron in Porphyromonas gingivalis interactions with host organisms
    • Lewis J.P. Metal uptake in host-pathogen interactions: Role of iron in Porphyromonas gingivalis interactions with host organisms. Periodontology 2010, 2000(52):94-116.
    • (2010) Periodontology , vol.2000 , Issue.52 , pp. 94-116
    • Lewis, J.P.1
  • 181
    • 0032855431 scopus 로고    scopus 로고
    • Hemoglobinase activity of the lysine gingipain protease (Kgp) of Porphyromonas gingivalis W83
    • Lewis J.P., Dawson J.A., Hannis J.C., Macrina F.L., Muddiman D. Hemoglobinase activity of the lysine gingipain protease (Kgp) of Porphyromonas gingivalis W83. Journal of Bacteriology 1999, 181:4905-4913.
    • (1999) Journal of Bacteriology , vol.181 , pp. 4905-4913
    • Lewis, J.P.1    Dawson, J.A.2    Hannis, J.C.3    Macrina, F.L.4    Muddiman, D.5
  • 182
    • 84863999494 scopus 로고    scopus 로고
    • Host sialoglycans and bacterial sialidases: A mucosal perspective
    • Lewis A.L., Lewis W.G. Host sialoglycans and bacterial sialidases: A mucosal perspective. Cellular Microbiology 2012, 14:1174-1182.
    • (2012) Cellular Microbiology , vol.14 , pp. 1174-1182
    • Lewis, A.L.1    Lewis, W.G.2
  • 183
    • 84906942903 scopus 로고    scopus 로고
    • Phylogenetic and functional gene structure shifts of the oral microbiomes in periodontitis patients
    • Li Y., He J., He Z., Zhou Y., Yuan M., Xu X., et al. Phylogenetic and functional gene structure shifts of the oral microbiomes in periodontitis patients. The ISME Journal 2014, 8:1879-1891.
    • (2014) The ISME Journal , vol.8 , pp. 1879-1891
    • Li, Y.1    He, J.2    He, Z.3    Zhou, Y.4    Yuan, M.5    Xu, X.6
  • 185
    • 84863231535 scopus 로고    scopus 로고
    • Abrogation of neuraminidase reduces biofilm formation, capsule biosynthesis, and virulence of Porphyromonas gingivalis
    • Li C., Kurniyati, Hu B., Bian J., Sun J., Zhang W., et al. Abrogation of neuraminidase reduces biofilm formation, capsule biosynthesis, and virulence of Porphyromonas gingivalis. Infection and Immunity 2012, 80:3-13.
    • (2012) Infection and Immunity , vol.80 , pp. 3-13
    • Li, C.1    Kurniyati, H.B.2    Bian, J.3    Sun, J.4    Zhang, W.5
  • 186
    • 0036233112 scopus 로고    scopus 로고
    • A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation
    • Li Y.H., Tang N., Aspiras M.B., Lau P.C., Lee J.H., Ellen R.P., et al. A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation. Journal of Bacteriology 2002, 184:2699-2708.
    • (2002) Journal of Bacteriology , vol.184 , pp. 2699-2708
    • Li, Y.H.1    Tang, N.2    Aspiras, M.B.3    Lau, P.C.4    Lee, J.H.5    Ellen, R.P.6
  • 187
    • 77950534036 scopus 로고    scopus 로고
    • Vaccination targeting surface FomA of Fusobacterium nucleatum against bacterial co-aggregation: Implication for treatment of periodontal infection and halitosis
    • Liu P.-F., Shi W., Zhu W., Smith J.W., Hsieh S.-L., Gallo R.L., et al. Vaccination targeting surface FomA of Fusobacterium nucleatum against bacterial co-aggregation: Implication for treatment of periodontal infection and halitosis. Vaccine 2010, 28:3496-3505.
    • (2010) Vaccine , vol.28 , pp. 3496-3505
    • Liu, P.-F.1    Shi, W.2    Zhu, W.3    Smith, J.W.4    Hsieh, S.-L.5    Gallo, R.L.6
  • 188
    • 80052384000 scopus 로고    scopus 로고
    • Differential response of Streptococcus mutans towards friend and foe in mixed-species cultures
    • Liu J., Wu C., Huang I.-H., Merritt J., Qi F. Differential response of Streptococcus mutans towards friend and foe in mixed-species cultures. Microbiology (Reading, England) 2011, 157:2433-2444.
    • (2011) Microbiology (Reading, England) , vol.157 , pp. 2433-2444
    • Liu, J.1    Wu, C.2    Huang, I.-H.3    Merritt, J.4    Qi, F.5
  • 190
    • 67650564928 scopus 로고    scopus 로고
    • Leucine-rich repeats of bacterial surface proteins serve as common pattern recognition motifs of human scavenger receptor gp340
    • Loimaranta V., Hytönen J., Pulliainen A.T., Sharma A., Tenovuo J., Strömberg N., et al. Leucine-rich repeats of bacterial surface proteins serve as common pattern recognition motifs of human scavenger receptor gp340. The Journal of Biological Chemistry 2009, 284:18614-18623.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 18614-18623
    • Loimaranta, V.1    Hytönen, J.2    Pulliainen, A.T.3    Sharma, A.4    Tenovuo, J.5    Strömberg, N.6
  • 191
  • 193
    • 0028608789 scopus 로고
    • Cloning and expression in Escherichia coli of the nahA gene from Porphyromonas gingivalis indicates that P-N-acetylhexosaminidase is an outer-membrane-associated lipoprotein
    • Lovatt A., Roberts I.S. Cloning and expression in Escherichia coli of the nahA gene from Porphyromonas gingivalis indicates that P-N-acetylhexosaminidase is an outer-membrane-associated lipoprotein. Microbiology 1994, 140:3399-3406.
    • (1994) Microbiology , vol.140 , pp. 3399-3406
    • Lovatt, A.1    Roberts, I.S.2
  • 195
    • 0033964156 scopus 로고    scopus 로고
    • Coinvasion of dentinal tubules by Porphyromonas gingivalis and Streptococcus gordonii depends upon binding specificity of streptococcal antigen I/II adhesin
    • Love R.M., McMillan M.D., Park Y., Jenkinson H.F. Coinvasion of dentinal tubules by Porphyromonas gingivalis and Streptococcus gordonii depends upon binding specificity of streptococcal antigen I/II adhesin. Infection and Immunity 2000, 68:1359-1365.
    • (2000) Infection and Immunity , vol.68 , pp. 1359-1365
    • Love, R.M.1    McMillan, M.D.2    Park, Y.3    Jenkinson, H.F.4
  • 196
    • 4544381795 scopus 로고    scopus 로고
    • Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae
    • Maeda K., Nagata H., Kuboniwa M., Kataoka K., Nishida N., Tanaka M., et al. Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae. Infection and Immunity 2004, 72:5475-5477.
    • (2004) Infection and Immunity , vol.72 , pp. 5475-5477
    • Maeda, K.1    Nagata, H.2    Kuboniwa, M.3    Kataoka, K.4    Nishida, N.5    Tanaka, M.6
  • 197
    • 0030064825 scopus 로고    scopus 로고
    • Rapid characterization of periodontal bacterial isolates by using fluorogenic substrate tests
    • Maiden M.F., Tanner A., Macuch P.J. Rapid characterization of periodontal bacterial isolates by using fluorogenic substrate tests. Journal of Clinical Microbiology 1996, 34:376-384.
    • (1996) Journal of Clinical Microbiology , vol.34 , pp. 376-384
    • Maiden, M.F.1    Tanner, A.2    Macuch, P.J.3
  • 198
    • 35748984396 scopus 로고    scopus 로고
    • Role of active-site residues of dispersin B, a biofilm-releasing beta-hexosaminidase from a periodontal pathogen, in substrate hydrolysis
    • Manuel S.G.A., Ragunath C., Sait H.B.R., Izano E.A., Kaplan J.B., Ramasubbu N. Role of active-site residues of dispersin B, a biofilm-releasing beta-hexosaminidase from a periodontal pathogen, in substrate hydrolysis. The FEBS Journal 2007, 274:5987-5999.
    • (2007) The FEBS Journal , vol.274 , pp. 5987-5999
    • Manuel, S.G.A.1    Ragunath, C.2    Sait, H.B.R.3    Izano, E.A.4    Kaplan, J.B.5    Ramasubbu, N.6
  • 200
    • 0037292394 scopus 로고    scopus 로고
    • Are dental diseases examples of ecological catastrophes?
    • Marsh P.D. Are dental diseases examples of ecological catastrophes?. Microbiology (Reading, England) 2003, 149:279-294.
    • (2003) Microbiology (Reading, England) , vol.149 , pp. 279-294
    • Marsh, P.D.1
  • 201
    • 0142043378 scopus 로고    scopus 로고
    • Recombinant influenza C hemagglutinin-esterase as a probe for sialic acid 9-O-acetylation
    • Martin L.T., Verhagen A., Varki A. Recombinant influenza C hemagglutinin-esterase as a probe for sialic acid 9-O-acetylation. Methods in Enzymology 2003, 363:489-498.
    • (2003) Methods in Enzymology , vol.363 , pp. 489-498
    • Martin, L.T.1    Verhagen, A.2    Varki, A.3
  • 202
    • 27744492254 scopus 로고    scopus 로고
    • Demonstration of factor H-like protein 1 binding to Treponema denticola, a pathogen associated with periodontal disease in humans
    • Mcdowell J.V., Lankford J., Stamm L., Sadlon T., Gordon D.L., Marconi R.T. Demonstration of factor H-like protein 1 binding to Treponema denticola, a pathogen associated with periodontal disease in humans. Infection and Immunity 2005, 73:7126-7132.
    • (2005) Infection and Immunity , vol.73 , pp. 7126-7132
    • Mcdowell, J.V.1    Lankford, J.2    Stamm, L.3    Sadlon, T.4    Gordon, D.L.5    Marconi, R.T.6
  • 203
    • 0030199688 scopus 로고    scopus 로고
    • The multiple-sugar metabolism (msm) gene cluster of Streptococcus mutans is transcribed as a single operon
    • McLaughlin R.E., Ferretti J.J. The multiple-sugar metabolism (msm) gene cluster of Streptococcus mutans is transcribed as a single operon. FEMS Microbiology Letters 1996, 140:261-264.
    • (1996) FEMS Microbiology Letters , vol.140 , pp. 261-264
    • McLaughlin, R.E.1    Ferretti, J.J.2
  • 204
    • 0029794139 scopus 로고    scopus 로고
    • Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin
    • McNab R., Holmes A.R., Clarke J.M., Tannock G.W., Jenkinson H.F. Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin. Infection and Immunity 1996, 64:4204-4210.
    • (1996) Infection and Immunity , vol.64 , pp. 4204-4210
    • McNab, R.1    Holmes, A.R.2    Clarke, J.M.3    Tannock, G.W.4    Jenkinson, H.F.5
  • 205
    • 0028149676 scopus 로고
    • Cell-surface-associated polypeptides CshA and CshB of high molecular mass are colonization determinants in the oral bacterium Streptococcus gordonii
    • McNab R., Jenkinson H.F., Loach D.M., Tannock G.W. Cell-surface-associated polypeptides CshA and CshB of high molecular mass are colonization determinants in the oral bacterium Streptococcus gordonii. Molecular Microbiology 1994, 14:743-754.
    • (1994) Molecular Microbiology , vol.14 , pp. 743-754
    • McNab, R.1    Jenkinson, H.F.2    Loach, D.M.3    Tannock, G.W.4
  • 206
    • 0037432698 scopus 로고    scopus 로고
    • Acid tolerance response of biofilm cells of Streptococcus mutans
    • McNeill K., Hamilton I.R. Acid tolerance response of biofilm cells of Streptococcus mutans. FEMS Microbiology Letters 2003, 221:25-30.
    • (2003) FEMS Microbiology Letters , vol.221 , pp. 25-30
    • McNeill, K.1    Hamilton, I.R.2
  • 208
    • 4444246066 scopus 로고    scopus 로고
    • Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen
    • Mintz K.P. Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen. Microbiology (Reading, England) 2004, 150:2677-2688.
    • (2004) Microbiology (Reading, England) , vol.150 , pp. 2677-2688
    • Mintz, K.P.1
  • 209
    • 79961096578 scopus 로고    scopus 로고
    • Tannerella forsythia invasion in oral epithelial cells requires phosphoinositide 3-kinase activation and clathrin-mediated endocytosis
    • Mishima E., Sharma A. Tannerella forsythia invasion in oral epithelial cells requires phosphoinositide 3-kinase activation and clathrin-mediated endocytosis. Microbiology 2011, 157:2382-2391.
    • (2011) Microbiology , vol.157 , pp. 2382-2391
    • Mishima, E.1    Sharma, A.2
  • 210
    • 34247876080 scopus 로고    scopus 로고
    • Sortase-catalyzed assembly of distinct heteromeric fimbriae in Actinomyces naeslundii
    • Mishra A., Das A., Cisar J.O., Ton-That H. Sortase-catalyzed assembly of distinct heteromeric fimbriae in Actinomyces naeslundii. Journal of Bacteriology 2007, 189:3156-3165.
    • (2007) Journal of Bacteriology , vol.189 , pp. 3156-3165
    • Mishra, A.1    Das, A.2    Cisar, J.O.3    Ton-That, H.4
  • 211
    • 80051936406 scopus 로고    scopus 로고
    • Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development
    • Mishra A., Devarajan B., Reardon M.E., Dwivedi P., Krishnan V., Cisar J.O., et al. Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development. Molecular Microbiology 2011, 81:1205-1220.
    • (2011) Molecular Microbiology , vol.81 , pp. 1205-1220
    • Mishra, A.1    Devarajan, B.2    Reardon, M.E.3    Dwivedi, P.4    Krishnan, V.5    Cisar, J.O.6
  • 212
    • 77955352031 scopus 로고    scopus 로고
    • The Actinomyces oris type 2 fimbrial shaft FimA mediates co-aggregation with oral streptococci, adherence to red blood cells and biofilm development
    • Mishra A., Wu C., Yang J., Cisar J.O., Das A., Ton-That H. The Actinomyces oris type 2 fimbrial shaft FimA mediates co-aggregation with oral streptococci, adherence to red blood cells and biofilm development. Molecular Microbiology 2010, 77:841-854.
    • (2010) Molecular Microbiology , vol.77 , pp. 841-854
    • Mishra, A.1    Wu, C.2    Yang, J.3    Cisar, J.O.4    Das, A.5    Ton-That, H.6
  • 213
    • 67651233733 scopus 로고    scopus 로고
    • Streptococcus mitis phage-encoded adhesins mediate attachment to {alpha}2-8-linked sialic acid residues on platelet membrane gangliosides
    • Mitchell J., Sullam P.M. Streptococcus mitis phage-encoded adhesins mediate attachment to {alpha}2-8-linked sialic acid residues on platelet membrane gangliosides. Infection and Immunity 2009, 77:3485-3490.
    • (2009) Infection and Immunity , vol.77 , pp. 3485-3490
    • Mitchell, J.1    Sullam, P.M.2
  • 215
    • 33846453283 scopus 로고    scopus 로고
    • Synovial inflammation in active rheumatoid arthritis and psoriatic arthritis facilitates trapping of a variety of oral bacterial DNAs
    • Moen K., Brun J.G., Valen M., Skartveit L., Eribe E.K.R., Olsen I., et al. Synovial inflammation in active rheumatoid arthritis and psoriatic arthritis facilitates trapping of a variety of oral bacterial DNAs. Clinical and Experimental Rheumatology 2006, 24:656-663.
    • (2006) Clinical and Experimental Rheumatology , vol.24 , pp. 656-663
    • Moen, K.1    Brun, J.G.2    Valen, M.3    Skartveit, L.4    Eribe, E.K.R.5    Olsen, I.6
  • 216
    • 0025164808 scopus 로고
    • Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria
    • Moncla B.J., Braham P., Hillier S.L. Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria. Journal of Clinical Microbiology 1990, 28:422-425.
    • (1990) Journal of Clinical Microbiology , vol.28 , pp. 422-425
    • Moncla, B.J.1    Braham, P.2    Hillier, S.L.3
  • 217
    • 0025989354 scopus 로고
    • Rapid presumptive identification of black-pigmented gram-negative anaerobic bacteria by using 4-methylumbelliferone derivatives
    • Moncla B.J., Braham P., Rabe L.K., Hillier S.L. Rapid presumptive identification of black-pigmented gram-negative anaerobic bacteria by using 4-methylumbelliferone derivatives. Journal of Clinical Microbiology 1991, 29:1955-1958.
    • (1991) Journal of Clinical Microbiology , vol.29 , pp. 1955-1958
    • Moncla, B.J.1    Braham, P.2    Rabe, L.K.3    Hillier, S.L.4
  • 218
    • 84870865474 scopus 로고    scopus 로고
    • Streptococcus gordonii collagen-binding domain protein CbdA may enhance bacterial survival in instrumented root canals ex vivo
    • Moses P.J., Power D.A., Jesionowski A.M., Jenkinson H.F., Pantera E.A., Vickerman M.M. Streptococcus gordonii collagen-binding domain protein CbdA may enhance bacterial survival in instrumented root canals ex vivo. Journal of Endodontics 2013, 39:39-43.
    • (2013) Journal of Endodontics , vol.39 , pp. 39-43
    • Moses, P.J.1    Power, D.A.2    Jesionowski, A.M.3    Jenkinson, H.F.4    Pantera, E.A.5    Vickerman, M.M.6
  • 221
    • 84900448201 scopus 로고    scopus 로고
    • Sialic acid residues are essential for cell lysis mediated by leukotoxin from Aggregatibacter actinomycetemcomitans
    • Munksgaard P.S., Skals M., Reinholdt J., Poulsen K., Jensen M.R., Yang C., et al. Sialic acid residues are essential for cell lysis mediated by leukotoxin from Aggregatibacter actinomycetemcomitans. Infection and Immunity 2014, 82:2219-2228.
    • (2014) Infection and Immunity , vol.82 , pp. 2219-2228
    • Munksgaard, P.S.1    Skals, M.2    Reinholdt, J.3    Poulsen, K.4    Jensen, M.R.5    Yang, C.6
  • 223
    • 4143067930 scopus 로고    scopus 로고
    • Analysis of major virulence factors in Porphyromonas gingivalis under various culture temperatures using specific antibodies
    • Murakami Y., Masuda T., Imai M., Iwami J., Nakamura H., Noguchi T., et al. Analysis of major virulence factors in Porphyromonas gingivalis under various culture temperatures using specific antibodies. Microbiology and Immunology 2004, 48:561-569.
    • (2004) Microbiology and Immunology , vol.48 , pp. 561-569
    • Murakami, Y.1    Masuda, T.2    Imai, M.3    Iwami, J.4    Nakamura, H.5    Noguchi, T.6
  • 224
    • 0036891933 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva
    • Murakami M., Ohtake T., Dorschner R.A., Gallo R.L. Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. Journal of Dental Research 2002, 81:845-850.
    • (2002) Journal of Dental Research , vol.81 , pp. 845-850
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.A.3    Gallo, R.L.4
  • 228
    • 77349112434 scopus 로고    scopus 로고
    • Fusobacterium nucleatum envelope protein FomA is immunogenic and binds to the salivary statherin-derived peptide
    • Nakagaki H., Sekine S., Terao Y., Toe M., Tanaka M., Ito H.-O., et al. Fusobacterium nucleatum envelope protein FomA is immunogenic and binds to the salivary statherin-derived peptide. Infection and Immunity 2010, 78:1185-1192.
    • (2010) Infection and Immunity , vol.78 , pp. 1185-1192
    • Nakagaki, H.1    Sekine, S.2    Terao, Y.3    Toe, M.4    Tanaka, M.5    Ito, H.-O.6
  • 229
    • 77956126019 scopus 로고    scopus 로고
    • Resistance to acidic environments of caries-associated bacteria: Bifidobacterium dentium and Bifidobacterium longum
    • Nakajo K., Takahashi N., Beighton D. Resistance to acidic environments of caries-associated bacteria: Bifidobacterium dentium and Bifidobacterium longum. Caries Research 2010, 44:431-437.
    • (2010) Caries Research , vol.44 , pp. 431-437
    • Nakajo, K.1    Takahashi, N.2    Beighton, D.3
  • 230
    • 72649091762 scopus 로고    scopus 로고
    • Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin
    • Nakano K., Nomura R., Taniguchi N., Lapirattanakul J., Kojima A., Naka S., et al. Molecular characterization of Streptococcus mutans strains containing the cnm gene encoding a collagen-binding adhesin. Archives of Oral Biology 2010, 55:34-39.
    • (2010) Archives of Oral Biology , vol.55 , pp. 34-39
    • Nakano, K.1    Nomura, R.2    Taniguchi, N.3    Lapirattanakul, J.4    Kojima, A.5    Naka, S.6
  • 231
    • 33846604620 scopus 로고    scopus 로고
    • Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-Negative bacteria?
    • Nguyen K.-A., Travis J., Potempa J. Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-Negative bacteria?. Journal of Bacteriology 2007, 189:833-843.
    • (2007) Journal of Bacteriology , vol.189 , pp. 833-843
    • Nguyen, K.-A.1    Travis, J.2    Potempa, J.3
  • 232
    • 84884554714 scopus 로고    scopus 로고
    • Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans
    • Nihira T., Suzuki E., Kitaoka M., Nishimoto M., Ohtsubo K., Nakai H. Discovery of β-1,4-D-mannosyl-N-acetyl-D-glucosamine phosphorylase involved in the metabolism of N-glycans. The Journal of Biological Chemistry 2013, 288:27366-27374.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 27366-27374
    • Nihira, T.1    Suzuki, E.2    Kitaoka, M.3    Nishimoto, M.4    Ohtsubo, K.5    Nakai, H.6
  • 233
    • 63649159948 scopus 로고    scopus 로고
    • Crystal structure of FadA adhesin from Fusobacterium nucleatum reveals a novel oligomerization motif, the leucine chain
    • Nithianantham S., Xu M., Yamada M., Ikegami A., Shoham M., Han Y.W. Crystal structure of FadA adhesin from Fusobacterium nucleatum reveals a novel oligomerization motif, the leucine chain. The Journal of Biological Chemistry 2009, 284:3865-3872.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 3865-3872
    • Nithianantham, S.1    Xu, M.2    Yamada, M.3    Ikegami, A.4    Shoham, M.5    Han, Y.W.6
  • 235
    • 33845406952 scopus 로고    scopus 로고
    • Adherence and internalization of Streptococcus gordonii by epithelial cells involves beta1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides
    • Nobbs A.H., Shearer B.H., Drobni M., Jepson M.A., Jenkinson H.F. Adherence and internalization of Streptococcus gordonii by epithelial cells involves beta1 integrin recognition by SspA and SspB (antigen I/II family) polypeptides. Cellular Microbiology 2007, 9:65-83.
    • (2007) Cellular Microbiology , vol.9 , pp. 65-83
    • Nobbs, A.H.1    Shearer, B.H.2    Drobni, M.3    Jepson, M.A.4    Jenkinson, H.F.5
  • 238
    • 65349089447 scopus 로고    scopus 로고
    • Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis
    • Oda H., Saiki K., Tonosaki M., Yajima A., Konishi K. Participation of the secreted dipeptidyl and tripeptidyl aminopeptidases in asaccharolytic growth of Porphyromonas gingivalis. Journal of Periodontal Research 2009, 44:362-367.
    • (2009) Journal of Periodontal Research , vol.44 , pp. 362-367
    • Oda, H.1    Saiki, K.2    Tonosaki, M.3    Yajima, A.4    Konishi, K.5
  • 240
  • 241
    • 80055075854 scopus 로고    scopus 로고
    • Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources
    • Ohara-Nemoto Y., Shimoyama Y., Kimura S., Kon A., Haraga H., Ono T., et al. Asp- and Glu-specific novel dipeptidyl peptidase 11 of Porphyromonas gingivalis ensures utilization of proteinaceous energy sources. The Journal of Biological Chemistry 2011, 286:38115-38127.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 38115-38127
    • Ohara-Nemoto, Y.1    Shimoyama, Y.2    Kimura, S.3    Kon, A.4    Haraga, H.5    Ono, T.6
  • 243
    • 79951578723 scopus 로고    scopus 로고
    • Pili of oral Streptococcus sanguinis bind to salivary amylase and promote the biofilm formation
    • Okahashi N., Nakata M., Terao Y., Isoda R., Sakurai A., Sumitomo T., et al. Pili of oral Streptococcus sanguinis bind to salivary amylase and promote the biofilm formation. Microbial Pathogenesis 2011, 50:148-154.
    • (2011) Microbial Pathogenesis , vol.50 , pp. 148-154
    • Okahashi, N.1    Nakata, M.2    Terao, Y.3    Isoda, R.4    Sakurai, A.5    Sumitomo, T.6
  • 244
    • 0024660048 scopus 로고
    • Molecular characterization of a surface protein antigen gene from serotype c Streptococcus mutans, implicated in dental caries
    • Okahashi N., Sasakawa C., Yoshikawa M. Molecular characterization of a surface protein antigen gene from serotype c Streptococcus mutans, implicated in dental caries. Molecular Microbiology 1989, 3:673-678.
    • (1989) Molecular Microbiology , vol.3 , pp. 673-678
    • Okahashi, N.1    Sasakawa, C.2    Yoshikawa, M.3
  • 245
    • 77956392378 scopus 로고    scopus 로고
    • Inhibition of Streptococcus mutans adherence and biofilm formation using analogues of the SspB peptide
    • Elsevier Ltd
    • Okuda K., Hanada N., Usui Y., Takeuchi H., Koba H., Nakao R., et al. Inhibition of Streptococcus mutans adherence and biofilm formation using analogues of the SspB peptide. Archives of Oral Biology 2010, 55:754-762. Elsevier Ltd.
    • (2010) Archives of Oral Biology , vol.55 , pp. 754-762
    • Okuda, K.1    Hanada, N.2    Usui, Y.3    Takeuchi, H.4    Koba, H.5    Nakao, R.6
  • 248
    • 84876190932 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of genomically-diverse isolates of Streptococcus mutans
    • Palmer S.R., Miller J.H., Abranches J., Zeng L., Lefebure T., Richards V.P., et al. Phenotypic heterogeneity of genomically-diverse isolates of Streptococcus mutans. PLoS One 2013, 8:e61358.
    • (2013) PLoS One , vol.8 , pp. e61358
    • Palmer, S.R.1    Miller, J.H.2    Abranches, J.3    Zeng, L.4    Lefebure, T.5    Richards, V.P.6
  • 249
    • 27444442409 scopus 로고    scopus 로고
    • Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans
    • Paramonov N., Rangarajan M., Hashim A., Gallagher A., Aduse-Opoku J., Slaney J.M., et al. Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Molecular Microbiology 2005, 58:847-863.
    • (2005) Molecular Microbiology , vol.58 , pp. 847-863
    • Paramonov, N.1    Rangarajan, M.2    Hashim, A.3    Gallagher, A.4    Aduse-Opoku, J.5    Slaney, J.M.6
  • 250
    • 21544462007 scopus 로고    scopus 로고
    • Short Fimbriae of Porphyromonas gingivalis and Their Role in Coadhesion with Streptococcus gordonii
    • Park Y., Simionato M.R., Sekiya K., Murakami Y., James D., Chen W., et al. Short Fimbriae of Porphyromonas gingivalis and Their Role in Coadhesion with Streptococcus gordonii. Infection and Immunity 2005, 73:3983-3989.
    • (2005) Infection and Immunity , vol.73 , pp. 3983-3989
    • Park, Y.1    Simionato, M.R.2    Sekiya, K.3    Murakami, Y.4    James, D.5    Chen, W.6
  • 251
    • 84862814575 scopus 로고    scopus 로고
    • Sialylation of epidermal growth factor receptor regulates receptor activity and chemosensitivity to gefitinib in colon cancer cells
    • Park J.-J., Yi J.Y., Jin Y.B., Lee Y.-J., Lee J.-S., Lee Y.-S., et al. Sialylation of epidermal growth factor receptor regulates receptor activity and chemosensitivity to gefitinib in colon cancer cells. Biochemical Pharmacology 2012, 83:849-857.
    • (2012) Biochemical Pharmacology , vol.83 , pp. 849-857
    • Park, J.-J.1    Yi, J.Y.2    Jin, Y.B.3    Lee, Y.-J.4    Lee, J.-S.5    Lee, Y.-S.6
  • 252
    • 33748993158 scopus 로고    scopus 로고
    • Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation
    • Perez B.A., Planet P.J., Kachlany S.C., Tomich M., Fine D.H., Figurski D.H. Genetic analysis of the requirement for flp-2, tadV, and rcpB in Actinobacillus actinomycetemcomitans biofilm formation. Journal of Bacteriology 2006, 188:6361-6375.
    • (2006) Journal of Bacteriology , vol.188 , pp. 6361-6375
    • Perez, B.A.1    Planet, P.J.2    Kachlany, S.C.3    Tomich, M.4    Fine, D.H.5    Figurski, D.H.6
  • 253
    • 73949116790 scopus 로고    scopus 로고
    • Evidence for a novel human-specific xeno-auto-antibody response against vascular endothelium
    • Pham T., Gregg C.J., Karp F., Chow R., Padler-karavani V., Cao H., et al. Evidence for a novel human-specific xeno-auto-antibody response against vascular endothelium. Blood 2012, 114:5225-5235.
    • (2012) Blood , vol.114 , pp. 5225-5235
    • Pham, T.1    Gregg, C.J.2    Karp, F.3    Chow, R.4    Padler-karavani, V.5    Cao, H.6
  • 254
    • 77956130622 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia
    • Pham T.K., Roy S., Noirel J., Douglas I., Wright P.C., Stafford G.P., et al. A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia. Proteomics 2010, 10:3130-3141.
    • (2010) Proteomics , vol.10 , pp. 3130-3141
    • Pham, T.K.1    Roy, S.2    Noirel, J.3    Douglas, I.4    Wright, P.C.5    Stafford, G.P.6
  • 255
    • 84896848081 scopus 로고    scopus 로고
    • Structural and functional characterisation of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling Bacteroidetes spp
    • Phansopa C., Roy S., Rafferty J.B., Douglas C.W.I., Pandhal J., Wright P.C., et al. Structural and functional characterisation of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling Bacteroidetes spp. The Biochemical Journal 2013, 458:499-511.
    • (2013) The Biochemical Journal , vol.458 , pp. 499-511
    • Phansopa, C.1    Roy, S.2    Rafferty, J.B.3    Douglas, C.W.I.4    Pandhal, J.5    Wright, P.C.6
  • 258
    • 0029913412 scopus 로고    scopus 로고
    • Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis
    • Pike R.N., Potempa J., McGraw W., Coetzer T.H., Travis J. Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis. Journal of Bacteriology 1996, 178:2876-2882.
    • (1996) Journal of Bacteriology , vol.178 , pp. 2876-2882
    • Pike, R.N.1    Potempa, J.2    McGraw, W.3    Coetzer, T.H.4    Travis, J.5
  • 259
    • 84881414476 scopus 로고    scopus 로고
    • Determining the presence of periodontopathic virulence factors in short-term postmortem Alzheimer's disease brain tissue
    • Poole S., Singhrao S.K., Kesavalu L., Curtis M.A., Crean S. Determining the presence of periodontopathic virulence factors in short-term postmortem Alzheimer's disease brain tissue. Journal of Alzheimer's Disease 2013, 36:665-677.
    • (2013) Journal of Alzheimer's Disease , vol.36 , pp. 665-677
    • Poole, S.1    Singhrao, S.K.2    Kesavalu, L.3    Curtis, M.A.4    Crean, S.5
  • 263
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa J., Mikolajczyk-Pawlinska J., Brassell D., Nelson D., Thøgersen I.B., Enghild J.J., et al. Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis. The Journal of Biological Chemistry 1998, 273:21648-21657.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 21648-21657
    • Potempa, J.1    Mikolajczyk-Pawlinska, J.2    Brassell, D.3    Nelson, D.4    Thøgersen, I.B.5    Enghild, J.J.6
  • 264
    • 0036855529 scopus 로고    scopus 로고
    • Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins
    • Puntervoll P., Ruud M., Bruseth L.J., Kleivdal H., Høgh B.T., Benz R., et al. Structural characterization of the fusobacterial non-specific porin FomA suggests a 14-stranded topology, unlike the classical porins. Microbiology 2002, 148:3395-3403.
    • (2002) Microbiology , vol.148 , pp. 3395-3403
    • Puntervoll, P.1    Ruud, M.2    Bruseth, L.J.3    Kleivdal, H.4    Høgh, B.T.5    Benz, R.6
  • 265
    • 0027489644 scopus 로고
    • Inactivation of the Streptococcus mutans wall-associated protein A gene (wapA) results in a decrease in sucrose-dependent adherence and aggregation
    • Qian H., Dao M.L. Inactivation of the Streptococcus mutans wall-associated protein A gene (wapA) results in a decrease in sucrose-dependent adherence and aggregation. Infection and Immunity 1993, 61(12):5021-5028.
    • (1993) Infection and Immunity , vol.61 , Issue.12 , pp. 5021-5028
    • Qian, H.1    Dao, M.L.2
  • 268
    • 70450223518 scopus 로고    scopus 로고
    • Neu1 desialylation of sialyl alpha-2,3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling
    • Ray S., Jayanth P., Franchuk S., Finlay T., Seyrantepe V., Beyaert R., et al. Neu1 desialylation of sialyl alpha-2,3-linked beta-galactosyl residues of TOLL-like receptor 4 is essential for receptor activation and cellular signaling. Cellular Signalling 2010, 22:314-324.
    • (2010) Cellular Signalling , vol.22 , pp. 314-324
    • Ray, S.1    Jayanth, P.2    Franchuk, S.3    Finlay, T.4    Seyrantepe, V.5    Beyaert, R.6
  • 270
    • 0025270701 scopus 로고
    • Molecular aspects of immunoglobulin A1 degradation by oral streptococci
    • Reinholdt J., Tomana M., Mortensen S.B., Kilian M. Molecular aspects of immunoglobulin A1 degradation by oral streptococci. Infection and Immunity 1990, 58:1186-1194.
    • (1990) Infection and Immunity , vol.58 , pp. 1186-1194
    • Reinholdt, J.1    Tomana, M.2    Mortensen, S.B.3    Kilian, M.4
  • 271
    • 79959826593 scopus 로고    scopus 로고
    • The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG
    • Renzi F., Manfredi P., Mally M., Moes S., Jenö P., Cornelis G.R., et al. The N-glycan glycoprotein deglycosylation complex (Gpd) from Capnocytophaga canimorsus deglycosylates human IgG. PLoS Pathogens 2011, 7:e1002118.
    • (2011) PLoS Pathogens , vol.7 , pp. e1002118
    • Renzi, F.1    Manfredi, P.2    Mally, M.3    Moes, S.4    Jenö, P.5    Cornelis, G.R.6
  • 273
    • 0344875610 scopus 로고    scopus 로고
    • Evidence of regio-specific glycosylation in human intestinal mucins: Presence of an acidic gradient along the intestinal tract
    • Robbe C., Capon C., Maes E., Rousset M., Zweibaum A., Zanetta J.-P., et al. Evidence of regio-specific glycosylation in human intestinal mucins: Presence of an acidic gradient along the intestinal tract. The Journal of Biological Chemistry 2003, 278:46337-46348.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 46337-46348
    • Robbe, C.1    Capon, C.2    Maes, E.3    Rousset, M.4    Zweibaum, A.5    Zanetta, J.-P.6
  • 274
    • 79955743569 scopus 로고    scopus 로고
    • Porphyromonas gingivalis mutY is involved in the repair of oxidative stress-induced DNA mispairing
    • Robles A.G., Reid K., Roy F., Fletcher H.M. Porphyromonas gingivalis mutY is involved in the repair of oxidative stress-induced DNA mispairing. Molecular Oral Microbiology 2011, 26:175-186.
    • (2011) Molecular Oral Microbiology , vol.26 , pp. 175-186
    • Robles, A.G.1    Reid, K.2    Roy, F.3    Fletcher, H.M.4
  • 275
  • 276
    • 0037407497 scopus 로고    scopus 로고
    • Aae, an autotransporter involved in adhesion of Actinobacillus actinomycetemcomitans to epithelial cells
    • Rose J.E., Meyer D.H., Fives-Taylor P.M. Aae, an autotransporter involved in adhesion of Actinobacillus actinomycetemcomitans to epithelial cells. Infection and Immunity 2003, 71:2384-2393.
    • (2003) Infection and Immunity , vol.71 , pp. 2384-2393
    • Rose, J.E.1    Meyer, D.H.2    Fives-Taylor, P.M.3
  • 277
    • 77951053020 scopus 로고    scopus 로고
    • A novel sialic acid utilization and uptake system in the periodontal pathogen Tannerella forsythia
    • Roy S., Douglas C.W.I., Stafford G.P. A novel sialic acid utilization and uptake system in the periodontal pathogen Tannerella forsythia. Journal of Bacteriology 2010, 192:2285-2293.
    • (2010) Journal of Bacteriology , vol.192 , pp. 2285-2293
    • Roy, S.1    Douglas, C.W.I.2    Stafford, G.P.3
  • 279
    • 84863400957 scopus 로고    scopus 로고
    • Beta-hexosaminidase activity of the oral pathogen Tannerella forsythia influences biofilm formation on glycoprotein substrates
    • Roy S., Phansopa C., Stafford P., Honma K., Douglas C.W.I., Sharma A., et al. Beta-hexosaminidase activity of the oral pathogen Tannerella forsythia influences biofilm formation on glycoprotein substrates. FEMS Immunology and Medical Microbiology 2012, 65:116-120.
    • (2012) FEMS Immunology and Medical Microbiology , vol.65 , pp. 116-120
    • Roy, S.1    Phansopa, C.2    Stafford, P.3    Honma, K.4    Douglas, C.W.I.5    Sharma, A.6
  • 280
    • 84882334105 scopus 로고    scopus 로고
    • Fusobacterium nucleatum promotes colorectal carcinogenesis by modulating E-cadherin/β-catenin signaling via its FadA adhesin
    • Rubinstein M.R., Wang X., Liu W., Hao Y., Cai G., Han Y.W. Fusobacterium nucleatum promotes colorectal carcinogenesis by modulating E-cadherin/β-catenin signaling via its FadA adhesin. Cell Host Z Microbe 2013, 14:195-206.
    • (2013) Cell Host Z Microbe , vol.14 , pp. 195-206
    • Rubinstein, M.R.1    Wang, X.2    Liu, W.3    Hao, Y.4    Cai, G.5    Han, Y.W.6
  • 281
    • 0035081315 scopus 로고    scopus 로고
    • Intracellular Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in buccal epithelial cells collected from human subjects
    • Rudney J.D., Chen R., Sedgewick G.J. Intracellular Actinobacillus actinomycetemcomitans and Porphyromonas gingivalis in buccal epithelial cells collected from human subjects. Infection and Immunity 2001, 69:2700-2707.
    • (2001) Infection and Immunity , vol.69 , pp. 2700-2707
    • Rudney, J.D.1    Chen, R.2    Sedgewick, G.J.3
  • 282
    • 84873285509 scopus 로고    scopus 로고
    • Cleavage of extracellular matrix in periodontitis: Gingipains differentially affect cell adhesion activities of fibronectin and tenascin-C
    • Ruggiero S., Cosgarea R., Potempa J., Potempa B., Eick S., Chiquet M. Cleavage of extracellular matrix in periodontitis: Gingipains differentially affect cell adhesion activities of fibronectin and tenascin-C. Biochimica et Biophysica Acta 2013, 1832:517-526.
    • (2013) Biochimica et Biophysica Acta , vol.1832 , pp. 517-526
    • Ruggiero, S.1    Cosgarea, R.2    Potempa, J.3    Potempa, B.4    Eick, S.5    Chiquet, M.6
  • 283
    • 0033785336 scopus 로고    scopus 로고
    • Identification of polymorphonuclear leukocyte and HL-60 cell receptors for adhesins of Streptococcus gordonii and Actinomyces naeslundii
    • Ruhl S., Cisar J.O., Sandberg A.L. Identification of polymorphonuclear leukocyte and HL-60 cell receptors for adhesins of Streptococcus gordonii and Actinomyces naeslundii. Infection and Immunity 2000, 68:6346-6354.
    • (2000) Infection and Immunity , vol.68 , pp. 6346-6354
    • Ruhl, S.1    Cisar, J.O.2    Sandberg, A.L.3
  • 284
    • 33750465551 scopus 로고    scopus 로고
    • Novel surface structures are associated with the adhesion of Actinobacillus actinomycetemcomitans to collagen
    • Ruiz T., Lenox C., Radermacher M., Mintz K.P. Novel surface structures are associated with the adhesion of Actinobacillus actinomycetemcomitans to collagen. Infection and Immunity 2006, 74:6163-6170.
    • (2006) Infection and Immunity , vol.74 , pp. 6163-6170
    • Ruiz, T.1    Lenox, C.2    Radermacher, M.3    Mintz, K.P.4
  • 285
  • 286
    • 0029353108 scopus 로고
    • Bacteria in human mouths involved in the production and utilization of hydrogen peroxide
    • Ryan C.S., Kleinberg I. Bacteria in human mouths involved in the production and utilization of hydrogen peroxide. Archives of Oral Biology 1995, 40:753-763.
    • (1995) Archives of Oral Biology , vol.40 , pp. 753-763
    • Ryan, C.S.1    Kleinberg, I.2
  • 287
    • 74049146346 scopus 로고    scopus 로고
    • The role of Sov protein in the secretion of gingipain protease virulence factors of Porphyromonas gingivalis
    • Saiki K., Konishi K. The role of Sov protein in the secretion of gingipain protease virulence factors of Porphyromonas gingivalis. FEMS Microbiology Letters 2010, 302:166-174.
    • (2010) FEMS Microbiology Letters , vol.302 , pp. 166-174
    • Saiki, K.1    Konishi, K.2
  • 288
    • 84891929978 scopus 로고    scopus 로고
    • Porphyromonas gingivalis C-terminal signal peptidase PG0026 and HagA interact with outer membrane protein PG27/LptO
    • Saiki K., Konishi K. Porphyromonas gingivalis C-terminal signal peptidase PG0026 and HagA interact with outer membrane protein PG27/LptO. Molecular Oral Microbiology 2014, 29:32-44.
    • (2014) Molecular Oral Microbiology , vol.29 , pp. 32-44
    • Saiki, K.1    Konishi, K.2
  • 289
    • 33947428014 scopus 로고    scopus 로고
    • Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of Tannerella forsythensis
    • Sakakibara J., Nagano K., Murakami Y., Higuchi N., Nakamura H., Shimozato K., et al. Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of Tannerella forsythensis. Microbiology 2007, 153:866-876.
    • (2007) Microbiology , vol.153 , pp. 866-876
    • Sakakibara, J.1    Nagano, K.2    Murakami, Y.3    Higuchi, N.4    Nakamura, H.5    Shimozato, K.6
  • 290
    • 84861214431 scopus 로고    scopus 로고
    • The branched-chain amino acid aminotransferase encoded by ilvE is involved in acid tolerance in Streptococcus mutans
    • Santiago B., MacGilvray M., Faustoferri R.C., Quivey R.G. The branched-chain amino acid aminotransferase encoded by ilvE is involved in acid tolerance in Streptococcus mutans. Journal of Bacteriology 2012, 194:2010-2019.
    • (2012) Journal of Bacteriology , vol.194 , pp. 2010-2019
    • Santiago, B.1    MacGilvray, M.2    Faustoferri, R.C.3    Quivey, R.G.4
  • 293
    • 20144366153 scopus 로고    scopus 로고
    • Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis
    • Sato K., Sakai E., Veith P.D., Shoji M., Kikuchi Y., Yukitake H., et al. Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. The Journal of Biological Chemistry 2005, 280:8668-8677.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 8668-8677
    • Sato, K.1    Sakai, E.2    Veith, P.D.3    Shoji, M.4    Kikuchi, Y.5    Yukitake, H.6
  • 296
    • 0029013679 scopus 로고
    • Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins
    • Schenkein H.A., Fletcher H.M., Bodnar M., Macrina F.L. Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins. Journal of Immunology 1995, 154:5331-5337.
    • (1995) Journal of Immunology , vol.154 , pp. 5331-5337
    • Schenkein, H.A.1    Fletcher, H.M.2    Bodnar, M.3    Macrina, F.L.4
  • 298
    • 0030814676 scopus 로고    scopus 로고
    • The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct binding domains
    • Sciotti M.A., Yamodo I., Klein J.P., Ogier J.A. The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct binding domains. FEMS Microbiology Letters 1997, 153:439-445.
    • (1997) FEMS Microbiology Letters , vol.153 , pp. 439-445
    • Sciotti, M.A.1    Yamodo, I.2    Klein, J.P.3    Ogier, J.A.4
  • 299
    • 78649377975 scopus 로고    scopus 로고
    • Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii
    • Seepersaud R., Bensing B.A., Yen Y.T., Sullam P.M. Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii. Molecular Microbiology 2010, 78:490-505.
    • (2010) Molecular Microbiology , vol.78 , pp. 490-505
    • Seepersaud, R.1    Bensing, B.A.2    Yen, Y.T.3    Sullam, P.M.4
  • 300
    • 33749023323 scopus 로고    scopus 로고
    • The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis
    • Seers C.A., Slakeski N., Veith P.D., Nikolof T., Chen Y.-Y., Dashper S.G., et al. The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. Journal of Bacteriology 2006, 188:6376-6386.
    • (2006) Journal of Bacteriology , vol.188 , pp. 6376-6386
    • Seers, C.A.1    Slakeski, N.2    Veith, P.D.3    Nikolof, T.4    Chen, Y.-Y.5    Dashper, S.G.6
  • 301
    • 84865860828 scopus 로고    scopus 로고
    • Analysis of the cell surface layer ultrastructure of the oral pathogen Tannerella forsythia
    • Sekot G., Posch G., Oh Y.J., Zayni S., Mayer H.F., Pum D., et al. Analysis of the cell surface layer ultrastructure of the oral pathogen Tannerella forsythia. Archives of Microbiology 2012, 194:525-539.
    • (2012) Archives of Microbiology , vol.194 , pp. 525-539
    • Sekot, G.1    Posch, G.2    Oh, Y.J.3    Zayni, S.4    Mayer, H.F.5    Pum, D.6
  • 302
    • 84874067867 scopus 로고    scopus 로고
    • A bacterial glycan core linked to surface (S)-layer proteins modulates host immunity through Th17 suppression
    • Settem R.P., Honma K., Nakajima T., Phansopa C., Roy S., Stafford G.P., et al. A bacterial glycan core linked to surface (S)-layer proteins modulates host immunity through Th17 suppression. Mucosal Immunology 2013, 6:415-426.
    • (2013) Mucosal Immunology , vol.6 , pp. 415-426
    • Settem, R.P.1    Honma, K.2    Nakajima, T.3    Phansopa, C.4    Roy, S.5    Stafford, G.P.6
  • 303
    • 84897944384 scopus 로고    scopus 로고
    • Protein-linked glycans in periodontal bacteria: Prevalence and role at the immune interface
    • Settem R.P., Honma K., Stafford G.P., Sharma A. Protein-linked glycans in periodontal bacteria: Prevalence and role at the immune interface. Frontiers in Microbiology 2013, 4:310.
    • (2013) Frontiers in Microbiology , vol.4 , pp. 310
    • Settem, R.P.1    Honma, K.2    Stafford, G.P.3    Sharma, A.4
  • 304
    • 77955739936 scopus 로고    scopus 로고
    • Virulence mechanisms of Tannerella forsythia
    • Sharma A. Virulence mechanisms of Tannerella forsythia. Periodontology 2010, 2000(54):106-116.
    • (2010) Periodontology , vol.2000 , Issue.54 , pp. 106-116
    • Sharma, A.1
  • 305
    • 12444307396 scopus 로고    scopus 로고
    • Synergy between Tannerella forsythia and Fusobacterium nucleatum in biofilm formation
    • Sharma A., Inagaki S., Sigurdson W., Kuramitsu H.K. Synergy between Tannerella forsythia and Fusobacterium nucleatum in biofilm formation. Oral Microbiology and Immunology 2005, 20(1):39-42.
    • (2005) Oral Microbiology and Immunology , vol.20 , Issue.1 , pp. 39-42
    • Sharma, A.1    Inagaki, S.2    Sigurdson, W.3    Kuramitsu, H.K.4
  • 306
    • 0031797896 scopus 로고    scopus 로고
    • Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037
    • Sharma A., Sojar H.T., Glurich I., Honma K., Kuramitsu H.K., Genco R.J. Cloning, expression, and sequencing of a cell surface antigen containing a leucine-rich repeat motif from Bacteroides forsythus ATCC 43037. Infection and. Immunity 1998, 66:5703-5710.
    • (1998) Infection and. Immunity , vol.66 , pp. 5703-5710
    • Sharma, A.1    Sojar, H.T.2    Glurich, I.3    Honma, K.4    Kuramitsu, H.K.5    Genco, R.J.6
  • 307
    • 33747054756 scopus 로고    scopus 로고
    • Enhanced acid resistance of oral streptococci at lethal pH values associated with acid-tolerant catabolism and with ATP synthase activity
    • Sheng J., Marquis R.E. Enhanced acid resistance of oral streptococci at lethal pH values associated with acid-tolerant catabolism and with ATP synthase activity. FEMS Microbiology Letters 2006, 262:93-98.
    • (2006) FEMS Microbiology Letters , vol.262 , pp. 93-98
    • Sheng, J.1    Marquis, R.E.2
  • 309
    • 0012330604 scopus 로고    scopus 로고
    • Purification and partial characterization of a dipeptidyl peptidase from Prevotella intermedia
    • Shibata Y., Miwa Y., Hirai K., Fujimura S. Purification and partial characterization of a dipeptidyl peptidase from Prevotella intermedia. Oral Microbiology and Immunology 2003, 18:196-198.
    • (2003) Oral Microbiology and Immunology , vol.18 , pp. 196-198
    • Shibata, Y.1    Miwa, Y.2    Hirai, K.3    Fujimura, S.4
  • 311
    • 84875516931 scopus 로고    scopus 로고
    • The surface layer of Tannerella forsythia contributes to serum resistance and oral bacterial coaggregation
    • Shimotahira N., Oogai Y., Kawada-Matsuo M., Yamada S., Fukutsuji K., Nagano K., et al. The surface layer of Tannerella forsythia contributes to serum resistance and oral bacterial coaggregation. Infection and Immunity 2013, 81:1198-1206.
    • (2013) Infection and Immunity , vol.81 , pp. 1198-1206
    • Shimotahira, N.1    Oogai, Y.2    Kawada-Matsuo, M.3    Yamada, S.4    Fukutsuji, K.5    Nagano, K.6
  • 312
    • 0036232069 scopus 로고    scopus 로고
    • Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: Cell surface polysaccharide as an anchorage for gingipains
    • Shoji M., Ratnayake D.B., Shi Y., Kadowaki T., Yamamoto K., Yoshimura F., et al. Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: Cell surface polysaccharide as an anchorage for gingipains. Microbiology (Reading, England) 2002, 148:1183-1191.
    • (2002) Microbiology (Reading, England) , vol.148 , pp. 1183-1191
    • Shoji, M.1    Ratnayake, D.B.2    Shi, Y.3    Kadowaki, T.4    Yamamoto, K.5    Yoshimura, F.6
  • 313
    • 78049445937 scopus 로고    scopus 로고
    • Interaction of Candida albicans cell wall Als3 protein with Streptococcus gordonii SspB adhesin promotes development of mixed-species communities
    • Silverman R.J., Nobbs A.H., Vickerman M.M., Barbour M.E., Jenkinson H.F. Interaction of Candida albicans cell wall Als3 protein with Streptococcus gordonii SspB adhesin promotes development of mixed-species communities. Infection and Immunity 2010, 78:4644-4652.
    • (2010) Infection and Immunity , vol.78 , pp. 4644-4652
    • Silverman, R.J.1    Nobbs, A.H.2    Vickerman, M.M.3    Barbour, M.E.4    Jenkinson, H.F.5
  • 315
    • 78650115933 scopus 로고    scopus 로고
    • C-terminal domain residues important for secretion and attachment of RgpB in Porphyromonas gingivalis
    • Slakeski N., Seers C.A., Ng K., Moore C., Cleal S.M., Veith P.D., et al. C-terminal domain residues important for secretion and attachment of RgpB in Porphyromonas gingivalis. Journal of Bacteriology 2011, 193:132-142.
    • (2011) Journal of Bacteriology , vol.193 , pp. 132-142
    • Slakeski, N.1    Seers, C.A.2    Ng, K.3    Moore, C.4    Cleal, S.M.5    Veith, P.D.6
  • 317
    • 0038825289 scopus 로고    scopus 로고
    • The haem pigment of the oral anaerobes Prevotella nigrescens and Prevotella intermedia is composed of iron(III) protoporphyrin IX in the monomeric form
    • Smalley J.W., Silver J., Birss A.J., Withnall R., Titler P.J. The haem pigment of the oral anaerobes Prevotella nigrescens and Prevotella intermedia is composed of iron(III) protoporphyrin IX in the monomeric form. Microbiology (Reading, England) 2003, 149:1711-1718.
    • (2003) Microbiology (Reading, England) , vol.149 , pp. 1711-1718
    • Smalley, J.W.1    Silver, J.2    Birss, A.J.3    Withnall, R.4    Titler, P.J.5
  • 318
    • 2542570174 scopus 로고    scopus 로고
    • A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin
    • Smalley J.W., Thomas M.F., Birss A.J., Withnall R., Silver J. A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin. The Biochemical Journal 2004, 379:833-840.
    • (2004) The Biochemical Journal , vol.379 , pp. 833-840
    • Smalley, J.W.1    Thomas, M.F.2    Birss, A.J.3    Withnall, R.4    Silver, J.5
  • 320
    • 84866163704 scopus 로고    scopus 로고
    • Porphyromonas gingivalis fimbriae carbohydrate specificity assessment by glycomics
    • Sojar H.T., Smith D.F. Porphyromonas gingivalis fimbriae carbohydrate specificity assessment by glycomics. FEMS Immunology and Medical Microbiology 2012, 66:83-87.
    • (2012) FEMS Immunology and Medical Microbiology , vol.66 , pp. 83-87
    • Sojar, H.T.1    Smith, D.F.2
  • 321
    • 84882920635 scopus 로고    scopus 로고
    • Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen Porphyromonas gingivalis during invasion
    • Stafford P., Higham J., Pinnock A., Murdoch C., Douglas C.W.I., Stafford G.P., et al. Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen Porphyromonas gingivalis during invasion. Molecular Oral Microbiology 2013, 28:366-378.
    • (2013) Molecular Oral Microbiology , vol.28 , pp. 366-378
    • Stafford, P.1    Higham, J.2    Pinnock, A.3    Murdoch, C.4    Douglas, C.W.I.5    Stafford, G.P.6
  • 322
    • 84863406922 scopus 로고    scopus 로고
    • Sialic acid, periodontal pathogens and Tannerella forsythia: Stick around and enjoy the feast!
    • Stafford G., Roy S., Honma K., Sharma A. Sialic acid, periodontal pathogens and Tannerella forsythia: Stick around and enjoy the feast!. Molecular Oral Microbiology 2012, 27:11-22.
    • (2012) Molecular Oral Microbiology , vol.27 , pp. 11-22
    • Stafford, G.1    Roy, S.2    Honma, K.3    Sharma, A.4
  • 324
    • 62849091082 scopus 로고    scopus 로고
    • Structures common to different glycans
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY), A. Varki, R. Cummings, J. Esko (Eds.)
    • Stanley P., Cummings R. Structures common to different glycans. Essentials in glycobiology 2009, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (NY). 2nd ed. A. Varki, R. Cummings, J. Esko (Eds.).
    • (2009) Essentials in glycobiology
    • Stanley, P.1    Cummings, R.2
  • 325
    • 70350468849 scopus 로고    scopus 로고
    • YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid
    • Steenbergen S.M., Jirik J.L., Vimr E.R. YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-acetylneuraminic acid. Journal of Bacteriology 2009, 191:7134-7139.
    • (2009) Journal of Bacteriology , vol.191 , pp. 7134-7139
    • Steenbergen, S.M.1    Jirik, J.L.2    Vimr, E.R.3
  • 326
    • 79955758639 scopus 로고    scopus 로고
    • Oxidative stress response in the opportunistic oral pathogen Fusobacterium nucleatum
    • Steeves C.H., Potrykus J., Barnett D.A., Bearne S.L. Oxidative stress response in the opportunistic oral pathogen Fusobacterium nucleatum. Proteomics 2011, 11:2027-2037.
    • (2011) Proteomics , vol.11 , pp. 2027-2037
    • Steeves, C.H.1    Potrykus, J.2    Barnett, D.A.3    Bearne, S.L.4
  • 327
    • 84902007666 scopus 로고    scopus 로고
    • Streptococcus mutans eDNA is up-regulated during growth in biofilms, actively released via membrane vesicles, and influenced by components of the protein secretion machinery
    • Sumei L., Klein M.I., Heim K.P., Fan Y., Bitoun J.P., Ahn S.-J., et al. Streptococcus mutans eDNA is up-regulated during growth in biofilms, actively released via membrane vesicles, and influenced by components of the protein secretion machinery. Journal of Bacteriology 2014, 196:2355-2366.
    • (2014) Journal of Bacteriology , vol.196 , pp. 2355-2366
    • Sumei, L.1    Klein, M.I.2    Heim, K.P.3    Fan, Y.4    Bitoun, J.P.5    Ahn, S.-J.6
  • 328
    • 77957870384 scopus 로고    scopus 로고
    • Identification of bistable populations of Porphyromonas gingivalis that differ in epithelial cell invasion
    • Suwannakul S., Stafford G.P., Whawell S.A., Douglas C.W.I. Identification of bistable populations of Porphyromonas gingivalis that differ in epithelial cell invasion. Microbiology (Reading, England) 2010, 156:3052-3064.
    • (2010) Microbiology (Reading, England) , vol.156 , pp. 3052-3064
    • Suwannakul, S.1    Stafford, G.P.2    Whawell, S.A.3    Douglas, C.W.I.4
  • 330
    • 0028942854 scopus 로고
    • In defense of the oral cavity: Structure, biosynthesis, and function of salivary mucins
    • Tabak L.A. In defense of the oral cavity: Structure, biosynthesis, and function of salivary mucins. Annual Review of Physiology 1995, 57:547-564.
    • (1995) Annual Review of Physiology , vol.57 , pp. 547-564
    • Tabak, L.A.1
  • 331
    • 0018827360 scopus 로고
    • Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans
    • Taichman N.S., Dean R.T., Sanderson C.J. Biochemical and morphological characterization of the killing of human monocytes by a leukotoxin derived from Actinobacillus actinomycetemcomitans. Infection and Immunity 1980, 28:258-268.
    • (1980) Infection and Immunity , vol.28 , pp. 258-268
    • Taichman, N.S.1    Dean, R.T.2    Sanderson, C.J.3
  • 332
    • 0038249024 scopus 로고    scopus 로고
    • Acid-neutralizing activity during amino acid fermentation by Porphyromonas gingivalis, Prevotella intermedia and Fusobacterium nucleatum
    • Takahashi N. Acid-neutralizing activity during amino acid fermentation by Porphyromonas gingivalis, Prevotella intermedia and Fusobacterium nucleatum. Oral Microbiology and Immunology 2003, 18:109-113.
    • (2003) Oral Microbiology and Immunology , vol.18 , pp. 109-113
    • Takahashi, N.1
  • 333
    • 0036176120 scopus 로고    scopus 로고
    • Identification and characterization of hsa, the gene encoding the sialic acid-binding adhesin of Streptococcus gordonii DL1
    • Takahashi Y., Konishi K., Cisar J.O., Yoshikawa M. Identification and characterization of hsa, the gene encoding the sialic acid-binding adhesin of Streptococcus gordonii DL1. Infection and Immunity 2002, 70:1209-1218.
    • (2002) Infection and Immunity , vol.70 , pp. 1209-1218
    • Takahashi, Y.1    Konishi, K.2    Cisar, J.O.3    Yoshikawa, M.4
  • 334
    • 79952065856 scopus 로고    scopus 로고
    • The role of bacteria in the caries process: Ecological perspectives
    • Takahashi N., Nyvad B. The role of bacteria in the caries process: Ecological perspectives. Journal of Dental Research 2011, 90:294-303.
    • (2011) Journal of Dental Research , vol.90 , pp. 294-303
    • Takahashi, N.1    Nyvad, B.2
  • 335
    • 0033873462 scopus 로고    scopus 로고
    • Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis
    • Takahashi N., Sato T., Yamada T. Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. Journal of Bacteriology 2000, 182:4704-4710.
    • (2000) Journal of Bacteriology , vol.182 , pp. 4704-4710
    • Takahashi, N.1    Sato, T.2    Yamada, T.3
  • 336
    • 3042554572 scopus 로고    scopus 로고
    • Functional analysis of the Streptococcus gordonii DL1 sialic acid-binding adhesin and its essential role in bacterial binding to platelets
    • Takahashi Y., Yajima A., Cisar J.O., Konishi K. Functional analysis of the Streptococcus gordonii DL1 sialic acid-binding adhesin and its essential role in bacterial binding to platelets. Infection and Immunity 2004, 72:3876-3882.
    • (2004) Infection and Immunity , vol.72 , pp. 3876-3882
    • Takahashi, Y.1    Yajima, A.2    Cisar, J.O.3    Konishi, K.4
  • 337
    • 12844258218 scopus 로고    scopus 로고
    • A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems
    • Takii R., Kadowaki T., Baba A., Tsukuba T., Yamamoto K. A functional virulence complex composed of gingipains, adhesins, and lipopolysaccharide shows high affinity to host cells and matrix proteins and escapes recognition by host immune systems. Infection and Immunity 2005, 73:883-893.
    • (2005) Infection and Immunity , vol.73 , pp. 883-893
    • Takii, R.1    Kadowaki, T.2    Baba, A.3    Tsukuba, T.4    Yamamoto, K.5
  • 338
    • 77749288958 scopus 로고    scopus 로고
    • Glycosylation of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans is dependent upon the lipopolysaccharide biosynthetic pathway
    • Tang G., Mintz K.P. Glycosylation of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans is dependent upon the lipopolysaccharide biosynthetic pathway. Journal of Bacteriology 2010, 192:1395-1404.
    • (2010) Journal of Bacteriology , vol.192 , pp. 1395-1404
    • Tang, G.1    Mintz, K.P.2
  • 339
    • 84864809139 scopus 로고    scopus 로고
    • O-polysaccharide glycosylation is required for stability and function of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans
    • Tang G., Ruiz T., Mintz K.P. O-polysaccharide glycosylation is required for stability and function of the collagen adhesin EmaA of Aggregatibacter actinomycetemcomitans. Infection and Immunity 2012, 80:2868-2877.
    • (2012) Infection and Immunity , vol.80 , pp. 2868-2877
    • Tang, G.1    Ruiz, T.2    Mintz, K.P.3
  • 340
    • 0027682636 scopus 로고
    • Transport of sugars, including sucrose, by the msm transport system of Streptococcus mutans
    • Tao L., Sutcliffe I.C., Russell R.R., Ferretti J.J. Transport of sugars, including sucrose, by the msm transport system of Streptococcus mutans. Journal of Dental Research 1993, 72:1386-1390.
    • (1993) Journal of Dental Research , vol.72 , pp. 1386-1390
    • Tao, L.1    Sutcliffe, I.C.2    Russell, R.R.3    Ferretti, J.J.4
  • 341
    • 84655163916 scopus 로고    scopus 로고
    • Signal peptide of FadA adhesin from Fusobacterium nucleatum plays a novel structural role by modulating the filament's length and width
    • Témoin S., Wu K.L., Wu V., Shoham M., Han Y.W. Signal peptide of FadA adhesin from Fusobacterium nucleatum plays a novel structural role by modulating the filament's length and width. FEBS Letters 2012, 586:1-6.
    • (2012) FEBS Letters , vol.586 , pp. 1-6
    • Témoin, S.1    Wu, K.L.2    Wu, V.3    Shoham, M.4    Han, Y.W.5
  • 342
    • 66149143854 scopus 로고    scopus 로고
    • An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia
    • Thompson H., Homer K.A., Rao S., Booth V., Hosie A.H. An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia. Journal of Bacteriology 2009, 191:3623-3628.
    • (2009) Journal of Bacteriology , vol.191 , pp. 3623-3628
    • Thompson, H.1    Homer, K.A.2    Rao, S.3    Booth, V.4    Hosie, A.H.5
  • 343
    • 0036123711 scopus 로고    scopus 로고
    • The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse
    • Thomsson K.A., Prakobphol A., Leffler H., Reddy M.S., Levine M.J., Fisher S.J., et al. The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse. Glycobiology 2002, 12:1-14.
    • (2002) Glycobiology , vol.12 , pp. 1-14
    • Thomsson, K.A.1    Prakobphol, A.2    Leffler, H.3    Reddy, M.S.4    Levine, M.J.5    Fisher, S.J.6
  • 345
    • 0036308656 scopus 로고    scopus 로고
    • Crystal structure of the V-region of Streptococcus mutans antigen I/II at 2.4 A resolution suggests a sugar preformed binding site
    • Troffer-Charlier N., Ogier J., Moras D., Cavarelli J. Crystal structure of the V-region of Streptococcus mutans antigen I/II at 2.4 A resolution suggests a sugar preformed binding site. Journal of Molecular Biology 2002, 318:179-188.
    • (2002) Journal of Molecular Biology , vol.318 , pp. 179-188
    • Troffer-Charlier, N.1    Ogier, J.2    Moras, D.3    Cavarelli, J.4
  • 346
    • 0018356472 scopus 로고
    • Extraction and partial characterization of a leukotoxin from a plaque-derived Gram-negative microorganism
    • Tsai C.C., McArthur W.P., Baehni P.C., Hammond B.F., Taichman N.S. Extraction and partial characterization of a leukotoxin from a plaque-derived Gram-negative microorganism. Infection and Immunity 1979, 25:427-439.
    • (1979) Infection and Immunity , vol.25 , pp. 427-439
    • Tsai, C.C.1    McArthur, W.P.2    Baehni, P.C.3    Hammond, B.F.4    Taichman, N.S.5
  • 347
    • 60849116153 scopus 로고    scopus 로고
    • Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology
    • Tseng T.-T., Tyler B.M., Setubal J.C. Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology. BMC Microbiology 2009, 9(Suppl. 1):S2.
    • (2009) BMC Microbiology , vol.9 , pp. S2
    • Tseng, T.-T.1    Tyler, B.M.2    Setubal, J.C.3
  • 349
    • 0037261958 scopus 로고    scopus 로고
    • Characterization of biologically active cell surface components of a periodontal pathogen. The roles of major and minor fimbriae of Porphyromonas gingivalis
    • Umemoto T., Hamada N. Characterization of biologically active cell surface components of a periodontal pathogen. The roles of major and minor fimbriae of Porphyromonas gingivalis. Journal of Periodontology 2003, 74:119-122.
    • (2003) Journal of Periodontology , vol.74 , pp. 119-122
    • Umemoto, T.1    Hamada, N.2
  • 352
    • 84899842537 scopus 로고    scopus 로고
    • Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors
    • Veith P.D., Chen Y.-Y., Gorasia D.G., Chen D., Glew M.D., O'Brien-Simpson N.M., et al. Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors. Journal of Proteome Research 2014, 13:2420-2432.
    • (2014) Journal of Proteome Research , vol.13 , pp. 2420-2432
    • Veith, P.D.1    Chen, Y.-Y.2    Gorasia, D.G.3    Chen, D.4    Glew, M.D.5    O'Brien-Simpson, N.M.6
  • 353
    • 84885234044 scopus 로고    scopus 로고
    • Protein substrates of a novel secretion system are numerous in the bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment
    • Veith P.D., Nor Muhammad N.A., Dashper S.G., Likić V.A., Gorasia D.G., Chen D., et al. Protein substrates of a novel secretion system are numerous in the bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. Journal of Proteome Research 2013, 12:4449-4461.
    • (2013) Journal of Proteome Research , vol.12 , pp. 4449-4461
    • Veith, P.D.1    Nor Muhammad, N.A.2    Dashper, S.G.3    Likić, V.A.4    Gorasia, D.G.5    Chen, D.6
  • 355
    • 0036533761 scopus 로고    scopus 로고
    • Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50
    • Veith P.D., Talbo G.H., Slakeski N., Dashper S.G., Moore C., Paolini R.A., et al. Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. The Biochemical Journal 2002, 363:105-115.
    • (2002) The Biochemical Journal , vol.363 , pp. 105-115
    • Veith, P.D.1    Talbo, G.H.2    Slakeski, N.3    Dashper, S.G.4    Moore, C.5    Paolini, R.A.6
  • 358
    • 79954574472 scopus 로고    scopus 로고
    • Proteases of an early colonizer can hinder Streptococcus mutans colonization in vitro
    • Wang B.-Y., Deutch A., Hong J., Kuramitsu H.K. Proteases of an early colonizer can hinder Streptococcus mutans colonization in vitro. Journal of Dental Research 2011, 90:501-505.
    • (2011) Journal of Dental Research , vol.90 , pp. 501-505
    • Wang, B.-Y.1    Deutch, A.2    Hong, J.3    Kuramitsu, H.K.4
  • 359
    • 79955726295 scopus 로고    scopus 로고
    • Analysis of interspecies adherence of oral bacteria using a membrane binding assay coupled with polymerase chain reaction-denaturing gradient gel electrophoresis profiling
    • Wang R., He X., Hu W., Lux R., Li J., Zhou X., et al. Analysis of interspecies adherence of oral bacteria using a membrane binding assay coupled with polymerase chain reaction-denaturing gradient gel electrophoresis profiling. International Journal of Oral Science 2011, 3:90-97.
    • (2011) International Journal of Oral Science , vol.3 , pp. 90-97
    • Wang, R.1    He, X.2    Hu, W.3    Lux, R.4    Li, J.5    Zhou, X.6
  • 362
    • 37549046795 scopus 로고    scopus 로고
    • Two closely related ABC transporters in Streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake
    • Webb A.J., Homer K.A., Hosie A.H.F. Two closely related ABC transporters in Streptococcus mutans are involved in disaccharide and/or oligosaccharide uptake. Journal of Bacteriology 2008, 190:168-178.
    • (2008) Journal of Bacteriology , vol.190 , pp. 168-178
    • Webb, A.J.1    Homer, K.A.2    Hosie, A.H.F.3
  • 363
    • 1942507978 scopus 로고    scopus 로고
    • LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation
    • Wen Z.T., Burne R.A. LuxS-mediated signaling in Streptococcus mutans is involved in regulation of acid and oxidative stress tolerance and biofilm formation. Journal of Bacteriology 2004, 186:2682-2691.
    • (2004) Journal of Bacteriology , vol.186 , pp. 2682-2691
    • Wen, Z.T.1    Burne, R.A.2
  • 365
    • 33644786139 scopus 로고    scopus 로고
    • Retrieved from
    • WHO: Fact sheet N°318 Oral health 2012, Retrieved from. http://www.who.int/mediacentre/factsheets/fs318/en/.
    • (2012) Oral health
  • 366
    • 0036249521 scopus 로고    scopus 로고
    • Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions
    • Wilkins J.C., Homer K.A., Beighton D. Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions. Applied and Environmental Microbiology 2002, 68:2382-2390.
    • (2002) Applied and Environmental Microbiology , vol.68 , pp. 2382-2390
    • Wilkins, J.C.1    Homer, K.A.2    Beighton, D.3
  • 368
    • 0024382807 scopus 로고
    • Dependence of proliferation of Bacteroides forsythus on exogenous N-acetylmuramic acid
    • Wyss C. Dependence of proliferation of Bacteroides forsythus on exogenous N-acetylmuramic acid. Infection and Immunity 1989, 57:1757-1759.
    • (1989) Infection and Immunity , vol.57 , pp. 1757-1759
    • Wyss, C.1
  • 369
    • 34548295825 scopus 로고    scopus 로고
    • FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells
    • Xu M., Yamada M., Li M., Liu H., Chen S.G., Han Y.W. FadA from Fusobacterium nucleatum utilizes both secreted and nonsecreted forms for functional oligomerization for attachment and invasion of host cells. The Journal of Biological Chemistry 2007, 282:25000-25009.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 25000-25009
    • Xu, M.1    Yamada, M.2    Li, M.3    Liu, H.4    Chen, S.G.5    Han, Y.W.6
  • 370
    • 51449098668 scopus 로고    scopus 로고
    • Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane
    • Yajima A., Urano-Tashiro Y., Shimazu K., Takashima E., Takahashi Y., Konishi K. Hsa, an adhesin of Streptococcus gordonii DL1, binds to alpha2-3-linked sialic acid on glycophorin A of the erythrocyte membrane. Microbiology and Immunology 2008, 52:69-77.
    • (2008) Microbiology and Immunology , vol.52 , pp. 69-77
    • Yajima, A.1    Urano-Tashiro, Y.2    Shimazu, K.3    Takashima, E.4    Takahashi, Y.5    Konishi, K.6
  • 371
    • 0019256031 scopus 로고
    • Evaluation of cariogenicity of glycosylsucrose by a new method of measuring pH under human dental plaque in situ
    • Yamada T., Igarashi K., Mitsutomi M. Evaluation of cariogenicity of glycosylsucrose by a new method of measuring pH under human dental plaque in situ. Journal of Dental Research 1980, 59:2157-2162.
    • (1980) Journal of Dental Research , vol.59 , pp. 2157-2162
    • Yamada, T.1    Igarashi, K.2    Mitsutomi, M.3
  • 372
    • 84919476336 scopus 로고    scopus 로고
    • Acid stress survival mechanisms of the cariogenic bacterium Streptococcus mutans
    • Intech Open, Rijeka, Croatia, J. Agboola (Ed.)
    • Yamashita Y., Shibata Y. Acid stress survival mechanisms of the cariogenic bacterium Streptococcus mutans. Relevant perspectives in global environmental change 2011, 39-54. Intech Open, Rijeka, Croatia. J. Agboola (Ed.).
    • (2011) Relevant perspectives in global environmental change , pp. 39-54
    • Yamashita, Y.1    Shibata, Y.2
  • 373
    • 0023184449 scopus 로고
    • Cloning and expression of a type 1 fimbrial subunit of Actinomyces viscosus T14V
    • Yeung M.K., Chassy B.M., Cisar J.O. Cloning and expression of a type 1 fimbrial subunit of Actinomyces viscosus T14V. Journal of Bacteriology 1987, 169:1678-1683.
    • (1987) Journal of Bacteriology , vol.169 , pp. 1678-1683
    • Yeung, M.K.1    Chassy, B.M.2    Cisar, J.O.3
  • 374
    • 0036265107 scopus 로고    scopus 로고
    • Involvement of integrins in fimbriae-mediated binding and invasion by Porphyromonas gingivalis
    • Yilmaz O., Watanabe K., Lamont R.J. Involvement of integrins in fimbriae-mediated binding and invasion by Porphyromonas gingivalis. Cellular Microbiology 2002, 4:305-314.
    • (2002) Cellular Microbiology , vol.4 , pp. 305-314
    • Yilmaz, O.1    Watanabe, K.2    Lamont, R.J.3
  • 375
    • 0036955805 scopus 로고    scopus 로고
    • Multiple Streptococcus mutans genes are involved in biofilm formation
    • Yoshida A., Kuramitsu H.K. Multiple Streptococcus mutans genes are involved in biofilm formation. Applied and Environmental Microbiology 2002, 68:6283-6291.
    • (2002) Applied and Environmental Microbiology , vol.68 , pp. 6283-6291
    • Yoshida, A.1    Kuramitsu, H.K.2
  • 376
    • 84875221360 scopus 로고    scopus 로고
    • Caveolin-1 up-regulates integrin α2,6-sialylation to promote integrin α5β1-dependent hepatocarcinoma cell adhesion
    • Yu S., Fan J., Liu L., Zhang L., Wang S., Zhang J. Caveolin-1 up-regulates integrin α2,6-sialylation to promote integrin α5β1-dependent hepatocarcinoma cell adhesion. FEBS Letters 2013, 587:782-787.
    • (2013) FEBS Letters , vol.587 , pp. 782-787
    • Yu, S.1    Fan, J.2    Liu, L.3    Zhang, L.4    Wang, S.5    Zhang, J.6
  • 377
    • 42549117252 scopus 로고    scopus 로고
    • Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans
    • Yu C., Ruiz T., Lenox C., Mintz K.P. Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans. Journal of Bacteriology 2008, 190:3098-3109.
    • (2008) Journal of Bacteriology , vol.190 , pp. 3098-3109
    • Yu, C.1    Ruiz, T.2    Lenox, C.3    Mintz, K.P.4
  • 378
    • 34548509519 scopus 로고    scopus 로고
    • A second Aggregatibacter actinomycetemcomitans autotransporter adhesin exhibits specificity for buccal epithelial cells in humans and Old World primates
    • Yue G., Kaplan J.B., Furgang D., Mansfield K.G., Fine D.H. A second Aggregatibacter actinomycetemcomitans autotransporter adhesin exhibits specificity for buccal epithelial cells in humans and Old World primates. Infection and Immunity 2007, 75:4440-4448.
    • (2007) Infection and Immunity , vol.75 , pp. 4440-4448
    • Yue, G.1    Kaplan, J.B.2    Furgang, D.3    Mansfield, K.G.4    Fine, D.H.5
  • 380
    • 77955939003 scopus 로고    scopus 로고
    • The native 67-kilodalton minor fimbria of Porphyromonas gingivalis is a novel glycoprotein with DC-SIGN-targeting motifs
    • Zeituni A.E., McCaig W., Scisci E., Thanassi D.G., Cutler C.W. The native 67-kilodalton minor fimbria of Porphyromonas gingivalis is a novel glycoprotein with DC-SIGN-targeting motifs. Journal of Bacteriology 2010, 192:4103-4110.
    • (2010) Journal of Bacteriology , vol.192 , pp. 4103-4110
    • Zeituni, A.E.1    McCaig, W.2    Scisci, E.3    Thanassi, D.G.4    Cutler, C.W.5
  • 381
    • 84891894494 scopus 로고    scopus 로고
    • The resveratrol tetramer (-)-hopeaphenol inhibits type III secretion in the gram-negative pathogens Yersinia pseudotuberculosis and Pseudomonas aeruginosa
    • Zetterström C.E., Hasselgren J., Salin O., Davis R.A., Quinn R.J., Sundin C., et al. The resveratrol tetramer (-)-hopeaphenol inhibits type III secretion in the gram-negative pathogens Yersinia pseudotuberculosis and Pseudomonas aeruginosa. PLoS One 2013, 8:e81969.
    • (2013) PLoS One , vol.8 , pp. e81969
    • Zetterström, C.E.1    Hasselgren, J.2    Salin, O.3    Davis, R.A.4    Quinn, R.J.5    Sundin, C.6
  • 382
    • 84861556820 scopus 로고    scopus 로고
    • A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis
    • Zhang T., Ding Y., Li T., Wan Y., Li W., Chen H., et al. A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis. BMC Microbiology 2012, 12:85.
    • (2012) BMC Microbiology , vol.12 , pp. 85
    • Zhang, T.1    Ding, Y.2    Li, T.3    Wan, Y.4    Li, W.5    Chen, H.6
  • 383
    • 84872107011 scopus 로고    scopus 로고
    • Integrin α5β1-fimbriae binding and actin rearrangement are essential for Porphyromonas gingivalis invasion of osteoblasts and subsequent activation of the JNK pathway
    • Zhang W., Ju J., Rigney T., Tribble G. Integrin α5β1-fimbriae binding and actin rearrangement are essential for Porphyromonas gingivalis invasion of osteoblasts and subsequent activation of the JNK pathway. BMC Microbiology 2013, 13:5.
    • (2013) BMC Microbiology , vol.13 , pp. 5
    • Zhang, W.1    Ju, J.2    Rigney, T.3    Tribble, G.4
  • 384
    • 84882779412 scopus 로고    scopus 로고
    • Involvement of gshAB in the interspecies competition within oral biofilm
    • Zheng X., Zhang K., Zhou X., Liu C., Li M., Li Y., et al. Involvement of gshAB in the interspecies competition within oral biofilm. Journal of Dental Research 2013, 92:819-824.
    • (2013) Journal of Dental Research , vol.92 , pp. 819-824
    • Zheng, X.1    Zhang, K.2    Zhou, X.3    Liu, C.4    Li, M.5    Li, Y.6
  • 385
    • 84883181202 scopus 로고    scopus 로고
    • Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis
    • Zhou X.-Y., Gao J.-L., Hunter N., Potempa J., Nguyen K.-A. Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis. Molecular Microbiology 2013, 89:903-917.
    • (2013) Molecular Microbiology , vol.89 , pp. 903-917
    • Zhou, X.-Y.1    Gao, J.-L.2    Hunter, N.3    Potempa, J.4    Nguyen, K.-A.5
  • 386
    • 33747103043 scopus 로고    scopus 로고
    • Functional characterization of cell-wall-associated protein WapA in Streptococcus mutans
    • Zhu L., Kreth J., Cross S.E., Gimzewski J.K., Shi W., Qi F. Functional characterization of cell-wall-associated protein WapA in Streptococcus mutans. Microbiology (Reading, England) 2006, 152(Pt 8):2395-2404.
    • (2006) Microbiology (Reading, England) , vol.152 , Issue.PART. 8 , pp. 2395-2404
    • Zhu, L.1    Kreth, J.2    Cross, S.E.3    Gimzewski, J.K.4    Shi, W.5    Qi, F.6
  • 388
    • 77953184633 scopus 로고    scopus 로고
    • Effect of alkaline growth pH on the expression of cell envelope proteins in Fusobacterium nucleatum
    • Zilm P.S., Mira A., Bagley C.J., Rogers A.H. Effect of alkaline growth pH on the expression of cell envelope proteins in Fusobacterium nucleatum. Microbiology (Reading, England) 2010, 156:1783-1794.
    • (2010) Microbiology (Reading, England) , vol.156 , pp. 1783-1794
    • Zilm, P.S.1    Mira, A.2    Bagley, C.J.3    Rogers, A.H.4


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