메뉴 건너뛰기




Volumn 55, Issue 4, 2013, Pages 169-174

Implications of salivary protein binding to commensal and pathogenic bacteria

Author keywords

Saliva Microbial adhesion Biofilm Oral diseases

Indexed keywords


EID: 84892616326     PISSN: 13490079     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.job.2013.06.004     Document Type: Review
Times cited : (15)

References (132)
  • 1
    • 34247237888 scopus 로고    scopus 로고
    • Dental plaque as a biofilm and a microbial community?implications for health and disease
    • Marsh PD. Dental plaque as a biofilm and a microbial community? implications for health and disease. BMC Oral Health 2006;6(Suppl. 1):S14.
    • (2006) BMC Oral Health , vol.6 , Issue.SUPPL. 1
    • Marsh, P.D.1
  • 4
    • 82555165922 scopus 로고    scopus 로고
    • Beyond the oral microbiome
    • Jenkinson HF. Beyond the oral microbiome. Environ Microbiol 2011;13: 3077-3087.
    • (2011) Environ Microbiol , vol.13 , pp. 3077-3087
    • Jenkinson, H.F.1
  • 6
    • 57849120751 scopus 로고    scopus 로고
    • Non-odontogenic infections in dentistry
    • Dahlen G. Non-odontogenic infections in dentistry. Periodontology 2000 2009;49:7-12.
    • (2009) Periodontology 2000 , vol.49 , pp. 7-12
    • Dahlen, G.1
  • 7
    • 78650059352 scopus 로고    scopus 로고
    • Bacterial and viral pathogens in saliva: Disease relationship and infectious risk
    • Slots J, Slots H. Bacterial and viral pathogens in saliva: disease relationship and infectious risk. Periodontology 2000 2011;55:48-69.
    • (2011) Periodontology 2000 , vol.55 , pp. 48-69
    • Slots, J.1    Slots, H.2
  • 8
    • 0015156689 scopus 로고
    • Quantitative studies on the salivary flora
    • Ross PW. Quantitative studies on the salivary flora. J Clin Pathol 1971;24:717-20.
    • (1971) J Clin Pathol , vol.24 , pp. 717-720
    • Ross, P.W.1
  • 9
  • 10
    • 79952847606 scopus 로고    scopus 로고
    • Helicobacter pylori in the oral cavity and gastric mucosa: A meta-analysis
    • Zou QH, Li RQ. Helicobacter pylori in the oral cavity and gastric mucosa: a meta-analysis. J Oral Pathol Med 2011;40:317-24.
    • (2011) J Oral Pathol Med , vol.40 , pp. 317-324
    • Zou, Q.H.1    Li, R.Q.2
  • 12
    • 0033456272 scopus 로고    scopus 로고
    • Bacterial diversity within the human subgingival crevice
    • Kroes I, Lepp PW, Relman DA. Bacterial diversity within the human subgingival crevice. Proc Natl Acad Sci USA 1999;96:14547-52.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14547-14552
    • Kroes, I.1    Lepp, P.W.2    Relman, D.A.3
  • 13
    • 0026780735 scopus 로고
    • Colonization of dental plaque by respiratory pathogens in medical intensive care patients
    • Scannapieco FA, Stewart EM, Mylotte JM. Colonization of dental plaque by respiratory pathogens in medical intensive care patients. Crit Care Med 1992;20:740-5.
    • (1992) Crit Care Med , vol.20 , pp. 740-745
    • Scannapieco, F.A.1    Stewart, E.M.2    Mylotte, J.M.3
  • 14
    • 0033159030 scopus 로고    scopus 로고
    • Role of oral bacteria in respiratory infection
    • Scannapieco FA. Role of oral bacteria in respiratory infection. J Periodontol 1999;70:793-802.
    • (1999) J Periodontol , vol.70 , pp. 793-802
    • Scannapieco, F.A.1
  • 15
    • 0041927893 scopus 로고    scopus 로고
    • Systemic diseases in association with microbial species in oral biofilm from elderly requiring care
    • Senpuku H, Sogame A, Inoshita E, Tsuha Y, Miyazaki H, Hanada N. Systemic diseases in association with microbial species in oral biofilm from elderly requiring care. Gerontology 2003;49:301-9.
    • (2003) Gerontology , vol.49 , pp. 301-309
    • Senpuku, H.1    Sogame, A.2    Inoshita, E.3    Tsuha, Y.4    Miyazaki, H.5    Hanada, N.6
  • 16
    • 24344436737 scopus 로고    scopus 로고
    • Respiratorypathogens in dental plaque of hospitalized patients with chronic lung diseases
    • Didilescu AC, Skaug N, Marica C, Didilescu C. Respiratorypathogens in dental plaque of hospitalized patients with chronic lung diseases. Clin Oral Invest 2005;9:141-7.
    • (2005) Clin Oral Invest , vol.9 , pp. 141-147
    • Didilescu, A.C.1    Skaug, N.2    Marica, C.3    Didilescu, C.4
  • 17
    • 0030254391 scopus 로고    scopus 로고
    • Relationships between periodontal disease and bacterial pneumonia
    • Scannapieco FA, Mylotte JM. Relationships between periodontal disease and bacterial pneumonia. J Periodontol 1996;67:1114-22.
    • (1996) J Periodontol , vol.67 , pp. 1114-1122
    • Scannapieco, F.A.1    Mylotte, J.M.2
  • 19
    • 56749168880 scopus 로고    scopus 로고
    • Genetic relationships between respiratory pathogens isolated from dental plaque and bronchoal- veolar lavage fluid from patients in the intensive care unit undergoing mechanical ventilation
    • Heo SM, Haase EM, Lesse AJ, Gill SR, Scannapieco FA. Genetic relationships between respiratory pathogens isolated from dental plaque and bronchoal- veolar lavage fluid from patients in the intensive care unit undergoing mechanical ventilation. Clin Infect Dis 2008;47:1562-70.
    • (2008) Clin Infect Dis , vol.47 , pp. 1562-1570
    • Heo, S.M.1    Haase, E.M.2    Lesse, A.J.3    Gill, S.R.4    Scannapieco, F.A.5
  • 21
    • 0026780735 scopus 로고
    • Colonization of dental plaque by respiratory pathogens in medical intensive care patients
    • Scannapieco FA, Stewart EM, Mylotte JM. Colonization of dental plaque by respiratory pathogens in medical intensive care patients. Crit Care Med 1992;20:740-5.
    • (1992) Crit Care Med , vol.20 , pp. 740-745
    • Scannapieco, F.A.1    Stewart, E.M.2    Mylotte, J.M.3
  • 22
    • 0023286455 scopus 로고
    • The functions of saliva
    • Mandel ID. The functions of saliva. J Dent Res 1987;66:623-7.
    • (1987) J Dent Res , vol.66 , pp. 623-627
    • Mandel, I.D.1
  • 24
    • 0028631078 scopus 로고
    • Saliva-bacterium interactions in oral microbial ecology
    • Scannapieco FA. Saliva-bacterium interactions in oral microbial ecology. Crit Rev Oral Biol Med 1994;5:203-48.
    • (1994) Crit Rev Oral Biol Med , vol.5 , pp. 203-248
    • Scannapieco, F.A.1
  • 25
    • 0036119654 scopus 로고    scopus 로고
    • Saliva?the defender of the oral cavity
    • Amerongen AV, Veerman EC. Saliva?the defender of the oral cavity. Oral Dis 2002;8:12-22.
    • (2002) Oral Dis , vol.8 , pp. 12-22
    • Amerongen, A.V.1    Veerman, E.C.2
  • 26
    • 84856603372 scopus 로고    scopus 로고
    • The scientific exploration of saliva in the post-proteomic era: From database back to basic function
    • Ruhl S. The scientific exploration of saliva in the post-proteomic era: from database back to basic function. Expert Rev Proteomics 2012;9:85-96.
    • (2012) Expert Rev Proteomics , vol.9 , pp. 85-96
    • Ruhl, S.1
  • 27
    • 15544376642 scopus 로고    scopus 로고
    • Design and validation of anti-inflammatory peptides from human parotid secretory protein
    • Geetha C, Venkatesh SG, Bingle L, Bingle CD, Gorr SU. Design and validation of anti-inflammatory peptides from human parotid secretory protein. J Dent Res 2005;84:149-53.
    • (2005) J Dent Res , vol.84 , pp. 149-153
    • Geetha, C.1    Venkatesh, S.G.2    Bingle, L.3    Bingle, C.D.4    Gorr, S.U.5
  • 28
    • 69149102398 scopus 로고    scopus 로고
    • Antimicrobial peptides of the oral cavity
    • Gorr SU. Antimicrobial peptides of the oral cavity. Periodontology 2000 2009;51:152-80.
    • (2009) Periodontology 2000 , vol.51 , pp. 152-180
    • Gorr, S.U.1
  • 29
    • 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;57:1100-9.
    • (2006) J Antimicrob Chemother , vol.57 , pp. 1100-1109
    • Wei, G.X.1    Campagna, A.N.2    Bobek, L.A.3
  • 30
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Defensins, cathe- licidins and histatins
    • De Smet K, Contreras R. Human antimicrobial peptides: defensins, cathe- licidins and histatins. Biotechnol Lett 2005;27:1337-47.
    • (2005) Biotechnol Lett , vol.27 , pp. 1337-1347
    • De Smet, K.1    Contreras, R.2
  • 32
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungi-static effects on Candida albicans
    • Oppenheim FG, Xu T, McMillian FM, Levitz SM, Diamond RD, Offner GD, Troxler RF. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungi-static effects on Candida albicans. J Biol Chem 1988;263:7472-7.
    • (1988) J Biol Chem , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 33
    • 38649127564 scopus 로고    scopus 로고
    • The P-113 fragment of histatin 5 requires a specific peptide sequence for intracellular translocation in Candida albicans, which is independent of cell wall binding
    • Jang WS, Li XS, Sun JN, Edgerton M. The P-113 fragment of histatin 5 requires a specific peptide sequence for intracellular translocation in Candida albicans, which is independent of cell wall binding. Antimicrob Agents Che- mother 2008;52:497-504.
    • (2008) Antimicrob Agents Che- Mother , vol.52 , pp. 497-504
    • Jang, W.S.1    Li, X.S.2    Sun, J.N.3    Edgerton, M.4
  • 34
    • 0027119547 scopus 로고
    • Fungicidal effect of human lactoferrin against Candida albicans
    • Soukka T, Tenovuo J, Lenander-Lumikari M. Fungicidal effect of human lactoferrin against Candida albicans. FEMS Microbiol Lett 1992;69:223-8.
    • (1992) FEMS Microbiol Lett , vol.69 , pp. 223-228
    • Soukka, T.1    Tenovuo, J.2    Lenander-Lumikari, M.3
  • 36
    • 0016628155 scopus 로고
    • Changing agglutination activities of salivary immu-noglobulin A preparations against oral streptococci
    • Bratthall D, Gibbons RJ. Changing agglutination activities of salivary immu-noglobulin A preparations against oral streptococci. Infect Immun 1975;11:603-6.
    • (1975) Infect Immun , vol.11 , pp. 603-606
    • Bratthall, D.1    Gibbons, R.J.2
  • 37
    • 0017802323 scopus 로고
    • Specificity of salivary-bacterial interactions: Role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans
    • Levine MJ, Herzberg MC, Levine MS, Ellison SA, Stinson MW, Li HC, van Dyke T. Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans. Infect Immun 1978;19:107-15.
    • (1978) Infect Immun , vol.19 , pp. 107-115
    • Levine, M.J.1    Herzberg, M.C.2    Levine, M.S.3    Ellison, S.A.4    Stinson, M.W.5    Li, H.C.6    Van Dyke, T.7
  • 38
    • 0019386186 scopus 로고
    • Effect of calcium on reactions between a salivary agglutinin and a serotype c strain of Streptococcus mutans
    • Rundegren J, Ericson T. Effect of calcium on reactions between a salivary agglutinin and a serotype c strain of Streptococcus mutans. J Oral Pathol 1981;10:269-75.
    • (1981) J Oral Pathol , vol.10 , pp. 269-275
    • Rundegren, J.1    Ericson, T.2
  • 39
    • 0022534440 scopus 로고
    • Calcium-dependent salivary agglutinin with reactivity to various oral bacterial species
    • Rundegren J. Calcium-dependent salivary agglutinin with reactivity to various oral bacterial species. Infect Immun 1986;53:173-8.
    • (1986) Infect Immun , vol.53 , pp. 173-178
    • Rundegren, J.1
  • 40
    • 36248948670 scopus 로고    scopus 로고
    • Salivary agglutinin/glycoprotein-340/DMBT1: A single molecule with variable composition and with different functions in infection, inflammation and cancer
    • Ligtenberg AJ, Veerman EC, Nieuw Amerongen AV, Mollenhauer J. Salivary agglutinin/glycoprotein-340/DMBT1: a single molecule with variable composition and with different functions in infection, inflammation and cancer. Biol Chem 2007;388:1275-89.
    • (2007) Biol Chem , vol.388 , pp. 1275-1289
    • Ligtenberg, A.J.1    Veerman, E.C.2    Nieuw Amerongen, A.V.3    Mollenhauer, J.4
  • 42
    • 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. JDent Res 2004;83:505-10.
    • (2004) JDent Res , vol.83 , pp. 505-510
    • Ruhl, S.1    Sandberg, A.L.2    Cisar, J.O.3
  • 43
    • 33644781570 scopus 로고    scopus 로고
    • Binding of the streptococcal surface glycoproteins GspB and Hsa to human salivary proteins
    • Takamatsu D, Bensing BA, Prakobphol A, Fisher SJ, Sullam PM. Binding of the streptococcal surface glycoproteins GspB and Hsa to human salivary proteins. Infect Immun 2006;74:1933-40.
    • (2006) Infect Immun , vol.74 , pp. 1933-1940
    • Takamatsu, D.1    Bensing, B.A.2    Prakobphol, A.3    Fisher, S.J.4    Sullam, P.M.5
  • 45
    • 0042845844 scopus 로고    scopus 로고
    • Specific ion effects: Why the properties of lysozyme in salt solutions follow a Hofmeister series
    • Bostrom M, Williams DR Ninham BW. Specific ion effects: why the properties of lysozyme in salt solutions follow a Hofmeister series. Biophys J 2003;85:686-94.
    • (2003) Biophys J , vol.85 , pp. 686-694
    • Bostrom, M.1    Williams Ninham, D.R.B.W.2
  • 46
    • 2642556412 scopus 로고    scopus 로고
    • Specific ion effects: Role of salt and buffer in protonation of cytochrome c
    • Bostrom M, Williams DR, Ninham BW. Specific ion effects: role of salt and buffer in protonation of cytochrome c. Eur Phys J E Soft Matter 2004;13:239-45.
    • (2004) Eur Phys J e Soft Matter , vol.13 , pp. 239-245
    • Bostrom, M.1    Williams, D.R.2    Ninham, B.W.3
  • 47
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • Perutz MF. Electrostatic effects in proteins. Science 1978;201:1187-91.
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.F.1
  • 48
    • 12344260902 scopus 로고    scopus 로고
    • Concise review of mechanisms of bacterial adhesion to biomaterials and of techniques used in estimating bacteria- material interactions
    • Katsikogianni M, Missirlis YF. Concise review of mechanisms of bacterial adhesion to biomaterials and of techniques used in estimating bacteria- material interactions. Eur Cells Mater 2004;8:37-57.
    • (2004) Eur Cells Mater , vol.8 , pp. 37-57
    • Katsikogianni, M.1    Missirlis, Y.F.2
  • 49
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion BJ, Daggett V. The molecular basis for the chemical denaturation of proteins by urea. Proc Natl Acad Sci USA 2003;100:5142-7.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 50
    • 32244431731 scopus 로고    scopus 로고
    • Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme
    • Eissa AS, Khan SA. Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme. Food Hydrocollids 2006;20:543-7.
    • (2006) Food Hydrocollids , vol.20 , pp. 543-547
    • Eissa, A.S.1    Khan, S.A.2
  • 53
    • 0001626736 scopus 로고    scopus 로고
    • Hydrophobicity and hydrophilicity of biosurfaces
    • van Oss CJ. Hydrophobicity and hydrophilicity of biosurfaces. Curr Opinion Colloid Interface Sci 1997;2:503-12.
    • (1997) Curr Opinion Colloid Interface Sci , vol.2 , pp. 503-512
    • Van Oss, C.J.1
  • 54
    • 0023251178 scopus 로고
    • Characterization of a rat salivary sialoglycoprotein complex which agglutinates Streptococcus mutans
    • Brack CM, Reynolds EC. Characterization of a rat salivary sialoglycoprotein complex which agglutinates Streptococcus mutans. Infect Immun 1987;55:1264-73.
    • (1987) Infect Immun , vol.55 , pp. 1264-1273
    • Brack, C.M.1    Reynolds, E.C.2
  • 55
    • 70350065920 scopus 로고    scopus 로고
    • Structural heterogeneity of 6M. GdmCl-denatured proteins: Implications for the mechanism of protein folding
    • Chang JY. Structural heterogeneity of 6M. GdmCl-denatured proteins: implications for the mechanism of protein folding. Biochemistry 2009;48:9340-6.
    • (2009) Biochemistry , vol.48 , pp. 9340-9346
    • Chang, J.Y.1
  • 56
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions ofelectrostatic interactions
    • Monera OD, Kay CM, Hodges RS. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions ofelectrostatic interactions. Protein Sci 1994;3:1984-91.
    • (1994) Protein Sci , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 57
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv Protein Chem 1970;24:1-95.
    • (1970) Adv Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 58
    • 0029760018 scopus 로고    scopus 로고
    • Binding of hisactophilin i and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch
    • Hanakam F, Gerisch G, Lotz S, Alt T, Seelig A. Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch. Biochemistry 1996;35:11036-44.
    • (1996) Biochemistry , vol.35 , pp. 11036-11044
    • Hanakam, F.1    Gerisch, G.2    Lotz, S.3    Alt, T.4    Seelig, A.5
  • 59
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • Ben-Tal N, Honig B, Miller C, McLaughlin S. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys J 1997;73:1717-27.
    • (1997) Biophys J , vol.73 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 60
    • 0025800503 scopus 로고
    • Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol
    • Sankaram MB, Brophy PJ, Marsh D. Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol. Biochemistry 1991;30:5866-73.
    • (1991) Biochemistry , vol.30 , pp. 5866-5873
    • Sankaram, M.B.1    Brophy, P.J.2    Marsh, D.3
  • 61
    • 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;74:2559-64.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 2559-2564
    • Busscher, H.J.1    Norde, W.2    Van Der Mei, H.C.3
  • 62
    • 0000303370 scopus 로고
    • Selective bacterial adherence to oral epithelial surfaces and its role as an ecological determinant
    • Gibbons RJ, van Houte J. Selective bacterial adherence to oral epithelial surfaces and its role as an ecological determinant. Infect Immun 1971;3:567-73.
    • (1971) Infect Immun , vol.3 , pp. 567-573
    • Gibbons, R.J.1    Van Houte, J.2
  • 63
    • 80053653808 scopus 로고    scopus 로고
    • Stick to your gums: Mechanisms of oral microbial adherence
    • Nobbs AH, Jenkinson HF, Jakubovics NS. Stick to your gums: mechanisms of oral microbial adherence. J Dent Res 2011;90:1271-8.
    • (2011) J Dent Res , vol.90 , pp. 1271-1278
    • Nobbs, A.H.1    Jenkinson, H.F.2    Jakubovics, N.S.3
  • 64
    • 0030732136 scopus 로고    scopus 로고
    • A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutina-tion and adhesion to alpha2-3-linked sialic acid-containing receptors
    • Takahashi Y, Sandberg AL, Ruhl S, Muller J, Cisar JO. A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutina-tion and adhesion to alpha2-3-linked sialic acid-containing receptors. Infect Immun 1997;65:5042-51.
    • (1997) Infect Immun , vol.65 , pp. 5042-5051
    • Takahashi, Y.1    Sandberg, A.L.2    Ruhl, S.3    Muller, J.4    Cisar, J.O.5
  • 65
    • 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 JO, Yoshikawa M. Identification and characterization of hsa, the gene encoding the sialic acid-binding adhesin of Streptococcus gordonii DL1. Infect Immun 2002;70:1209-18.
    • (2002) Infect Immun , vol.70 , pp. 1209-1218
    • Takahashi, Y.1    Konishi, K.2    Cisar, J.O.3    Yoshikawa, M.4
  • 66
    • 34248365541 scopus 로고    scopus 로고
    • Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathway
    • Bensing BA, Siboo IR, Sullam PM. Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathway. J Bacteriol 2007;189:3846-54.
    • (2007) J Bacteriol , vol.189 , pp. 3846-3854
    • Bensing, B.A.1    Siboo, I.R.2    Sullam, P.M.3
  • 67
    • 48749094614 scopus 로고    scopus 로고
    • Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge
    • Rose L, Shivshankar P, Hinojosa E, Rodriguez A, Sanchez CJ, Orihuela CJ. Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge. J Infect Dis 2008;198:375-83.
    • (2008) J Infect Dis , vol.198 , pp. 375-383
    • Rose, L.1    Shivshankar, P.2    Hinojosa, E.3    Rodriguez, A.4    Sanchez, C.J.5    Orihuela, C.J.6
  • 68
    • 84855841407 scopus 로고    scopus 로고
    • Serine-rich repeat proteins and pili promote Streptococcus agalactiae colonization of the vaginal tract
    • Sheen TR, Jimenez A, Wang NY, Banerjee A, van Sorge NM, Doran KS. Serine-rich repeat proteins and pili promote Streptococcus agalactiae colonization of the vaginal tract. J Bacteriol 2011;193:6834-42.
    • (2011) J Bacteriol , vol.193 , pp. 6834-6842
    • Sheen, T.R.1    Jimenez, A.2    Wang, N.Y.3    Banerjee, A.4    Van Sorge, N.M.5    Doran, K.S.6
  • 69
    • 16244372364 scopus 로고    scopus 로고
    • Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in binding to human platelets
    • Siboo IR, Chambers HF, Sullam PM. Role of SraP, a Serine-Rich Surface Protein of Staphylococcus aureus, in binding to human platelets. Infect Immun 2005;73:2273-80.
    • (2005) Infect Immun , vol.73 , pp. 2273-2280
    • Siboo, I.R.1    Chambers, H.F.2    Sullam, P.M.3
  • 70
    • 84863566088 scopus 로고    scopus 로고
    • A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis
    • Lizcano A, Sanchez CJ, Orihuela CJ. A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis. Mol Oral Microbiol 2012;27:257-69.
    • (2012) Mol Oral Microbiol , vol.27 , pp. 257-269
    • Lizcano, A.1    Sanchez, C.J.2    Orihuela, C.J.3
  • 71
    • 78651457518 scopus 로고    scopus 로고
    • Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homolo-gues
    • Lofling J, Vimberg V, Battig P, Henriques-Normark B. Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homolo-gues. Cell Microbiol 2011;13:186-97.
    • (2011) Cell Microbiol , vol.13 , pp. 186-197
    • Lofling, J.1    Vimberg, V.2    Battig, P.3    Henriques-Normark, B.4
  • 72
    • 62249166648 scopus 로고    scopus 로고
    • Glycosylation and biogenesis of a family of serine-rich bacterial adhesins
    • Zhou M, Wu H. Glycosylation and biogenesis of a family of serine-rich bacterial adhesins. Microbiology 2009;155:317-27.
    • (2009) Microbiology , vol.155 , pp. 317-327
    • Zhou, M.1    Wu, H.2
  • 73
    • 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 BA, Sullam PM. 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. Mol Microbiol 2002;44:1081-94.
    • (2002) Mol Microbiol , vol.44 , pp. 1081-1094
    • Bensing, B.A.1    Sullam, P.M.2
  • 74
    • 0029810199 scopus 로고    scopus 로고
    • Recognition of immunoglobulin A1 by oral actinomyces and streptococcal lectins
    • Ruhl S, Sandberg AL, Cole MF, Cisar JO. Recognition of immunoglobulin A1 by oral actinomyces and streptococcal lectins. Infect Immun 1996;64:5421-4.
    • (1996) Infect Immun , vol.64 , pp. 5421-5424
    • Ruhl, S.1    Sandberg, A.L.2    Cole, M.F.3    Cisar, J.O.4
  • 75
  • 77
    • 80051570468 scopus 로고    scopus 로고
    • Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation
    • Maddocks SE, Wright CJ, Nobbs AH, Brittan JL, Franklin L, Stromberg N, et al. Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation. Mol Microbiol 2011;81:1034-49.
    • (2011) Mol Microbiol , vol.81 , pp. 1034-1049
    • Maddocks, S.E.1    Wright, C.J.2    Nobbs, A.H.3    Brittan, J.L.4    Franklin, L.5    Stromberg, N.6
  • 78
    • 84871903285 scopus 로고    scopus 로고
    • Taking the starch out of oral biofilm formation: Molecular basis and functional significance of salivary alpha-amylase binding to oral Streptococci
    • Nikitkova AE, Haase EM, Scannapieco FA. Taking the starch out of oral biofilm formation: molecular basis and functional significance of salivary alpha-amylase binding to oral Streptococci. Appl Environ Microbiol 2013;79: 416-423.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 416-423
    • Nikitkova, A.E.1    Haase, E.M.2    Scannapieco, F.A.3
  • 79
    • 0027292301 scopus 로고
    • Salivary alpha-amylase: Role in dental plaque and caries formation
    • Scannapieco FA, Torres G, Levine MJ. Salivary alpha-amylase: role in dental plaque and caries formation. Crit Rev Oral Biol Med 1993;4:301-7.
    • (1993) Crit Rev Oral Biol Med , vol.4 , pp. 301-307
    • Scannapieco, F.A.1    Torres, G.2    Levine, M.J.3
  • 80
    • 0020653638 scopus 로고
    • The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria
    • Douglas CW. The binding of human salivary alpha-amylase by oral strains of streptococcal bacteria. Arch Oral Biol 1983;28:567-73.
    • (1983) Arch Oral Biol , vol.28 , pp. 567-573
    • Douglas, C.W.1
  • 81
    • 0024386609 scopus 로고
    • Characterization of salivary alpha-amylase binding to Streptococcus sanguis
    • Scannapieco FA, Bergey EJ, Reddy MS, Levine MJ. Characterization of salivary alpha-amylase binding to Streptococcus sanguis. Infect Immun 1989;57:2853-63.
    • (1989) Infect Immun , vol.57 , pp. 2853-2863
    • Scannapieco, F.A.1    Bergey, E.J.2    Reddy, M.S.3    Levine, M.J.4
  • 82
    • 0025026949 scopus 로고
    • Amylase-binding as a discriminator among oral streptococci
    • Douglas CW, Pease AA, Whiley RA. Amylase-binding as a discriminator among oral streptococci. FEMS Microbiol Lett 1990;54:193-7.
    • (1990) FEMS Microbiol Lett , vol.54 , pp. 193-197
    • Douglas, C.W.1    Pease, A.A.2    Whiley, R.A.3
  • 83
    • 0025107844 scopus 로고
    • Ability to bind salivary alpha-amylase discriminates certain viridans group streptococcal species
    • Kilian M, Nyvad B. Ability to bind salivary alpha-amylase discriminates certain viridans group streptococcal species. J Clin Microbiol 1990;28:2576-7.
    • (1990) J Clin Microbiol , vol.28 , pp. 2576-2577
    • Kilian, M.1    Nyvad, B.2
  • 84
    • 0028519945 scopus 로고
    • Emergence in human dental plaque and host distribution of amylase-binding streptococci
    • Scannapieco FA, Solomon L, Wadenya RO. Emergence in human dental plaque and host distribution of amylase-binding streptococci. J Dent Res 1994;73:1627-35.
    • (1994) J Dent Res , vol.73 , pp. 1627-1635
    • Scannapieco, F.A.1    Solomon, L.2    Wadenya, R.O.3
  • 85
    • 0028191533 scopus 로고
    • Comparison of amylase-binding proteins in oral streptococci
    • Gwynn JP, Douglas CW. Comparison of amylase-binding proteins in oral streptococci. FEMS Microbiol Lett 1994;124:373-9.
    • (1994) FEMS Microbiol Lett , vol.124 , pp. 373-379
    • Gwynn, J.P.1    Douglas, C.W.2
  • 86
    • 0026445987 scopus 로고
    • Characterization of an amylase-binding component of Streptococcus gordonii G9B
    • Scannapieco FA, Haraszthy GG, Cho MI, Levine MJ. Characterization of an amylase-binding component of Streptococcus gordonii G9B. Infect Immun 1992;60:4726-33.
    • (1992) Infect Immun , vol.60 , pp. 4726-4733
    • Scannapieco, F.A.1    Haraszthy, G.G.2    Cho, M.I.3    Levine, M.J.4
  • 87
    • 0034778554 scopus 로고    scopus 로고
    • Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation
    • Rogers JD, Palmer Jr. RJ, Kolenbrander PE, Scannapieco FA. Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation. Infect Immun 2001;69:7046-56.
    • (2001) Infect Immun , vol.69 , pp. 7046-7056
    • Rogers, J.D.1    Palmer, Jr.R.J.2    Kolenbrander, P.E.3    Scannapieco, F.A.4
  • 89
    • 0141814781 scopus 로고    scopus 로고
    • Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii
    • Tanzer JM, Grant L, Thompson A, Li L, Rogers JD, Haase EM, Scannapieco FA. Amylase-binding proteins A (AbpA) and B (AbpB) differentially affect colonization of rats' teeth by Streptococcus gordonii. Microbiology 2003;149:2653-60.
    • (2003) Microbiology , vol.149 , pp. 2653-2660
    • Tanzer, J.M.1    Grant, L.2    Thompson, A.3    Li, L.4    Rogers, J.D.5    Haase, E.M.6    Scannapieco, F.A.7
  • 90
    • 84857812295 scopus 로고    scopus 로고
    • Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii
    • Nikitkova AE, Haase EM, Vickerman MM, Gill SR, Scannapieco FA. Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii. Appl Environ Microbiol 2012;78:1865-75.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1865-1875
    • Nikitkova, A.E.1    Haase, E.M.2    Vickerman, M.M.3    Gill, S.R.4    Scannapieco, F.A.5
  • 91
    • 27644485867 scopus 로고    scopus 로고
    • Central role of a bacterial two-component gene regulatory system of previously unknown function in pathogen persistence in human saliva
    • Shelburne 3rd SA, Sumby P, Sitkiewicz I, Granville C, DeLeo FR, Musser JM. Central role of a bacterial two-component gene regulatory system of previously unknown function in pathogen persistence in human saliva. Proc Natl Acad Sci USA 2005;102:16037-42.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16037-16042
    • Shelburne III, S.A.1    Sumby, P.2    Sitkiewicz, I.3    Granville, C.4    Deleo, F.R.5    Musser, J.M.6
  • 93
    • 80052745674 scopus 로고    scopus 로고
    • The changing face of Staphylococcus aureus: A continuing surgical challenge
    • Fry DE, Barie PS. The changing face of Staphylococcus aureus: a continuing surgical challenge. Surg Infect 2011;12:191-203.
    • (2011) Surg Infect , vol.12 , pp. 191-203
    • Fry, D.E.1    Barie, P.S.2
  • 96
    • 31044456290 scopus 로고    scopus 로고
    • Changes in the epidemiology of methicillin-resistant Staphylococcus aureus in intensive care units in US hospitals, 1992-2003
    • Klevens RM, Edwards JR, Tenover FC, McDonald LC, Horan T, Gaynes R. Changes in the epidemiology of methicillin-resistant Staphylococcus aureus in intensive care units in US hospitals, 1992-2003. Clin Infect Dis 2006;42:389-91.
    • (2006) Clin Infect Dis , vol.42 , pp. 389-391
    • Klevens, R.M.1    Edwards, J.R.2    Tenover, F.C.3    McDonald, L.C.4    Horan, T.5    Gaynes, R.6
  • 97
    • 77955694435 scopus 로고    scopus 로고
    • Microbial etiologies of hospital-acquired bacterial pneumonia and ventilator-associated bacterial pneumonia
    • Jones RN. Microbial etiologies of hospital-acquired bacterial pneumonia and ventilator-associated bacterial pneumonia. Clin Infect Dis 2010;51(Suppl. 1): S81-S87.
    • (2010) Clin Infect Dis , vol.51 , Issue.SUPPL. 1
    • Jones, R.N.1
  • 98
    • 73649174739 scopus 로고
    • Relative constancy of specific bacteriophage patterns of staphylococci isolated from oral and nasal areas
    • Knighton HT. Relative constancy of specific bacteriophage patterns of staphylococci isolated from oral and nasal areas. J Dent Res 1962;41:701-6.
    • (1962) J Dent Res , vol.41 , pp. 701-706
    • Knighton, H.T.1
  • 99
    • 76949128073 scopus 로고
    • Salivary bacteria. III.The pathogenicity of oral staphylococci
    • Singer AJ. Salivary bacteria. III. The pathogenicity of oral staphylococci. J Dent Res 1952;31:591-7.
    • (1952) J Dent Res , vol.31 , pp. 591-597
    • Singer, A.J.1
  • 100
    • 45849107241 scopus 로고    scopus 로고
    • Staphylococcus aureus and other bacteria in untreated periodontitis
    • Fritschi BZ, Albert-Kiszely A, Persson GR. Staphylococcus aureus and other bacteria in untreated periodontitis. J Dent Res 2008;87:589-93.
    • (2008) J Dent Res , vol.87 , pp. 589-593
    • Fritschi, B.Z.1    Albert-Kiszely, A.2    Persson, G.R.3
  • 101
    • 0028369499 scopus 로고
    • Microbial identification and antibiotic sensitivity testing, an aid for patients refractory to periodontal therapy. A report of 3 cases
    • Fine DH. Microbial identification and antibiotic sensitivity testing, an aid for patients refractory to periodontal therapy. A report of 3 cases. J Clin Period- ontol 1994;21:98-106.
    • (1994) J Clin Period- Ontol , vol.21 , pp. 98-106
    • Fine, D.H.1
  • 103
    • 77952412046 scopus 로고    scopus 로고
    • Mechanical non-surgical treatment of peri-implantitis: A single-blinded randomized longitudinal clinical study. II. Microbiological results
    • Persson GR, Samuelsson E, Lindahl C, Renvert S. Mechanical non-surgical treatment of peri-implantitis: a single-blinded randomized longitudinal clinical study. II. Microbiological results. J Clin Periodontol 2010;37:563-73.
    • (2010) J Clin Periodontol , vol.37 , pp. 563-573
    • Persson, G.R.1    Samuelsson, E.2    Lindahl, C.3    Renvert, S.4
  • 104
    • 0028693401 scopus 로고
    • Refractory endodontic lesion associated with Staphylococci aureus
    • Reader CM, Boniface M, Bujanda-Wagner S. Refractory endodontic lesion associated with Staphylococci aureus. J Endodontics 1994;20:607-9.
    • (1994) J Endodontics , vol.20 , pp. 607-609
    • Reader, C.M.1    Boniface, M.2    Bujanda-Wagner, S.3
  • 105
    • 57449087859 scopus 로고    scopus 로고
    • An implant periapical lesion leading to acute osteomyelitis with isolation of Staphylococcus aureus
    • Rokadiya S, Malden NJ. An implant periapical lesion leading to acute osteomyelitis with isolation of Staphylococcus aureus. Br Dent J 2008;205:489-91.
    • (2008) Br Dent J , vol.205 , pp. 489-491
    • Rokadiya, S.1    Malden, N.J.2
  • 106
    • 0034771017 scopus 로고    scopus 로고
    • The ecology of Staphylococcus species in the oral cavity
    • Smith AJ, Jackson MS, Bagg J. The ecology of Staphylococcus species in the oral cavity. J Med Microbiol 2001;50:940-6.
    • (2001) J Med Microbiol , vol.50 , pp. 940-946
    • Smith, A.J.1    Jackson, M.S.2    Bagg, J.3
  • 108
    • 0026664624 scopus 로고
    • Oral carriage of yeasts, coliforms and staphylococci in patients with advanced malignant disease
    • Jobbins J, Bagg J, Parsons K, Finlay I, Addy M, Newcombe RG. Oral carriage of yeasts, coliforms and staphylococci in patients with advanced malignant disease. J Oral Pathol Med 1992;21:305-8.
    • (1992) J Oral Pathol Med , vol.21 , pp. 305-308
    • Jobbins, J.1    Bagg, J.2    Parsons, K.3    Finlay, I.4    Addy, M.5    Newcombe, R.G.6
  • 112
    • 0026197597 scopus 로고
    • Incidence and characterization of Staphylococcus aureus from the tongues of children
    • Miyake Y, Iwai T, Sugai M, Miura K, Suginaka H, Nagasaka N. Incidence and characterization of Staphylococcus aureus from the tongues of children. JDent Res 1991;70:1045-7.
    • (1991) JDent Res , vol.70 , pp. 1045-1047
    • Miyake, Y.1    Iwai, T.2    Sugai, M.3    Miura, K.4    Suginaka, H.5    Nagasaka, N.6
  • 114
    • 0026094266 scopus 로고
    • Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens
    • Biesbrock AR, Reddy MS, Levine MJ. Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens. Infect Immun 1991;59:3492-7.
    • (1991) Infect Immun , vol.59 , pp. 3492-3497
    • Biesbrock, A.R.1    Reddy, M.S.2    Levine, M.J.3
  • 117
    • 0032436996 scopus 로고    scopus 로고
    • Surface protein adhesins of Staphylococcus aureus
    • Foster TJ, Hook M. Surface protein adhesins of Staphylococcus aureus. Trends Microbiol 1998;6:484-8.
    • (1998) Trends Microbiol , vol.6 , pp. 484-488
    • Foster, T.J.1    Hook, M.2
  • 118
    • 84890994963 scopus 로고
    • A type-specific antigenic protein derived from the Staphylococcus
    • Verwey WF. A type-specific antigenic protein derived from the Staphylococcus. J Exp Med 1940;71:635-44.
    • (1940) J Exp Med , vol.71 , pp. 635-644
    • Verwey, W.F.1
  • 119
    • 84979141151 scopus 로고
    • A normally occurring Staphylococcus antibody in human serum
    • Jensen K. A normally occurring Staphylococcus antibody in human serum. Acta Pathol Microbiol Scand 1958;44:421-8.
    • (1958) Acta Pathol Microbiol Scand , vol.44 , pp. 421-428
    • Jensen, K.1
  • 121
    • 0030976395 scopus 로고    scopus 로고
    • Regulation of protein A synthesis by the sar and agr loci of Staphylococcus aureus
    • Cheung AL, Eberhardt K, Heinrichs JH. Regulation of protein A synthesis by the sar and agr loci of Staphylococcus aureus. Infect Immun 1997;65:2243-9.
    • (1997) Infect Immun , vol.65 , pp. 2243-2249
    • Cheung, A.L.1    Eberhardt, K.2    Heinrichs, J.H.3
  • 122
    • 0014457219 scopus 로고
    • Protein A from Staphylococcus aureus. 8. Production of protein A by bacterial and L-forms of S.Aureus
    • Forsgren A. Protein A from Staphylococcus aureus. 8. Production of protein A by bacterial and L-forms of S. aureus. Acta Pathol Microbiol Scand 1969;75:481-90.
    • (1969) Acta Pathol Microbiol Scand , vol.75 , pp. 481-490
    • Forsgren, A.1
  • 124
    • 0014701547 scopus 로고
    • Phylogenetic insight into evolution of mammalian Fc fragment of gamma G globulin using staphylo- coccal protein A
    • Kronvall G, Seal US, Finstad J, Williams Jr RC. Phylogenetic insight into evolution of mammalian Fc fragment of gamma G globulin using staphylo- coccal protein A. J Immunol 1970;104:140-7.
    • (1970) J Immunol , vol.104 , pp. 140-147
    • Kronvall, G.1    Seal, U.S.2    Finstad, J.3    Williams Jr., R.C.4
  • 125
    • 0019493843 scopus 로고
    • Comparison of mechanisms of interaction between protein A from Staphylococcus aureus and human monoclonal IgG, IgA and IgM in relation to the classical Fc gamma and the alternative F(ab')2 epsilon protein A interactions
    • Inganas M. Comparison of mechanisms of interaction between protein A from Staphylococcus aureus and human monoclonal IgG, IgA and IgM in relation to the classical Fc gamma and the alternative F(ab')2 epsilon protein A interactions. Scand J Immunol 1981;13:343-52.
    • (1981) Scand J Immunol , vol.13 , pp. 343-352
    • Inganas, M.1
  • 126
    • 0024595964 scopus 로고
    • Human IgM molecules that bind staphylococcal protein A contain VHIII H chains
    • Sasso EH, Silverman GJ, Mannik M. Human IgM molecules that bind staphylococcal protein A contain VHIII H chains. J Immunol 1989;142:2778-83.
    • (1989) J Immunol , vol.142 , pp. 2778-2783
    • Sasso, E.H.1    Silverman, G.J.2    Mannik, M.3
  • 129
    • 4043059295 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A induces airway epithelial inflammatory responses by activating TNFR1
    • Gomez MI, Lee A, Reddy B, Muir A, Soong G, Pitt A, Cheung A, Prince A. Staphylococcus aureus protein A induces airway epithelial inflammatory responses by activating TNFR1. Nat Med 2004;10:842-8.
    • (2004) Nat Med , vol.10 , pp. 842-848
    • Gomez, M.I.1    Lee, A.2    Reddy, B.3    Muir, A.4    Soong, G.5    Pitt, A.6    Cheung, A.7    Prince, A.8
  • 130
    • 33745983268 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A activates TNFR1 signaling through conserved IgG binding domains
    • Gomez MI, O'Seaghdha M, Magargee M, Foster TJ, Prince AS. Staphylococcus aureus protein A activates TNFR1 signaling through conserved IgG binding domains. J Biol Chem 2006;281:20190-6.
    • (2006) J Biol Chem , vol.281 , pp. 20190-20196
    • Gomez, M.I.1    O'Seaghdha, M.2    Magargee, M.3    Foster, T.J.4    Prince, A.S.5
  • 131
    • 33846965544 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A activates TACE through EGFR-dependent signaling
    • Gomez MI, Seaghdha MO, Prince AS. Staphylococcus aureus protein A activates TACE through EGFR-dependent signaling. EMBO J 2007;26:701-9.
    • (2007) EMBO J , vol.26 , pp. 701-709
    • Gomez, M.I.1    Seaghdha, M.O.2    Prince, A.S.3
  • 132
    • 85030414521 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A mediates invasion across airway epithelial cells through activation of RhoA signaling and proteolytic activity
    • Soong G, Martin FJ, Chun J, Cohen TS, Ahn DS, Prince A. Staphylococcus aureus protein A mediates invasion across airway epithelial cells through activation of RhoA signaling and proteolytic activity. J Biol Chem 2011;205:1571-9.
    • (2011) J Biol Chem , vol.205 , pp. 1571-1579
    • Soong, G.1    Martin, F.J.2    Chun, J.3    Cohen, T.S.4    Ahn, D.S.5    Prince, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.