메뉴 건너뛰기




Volumn 70, Issue 1, 2016, Pages 80-92

Influence of saliva on the oral microbiota

Author keywords

[No Author keywords available]

Indexed keywords

SALIVA PROTEIN;

EID: 84949656937     PISSN: 09066713     EISSN: 16000757     Source Type: Journal    
DOI: 10.1111/prd.12098     Document Type: Review
Times cited : (226)

References (114)
  • 1
    • 83555173386 scopus 로고    scopus 로고
    • Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain
    • Abdolhosseini M, Sotsky JB, Shelar AP, Joyce PB, Gorr SU. Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain. Mol Cell Biochem 2012: 359: 1-8.
    • (2012) Mol Cell Biochem , vol.359 , pp. 1-8
    • Abdolhosseini, M.1    Sotsky, J.B.2    Shelar, A.P.3    Joyce, P.B.4    Gorr, S.U.5
  • 2
    • 0035983426 scopus 로고    scopus 로고
    • Roles of salivary proteins in the adherence of oral streptococci to various orthodontic brackets
    • Ahn SJ, Kho HS, Lee SW, Nahm DS. Roles of salivary proteins in the adherence of oral streptococci to various orthodontic brackets. J Dent Res 2002: 81: 411-415.
    • (2002) J Dent Res , vol.81 , pp. 411-415
    • Ahn, S.J.1    Kho, H.S.2    Lee, S.W.3    Nahm, D.S.4
  • 3
    • 84155172894 scopus 로고    scopus 로고
    • Potential uses of human salivary protein and peptide analysis in the diagnosis of disease
    • Al Kawas S, Rahim ZH, Ferguson DB. Potential uses of human salivary protein and peptide analysis in the diagnosis of disease. Arch Oral Biol 2012: 57: 1-9.
    • (2012) Arch Oral Biol , vol.57 , pp. 1-9
    • Al Kawas, S.1    Rahim, Z.H.2    Ferguson, D.B.3
  • 4
    • 77951044334 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 modulates the inflammatory and host defense response of human neutrophils
    • Alalwani SM, Sierigk J, Herr C, Pinkenberg O, Gallo R, Vogelmeier C, Bals R. The antimicrobial peptide LL-37 modulates the inflammatory and host defense response of human neutrophils. Eur J Immunol 2010: 40: 1118-1126.
    • (2010) Eur J Immunol , vol.40 , pp. 1118-1126
    • Alalwani, S.M.1    Sierigk, J.2    Herr, C.3    Pinkenberg, O.4    Gallo, R.5    Vogelmeier, C.6    Bals, R.7
  • 6
    • 70449366352 scopus 로고    scopus 로고
    • Quantitative analysis of age specific variation in the abundance of human female parotid salivary proteins
    • Ambatipudi KS, Lu BW, Hagen FK, Melvin JE, Yates JR. Quantitative analysis of age specific variation in the abundance of human female parotid salivary proteins. J Proteome Res 2009: 8: 5093-5102.
    • (2009) J Proteome Res , vol.8 , pp. 5093-5102
    • Ambatipudi, K.S.1    Lu, B.W.2    Hagen, F.K.3    Melvin, J.E.4    Yates, J.R.5
  • 7
    • 84865641332 scopus 로고    scopus 로고
    • Role of surface proteins SspA and SspB of Streptococcus gordonii in innate immunity
    • Andrian E, Qi GF, Wang J, Halperin SA, Lee SF. Role of surface proteins SspA and SspB of Streptococcus gordonii in innate immunity. Microbiology 2012: 158: 2099-2106.
    • (2012) Microbiology , vol.158 , pp. 2099-2106
    • Andrian, E.1    Qi, G.F.2    Wang, J.3    Halperin, S.A.4    Lee, S.F.5
  • 8
    • 68949202993 scopus 로고    scopus 로고
    • The effect of lactoferrin on oral bacterial attachment
    • Arslan SY, Leung KP, Wu CD. The effect of lactoferrin on oral bacterial attachment. Oral Microbiol Immunol 2009: 24: 411-416.
    • (2009) Oral Microbiol Immunol , vol.24 , pp. 411-416
    • Arslan, S.Y.1    Leung, K.P.2    Wu, C.D.3
  • 13
    • 82155195889 scopus 로고    scopus 로고
    • The potter's wheel: the host's role in sculpting its microbiota
    • Bevins CL, Salzman NH. The potter's wheel: the host's role in sculpting its microbiota. Cell Mol Life Sci 2011: 68: 3675-3685.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3675-3685
    • Bevins, C.L.1    Salzman, N.H.2
  • 14
    • 0031610167 scopus 로고    scopus 로고
    • Analysis of pH-driven disruption of oral microbial communities in vitro
    • Bradshaw D, Marsh P. Analysis of pH-driven disruption of oral microbial communities in vitro. Caries Res 1998: 32: 456-462.
    • (1998) Caries Res , vol.32 , pp. 456-462
    • Bradshaw, D.1    Marsh, P.2
  • 15
    • 0028604333 scopus 로고
    • Metabolic cooperation in oral microbial communities during growth on mucin
    • Bradshaw DJ, Homer KA, Marsh PD, Beighton D. Metabolic cooperation in oral microbial communities during growth on mucin. Microbiology 1994: 140: 3407-3412.
    • (1994) Microbiology , vol.140 , pp. 3407-3412
    • Bradshaw, D.J.1    Homer, K.A.2    Marsh, P.D.3    Beighton, D.4
  • 17
    • 34248356762 scopus 로고    scopus 로고
    • Mechanisms of decreased susceptibility to beta-defensins by Treponema denticola
    • Brissette CA, Lukehart SA. Mechanisms of decreased susceptibility to beta-defensins by Treponema denticola. Infect Immun 2007: 75: 2307-2315.
    • (2007) Infect Immun , vol.75 , pp. 2307-2315
    • Brissette, C.A.1    Lukehart, S.A.2
  • 18
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005: 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 19
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock REW. Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 2006: 18: 24-30.
    • (2006) Curr Opin Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 20
    • 43049116831 scopus 로고    scopus 로고
    • Specific molecular recognition and nonspecific contributions to bacterial interaction forces
    • Busscher HJ, Norde W, van der Mei HC. Specific molecular recognition and nonspecific contributions to bacterial interaction forces. Appl Environ Microbiol 2008: 74: 2559-2564.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 2559-2564
    • Busscher, H.J.1    Norde, W.2    van der Mei, H.C.3
  • 21
    • 0030307332 scopus 로고    scopus 로고
    • Utilization of sialic acid by viridans streptococci
    • Byers HL, Homer KA, Beighton D. Utilization of sialic acid by viridans streptococci. J Dent Res 1996: 75: 1564-1571.
    • (1996) J Dent Res , vol.75 , pp. 1564-1571
    • Byers, H.L.1    Homer, K.A.2    Beighton, D.3
  • 22
    • 84880077164 scopus 로고    scopus 로고
    • Significant modifications of the salivary proteome potentially associated with complications of Down Syndrome revealed by top-down proteomics
    • Cabras T, Pisano E, Montaldo C, Giuca MR, Lavarone F, Zampino G, Castagnola M, Messana I. Significant modifications of the salivary proteome potentially associated with complications of Down Syndrome revealed by top-down proteomics. Mol Cell Proteomics 2013: 12: 1844-1852.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1844-1852
    • Cabras, T.1    Pisano, E.2    Montaldo, C.3    Giuca, M.R.4    Lavarone, F.5    Zampino, G.6    Castagnola, M.7    Messana, I.8
  • 25
    • 80051945663 scopus 로고    scopus 로고
    • Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva
    • Choi S, Baik JE, Jeon JH, Cho K, Seo DG, Kum KY, Yun CH, Han SH. Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva. Mol Immunol 2011: 48: 2207-2213.
    • (2011) Mol Immunol , vol.48 , pp. 2207-2213
    • Choi, S.1    Baik, J.E.2    Jeon, J.H.3    Cho, K.4    Seo, D.G.5    Kum, K.Y.6    Yun, C.H.7    Han, S.H.8
  • 26
    • 84858297915 scopus 로고    scopus 로고
    • Tn916-like elements from human, oral, commensal streptococci possess a variety of antibiotic and antiseptic resistance genes
    • Ciric L, Ellatif M, Sharma P, Patel R, Song X, Mullany P, Roberts AP. Tn916-like elements from human, oral, commensal streptococci possess a variety of antibiotic and antiseptic resistance genes. Int J Antimicrob Agents 2012: 39: 360-361.
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 360-361
    • Ciric, L.1    Ellatif, M.2    Sharma, P.3    Patel, R.4    Song, X.5    Mullany, P.6    Roberts, A.P.7
  • 29
    • 84893394396 scopus 로고    scopus 로고
    • Saliva: a fluid of study for OMICS
    • Cuevas-Cordoba B, Santiago-Garcia J. Saliva: a fluid of study for OMICS. OMICS 2014: 18: 87-97.
    • (2014) OMICS , vol.18 , pp. 87-97
    • Cuevas-Cordoba, B.1    Santiago-Garcia, J.2
  • 30
  • 31
    • 84862871084 scopus 로고    scopus 로고
    • Salivary concentration of the antimicrobial peptide LL-37 in children
    • Davidopoulou S, Diza E, Menexes G, Kalfas S. Salivary concentration of the antimicrobial peptide LL-37 in children. Arch Oral Biol 2012: 57: 865-869.
    • (2012) Arch Oral Biol , vol.57 , pp. 865-869
    • Davidopoulou, S.1    Diza, E.2    Menexes, G.3    Kalfas, S.4
  • 32
    • 33748042966 scopus 로고    scopus 로고
    • Role of polymorphonuclear leukocyte-derived serine proteinases in defense against Actinobacillus actinomycetemcomitans
    • de Haar SF, Hiemstra PS, van Steenbergen M, Everts V, Beertsen W. Role of polymorphonuclear leukocyte-derived serine proteinases in defense against Actinobacillus actinomycetemcomitans. Infect Immun 2006: 74: 5284-5291.
    • (2006) Infect Immun , vol.74 , pp. 5284-5291
    • de Haar, S.F.1    Hiemstra, P.S.2    van Steenbergen, M.3    Everts, V.4    Beertsen, W.5
  • 33
    • 41449093480 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides in regulation of commensal and pathogenic microbial populations
    • In: Devine DA, Hancock REW, editors. Cambridge: Cambridge University Press
    • Devine DA. Cationic antimicrobial peptides in regulation of commensal and pathogenic microbial populations. In: Devine DA, Hancock REW, editors. Mammalian host defense peptides. Cambridge: Cambridge University Press, 2004: 9-37.
    • (2004) Mammalian host defense peptides , pp. 9-37
    • Devine, D.A.1
  • 34
    • 41449087185 scopus 로고    scopus 로고
    • Host defence peptides in the oral cavity
    • Devine DA, Cosseau C. Host defence peptides in the oral cavity. Adv Appl Microbiol 2008: 63: 281-322.
    • (2008) Adv Appl Microbiol , vol.63 , pp. 281-322
    • Devine, D.A.1    Cosseau, C.2
  • 35
    • 0032899780 scopus 로고    scopus 로고
    • Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella spp
    • Devine DA, Marsh PD, Percival RS, Rangarajan M, Curtis MA. Modulation of antibacterial peptide activity by products of Porphyromonas gingivalis and Prevotella spp. Microbiology 1999: 145: 965-971.
    • (1999) Microbiology , vol.145 , pp. 965-971
    • Devine, D.A.1    Marsh, P.D.2    Percival, R.S.3    Rangarajan, M.4    Curtis, M.A.5
  • 36
    • 80051552897 scopus 로고    scopus 로고
    • Beta-defensins: what are they REALLY doing in the oral cavity?
    • Diamond G, Ryan LK. Beta-defensins: what are they REALLY doing in the oral cavity? Oral Dis 2011: 17: 628-635.
    • (2011) Oral Dis , vol.17 , pp. 628-635
    • Diamond, G.1    Ryan, L.K.2
  • 38
    • 70449686062 scopus 로고    scopus 로고
    • Antimicrobial peptide inhibition of Porphyromonas gingivalis 381-induced hemagglutination is improved with a synthetic decapeptide
    • Dixon DR, Jeffrey NR, Dubey VS, Leung KP. Antimicrobial peptide inhibition of Porphyromonas gingivalis 381-induced hemagglutination is improved with a synthetic decapeptide. Peptides 2009: 30: 2161-2167.
    • (2009) Peptides , vol.30 , pp. 2161-2167
    • Dixon, D.R.1    Jeffrey, N.R.2    Dubey, V.S.3    Leung, K.P.4
  • 40
    • 84860204140 scopus 로고    scopus 로고
    • Salivary defense proteins: their network and role in innate and acquired oral immunity
    • Fabian TK, Hermann P, Beck A, Fejérdy P, Fábián G. Salivary defense proteins: their network and role in innate and acquired oral immunity. Int J Mol Sci 2012: 13: 4295-4320.
    • (2012) Int J Mol Sci , vol.13 , pp. 4295-4320
    • Fabian, T.K.1    Hermann, P.2    Beck, A.3    Fejérdy, P.4    Fábián, G.5
  • 41
    • 0025687112 scopus 로고
    • Role of cryptic receptors (cryptitopes) in bacterial adhesion to oral surfaces
    • Gibbons RJ, Hay DI, Childs WC 3rd, Davis G. Role of cryptic receptors (cryptitopes) in bacterial adhesion to oral surfaces. Arch Oral Biol 1990: 35(Suppl): 107s-114s.
    • (1990) Arch Oral Biol , vol.35 , pp. 107s-114s
    • Gibbons, R.J.1    Hay, D.I.2    Childs, W.C.3    Davis, G.4
  • 43
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • Gorr SU. Antimicrobial peptides of the oral cavity. Periodontol 2000 2009: 51: 152-180.
    • (2009) Periodontol 2000 , vol.51 , pp. 152-180
    • Gorr, S.U.1
  • 44
    • 79951917226 scopus 로고    scopus 로고
    • Antimicrobial peptides and periodontal disease
    • Gorr SU, Abdolhosseini M. Antimicrobial peptides and periodontal disease. J Clin Periodontol 2011: 38: 126-141.
    • (2011) J Clin Periodontol , vol.38 , pp. 126-141
    • Gorr, S.U.1    Abdolhosseini, M.2
  • 45
    • 72449155528 scopus 로고    scopus 로고
    • Saliva enables the antimicrobial activity of LL-37 in the presence of proteases of Porphyromonas gingivalis
    • Gutner M, Chaushu S, Balter D, Bachrach G. Saliva enables the antimicrobial activity of LL-37 in the presence of proteases of Porphyromonas gingivalis. Infect Immun 2009: 77: 5558-5563.
    • (2009) Infect Immun , vol.77 , pp. 5558-5563
    • Gutner, M.1    Chaushu, S.2    Balter, D.3    Bachrach, G.4
  • 46
    • 14644439885 scopus 로고    scopus 로고
    • Enzymes in the acquired enamel pellicle
    • Hannig C, Hannig M, Attin T. Enzymes in the acquired enamel pellicle. Eur J Oral Sci 2005: 113: 2-13.
    • (2005) Eur J Oral Sci , vol.113 , pp. 2-13
    • Hannig, C.1    Hannig, M.2    Attin, T.3
  • 47
    • 14344257981 scopus 로고    scopus 로고
    • Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry
    • Hardt M, Thomas LR, Dixon SE, Newport G, Agabian N, Prakobphol A, Hall SC, Witkowska HE, Fisher SJ. Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry. Biochemistry 2005: 44: 2885-2899.
    • (2005) Biochemistry , vol.44 , pp. 2885-2899
    • Hardt, M.1    Thomas, L.R.2    Dixon, S.E.3    Newport, G.4    Agabian, N.5    Prakobphol, A.6    Hall, S.C.7    Witkowska, H.E.8    Fisher, S.J.9
  • 49
    • 84928527505 scopus 로고    scopus 로고
    • Non-lethal control of the cariogenic potential of an agent-based model for dental plaque
    • Head D, Marsh P, Devine D. Non-lethal control of the cariogenic potential of an agent-based model for dental plaque. PLoS ONE 2014: 9: e105012.
    • (2014) PLoS ONE , vol.9 , pp. e105012
    • Head, D.1    Marsh, P.2    Devine, D.3
  • 50
    • 74049150646 scopus 로고    scopus 로고
    • Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis
    • Hell E, Giske CG, Nelson A, Römling U, Marchini G. Human cathelicidin peptide LL37 inhibits both attachment capability and biofilm formation of Staphylococcus epidermidis. Lett Appl Microbiol 2010: 50: 211-215.
    • (2010) Lett Appl Microbiol , vol.50 , pp. 211-215
    • Hell, E.1    Giske, C.G.2    Nelson, A.3    Römling, U.4    Marchini, G.5
  • 51
    • 33644653705 scopus 로고    scopus 로고
    • The antifungal mechanisms of antimicrobial peptides
    • In: Devine DA, Hancock REW, editors. Cambridge: Cambridge University Press
    • Helmerhorst EJ, Oppenheim FG. The antifungal mechanisms of antimicrobial peptides. In: Devine DA, Hancock REW, editors. Mammalian host defense peptides. Cambridge: Cambridge University Press, 2004: 245-277.
    • (2004) Mammalian host defense peptides , pp. 245-277
    • Helmerhorst, E.J.1    Oppenheim, F.G.2
  • 52
    • 0018373474 scopus 로고
    • Current concepts of the structure and nature of mammalian salivary mucous glycoproteins
    • Herp A, Wu AM, Moschera J. Current concepts of the structure and nature of mammalian salivary mucous glycoproteins. Mol Cell Biochem 1979: 23: 27-44.
    • (1979) Mol Cell Biochem , vol.23 , pp. 27-44
    • Herp, A.1    Wu, A.M.2    Moschera, J.3
  • 53
    • 0026595091 scopus 로고
    • Synergistic degradation of bovine serum albumin by mutans streptococci and other dental plaque bacteria
    • Homer KA, Beighton D. Synergistic degradation of bovine serum albumin by mutans streptococci and other dental plaque bacteria. FEMS Microbiol Lett 1992: 69: 259-262.
    • (1992) FEMS Microbiol Lett , vol.69 , pp. 259-262
    • Homer, K.A.1    Beighton, D.2
  • 54
    • 0027390473 scopus 로고
    • Effects of N-acetylglucosamine on carbohydrate fermentation by Streptococcus mutans NCTC 10449 and Streptococcus sobrinus SL-1
    • Homer KA, Patel R, Beighton D. Effects of N-acetylglucosamine on carbohydrate fermentation by Streptococcus mutans NCTC 10449 and Streptococcus sobrinus SL-1. Infect Immun 1993: 61: 295-302.
    • (1993) Infect Immun , vol.61 , pp. 295-302
    • Homer, K.A.1    Patel, R.2    Beighton, D.3
  • 55
    • 35848942181 scopus 로고    scopus 로고
    • A review of the salivary proteome and peptidome and saliva-derived peptide therapeutics
    • Huq NL, Cross K, Ung M, Reynolds EC. A review of the salivary proteome and peptidome and saliva-derived peptide therapeutics. Int J Pept Res Ther 2007: 13: 547-564.
    • (2007) Int J Pept Res Ther , vol.13 , pp. 547-564
    • Huq, N.L.1    Cross, K.2    Ung, M.3    Reynolds, E.C.4
  • 56
    • 0032101863 scopus 로고    scopus 로고
    • The relationship between salivary histatin levels and oral yeast carriage
    • Jainkittivong A, Johnson DA, Yeh CK. The relationship between salivary histatin levels and oral yeast carriage. Oral Microbiol Immunol 1998: 13: 181-187.
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 181-187
    • Jainkittivong, A.1    Johnson, D.A.2    Yeh, C.K.3
  • 58
    • 0037231945 scopus 로고    scopus 로고
    • Single-nucleotide polymorphisms (SNPs) in human beta-defensin 1: high-throughput SNP assays and association with Candida carriage in type I diabetics and nondiabetic controls
    • Jurevic RJ, Bai M, Chadwick RB, White TC, Dale BA. Single-nucleotide polymorphisms (SNPs) in human beta-defensin 1: high-throughput SNP assays and association with Candida carriage in type I diabetics and nondiabetic controls. J Clin Microbiol 2003: 41: 90-96.
    • (2003) J Clin Microbiol , vol.41 , pp. 90-96
    • Jurevic, R.J.1    Bai, M.2    Chadwick, R.B.3    White, T.C.4    Dale, B.A.5
  • 59
    • 0024453078 scopus 로고
    • Taxonomic studies of viridans streptococci: description of Streptococcus gordonii sp. nov. and emended descriptions of Streptococcus sanguis (White and Niven 1946), Streptococcus oralis (Bridge and Sneath 1982), and Streptococcus mitis (Andrewes and Horder 1906)
    • Kilian M, Mikkelsen L, Henrichsen J. Taxonomic studies of viridans streptococci: description of Streptococcus gordonii sp. nov. and emended descriptions of Streptococcus sanguis (White and Niven 1946), Streptococcus oralis (Bridge and Sneath 1982), and Streptococcus mitis (Andrewes and Horder 1906). Int J Syst Bacteriol 1989: 39: 471-484.
    • (1989) Int J Syst Bacteriol , vol.39 , pp. 471-484
    • Kilian, M.1    Mikkelsen, L.2    Henrichsen, J.3
  • 61
    • 0032403148 scopus 로고    scopus 로고
    • Actinomyces serovar WVA963 coaggregation-defective mutant strain PK2407 secretes lactose-sensitive adhesin that binds to coaggregation partner Streptococcus oralis 34
    • Klier CM, Roble AG, Kolenbrander PE. Actinomyces serovar WVA963 coaggregation-defective mutant strain PK2407 secretes lactose-sensitive adhesin that binds to coaggregation partner Streptococcus oralis 34. Oral Microbiol Immunol 1998: 13: 337-340.
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 337-340
    • Klier, C.M.1    Roble, A.G.2    Kolenbrander, P.E.3
  • 63
  • 64
    • 72449156168 scopus 로고    scopus 로고
    • Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens
    • Lee SH, Jun HK, Lee HR, Chung CP, Choi BK. Antibacterial and lipopolysaccharide (LPS)-neutralising activity of human cationic antimicrobial peptides against periodontopathogens. Int J Antimicrob Agents 2009: 35: 138-145.
    • (2009) Int J Antimicrob Agents , vol.35 , pp. 138-145
    • Lee, S.H.1    Jun, H.K.2    Lee, H.R.3    Chung, C.P.4    Choi, B.K.5
  • 66
    • 70350022242 scopus 로고    scopus 로고
    • Identification of salivary components that induce transition of hyphae to yeast in Candida albicans
    • Leito JT, Ligtenberg AJM, Nazmi K, Veerman EC. Identification of salivary components that induce transition of hyphae to yeast in Candida albicans. FEMS Yeast Res 2009: 9: 1102-1110.
    • (2009) FEMS Yeast Res , vol.9 , pp. 1102-1110
    • Leito, J.T.1    Ligtenberg, A.J.M.2    Nazmi, K.3    Veerman, E.C.4
  • 67
    • 0030064825 scopus 로고    scopus 로고
    • Rapid characterization of periodontal bacterial isolates by using fluorogenic substrate tests
    • Maiden MF, Tanner A, Macuch PJ. Rapid characterization of periodontal bacterial isolates by using fluorogenic substrate tests. J Clin Microbiol 1996: 34: 376-384.
    • (1996) J Clin Microbiol , vol.34 , pp. 376-384
    • Maiden, M.F.1    Tanner, A.2    Macuch, P.J.3
  • 68
    • 14744281431 scopus 로고    scopus 로고
    • Susceptibility of Streptococcus mutans and Actinobacillus actinomycetemcomitans to bactericidal activity of human beta-defensin 3 in biological fluids
    • Maisetta G, Batoni G, Esin S, Raco G, Bottai D, Favilli F, Florio W, Campa M. Susceptibility of Streptococcus mutans and Actinobacillus actinomycetemcomitans to bactericidal activity of human beta-defensin 3 in biological fluids. Antimicrob Agents Chemother 2005: 49: 1245-1248.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1245-1248
    • Maisetta, G.1    Batoni, G.2    Esin, S.3    Raco, G.4    Bottai, D.5    Favilli, F.6    Florio, W.7    Campa, M.8
  • 69
    • 79955471798 scopus 로고    scopus 로고
    • Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptide's antibacterial activity in vitro
    • Maisetta G, Brancatisano FL, Esin S, Campa M, Batoni G. Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptide's antibacterial activity in vitro. Peptides 2011: 32: 1073-1077.
    • (2011) Peptides , vol.32 , pp. 1073-1077
    • Maisetta, G.1    Brancatisano, F.L.2    Esin, S.3    Campa, M.4    Batoni, G.5
  • 70
    • 84987850892 scopus 로고    scopus 로고
    • Prospects of oral disease control in the future - an opinion
    • Marsh P, Head D, Devine D. Prospects of oral disease control in the future - an opinion. J Oral Microbiol 2014: 6: 26176.
    • (2014) J Oral Microbiol , vol.6 , pp. 26176
    • Marsh, P.1    Head, D.2    Devine, D.3
  • 72
    • 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 AR, Clarke JM, Tannock GW, Jenkinson HF. Cell surface polypeptide CshA mediates binding of Streptococcus gordonii to other oral bacteria and to immobilized fibronectin. Infect Immun 1996: 64: 4204-4210.
    • (1996) Infect Immun , vol.64 , pp. 4204-4210
    • McNab, R.1    Holmes, A.R.2    Clarke, J.M.3    Tannock, G.W.4    Jenkinson, H.F.5
  • 73
    • 0025164808 scopus 로고
    • Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria
    • Moncla BJ, Braham P, Hillier SL. Sialidase (neuraminidase) activity among gram-negative anaerobic and capnophilic bacteria. J Clin Microbiol 1990: 28: 422-425.
    • (1990) J Clin Microbiol , vol.28 , pp. 422-425
    • Moncla, B.J.1    Braham, P.2    Hillier, S.L.3
  • 74
    • 0025989354 scopus 로고
    • Rapid presumptive identification of black-pigmented gram-negative anaerobic bacteria by using 4-methylumbelliferone derivatives
    • Moncla BJ, Braham P, Rabe LK, Hillier SL. Rapid presumptive identification of black-pigmented gram-negative anaerobic bacteria by using 4-methylumbelliferone derivatives. J Clin Microbiol 1991: 29: 1955-1958.
    • (1991) J Clin Microbiol , vol.29 , pp. 1955-1958
    • Moncla, B.J.1    Braham, P.2    Rabe, L.K.3    Hillier, S.L.4
  • 77
    • 77952791627 scopus 로고    scopus 로고
    • The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity
    • Oudhoff MJ, Blaauboer ME, Nazmi K, Scheres N, Bolscher JG, Veerman EC. The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity. Biol Chem 2010: 391: 541-548.
    • (2010) Biol Chem , vol.391 , pp. 541-548
    • Oudhoff, M.J.1    Blaauboer, M.E.2    Nazmi, K.3    Scheres, N.4    Bolscher, J.G.5    Veerman, E.C.6
  • 79
    • 77953246270 scopus 로고    scopus 로고
    • The antimicrobial peptide DEFB1 is associated with caries
    • Ozturk A, Famili P, Vieira AR. The antimicrobial peptide DEFB1 is associated with caries. J Dent Res 2010: 89: 631-636.
    • (2010) J Dent Res , vol.89 , pp. 631-636
    • Ozturk, A.1    Famili, P.2    Vieira, A.R.3
  • 80
  • 81
    • 33745217570 scopus 로고    scopus 로고
    • The co-evolution of host cationic antimicrobial peptides and microbial resistance
    • Peschel A, Sahl HG. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat Rev Microbiol 2006: 4: 529-536.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 529-536
    • Peschel, A.1    Sahl, H.G.2
  • 82
    • 79955718024 scopus 로고    scopus 로고
    • Streptococcus mutans strains recovered from caries-active or caries-free individuals differ in sensitivity to host antimicrobial peptides
    • Phattarataratip E, Olson B, Broffitt B, Qian F, Brogden KA, Drake DR, Levy SM, Banas JA. Streptococcus mutans strains recovered from caries-active or caries-free individuals differ in sensitivity to host antimicrobial peptides. Mol Oral Microbiol 2011: 26: 187-199.
    • (2011) Mol Oral Microbiol , vol.26 , pp. 187-199
    • Phattarataratip, E.1    Olson, B.2    Broffitt, B.3    Qian, F.4    Brogden, K.A.5    Drake, D.R.6    Levy, S.M.7    Banas, J.A.8
  • 83
    • 67649388653 scopus 로고    scopus 로고
    • The proteome of the human parotid gland secretion in elderly with and without root caries
    • Preza D, Thiede B, Olsen I, Grinde B. The proteome of the human parotid gland secretion in elderly with and without root caries. Acta Odontol Scand 2009: 67: 161-169.
    • (2009) Acta Odontol Scand , vol.67 , pp. 161-169
    • Preza, D.1    Thiede, B.2    Olsen, I.3    Grinde, B.4
  • 84
    • 0037068959 scopus 로고    scopus 로고
    • Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study
    • Putsep K, Carlsson G, Boman HG, Andersson M. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 2002: 360: 1144-1149.
    • (2002) Lancet , vol.360 , pp. 1144-1149
    • Putsep, K.1    Carlsson, G.2    Boman, H.G.3    Andersson, M.4
  • 87
    • 84857677420 scopus 로고    scopus 로고
    • The antibacterial activity of LL-37 against Treponema denticola is dentilisin protease independent and facilitated by the major outer sheath protein virulence factor
    • Rosen G, Sela MN, Bachrach G. The antibacterial activity of LL-37 against Treponema denticola is dentilisin protease independent and facilitated by the major outer sheath protein virulence factor. Infect Immun 2012: 80: 1107-1114.
    • (2012) Infect Immun , vol.80 , pp. 1107-1114
    • Rosen, G.1    Sela, M.N.2    Bachrach, G.3
  • 88
    • 3042783272 scopus 로고    scopus 로고
    • Salivary receptors for the proline-rich protein-binding and lectin-like adhesins of oral actinomyces and streptococci
    • Ruhl S, Sandberg AL, Cisar JO. Salivary receptors for the proline-rich protein-binding and lectin-like adhesins of oral actinomyces and streptococci. J Dent Res 2004: 83: 505-510.
    • (2004) J Dent Res , vol.83 , pp. 505-510
    • Ruhl, S.1    Sandberg, A.L.2    Cisar, J.O.3
  • 89
    • 84866951984 scopus 로고    scopus 로고
    • D-alanylation of lipoteichoic acids confers resistance to cationic peptides in group b streptococcus by increasing the cell wall density
    • Saar-Dover R, Bitler A, Nezer R, Shmuel-Galia L, Firon A, Shimoni E, Trieu-Cuot P, Shai Y. D-alanylation of lipoteichoic acids confers resistance to cationic peptides in group b streptococcus by increasing the cell wall density. PLoS Pathog 2012: 8: e1002891.
    • (2012) PLoS Pathog , vol.8 , pp. e1002891
    • Saar-Dover, R.1    Bitler, A.2    Nezer, R.3    Shmuel-Galia, L.4    Firon, A.5    Shimoni, E.6    Trieu-Cuot, P.7    Shai, Y.8
  • 91
    • 78650883355 scopus 로고    scopus 로고
    • A review of the critical role of vitamin D in the functioning of the immune system and the clinical implications of vitamin D deficiency
    • Schwalfenberg GK. A review of the critical role of vitamin D in the functioning of the immune system and the clinical implications of vitamin D deficiency. Mol Nutrit Food Res 2011: 55: 96-108.
    • (2011) Mol Nutrit Food Res , vol.55 , pp. 96-108
    • Schwalfenberg, G.K.1
  • 92
    • 0034665513 scopus 로고    scopus 로고
    • An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression
    • Scott MG, Rosenberger CM, Gold MR, Finlay BB, Hancock RE. An alpha-helical cationic antimicrobial peptide selectively modulates macrophage responses to lipopolysaccharide and directly alters macrophage gene expression. J Immunol 2000: 165: 3358-3365.
    • (2000) J Immunol , vol.165 , pp. 3358-3365
    • Scott, M.G.1    Rosenberger, C.M.2    Gold, M.R.3    Finlay, B.B.4    Hancock, R.E.5
  • 96
    • 33748298908 scopus 로고    scopus 로고
    • Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces
    • Shimotoyodome A, Kobayashi H, Tokimitsu I, Matsukubo T, Takaesu Y. Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces. Caries Res 2006: 40: 403-411.
    • (2006) Caries Res , vol.40 , pp. 403-411
    • Shimotoyodome, A.1    Kobayashi, H.2    Tokimitsu, I.3    Matsukubo, T.4    Takaesu, Y.5
  • 98
    • 1842539547 scopus 로고    scopus 로고
    • Salivary micelles: identification of complexes containing MG2, slgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme
    • Soares RV, Lin T, Siqueira CC, Bruno LS, Li X, Oppenheim FG, Offner G, Troxler RF. Salivary micelles: identification of complexes containing MG2, slgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme. Arch Oral Biol 2004: 49: 337-343.
    • (2004) Arch Oral Biol , vol.49 , pp. 337-343
    • Soares, R.V.1    Lin, T.2    Siqueira, C.C.3    Bruno, L.S.4    Li, X.5    Oppenheim, F.G.6    Offner, G.7    Troxler, R.F.8
  • 99
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, Hiemstra PS, Borregaard N. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001: 97: 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 100
    • 79251599753 scopus 로고    scopus 로고
    • Host defense peptides and their antimicrobial-immunomodulatory duality
    • Steinstraesser L, Kraneburg U, Jacobsen F, Al-Benna S. Host defense peptides and their antimicrobial-immunomodulatory duality. Immunobiology 2011: 216: 322-333.
    • (2011) Immunobiology , vol.216 , pp. 322-333
    • Steinstraesser, L.1    Kraneburg, U.2    Jacobsen, F.3    Al-Benna, S.4
  • 102
    • 0032212856 scopus 로고    scopus 로고
    • Evidence for mannosidase activities in Streptococcus oralis when grown on glycoproteins as carbohydrate source
    • Tarelli E, Byers HL, Homer KA, Beighton D. Evidence for mannosidase activities in Streptococcus oralis when grown on glycoproteins as carbohydrate source. Carbohydr Res 1998: 312: 159-164.
    • (1998) Carbohydr Res , vol.312 , pp. 159-164
    • Tarelli, E.1    Byers, H.L.2    Homer, K.A.3    Beighton, D.4
  • 103
    • 0023260869 scopus 로고
    • Enrichment of subgingival microflora on human serum leading to accumulation of Bacteroides species, peptostreptococci and fusobacteria
    • ter Steeg PF, van der Hoeven JS, de Jong MH, van Munster PJ, Jansen MJH. Enrichment of subgingival microflora on human serum leading to accumulation of Bacteroides species, peptostreptococci and fusobacteria. Antonie Van Leeuwenhoek 1987: 53: 261-272.
    • (1987) Antonie Van Leeuwenhoek , vol.53 , pp. 261-272
    • ter Steeg, P.F.1    van der Hoeven, J.S.2    de Jong, M.H.3    van Munster, P.J.4    Jansen, M.J.H.5
  • 104
    • 84890460096 scopus 로고    scopus 로고
    • Antibiotic concentrations in saliva: a systematic review of the literature, with clinical implications for the treatment of sialadenitis
    • Troeltzsch M, Pache C, Probst FA, Troeltzsch M, Ehrenfeld M, Otto S. Antibiotic concentrations in saliva: a systematic review of the literature, with clinical implications for the treatment of sialadenitis. J Oral Maxillofac Surg 2014: 72: 67-75.
    • (2014) J Oral Maxillofac Surg , vol.72 , pp. 67-75
    • Troeltzsch, M.1    Pache, C.2    Probst, F.A.3    Troeltzsch, M.4    Ehrenfeld, M.5    Otto, S.6
  • 105
    • 79952679401 scopus 로고    scopus 로고
    • Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates
    • Tsai PW, Yang CY, Chang HT, Lan CY. Human antimicrobial peptide LL-37 inhibits adhesion of Candida albicans by interacting with yeast cell-wall carbohydrates. PLoS ONE 2011: 6: e17755.
    • (2011) PLoS ONE , vol.6 , pp. e17755
    • Tsai, P.W.1    Yang, C.Y.2    Chang, H.T.3    Lan, C.Y.4
  • 107
    • 0034128207 scopus 로고    scopus 로고
    • Sialic acid metabolism's dual function in Haemophilus influenzae
    • Vimr E, Lichtensteiger C, Steenbergen S. Sialic acid metabolism's dual function in Haemophilus influenzae. Mol Microbiol 2000: 36: 1113-1123.
    • (2000) Mol Microbiol , vol.36 , pp. 1113-1123
    • Vimr, E.1    Lichtensteiger, C.2    Steenbergen, S.3
  • 110
    • 67749086601 scopus 로고    scopus 로고
    • Inhibitory effects of lactoferrin on growth and biofilm formation of Porphyromonas gingivalis and Prevotella intermedia
    • Wakabayashi H, Yamauchi K, Kobayashi T, Yaeshima T, Iwatsuki K, Yoshie H. Inhibitory effects of lactoferrin on growth and biofilm formation of Porphyromonas gingivalis and Prevotella intermedia. Antimicrob Agents Chemother 2009: 53: 3308-3316.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 3308-3316
    • Wakabayashi, H.1    Yamauchi, K.2    Kobayashi, T.3    Yaeshima, T.4    Iwatsuki, K.5    Yoshie, H.6
  • 111
    • 33749170651 scopus 로고    scopus 로고
    • Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm
    • Wei GX, Campagna AN, Bobek LA. Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm. J Antimicrob Chemother 2006: 57: 1100-1109.
    • (2006) J Antimicrob Chemother , vol.57 , pp. 1100-1109
    • Wei, G.X.1    Campagna, A.N.2    Bobek, L.A.3
  • 114
    • 77951061673 scopus 로고    scopus 로고
    • Utilization of lactose and galactose by Streptococcus mutans: transport, toxicity, and carbon catabolite repression
    • Zeng L, Das S, Burne RA. Utilization of lactose and galactose by Streptococcus mutans: transport, toxicity, and carbon catabolite repression. J Bacteriol 2010: 192: 2434-2444.
    • (2010) J Bacteriol , vol.192 , pp. 2434-2444
    • Zeng, L.1    Das, S.2    Burne, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.