메뉴 건너뛰기




Volumn 24, Issue 1, 2000, Pages 153-192

Role of bacterial proteinases in matrix destruction and modulation of host responses

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ARGINGIPAIN, PORPHYROMONAS GINGIVALIS; BACTERIAL PROTEIN; CLOSTRIDIOPEPTIDASE A; CYSTEINE PROTEINASE; HEMAGGLUTININ; MATRIX METALLOPROTEINASE; PROTEINASE; SCLEROPROTEIN; TPR PROTEASE;

EID: 0034303490     PISSN: 09066713     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0757.2000.2240108.x     Document Type: Article
Times cited : (287)

References (381)
  • 1
    • 0031887213 scopus 로고    scopus 로고
    • Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease
    • Abe N, Kadowaki T, Okamoto K, Nakayma K, Ohishi M, Yamamoto K. Biochemical and functional properties of lysine-specific cysteine proteinase (Lys-gingipain) as a virulence factor of Porphyromonas gingivalis in periodontal disease. J Biochem 1998: 123: 305-312.
    • (1998) J Biochem , vol.123 , pp. 305-312
    • Abe, N.1    Kadowaki, T.2    Okamoto, K.3    Nakayma, K.4    Ohishi, M.5    Yamamoto, K.6
  • 2
    • 0022018934 scopus 로고
    • Glycylprolyl dipeptidylaminopeptidase from Bacteroides gingivalis
    • Abiko Y, Hayakawa M, Murai S, Takiguchi H. Glycylprolyl dipeptidylaminopeptidase from Bacteroides gingivalis. J Dent Res 1985: 64: 106-111.
    • (1985) J Dent Res , vol.64 , pp. 106-111
    • Abiko, Y.1    Hayakawa, M.2    Murai, S.3    Takiguchi, H.4
  • 3
    • 0031441656 scopus 로고    scopus 로고
    • Modification of cystatin C activity by bacterial proteinases and neutrophil elastase in periodontitis
    • Abrahamson M, Wikstrom M, Potempa J, Renvert S, Hall A. Modification of cystatin C activity by bacterial proteinases and neutrophil elastase in periodontitis. Mol Pathol 1997: 50: 291-297.
    • (1997) Mol Pathol , vol.50 , pp. 291-297
    • Abrahamson, M.1    Wikstrom, M.2    Potempa, J.3    Renvert, S.4    Hall, A.5
  • 4
    • 0028875640 scopus 로고
    • Characterization, genetic-analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50
    • Aduse-Opoku J, Muir J, Slaney JM, Rangarajan M, Curtis MA. Characterization, genetic-analysis, and expression of a protease antigen (PrpRI) of Porphyromonas gingivalis W50. Infect Immun 1995: 63: 4744-4754.
    • (1995) Infect Immun , vol.63 , pp. 4744-4754
    • Aduse-Opoku, J.1    Muir, J.2    Slaney, J.M.3    Rangarajan, M.4    Curtis, M.A.5
  • 5
    • 0030792046 scopus 로고    scopus 로고
    • The Tla of Porphyromonas gingivalis W50: A homologue of the arginine-specific protease precursor (PrpR1) which shares sequence similarity to TonB linked receptors
    • Aduse-Opoku J, Slaney JM, Rangarajan M, Muir J, Young KA, Curtis MA. The Tla of Porphyromonas gingivalis W50: a homologue of the arginine-specific protease precursor (PrpR1) which shares sequence similarity to TonB linked receptors. J Bacteriol 1997: 179: 4778-4788.
    • (1997) J Bacteriol , vol.179 , pp. 4778-4788
    • Aduse-Opoku, J.1    Slaney, J.M.2    Rangarajan, M.3    Muir, J.4    Young, K.A.5    Curtis, M.A.6
  • 6
    • 0031254282 scopus 로고    scopus 로고
    • Putative periodontal pathogens in subgingival plaque of young adults with and without early-onset periodontitis
    • Albandar JM, Brown LJ, Löe H. Putative periodontal pathogens in subgingival plaque of young adults with and without early-onset periodontitis. J Periodontol 1997: 68: 973-981.
    • (1997) J Periodontol , vol.68 , pp. 973-981
    • Albandar, J.M.1    Brown, L.J.2    Löe, H.3
  • 7
    • 0025582626 scopus 로고
    • Associations between six DNA probe-detected periodontal bacteria and alveolar bone loss and other clinical signs of periodontitis
    • Albandar JM, Olsen I, Gjermo P. Associations between six DNA probe-detected periodontal bacteria and alveolar bone loss and other clinical signs of periodontitis. Acta Odontol Scand 1990: 48: 415-423.
    • (1990) Acta Odontol Scand , vol.48 , pp. 415-423
    • Albandar, J.M.1    Olsen, I.2    Gjermo, P.3
  • 9
    • 0031260550 scopus 로고    scopus 로고
    • Natural variation within the principal arginine-specific protease gene, prpR1, of Porphyromonas gingivalis
    • Allaker RP, Aduse-Opoku J, Batten JE, Curtis MA. Natural variation within the principal arginine-specific protease gene, prpR1, of Porphyromonas gingivalis. Oral Microbiol Immunol 1997: 12: 298-302.
    • (1997) Oral Microbiol Immunol , vol.12 , pp. 298-302
    • Allaker, R.P.1    Aduse-Opoku, J.2    Batten, J.E.3    Curtis, M.A.4
  • 10
    • 0029379644 scopus 로고
    • Interleukin 4 (IL-4) and IL-6-producing memory T-cells in peripheral blood and gingival tissue in periodontitis patients with high serum antibody titers to Porphyromonas gingivalis
    • Aoyagi T, Sugawara-Aoyagi M, Yamazaki K, Hara K. Interleukin 4 (IL-4) and IL-6-producing memory T-cells in peripheral blood and gingival tissue in periodontitis patients with high serum antibody titers to Porphyromonas gingivalis. Oral Microbiol Immunol 1995: 10: 304-310.
    • (1995) Oral Microbiol Immunol , vol.10 , pp. 304-310
    • Aoyagi, T.1    Sugawara-Aoyagi, M.2    Yamazaki, K.3    Hara, K.4
  • 11
    • 0027998661 scopus 로고
    • Cloning and sequence analysis of a chymotrypsinlike protease from Treponema denticola
    • Arakawa S, Kuramitsu HK. Cloning and sequence analysis of a chymotrypsinlike protease from Treponema denticola. Infect Immun 1994: 62: 3424-3433.
    • (1994) Infect Immun , vol.62 , pp. 3424-3433
    • Arakawa, S.1    Kuramitsu, H.K.2
  • 12
    • 0026643195 scopus 로고
    • Interleukin-8, a chemotactic and inflammatory cytokine
    • Baggiolini M, Clark-Lewis I. Interleukin-8, a chemotactic and inflammatory cytokine. FEBS Lett 1992: 27: 97-101.
    • (1992) FEBS Lett , vol.27 , pp. 97-101
    • Baggiolini, M.1    Clark-Lewis, I.2
  • 13
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokines; CXC and CC chemokines
    • Baggiolini M, Dewald B, Moser B. Interleukin-8 and related chemotactic cytokines; CXC and CC chemokines. Adv Immunol 1994: 55: 197-179.
    • (1994) Adv Immunol , vol.55 , pp. 197-1179
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 14
    • 0031863621 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone
    • 1998
    • Banbula A, Potempa J, Travis J, Bode W, Medrano FJ. (1998) Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone. Protein Sci 1998: 7: 1259-1261.
    • (1998) Protein Sci , vol.7 , pp. 1259-1261
    • Banbula, A.1    Potempa, J.2    Travis, J.3    Bode, W.4    Medrano, F.J.5
  • 15
    • 0033515503 scopus 로고    scopus 로고
    • Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis
    • Banbula A, Mak P, Bugno M, Silberring J, Dubin A, Nelson D, Travis J, Potempa J. Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis. J Biol Chem 1999: 274: 9246-9252.
    • (1999) J Biol Chem , vol.274 , pp. 9246-9252
    • Banbula, A.1    Mak, P.2    Bugno, M.3    Silberring, J.4    Dubin, A.5    Nelson, D.6    Travis, J.7    Potempa, J.8
  • 16
    • 0033546749 scopus 로고    scopus 로고
    • Rapid and efficient inactivation of IL-6 gingipains' lysine- and arginine-specific proteinases from Porphyromonas gingivalis
    • Banbula A, Bugno M, Kuster A, Heinrich PC, Travis J, Potempa J. Rapid and efficient inactivation of IL-6 gingipains' lysine-and arginine-specific proteinases from Porphyromonas gingivalis. Biochem Biophys Res Commun 1999: 261: 598-602.
    • (1999) Biochem Biophys Res Commun , vol.261 , pp. 598-602
    • Banbula, A.1    Bugno, M.2    Kuster, A.3    Heinrich, P.C.4    Travis, J.5    Potempa, J.6
  • 18
    • 0032957438 scopus 로고    scopus 로고
    • Activities of the Porphyromonas gingivalis PrtP proteinase determined by construction of prtP-deficient mutants and expression of the gene in Bacteroides species
    • Barkocy-Gallagher GA, Foley JW, Lantz MS. Activities of the Porphyromonas gingivalis PrtP proteinase determined by construction of prtP-deficient mutants and expression of the gene in Bacteroides species. J Bacteriol 1999: 181: 246-255.
    • (1999) J Bacteriol , vol.181 , pp. 246-255
    • Barkocy-Gallagher, G.A.1    Foley, J.W.2    Lantz, M.S.3
  • 22
    • 0030611784 scopus 로고    scopus 로고
    • Activation of the interleukin-1beta precursor by Treponema denticola: A potential role in chronic inflammatory periodontal diseases
    • Beausejour A, Deslauriers N, Grenier D. Activation of the interleukin-1beta precursor by Treponema denticola: a potential role in chronic inflammatory periodontal diseases. Infect Immun 1997: 65: 3199-3202.
    • (1997) Infect Immun , vol.65 , pp. 3199-3202
    • Beausejour, A.1    Deslauriers, N.2    Grenier, D.3
  • 24
    • 0028533720 scopus 로고
    • Purification and characterization of lysine- and arginine-specific gingivain proteases from Porphyromonas gingivalis
    • Bedi GS. Purification and characterization of lysine-and arginine-specific gingivain proteases from Porphyromonas gingivalis. Prep Biochem 1994: 24: 251-261.
    • (1994) Prep Biochem , vol.24 , pp. 251-261
    • Bedi, G.S.1
  • 25
    • 0028118622 scopus 로고
    • Purification and characterization of a collagen-degrading protease from Porphyromonas gingivalis
    • Bedi GS, Williams T. Purification and characterization of a collagen-degrading protease from Porphyromonas gingivalis. J Biol Chem 1994: 269: 599-606.
    • (1994) J Biol Chem , vol.269 , pp. 599-606
    • Bedi, G.S.1    Williams, T.2
  • 26
    • 0029016550 scopus 로고
    • Signals and receptors involved in recruitment of inflammatory cells
    • Ben-Baruch A, Michiel DF, Oppenheim JJ. Signals and receptors involved in recruitment of inflammatory cells. J Biol Chem 1995: 19: 11703-11706.
    • (1995) J Biol Chem , vol.19 , pp. 11703-11706
    • Ben-Baruch, A.1    Michiel, D.F.2    Oppenheim, J.J.3
  • 27
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge A, Bjorck L. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J Biol Chem 1995: 270: 9862-9867.
    • (1995) J Biol Chem , vol.270 , pp. 9862-9867
    • Berge, A.1    Bjorck, L.2
  • 28
    • 0030737648 scopus 로고    scopus 로고
    • A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins
    • Bhogal PS, Slakeski N, Reynolds EC. A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg-and Lys-specific cysteine proteinases and adhesins. Microbiology-UK 1997: 143: 2485-2495.
    • (1997) Microbiology-UK , vol.143 , pp. 2485-2495
    • Bhogal, P.S.1    Slakeski, N.2    Reynolds, E.C.3
  • 29
    • 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. J Periodontal Res 1985: 20: 35-10.
    • (1985) J Periodontal Res , vol.20 , pp. 35-110
    • Bickel, M.1    Cimasoni, G.2
  • 30
    • 0021716333 scopus 로고
    • Activation of keratinocyte-mediated collagen (type I) breakdown by suspected human periodontopathogen. Evidence of a novel mechanism of connective tissue breakdown
    • Birkedal-Hansen H, Wells BR, Lin HY, Caufield PW, Taylor RE. Activation of keratinocyte-mediated collagen (type I) breakdown by suspected human periodontopathogen. Evidence of a novel mechanism of connective tissue breakdown. J Periodontal Res 1984: 19: 645-650.
    • (1984) J Periodontal Res , vol.19 , pp. 645-650
    • Birkedal-Hansen, H.1    Wells, B.R.2    Lin, H.Y.3    Caufield, P.W.4    Taylor, R.E.5
  • 32
    • 0024546648 scopus 로고
    • Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
    • 32: Bjorck L, Akesson P, Bohus M, Trojnar J, Abrahamson M, Olafsson I, Grubb A. Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 1989: 337: 385-386.
    • (1989) Nature , vol.337 , pp. 385-386
    • Bjorck, L.1    Akesson, P.2    Bohus, M.3    Trojnar, J.4    Abrahamson, M.5    Olafsson, I.6    Grubb, A.7
  • 33
    • 0030068076 scopus 로고    scopus 로고
    • Passive immunization with monoclonal antibodies against Porphyromonas gingivalis in patients with periodontitis
    • Booth V, Ashley FP, Lehner T. Passive immunization with monoclonal antibodies against Porphyromonas gingivalis in patients with periodontitis. Infect Immun 1996: 64: 422-427.
    • (1996) Infect Immun , vol.64 , pp. 422-427
    • Booth, V.1    Ashley, F.P.2    Lehner, T.3
  • 34
    • 0030632343 scopus 로고    scopus 로고
    • Characterization of the Porphyromonas gingivalis antigen recognized by a monoclonal antibody which prevents colonization by this organism
    • Booth V, Lehner T. Characterization of the Porphyromonas gingivalis antigen recognized by a monoclonal antibody which prevents colonization by this organism. J Periodontal Res 1997: 32: 54-60.
    • (1997) J Periodontal Res , vol.32 , pp. 54-60
    • Booth, V.1    Lehner, T.2
  • 35
    • 0026642511 scopus 로고
    • Cloning, expression, and sequencing of a protease gene (tpr) from Porpliyromonas gingivalis W83 in Escherichia coli
    • Bourgeau G, Lapointe H, Peloquin P, Mayrand D. Cloning, expression, and sequencing of a protease gene (tpr) from Porpliyromonas gingivalis W83 in Escherichia coli. Infect Immun 1992: 60: 3186-3192.
    • (1992) Infect Immun , vol.60 , pp. 3186-3192
    • Bourgeau, G.1    Lapointe, H.2    Peloquin, P.3    Mayrand, D.4
  • 36
    • 0026899697 scopus 로고
    • Effect of porphyrins and host iron transport proteins on outer membrane protein expression in Porphyromonas (Bacteroides) gingivalis: Identification of a novel 26 kDa hemin-repressible surface protein
    • Bramanti TE, Holt SC. Effect of porphyrins and host iron transport proteins on outer membrane protein expression in Porphyromonas (Bacteroides) gingivalis: identification of a novel 26 kDa hemin-repressible surface protein. Microb Pathog 1992: 13: 61-73.
    • (1992) Microb Pathog , vol.13 , pp. 61-73
    • Bramanti, T.E.1    Holt, S.C.2
  • 37
    • 0032981308 scopus 로고    scopus 로고
    • Pathogenesis of joint damage in rheumatoid arthritis
    • Bresnihan B. Pathogenesis of joint damage in rheumatoid arthritis. J Rheumatol 1999: 26: 717-719.
    • (1999) J Rheumatol , vol.26 , pp. 717-719
    • Bresnihan, B.1
  • 39
    • 0032549590 scopus 로고    scopus 로고
    • Inactivation of tumor necrosis factor-alpha by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion
    • Calkins CC, Platt K, Potempa J, Travis J. Inactivation of tumor necrosis factor-alpha by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion. J Biol Chem 1998: 273: 6611-6614.
    • (1998) J Biol Chem , vol.273 , pp. 6611-6614
    • Calkins, C.C.1    Platt, K.2    Potempa, J.3    Travis, J.4
  • 40
    • 0021240552 scopus 로고
    • Degradation of albumin, haemopexin, haptoglobin and transferrin, by black-pigmented Bacteroides species
    • Carlsson J, Hofling JF, Sundqvist GK. Degradation of albumin, haemopexin, haptoglobin and transferrin, by black-pigmented Bacteroides species. J Med Microbiol 1984: 18: 39-46.
    • (1984) J Med Microbiol , vol.18 , pp. 39-46
    • Carlsson, J.1    Hofling, J.F.2    Sundqvist, G.K.3
  • 41
    • 0025635881 scopus 로고
    • Hemin levels in culture medium of Porphyromonas (Bacteroides) gingivalis regulate both hemin binding and trypsinlike protease production
    • Carman RJ, Ramakrishnan MD, Harper FH. Hemin levels in culture medium of Porphyromonas (Bacteroides) gingivalis regulate both hemin binding and trypsinlike protease production. Infect Immun 1990: 58: 4016-4019.
    • (1990) Infect Immun , vol.58 , pp. 4016-4019
    • Carman, R.J.1    Ramakrishnan, M.D.2    Harper, F.H.3
  • 42
    • 0022395406 scopus 로고
    • 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis
    • 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature 1985: 317: 730-732.
    • (1985) Nature , vol.317 , pp. 730-732
    • Carrell, R.W.1    Owen, M.C.2
  • 43
    • 0022852281 scopus 로고
    • 1-Antitrypsin: Molecular pathology, leukocytes, and tissue damage
    • 1-Antitrypsin: molecular pathology, leukocytes, and tissue damage. J Clin Invest 1986: 78: 1427-1431.
    • (1986) J Clin Invest , vol.78 , pp. 1427-1431
    • Carrell, R.W.1
  • 45
    • 0026569242 scopus 로고
    • Regulation of platelet-activating factor (PAF) synthesis and PAF-mediated neutrophil adhesion to endothelial cells activated by thrombin
    • Carveth HJ, Shaddy RE, Whatley RE, McIntyre TM, Prescott SM, Zimmerman GA. Regulation of platelet-activating factor (PAF) synthesis and PAF-mediated neutrophil adhesion to endothelial cells activated by thrombin. Semin Thromb Hemost 1992: 18: 126-134.
    • (1992) Semin Thromb Hemost , vol.18 , pp. 126-134
    • Carveth, H.J.1    Shaddy, R.E.2    Whatley, R.E.3    McIntyre, T.M.4    Prescott, S.M.5    Zimmerman, G.A.6
  • 46
    • 0031788196 scopus 로고    scopus 로고
    • Failure of macrophage activation in destructive periodontal disease
    • Chapple CC, Srivastava M, Hunter N. Failure of macrophage activation in destructive periodontal disease. J Pathol 1998: 186: 281-286.
    • (1998) J Pathol , vol.186 , pp. 281-286
    • Chapple, C.C.1    Srivastava, M.2    Hunter, N.3
  • 47
    • 0032435254 scopus 로고    scopus 로고
    • Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases
    • Chen JM, Rawlings ND, Stevens FEE, Barrett JA. Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett 1998: 441: 361-365.
    • (1998) FEBS Lett , vol.441 , pp. 361-365
    • Chen, J.M.1    Rawlings, N.D.2    Stevens, F.E.E.3    Barrett, J.A.4
  • 48
    • 0028124266 scopus 로고
    • Purification and characterization of two forms of a high-molecular-weight cysteine proteinase (porphypain) from Porphyromonas gingivalis
    • Ciborowski P, Nishikata M, Allen RD, Lantz MS. Purification and characterization of two forms of a high-molecular-weight cysteine proteinase (porphypain) from Porphyromonas gingivalis. J Bacteriol 1994: 176: 4549-4557.
    • (1994) J Bacteriol , vol.176 , pp. 4549-4557
    • Ciborowski, P.1    Nishikata, M.2    Allen, R.D.3    Lantz, M.S.4
  • 49
    • 0029874404 scopus 로고    scopus 로고
    • An investigation into the use of SDS-PAGE of cell surface extracts and proteolytic activity to differentiate Prevotella nigrescens and Prevotella intermedia
    • Cookson AL, Wray A, Handley PS, Jacob AE. An investigation into the use of SDS-PAGE of cell surface extracts and proteolytic activity to differentiate Prevotella nigrescens and Prevotella intermedia. FEMS Microbiol Lett 1996: 136: 109-115.
    • (1996) FEMS Microbiol Lett , vol.136 , pp. 109-115
    • Cookson, A.L.1    Wray, A.2    Handley, P.S.3    Jacob, A.E.4
  • 50
    • 0027637176 scopus 로고
    • Pathogenesis of glomerulonephritis
    • Couser WG. Pathogenesis of glomerulonephritis. Kidney Int 1993: 44(suppl 42): 19-26.
    • (1993) Kidney Int , vol.44 , Issue.42 SUPPL. , pp. 19-26
    • Couser, W.G.1
  • 51
    • 0024820274 scopus 로고
    • Detection of cathepsin B- and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin
    • Cox SW, Eley BM. Detection of cathepsin B-and L-, elastase-, tryptase-, trypsin-, and dipeptidyl peptidase IV-like activities in crevicular fluid from gingivitis and periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. J Periodontal Res 1989: 24: 353-361.
    • (1989) J Periodontal Res , vol.24 , pp. 353-361
    • Cox, S.W.1    Eley, B.M.2
  • 52
    • 0028511353 scopus 로고
    • Preliminary characterization of antigens recognized by monoclonal antibodies raised to Porphyromonas gingivalis and by sera from patients with periodontitis
    • Cridland JC, Booth V, Ashley FP, Curtis MA, Wilson RF, Shepherd P. Preliminary characterization of antigens recognized by monoclonal antibodies raised to Porphyromonas gingivalis and by sera from patients with periodontitis. J Periodontal Res 1994: 29: 339-347.
    • (1994) J Periodontal Res , vol.29 , pp. 339-347
    • Cridland, J.C.1    Booth, V.2    Ashley, F.P.3    Curtis, M.A.4    Wilson, R.F.5    Shepherd, P.6
  • 53
    • 0027167692 scopus 로고
    • Characterization of the trypsin-like enzymes of Porphyromonas gingivalis W83 using a radiolabelled active-site-directed inhibitor
    • Curtis MA, Ramakrishnan M, Slaney JM. Characterization of the trypsin-like enzymes of Porphyromonas gingivalis W83 using a radiolabelled active-site-directed inhibitor. J Gen Microbiol 1993: 139: 949-955.
    • (1993) J Gen Microbiol , vol.139 , pp. 949-955
    • Curtis, M.A.1    Ramakrishnan, M.2    Slaney, J.M.3
  • 54
  • 55
    • 0029933060 scopus 로고    scopus 로고
    • Characterisation of an adherence and antigenic determinant of the Arg1 protease of Porphyromonas gingivalis which is present on multiple gene products
    • Curtis MA, Aduse-Opoku J, Slaney JM, Rangarajan M, Booth V, Cridland J, Shephard P. Characterisation of an adherence and antigenic determinant of the Arg1 protease of Porphyromonas gingivalis which is present on multiple gene products. Infect Immun 1996: 64: 2532-2539.
    • (1996) Infect Immun , vol.64 , pp. 2532-2539
    • Curtis, M.A.1    Aduse-Opoku, J.2    Slaney, J.M.3    Rangarajan, M.4    Booth, V.5    Cridland, J.6    Shephard, P.7
  • 58
    • 0027135337 scopus 로고
    • Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis
    • Cutler CW, Arnold RR, Schenkein HA. Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis. J Immunol 1993: 151: 7016-7029.
    • (1993) J Immunol , vol.151 , pp. 7016-7029
    • Cutler, C.W.1    Arnold, R.R.2    Schenkein, H.A.3
  • 59
    • 0028813652 scopus 로고
    • Pathogenic strategies of the oral anaerobe, Porphyromonas gingivalis
    • Cutler CW, Kalmar JR, Genco CA. Pathogenic strategies of the oral anaerobe, Porphyromonas gingivalis. Trends Microbiol 1995: 3: 45-51.
    • (1995) Trends Microbiol , vol.3 , pp. 45-51
    • Cutler, C.W.1    Kalmar, J.R.2    Genco, C.A.3
  • 60
    • 0026667707 scopus 로고
    • Intrinsic pathway activation of factor X and its activation peptide-deficient derivative, factor Xdes-143-191
    • Duffy EJ, Lollar P. Intrinsic pathway activation of factor X and its activation peptide-deficient derivative, factor Xdes-143-191. J Biol Chem 1992: 267: 7821-7827.
    • (1992) J Biol Chem , vol.267 , pp. 7821-7827
    • Duffy, E.J.1    Lollar, P.2
  • 61
    • 0030256818 scopus 로고    scopus 로고
    • Alterations in phagocyte function and periodontal infection
    • Daniel MA, Van Dyke TE. Alterations in phagocyte function and periodontal infection. J Periodontol 1996: 67: 1070-1075.
    • (1996) J Periodontol , vol.67 , pp. 1070-1075
    • Daniel, M.A.1    Van Dyke, T.E.2
  • 63
    • 0031076322 scopus 로고    scopus 로고
    • Hemagglutinin activity and heterogeneity of related Porphyromonas gingivalis proteinases
    • DeCarlo AA, Harber GJ. Hemagglutinin activity and heterogeneity of related Porphyromonas gingivalis proteinases. Oral Microbiol Immunol 1997: 12: 47-56.
    • (1997) Oral Microbiol Immunol , vol.12 , pp. 47-56
    • DeCarlo, A.A.1    Harber, G.J.2
  • 64
    • 0031158475 scopus 로고    scopus 로고
    • Activation and novel processing of matrix metalloproteinases by a thiol-proteinase from the oral anaerobe Porphyromonas gingivalis
    • DeCarlo AA, Windsor LJ, Bodden MK, Harber GJ, Birkedal-Hansen B, Birkedal-Hansen H. Activation and novel processing of matrix metalloproteinases by a thiol-proteinase from the oral anaerobe Porphyromonas gingivalis. J Dent Res 1997: 76: 1260-1270.
    • (1997) J Dent Res , vol.76 , pp. 1260-1270
    • DeCarlo, A.A.1    Windsor, L.J.2    Bodden, M.K.3    Harber, G.J.4    Birkedal-Hansen, B.5    Birkedal-Hansen, H.6
  • 65
    • 0032176423 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinases and a collagen-degrading phenotype in fibroblasts and epithelial cells by secreted Porphyromonas gingivalis proteinase
    • DeCarlo AA, Grenett HE, Harber GJ, Windsor LJ, Bodden MK, Birkedal-Hansen B, Birkedal-Hansen H. Induction of matrix metalloproteinases and a collagen-degrading phenotype in fibroblasts and epithelial cells by secreted Porphyromonas gingivalis proteinase. J Periodontal Res 1998: 33: 408-420.
    • (1998) J Periodontal Res , vol.33 , pp. 408-420
    • DeCarlo, A.A.1    Grenett, H.E.2    Harber, G.J.3    Windsor, L.J.4    Bodden, M.K.5    Birkedal-Hansen, B.6    Birkedal-Hansen, H.7
  • 66
    • 0032981525 scopus 로고    scopus 로고
    • Porphyrin-mediated binding to hemoglobin by the HA2 domain of cysteine proteinases (gingipains) and hemagglutinins from the periodontal pathogen Porphyromonas gingivalis
    • DeCarlo AA, Paramaesvaran M, Yun PLWE, Collyer C, Hunter N. Porphyrin-mediated binding to hemoglobin by the HA2 domain of cysteine proteinases (gingipains) and hemagglutinins from the periodontal pathogen Porphyromonas gingivalis. J Bacteriol 1999: 181: 3784-3791.
    • (1999) J Bacteriol , vol.181 , pp. 3784-3791
    • DeCarlo, A.A.1    Paramaesvaran, M.2    Yun, P.L.W.E.3    Collyer, C.4    Hunter, N.5
  • 67
    • 0023894013 scopus 로고
    • Molecular cloning and sequencing of the gene encoding the fimbrial subunit protein of Bacteroides gingivalis
    • Dickinson DP, Kubiniec MA, Yoshimura F, Genco RJ. Molecular cloning and sequencing of the gene encoding the fimbrial subunit protein of Bacteroides gingivalis. J Bacteriol 1988: 170: 1658-1665.
    • (1988) J Bacteriol , vol.170 , pp. 1658-1665
    • Dickinson, D.P.1    Kubiniec, M.A.2    Yoshimura, F.3    Genco, R.J.4
  • 68
  • 69
    • 0029870771 scopus 로고    scopus 로고
    • Cleavage of human complement component C5 by cysteine proteinases from Porphyromonas (Bacteroides) gingivalis. Prior oxidation of C5 augments proteinase digestion of C5
    • DiScipio RG, Daffern PJ, Kawahara M, Pike R, Travis J, Hugli TE, Potempa J. Cleavage of human complement component C5 by cysteine proteinases from Porphyromonas (Bacteroides) gingivalis. Prior oxidation of C5 augments proteinase digestion of C5. Immunology 1996: 87: 660-667.
    • (1996) Immunology , vol.87 , pp. 660-667
    • DiScipio, R.G.1    Daffern, P.J.2    Kawahara, M.3    Pike, R.4    Travis, J.5    Hugli, T.E.6    Potempa, J.7
  • 70
    • 0004667983 scopus 로고
    • Porphyromonas gingivalis: Presence of a species specific antigen which is distinguished in chronic inflammatory adult periodontal disease
    • Duncan AJ, Carman RJ, Harper FH, Griffiths GS, Curtis MA. Porphyromonas gingivalis: presence of a species specific antigen which is distinguished in chronic inflammatory adult periodontal disease. Microb Ecol Health Dis 1992: 5: 15-20.
    • (1992) Microb Ecol Health Dis , vol.5 , pp. 15-20
    • Duncan, A.J.1    Carman, R.J.2    Harper, F.H.3    Griffiths, G.S.4    Curtis, M.A.5
  • 71
    • 0023884997 scopus 로고
    • The predominant cultivable microbiota of active and inactive lesions of destructive periodontal diseases
    • Dzink JL, Smith C, Socransky SS. The predominant cultivable microbiota of active and inactive lesions of destructive periodontal diseases. J Clin Periodontol 1988: 15: 316-323.
    • (1988) J Clin Periodontol , vol.15 , pp. 316-323
    • Dzink, J.L.1    Smith, C.2    Socransky, S.S.3
  • 73
    • 0026009148 scopus 로고
    • Effects of immunization with Porphyromonas gingivalis and Prevotella intermedia on progression of ligature-induced periodontitis in the nonhuman primate Macaca fascicularis
    • Ebersole JL, Brunsvold M, Steffensen B, Wood R, Holt SC. Effects of immunization with Porphyromonas gingivalis and Prevotella intermedia on progression of ligature-induced periodontitis in the nonhuman primate Macaca fascicularis. Infect Immun 1991: 59: 3351-3359.
    • (1991) Infect Immun , vol.59 , pp. 3351-3359
    • Ebersole, J.L.1    Brunsvold, M.2    Steffensen, B.3    Wood, R.4    Holt, S.C.5
  • 75
    • 0029651856 scopus 로고
    • Bacterial proteases in gingival crevicular fluid before and after periodontal treatment
    • Eley BM, Cox SW. Bacterial proteases in gingival crevicular fluid before and after periodontal treatment. Br Dent J 1995: 178: 133-139.
    • (1995) Br Dent J , vol.178 , pp. 133-139
    • Eley, B.M.1    Cox, S.W.2
  • 76
    • 0026863493 scopus 로고
    • Cathepsin B/L-, elastase-, tryptase-, trypsin- and dipeptidyl peptidase IV-like activities in gingival crevicular fluid: A comparison of levels before and after periodontal surgery in chronic periodontitis patients
    • Eley BM, Cox SW. Cathepsin B/L-, elastase-, tryptase-, trypsin-and dipeptidyl peptidase IV-like activities in gingival crevicular fluid: a comparison of levels before and after periodontal surgery in chronic periodontitis patients. J Periodontol 1992: 63: 412-417.
    • (1992) J Periodontol , vol.63 , pp. 412-417
    • Eley, B.M.1    Cox, S.W.2
  • 77
    • 0030183377 scopus 로고    scopus 로고
    • A 2-year longitudinal study of elastase in human gingival crevicular fluid and periodontal attachment loss
    • Eley BM, Cox SW. A 2-year longitudinal study of elastase in human gingival crevicular fluid and periodontal attachment loss. J Clin Periodontol 1996: 23: 681-692.
    • (1996) J Clin Periodontol , vol.23 , pp. 681-692
    • Eley, B.M.1    Cox, S.W.2
  • 78
    • 0030207881 scopus 로고    scopus 로고
    • The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: A 2-year longitudinal study
    • Eley BM, Cox SW. The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: a 2-year longitudinal study. J Periodontal Res 1996: 31: 381-392.
    • (1996) J Periodontal Res , vol.31 , pp. 381-392
    • Eley, B.M.1    Cox, S.W.2
  • 79
    • 0030183666 scopus 로고    scopus 로고
    • Correlation between gingivain/gingipain and bacterial dipeptidyl peptidase activity in gingival crevicular fluid and periodontal attachment loss in chronic periodontitis patients. A 2-year longitudinal study
    • Eley BM, Cox SW. Correlation between gingivain/gingipain and bacterial dipeptidyl peptidase activity in gingival crevicular fluid and periodontal attachment loss in chronic periodontitis patients. A 2-year longitudinal study. J Periodontol 1996: 67: 703-716.
    • (1996) J Periodontol , vol.67 , pp. 703-716
    • Eley, B.M.1    Cox, S.W.2
  • 80
    • 0028229045 scopus 로고
    • Degradation of endogenous plasma membrane fibronectin concomitant with Treponema denticola 35405 adhesion to gingival fibroblasts
    • Ellen RP, Song M, McCulloch CA. Degradation of endogenous plasma membrane fibronectin concomitant with Treponema denticola 35405 adhesion to gingival fibroblasts. Infect Immun 1994: 62: 3033-3037.
    • (1994) Infect Immun , vol.62 , pp. 3033-3037
    • Ellen, R.P.1    Song, M.2    McCulloch, C.A.3
  • 84
    • 6844239519 scopus 로고    scopus 로고
    • Alpha-1-antrypsin phenotyping in ANCA-associated diseases: One of several arguments for protease/antiprotease imbalance in systemic vasculitis
    • Esnault VLM, Audrain MAP, Sesboue R. Alpha-1-antrypsin phenotyping in ANCA-associated diseases: one of several arguments for protease/antiprotease imbalance in systemic vasculitis. Exp Clin Immunogenet 1997: 14: 206-213.
    • (1997) Exp Clin Immunogenet , vol.14 , pp. 206-213
    • Esnault, V.L.M.1    Audrain, M.A.P.2    Sesboue, R.3
  • 85
    • 0026437024 scopus 로고
    • Temperature differences at periodontal sites in health and disease
    • Fedi PF Jr, Killoy WJ. Temperature differences at periodontal sites in health and disease. J Periodontol 1992: 63: 24-27.
    • (1992) J Periodontol , vol.63 , pp. 24-27
    • Fedi Jr., P.F.1    Killoy, W.J.2
  • 86
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
    • Fenno JC, Hannam PM, Leung WK, Tamura M, Uitto VJ, McBride BC. Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect Immun 1998: 66: 1869-1877.
    • (1998) Infect Immun , vol.66 , pp. 1869-1877
    • Fenno, J.C.1    Hannam, P.M.2    Leung, W.K.3    Tamura, M.4    Uitto, V.J.5    McBride, B.C.6
  • 87
    • 0028037802 scopus 로고
    • Cloning and characterization of a new protease gene (prtH) from Porphyromonas gingivalis
    • Fletcher HM, Schenkein HA, Macrina FL. Cloning and characterization of a new protease gene (prtH) from Porphyromonas gingivalis. Infect Immun 1994: 62: 4279-4286.
    • (1994) Infect Immun , vol.62 , pp. 4279-4286
    • Fletcher, H.M.1    Schenkein, H.A.2    Macrina, F.L.3
  • 91
    • 0029379771 scopus 로고
    • In vivo cleavage of immunoglobulin A1 by immunoglobulin A1 proteases from Prevotella and Capnocytophaga species
    • Frandsen EV, Reinholdt J, Kjeldsen M, Kilian M. In vivo cleavage of immunoglobulin A1 by immunoglobulin A1 proteases from Prevotella and Capnocytophaga species. Oral Microbiol Immunol 1995: 10: 291-296.
    • (1995) Oral Microbiol Immunol , vol.10 , pp. 291-296
    • Frandsen, E.V.1    Reinholdt, J.2    Kjeldsen, M.3    Kilian, M.4
  • 93
    • 0023114575 scopus 로고
    • Isolation and characterization of a protease from Bacteroides gingivalis
    • Fujimura S, Nakamura T. Isolation and characterization of a protease from Bacteroides gingivalis. Infect Immun 1987: 55: 716-720.
    • (1987) Infect Immun , vol.55 , pp. 716-720
    • Fujimura, S.1    Nakamura, T.2
  • 94
    • 0025582585 scopus 로고
    • Purification and characterization of a 43-kDa protease of Bacteroides gingivalis
    • Fujimura S, Nakamura T. Purification and characterization of a 43-kDa protease of Bacteroides gingivalis. Oral Microbiol Immunol 1990: 5: 360-362.
    • (1990) Oral Microbiol Immunol , vol.5 , pp. 360-362
    • Fujimura, S.1    Nakamura, T.2
  • 95
    • 0026903380 scopus 로고
    • Comparative studies of three proteases of Porphyromonas gingivalis
    • Fujimura S, Shibata Y, Nakamura T. Comparative studies of three proteases of Porphyromonas gingivalis. Oral Microbiol Immunol 1992: 7: 212-217.
    • (1992) Oral Microbiol Immunol , vol.7 , pp. 212-217
    • Fujimura, S.1    Shibata, Y.2    Nakamura, T.3
  • 96
    • 0027428951 scopus 로고
    • Purification and partial characterization of a lysine-specific protease of Porphyromonas gingivalis
    • Fujimura S, Shibata Y, Nakamura T. Purification and partial characterization of a lysine-specific protease of Porphyromonas gingivalis. FEMS Microbiol Lett 1993: 113: 133-137.
    • (1993) FEMS Microbiol Lett , vol.113 , pp. 133-137
    • Fujimura, S.1    Shibata, Y.2    Nakamura, T.3
  • 97
    • 0032526398 scopus 로고    scopus 로고
    • Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis
    • Fujimura S, Hirai K, Shibata Y, Nakayama K, Nakamura T. Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis. FEMS Microbiol Lett 1998: 163: 173-179.
    • (1998) FEMS Microbiol Lett , vol.163 , pp. 173-179
    • Fujimura, S.1    Hirai, K.2    Shibata, Y.3    Nakayama, K.4    Nakamura, T.5
  • 98
    • 0025169073 scopus 로고
    • Identification of polymorphonuclear leukocyte collagenase and gelatinase activities in mouthrinse samples: Correlation with periodontal disease activity in adult and juvenile periodontitis
    • Gangbar S, Overall CM, McCulloch CA, Sodek J. Identification of polymorphonuclear leukocyte collagenase and gelatinase activities in mouthrinse samples: correlation with periodontal disease activity in adult and juvenile periodontitis. J Periodontal Res 1990: 25: 257-267.
    • (1990) J Periodontal Res , vol.25 , pp. 257-267
    • Gangbar, S.1    Overall, C.M.2    McCulloch, C.A.3    Sodek, J.4
  • 99
    • 0029347121 scopus 로고
    • Comparison of host tissue and bacterial dipeptidyl peptidases in human gingival crevicular fluid by analytical isoelectric focusing
    • Gazi MI, Cox SW, Clark DT, Eley BM. Comparison of host tissue and bacterial dipeptidyl peptidases in human gingival crevicular fluid by analytical isoelectric focusing. Arch Oral Biol 1995: 40: 731-736.
    • (1995) Arch Oral Biol , vol.40 , pp. 731-736
    • Gazi, M.I.1    Cox, S.W.2    Clark, D.T.3    Eley, B.M.4
  • 100
    • 0028089643 scopus 로고
    • Adhesion molecule expression in chronic inflammatory periodontal disease tissue
    • Gemmell E, Walsh LJ, Savage NW, Seymour GJ. Adhesion molecule expression in chronic inflammatory periodontal disease tissue. J Periodontal Res 1994: 29: 46-53.
    • (1994) J Periodontal Res , vol.29 , pp. 46-53
    • Gemmell, E.1    Walsh, L.J.2    Savage, N.W.3    Seymour, G.J.4
  • 101
    • 0031152114 scopus 로고    scopus 로고
    • Cytokines and prostaglandins in immune homeostasis and tissue destruction in periodontal disease
    • Gemmell E, Marshall RI, Seymour GJ. Cytokines and prostaglandins in immune homeostasis and tissue destruction in periodontal disease. Periodontol 2000 1997: 14: 112-143.
    • (1997) Periodontol 2000 , vol.14 , pp. 112-143
    • Gemmell, E.1    Marshall, R.I.2    Seymour, G.J.3
  • 102
    • 0032176728 scopus 로고    scopus 로고
    • Cytokine profiles of lesional and splenic T cells in Porphyromonas gingivalis infection in a murine model
    • Gemmell E, Winning TA, Bird PS, Seymour GJ. Cytokine profiles of lesional and splenic T cells in Porphyromonas gingivalis infection in a murine model. J Periodontol 1998: 69: 1131-1138.
    • (1998) J Periodontol , vol.69 , pp. 1131-1138
    • Gemmell, E.1    Winning, T.A.2    Bird, P.S.3    Seymour, G.J.4
  • 103
    • 0028980295 scopus 로고
    • Characterization of a Tn4351-generated hemin uptake mutant of Porphyromonas gingivalis: Evidence for the coordinate regulation of virulence factors by hemin
    • Genco CA, Simpson W, Forng RY, Egal M, Odusanya BM. Characterization of a Tn4351-generated hemin uptake mutant of Porphyromonas gingivalis: evidence for the coordinate regulation of virulence factors by hemin. Infect Immun 1995: 63: 2459-2466.
    • (1995) Infect Immun , vol.63 , pp. 2459-2466
    • Genco, C.A.1    Simpson, W.2    Forng, R.Y.3    Egal, M.4    Odusanya, B.M.5
  • 104
    • 0031690172 scopus 로고    scopus 로고
    • A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice
    • Genco CA, Odusanya BM, Mikolajczyk-Pawlinska J, Potempa J, Travis J. A peptide domain on gingipain R which confers immunity against Porphyromonas gingivalis infection in mice. Infect Immun 1998: 66: 4108-4114.
    • (1998) Infect Immun , vol.66 , pp. 4108-4114
    • Genco, C.A.1    Odusanya, B.M.2    Mikolajczyk-Pawlinska, J.3    Potempa, J.4    Travis, J.5
  • 105
    • 0033014560 scopus 로고    scopus 로고
    • Role of gingipains R in the pathogenesis of Porphyromonas gingivalis-mcdiated periodontal disease
    • Genco CA, Potempa J, Mikolajczyk-Pawlinska J, Travis J. Role of gingipains R in the pathogenesis of Porphyromonas gingivalis-mcdiated periodontal disease. Clin Infect Dis 1999: 28: 456-463.
    • (1999) Clin Infect Dis , vol.28 , pp. 456-463
    • Genco, C.A.1    Potempa, J.2    Mikolajczyk-Pawlinska, J.3    Travis, J.4
  • 106
    • 0005483377 scopus 로고
    • Degradation of collagenous substrates by Bacteroides melaninogenicus
    • Gibbons RJ, MacDonald JB. Degradation of collagenous substrates by Bacteroides melaninogenicus. J Bacteriol 1961: 81: 614-621.
    • (1961) J Bacteriol , vol.81 , pp. 614-621
    • Gibbons, R.J.1    MacDonald, J.B.2
  • 108
    • 0028658357 scopus 로고
    • A non-antimicrobial tetracycline inhibits gingival matrix metalloproteinases and bone loss in Porphyromonas gingivalis-induced periodontitis in rats
    • Golub LM, Evans RT, McNamara TF, Lee HM, Ramamurthy NS. A non-antimicrobial tetracycline inhibits gingival matrix metalloproteinases and bone loss in Porphyromonas gingivalis-induced periodontitis in rats. Ann N Y Acad Sci 1994: 732: 96-111.
    • (1994) Ann N Y Acad Sci , vol.732 , pp. 96-111
    • Golub, L.M.1    Evans, R.T.2    McNamara, T.F.3    Lee, H.M.4    Ramamurthy, N.S.5
  • 110
    • 0030862107 scopus 로고    scopus 로고
    • A matrix metalloproteinase inhibitor reduces bone-type collagen degradation fragments and specific collagenases in gingival crevicular fluid during adult periodontitis
    • Golub LM, Lee HM, Greenwald RA, Ryan ME, Sorsa T, Salo T, Giannobile WV. A matrix metalloproteinase inhibitor reduces bone-type collagen degradation fragments and specific collagenases in gingival crevicular fluid during adult periodontitis. Inflamm Res 1997: 46: 310-319.
    • (1997) Inflamm Res , vol.46 , pp. 310-319
    • Golub, L.M.1    Lee, H.M.2    Greenwald, R.A.3    Ryan, M.E.4    Sorsa, T.5    Salo, T.6    Giannobile, W.V.7
  • 111
    • 0032200444 scopus 로고    scopus 로고
    • Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms
    • Golub LM, Lee HM, Ryan ME, Giannobile WV, Payne J, Sorsa T. Tetracyclines inhibit connective tissue breakdown by multiple non-antimicrobial mechanisms. Adv Dent Res 1998: 12: 12-26.
    • (1998) Adv Dent Res , vol.12 , pp. 12-26
    • Golub, L.M.1    Lee, H.M.2    Ryan, M.E.3    Giannobile, W.V.4    Payne, J.5    Sorsa, T.6
  • 112
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: Properties and functions
    • Gonzales T, Robert-Baudouy J. Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev 1996: 18: 319-344.
    • (1996) FEMS Microbiol Rev , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 114
    • 0032974306 scopus 로고    scopus 로고
    • The potential role of chemokines and inflammatory cytokines in periodontal disease progression
    • Graves DT. The potential role of chemokines and inflammatory cytokines in periodontal disease progression. Clin Infect Dis 1999: 28: 482-490.
    • (1999) Clin Infect Dis , vol.28 , pp. 482-490
    • Graves, D.T.1
  • 115
    • 0021668366 scopus 로고
    • The role of bleeding upon probing in the diagnosis of periodontal disease. A literature review
    • Greenstein G. The role of bleeding upon probing in the diagnosis of periodontal disease. A literature review. J Periodontol 1984: 55: 684-688.
    • (1984) J Periodontol , vol.55 , pp. 684-688
    • Greenstein, G.1
  • 116
    • 0346503532 scopus 로고
    • Effect of protease inhibitors on in vitro growth of Porphyromonas gingivalis
    • Grenier D. Effect of protease inhibitors on in vitro growth of Porphyromonas gingivalis. Microb Ecol Health Dis 1992: 5: 133-138.
    • (1992) Microb Ecol Health Dis , vol.5 , pp. 133-138
    • Grenier, D.1
  • 117
    • 0027103765 scopus 로고
    • Further evidence for a possible role of trypsin-like activity in the adherence of Porphyromonas gingivalis
    • Grenier D. Further evidence for a possible role of trypsin-like activity in the adherence of Porphyromonas gingivalis. Can J Microbiol 1992: 38: 1189-1192.
    • (1992) Can J Microbiol , vol.38 , pp. 1189-1192
    • Grenier, D.1
  • 118
    • 0026724045 scopus 로고
    • Inactivation of human serum bactericidal activity by a trypsinlike protease isolated from Porphyromonas gingivalis
    • Grenier D. Inactivation of human serum bactericidal activity by a trypsinlike protease isolated from Porphyromonas gingivalis. Infect Immun 1992: 60: 1854-1857.
    • (1992) Infect Immun , vol.60 , pp. 1854-1857
    • Grenier, D.1
  • 119
    • 0029059892 scopus 로고
    • Characterization of the trypsin like activity of Bacteroides forsythus
    • Grenier D. Characterization of the trypsin like activity of Bacteroides forsythus. Microbiology 1995: 141: 921-926.
    • (1995) Microbiology , vol.141 , pp. 921-926
    • Grenier, D.1
  • 120
    • 0025822913 scopus 로고
    • Protective effect of Porphyromonas gingivalis outer membrane vesicles against bactericidal activity of human serum
    • Grenier D, Belanger M. Protective effect of Porphyromonas gingivalis outer membrane vesicles against bactericidal activity of human serum. Infect Immun 1991: 59: 3004-3008.
    • (1991) Infect Immun , vol.59 , pp. 3004-3008
    • Grenier, D.1    Belanger, M.2
  • 121
    • 0023470650 scopus 로고
    • Isolation of a membrane-associated Bacteroides gingivalis glycylprolyl protease
    • Grenier D, McBride BC. Isolation of a membrane-associated Bacteroides gingivalis glycylprolyl protease. Infect Immun 1987: 55: 3131-3136.
    • (1987) Infect Immun , vol.55 , pp. 3131-3136
    • Grenier, D.1    McBride, B.C.2
  • 122
    • 0024466217 scopus 로고
    • Surface location of a Bacteroides gingivalis glycylprolyl protease
    • Grenier D, McBride BC. Surface location of a Bacteroides gingivalis glycylprolyl protease. Infect Immun 1989: 57: 3265-3269.
    • (1989) Infect Immun , vol.57 , pp. 3265-3269
    • Grenier, D.1    McBride, B.C.2
  • 123
    • 0027942032 scopus 로고
    • Selective growth inhibition of Porphyromonas gingivalis by bestatin
    • Grenier D, Michaud J. Selective growth inhibition of Porphyromonas gingivalis by bestatin. FEMS Microbiol Lett 1994: 123: 193-200.
    • (1994) FEMS Microbiol Lett , vol.123 , pp. 193-200
    • Grenier, D.1    Michaud, J.2
  • 124
    • 0025117758 scopus 로고
    • Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane
    • Grenier D, Uitto VJ, McBride BC. Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane. Infect Immun 1990: 58: 347-351.
    • (1990) Infect Immun , vol.58 , pp. 347-351
    • Grenier, D.1    Uitto, V.J.2    McBride, B.C.3
  • 125
    • 0019955823 scopus 로고
    • Protein C, an antithrombotic protein, is reduced in hospitalized patients with intravascular coagulation
    • Griffin JH, Mosher DF, Zimmerman TS, Kleiss AJ. Protein C, an antithrombotic protein, is reduced in hospitalized patients with intravascular coagulation. Blood 1982: 60: 261-264.
    • (1982) Blood , vol.60 , pp. 261-264
    • Griffin, J.H.1    Mosher, D.F.2    Zimmerman, T.S.3    Kleiss, A.J.4
  • 126
    • 0003054849 scopus 로고    scopus 로고
    • The potential role of alpha 2-macroglobulin in the control of cysteine proteinases (gingipains) from Porphyromonas gingivalis
    • Gron H, Pike R, Potempa J, Travis J, Thogersen IB, Enghild JJ, Pizzo SV. The potential role of alpha 2-macroglobulin in the control of cysteine proteinases (gingipains) from Porphyromonas gingivalis. J Periodontal Res 1997: 32: 61-68.
    • (1997) J Periodontal Res , vol.32 , pp. 61-68
    • Gron, H.1    Pike, R.2    Potempa, J.3    Travis, J.4    Thogersen, I.B.5    Enghild, J.J.6    Pizzo, S.V.7
  • 127
    • 0026926990 scopus 로고
    • Granulocyte elastase in gingival crevicular fluid. A possible discriminator between gingivitis and periodontitis
    • Gustafsson A, Asman B, Bergstrom K, Soder PO. Granulocyte elastase in gingival crevicular fluid. A possible discriminator between gingivitis and periodontitis. J Clin Periodontol 1992: 19: 535-540.
    • (1992) J Clin Periodontol , vol.19 , pp. 535-540
    • Gustafsson, A.1    Asman, B.2    Bergstrom, K.3    Soder, P.O.4
  • 128
    • 0029819454 scopus 로고    scopus 로고
    • The hemagglutinin gene A (hagA) of Porphyromonas gingivalis 381 contains four large, contiguous, direct repeats
    • Han N, Whitlock J, Progulske-Fox A. The hemagglutinin gene A (hagA) of Porphyromonas gingivalis 381 contains four large, contiguous, direct repeats. Infect Immun 1996: 64: 4000-4007.
    • (1996) Infect Immun , vol.64 , pp. 4000-4007
    • Han, N.1    Whitlock, J.2    Progulske-Fox, A.3
  • 129
    • 0031751890 scopus 로고    scopus 로고
    • The Porphyromonas gingivalis prtP/kgp homologue exists as two open reading frames in strain 381
    • Han N, Lepine G, Whitlock J, Wojciechowski L, Progulske-Fox A. The Porphyromonas gingivalis prtP/kgp homologue exists as two open reading frames in strain 381. Oral Dis 1998: 4: 170-179.
    • (1998) Oral Dis , vol.4 , pp. 170-179
    • Han, N.1    Lepine, G.2    Whitlock, J.3    Wojciechowski, L.4    Progulske-Fox, A.5
  • 130
    • 0029991619 scopus 로고    scopus 로고
    • Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease
    • Harrington DJ. Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease. Infect Immun 1996: 64: 1885-1891.
    • (1996) Infect Immun , vol.64 , pp. 1885-1891
    • Harrington, D.J.1
  • 131
    • 0028432024 scopus 로고
    • Neutrophil defects as risk factors for periodontal diseases
    • Hart TC, Shapira L, Van Dyke TE. Neutrophil defects as risk factors for periodontal diseases. J Periodontol 1994: 65: 521-529.
    • (1994) J Periodontol , vol.65 , pp. 521-529
    • Hart, T.C.1    Shapira, L.2    Van Dyke, T.E.3
  • 133
    • 0026903581 scopus 로고
    • Survey of a receptor protein in human erythrocytes for hemagglutinin of Porphyromonas gingivalis
    • Hayashi H, Nagata A, Hinode D, Sato M, Nakamura R. Survey of a receptor protein in human erythrocytes for hemagglutinin of Porphyromonas gingivalis. Oral Microbiol Immunol 1992: 7: 204-211.
    • (1992) Oral Microbiol Immunol , vol.7 , pp. 204-211
    • Hayashi, H.1    Nagata, A.2    Hinode, D.3    Sato, M.4    Nakamura, R.5
  • 134
    • 0031068831 scopus 로고    scopus 로고
    • Detection of neutral protease (Periocheck) and BANA hydrolase (Perioscan) compared with traditional clinical methods of diagnosis and monitoring of chronic inflammatory periodontal disease
    • Hemmings KW, Griffiths GS, Bulman JS. Detection of neutral protease (Periocheck) and BANA hydrolase (Perioscan) compared with traditional clinical methods of diagnosis and monitoring of chronic inflammatory periodontal disease. J Clin Periodontol 1997: 24: 110-114.
    • (1997) J Clin Periodontol , vol.24 , pp. 110-114
    • Hemmings, K.W.1    Griffiths, G.S.2    Bulman, J.S.3
  • 135
    • 0031107876 scopus 로고    scopus 로고
    • Host-pathogen interactions in bacterial endocarditis: Streptococcal virulence in the host
    • Herzberg MC, Meyer MW, Kilic A, Tao L. Host-pathogen interactions in bacterial endocarditis: streptococcal virulence in the host. Adv Dent Res 1997: 11: 69-74.
    • (1997) Adv Dent Res , vol.11 , pp. 69-74
    • Herzberg, M.C.1    Meyer, M.W.2    Kilic, A.3    Tao, L.4
  • 136
    • 0025785877 scopus 로고
    • Purification and characterization of three types of proteases from culture supernatants of Porphyromonas gingivalis
    • Hinode D, Hayashi H, Nakamura R. Purification and characterization of three types of proteases from culture supernatants of Porphyromonas gingivalis. Infect Immun 1991: 59: 3060-3068.
    • (1991) Infect Immun , vol.59 , pp. 3060-3068
    • Hinode, D.1    Hayashi, H.2    Nakamura, R.3
  • 137
    • 0026941459 scopus 로고
    • Generation of plasma kinin by three types of protease isolated from Porphyromonas gingivalis 381
    • Hinode D, Nagata A, Ichimiya S, Hayashi H, Morioka M, Nakamura R. Generation of plasma kinin by three types of protease isolated from Porphyromonas gingivalis 381. Arch Oral Biol 1992: 37: 859-861.
    • (1992) Arch Oral Biol , vol.37 , pp. 859-861
    • Hinode, D.1    Nagata, A.2    Ichimiya, S.3    Hayashi, H.4    Morioka, M.5    Nakamura, R.6
  • 138
    • 0030087871 scopus 로고    scopus 로고
    • Biological and antigenic characterization of three BApNA-hydrolyzing proteases from the culture supernatant of Porphyromonas gingivalis
    • Hinode D, Masuda K, Yoshioka M, Hayashi H, Nakamura R, Grenier D, Mayrand D. Biological and antigenic characterization of three BApNA-hydrolyzing proteases from the culture supernatant of Porphyromonas gingivalis. Oral Microbiol Immunol 1996: 11: 8-14.
    • (1996) Oral Microbiol Immunol , vol.11 , pp. 8-14
    • Hinode, D.1    Masuda, K.2    Yoshioka, M.3    Hayashi, H.4    Nakamura, R.5    Grenier, D.6    Mayrand, D.7
  • 140
    • 0032962004 scopus 로고    scopus 로고
    • Activation of protein C by arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis
    • Hosotaki K, Imamura T, Potempa J, Kitamura N, Travis J. Activation of protein C by arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis. Biol Chem 1999: 380: 75-80.
    • (1999) Biol Chem , vol.380 , pp. 75-80
    • Hosotaki, K.1    Imamura, T.2    Potempa, J.3    Kitamura, N.4    Travis, J.5
  • 141
    • 0026619011 scopus 로고
    • Correlation of hemagglutination activity with trypsin-like protease activity of Porphyromonas gingivalis
    • Hoover CI, Ng CY, Felton JR. Correlation of hemagglutination activity with trypsin-like protease activity of Porphyromonas gingivalis. Arch Oral Biol 1992: 37: 515-520.
    • (1992) Arch Oral Biol , vol.37 , pp. 515-520
    • Hoover, C.I.1    Ng, C.Y.2    Felton, J.R.3
  • 143
    • 0029887074 scopus 로고    scopus 로고
    • Cathepsin B in gingival crevicular fluid of adult periodontitis patients: Identification by immunological and enzymological methods
    • Ichimaru E, Tanoue M, Tani M, Tani Y, Kaneko T, Iwasaki Y, Kunimatsu K, Kato I. Cathepsin B in gingival crevicular fluid of adult periodontitis patients: identification by immunological and enzymological methods. Inflamm Res 1996: 45: 277-282.
    • (1996) Inflamm Res , vol.45 , pp. 277-282
    • Ichimaru, E.1    Tanoue, M.2    Tani, M.3    Tani, Y.4    Kaneko, T.5    Iwasaki, Y.6    Kunimatsu, K.7    Kato, I.8
  • 144
    • 0028242731 scopus 로고
    • Pathogenesis of periodontitis: A major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway
    • Imamura T, Pike RN, Potempa J, Travis J. Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway. J Clin Invest 1994: 94: 361-367.
    • (1994) J Clin Invest , vol.94 , pp. 361-367
    • Imamura, T.1    Pike, R.N.2    Potempa, J.3    Travis, J.4
  • 145
    • 0028909491 scopus 로고
    • Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis
    • Imamura T, Potempa J, Pike RN, Travis J. Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis. Infect Immun 1995: 63: 1999-2003.
    • (1995) Infect Immun , vol.63 , pp. 1999-2003
    • Imamura, T.1    Potempa, J.2    Pike, R.N.3    Travis, J.4
  • 146
    • 0028818827 scopus 로고
    • Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation: Implications for bleeding tendency at periodontitis sites
    • Imamura T, Potempa J, Pike RN, Moore JN, Barton MH, Travis J. Effect of free and vesicle-bound cysteine proteinases of Porphyromonas gingivalis on plasma clot formation: implications for bleeding tendency at periodontitis sites. Infect Immun 1995: 63: 4877-4882.
    • (1995) Infect Immun , vol.63 , pp. 4877-4882
    • Imamura, T.1    Potempa, J.2    Pike, R.N.3    Moore, J.N.4    Barton, M.H.5    Travis, J.6
  • 147
    • 0030941836 scopus 로고    scopus 로고
    • Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis
    • Imamura T, Potempa J, Tanase S, Travis J. Activation of blood coagulation factor X by arginine-specific cysteine proteinases (gingipain-Rs) from Porphyromonas gingivalis. J Biol Chem 1997: 272: 16062-16067.
    • (1997) J Biol Chem , vol.272 , pp. 16062-16067
    • Imamura, T.1    Potempa, J.2    Tanase, S.3    Travis, J.4
  • 149
    • 0029833178 scopus 로고    scopus 로고
    • Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylalanine-specific protease (dentilisin)
    • Ishihara K, Miura T, Kuramitsu HK, Okuda K. Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylalanine-specific protease (dentilisin). Infect Immun 1996: 64: 5178-5186.
    • (1996) Infect Immun , vol.64 , pp. 5178-5186
    • Ishihara, K.1    Miura, T.2    Kuramitsu, H.K.3    Okuda, K.4
  • 150
    • 0030004180 scopus 로고    scopus 로고
    • Proteolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis
    • Jagels MA, Travis J, Potempa J, Pike R, Hugli TE. Proteolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis. Infect Immun 1996: 64: 1984-1991.
    • (1996) Infect Immun , vol.64 , pp. 1984-1991
    • Jagels, M.A.1    Travis, J.2    Potempa, J.3    Pike, R.4    Hugli, T.E.5
  • 151
    • 0030344904 scopus 로고    scopus 로고
    • Cleavage of the human C5A receptor by proteinases derived from Porphyromonas gingivalis: Cleavage of leukocyte C5a receptor
    • Jagels MA, Ember JA, Travis J, Potempa J, Pike R, Hugli TE. Cleavage of the human C5A receptor by proteinases derived from Porphyromonas gingivalis: cleavage of leukocyte C5a receptor. Adv Exp Med Biol 1996: 389: 155-164.
    • (1996) Adv Exp Med Biol , vol.389 , pp. 155-164
    • Jagels, M.A.1    Ember, J.A.2    Travis, J.3    Potempa, J.4    Pike, R.5    Hugli, T.E.6
  • 152
    • 0023984742 scopus 로고
    • The antigenic index: A novel algorithm for predicting antigenic determinants
    • Jameson BA, Wolf H. The antigenic index: a novel algorithm for predicting antigenic determinants. Comput Appl Biosci 1988: 4: 181-186.
    • (1988) Comput Appl Biosci , vol.4 , pp. 181-186
    • Jameson, B.A.1    Wolf, H.2
  • 153
    • 0029311217 scopus 로고
    • Characterization of immunoglobulin G-degrading proteases of Prevotella intermedia and Prevotella nigrescens
    • Jansen HJ, Grenier D, Van der Hoeven JS. Characterization of immunoglobulin G-degrading proteases of Prevotella intermedia and Prevotella nigrescens. Oral Microbiol Immunol 1995: 10: 138-145.
    • (1995) Oral Microbiol Immunol , vol.10 , pp. 138-145
    • Jansen, H.J.1    Grenier, D.2    Van Der Hoeven, J.S.3
  • 154
    • 9044220226 scopus 로고    scopus 로고
    • C5a peptidase alters clearance and trafficking of group A streptococci by infected mice
    • Ji Y, McLandsborough L, Kondagunta A, Cleary PP. C5a peptidase alters clearance and trafficking of group A streptococci by infected mice. Infect Immun 1996: 64: 503-510.
    • (1996) Infect Immun , vol.64 , pp. 503-510
    • Ji, Y.1    McLandsborough, L.2    Kondagunta, A.3    Cleary, P.P.4
  • 155
    • 85005586861 scopus 로고
    • Variations in crevicular fluid elastase levels in periodontitis patients on long-term maintenance
    • Jin LJ, Soder PO, Asman B, Soder B, Puriene A, Bergstrom K. Variations in crevicular fluid elastase levels in periodontitis patients on long-term maintenance. Eur J Oral Sci 1995: 103: 84-89.
    • (1995) Eur J Oral Sci , vol.103 , pp. 84-89
    • Jin, L.J.1    Soder, P.O.2    Asman, B.3    Soder, B.4    Puriene, A.5    Bergstrom, K.6
  • 156
    • 0025133268 scopus 로고
    • Thrombin and factor Xa enhance the production of interleukin-1
    • Jones A, Geczy CL. Thrombin and factor Xa enhance the production of interleukin-1. Immunology 1990: 71: 236-241.
    • (1990) Immunology , vol.71 , pp. 236-241
    • Jones, A.1    Geczy, C.L.2
  • 157
    • 0024340631 scopus 로고
    • Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction
    • Jordan RE, Nelson RM, Kilpatrick J, Newgren JO, Esmon PC, Fournel MA. Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction. J Biol Chem 1989: 264: 10493-10500.
    • (1989) J Biol Chem , vol.264 , pp. 10493-10500
    • Jordan, R.E.1    Nelson, R.M.2    Kilpatrick, J.3    Newgren, J.O.4    Esmon, P.C.5    Fournel, M.A.6
  • 159
    • 0027965730 scopus 로고
    • Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis
    • Kadowaki T, Yoneda M, Okamoto K, Maeda K, Yamamoto K. Purification and characterization of a novel arginine-specific cysteine proteinase (argingipain) involved in the pathogenesis of periodontal disease from the culture supernatant of Porphyromonas gingivalis. J Biol Chem 1994: 269: 21371-21378.
    • (1994) J Biol Chem , vol.269 , pp. 21371-21378
    • Kadowaki, T.1    Yoneda, M.2    Okamoto, K.3    Maeda, K.4    Yamamoto, K.5
  • 160
    • 0032582491 scopus 로고    scopus 로고
    • Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis
    • Kadowaki T, Nakayama K, Yoshimura F, Okamoto K, Abe N, Yamamoto K. Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. J Biol Chem 1998: 273: 29072-29076.
    • (1998) J Biol Chem , vol.273 , pp. 29072-29076
    • Kadowaki, T.1    Nakayama, K.2    Yoshimura, F.3    Okamoto, K.4    Abe, N.5    Yamamoto, K.6
  • 161
    • 0030731603 scopus 로고    scopus 로고
    • The relationship between colonization and hemagglutination inhibiting and B cell epitopes of Porphyromonas gingivalis
    • Kelly CG, Booth V, Kendal H, Slaney JM, Curtis MA, Lehner T. The relationship between colonization and hemagglutination inhibiting and B cell epitopes of Porphyromonas gingivalis. Clin Exp Immunol 1997: 110: 285-291.
    • (1997) Clin Exp Immunol , vol.110 , pp. 285-291
    • Kelly, C.G.1    Booth, V.2    Kendal, H.3    Slaney, J.M.4    Curtis, M.A.5    Lehner, T.6
  • 163
    • 0023201944 scopus 로고
    • The coagulation-kinin pathway of human plasma
    • Kaplan AP, Silverberg M. The coagulation-kinin pathway of human plasma. Blood 1987: 70: 1-15.
    • (1987) Blood , vol.70 , pp. 1-15
    • Kaplan, A.P.1    Silverberg, M.2
  • 164
    • 0026772150 scopus 로고
    • Sequence analysis and characterization of the Porphyromonas gingivalis prtC gene, which expresses a novel collagenase activity
    • Kato T, Takahashi N, Kuramitsu HK. Sequence analysis and characterization of the Porphyromonas gingivalis prtC gene, which expresses a novel collagenase activity. J Bacteriol 1992: 174: 3889-3895.
    • (1992) J Bacteriol , vol.174 , pp. 3889-3895
    • Kato, T.1    Takahashi, N.2    Kuramitsu, H.K.3
  • 165
    • 0024526704 scopus 로고
    • Glycylprolyl dipeptidase activity of Bacteroides gingivalis W50 and the avirulent variant W50/BEI
    • Kay HM, Birss AJ, Smalley JW. Glycylprolyl dipeptidase activity of Bacteroides gingivalis W50 and the avirulent variant W50/BEI. FEMS Microbiol Lett 1989: 48: 93-96.
    • (1989) FEMS Microbiol Lett , vol.48 , pp. 93-96
    • Kay, H.M.1    Birss, A.J.2    Smalley, J.W.3
  • 166
    • 0027669534 scopus 로고
    • Comparative histochemical and biochemical studies of mast cell tryptase in human gingiva
    • Kennett CN, Cox SW, Eley BM, Osman IA. Comparative histochemical and biochemical studies of mast cell tryptase in human gingiva. J Periodontol 1993: 64: 870-877.
    • (1993) J Periodontol , vol.64 , pp. 870-877
    • Kennett, C.N.1    Cox, S.W.2    Eley, B.M.3    Osman, I.A.4
  • 167
    • 0029936655 scopus 로고    scopus 로고
    • Trypsin-like protease activity of Porphyromonas gingivalis as a potential virulence factor in a murine lesion model
    • Kesavalu L, Holt SC, Ebersole JL. Trypsin-like protease activity of Porphyromonas gingivalis as a potential virulence factor in a murine lesion model. Microb Pathog 1996: 20: 1-10.
    • (1996) Microb Pathog , vol.20 , pp. 1-10
    • Kesavalu, L.1    Holt, S.C.2    Ebersole, J.L.3
  • 168
    • 0032404139 scopus 로고    scopus 로고
    • Virulence of a polymicrobic complex, Treponema denticola and Porphyromonas gingivalis, in a murine model
    • Kesavalu L, Holt SC, Ebersole JL. Virulence of a polymicrobic complex, Treponema denticola and Porphyromonas gingivalis, in a murine model. Oral Microbiol Immunol 1998: 13: 373-377.
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 373-377
    • Kesavalu, L.1    Holt, S.C.2    Ebersole, J.L.3
  • 169
    • 0030200413 scopus 로고    scopus 로고
    • Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis
    • Kim SJ, Chu L, Holt SC. Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis. Microb Pathog 1996: 21: 65-70.
    • (1996) Microb Pathog , vol.21 , pp. 65-70
    • Kim, S.J.1    Chu, L.2    Holt, S.C.3
  • 170
    • 0026006804 scopus 로고
    • Tissue plasminogen activator and placental plasminogen activator inhibitor in human gingival fluid
    • Kinnby B, Lecander G, Martinsson B, Astedt B. Tissue plasminogen activator and placental plasminogen activator inhibitor in human gingival fluid. Fibrinolysis 1991: 5: 235-242.
    • (1991) Fibrinolysis , vol.5 , pp. 235-242
    • Kinnby, B.1    Lecander, G.2    Martinsson, B.3    Astedt, B.4
  • 171
    • 85005426291 scopus 로고
    • The plasminogen-activating system in gingival fluid from adults. An intra-individual study before and after treatment of gingivitis
    • Kinnby B, Matsson L, Lecander I. The plasminogen-activating system in gingival fluid from adults. An intra-individual study before and after treatment of gingivitis. Scand J Dent Res 1994: 102: 334-341.
    • (1994) Scand J Dent Res , vol.102 , pp. 334-341
    • Kinnby, B.1    Matsson, L.2    Lecander, I.3
  • 173
    • 0027691090 scopus 로고
    • Marginal periodontitis and cytokines: A review of the literature
    • Kjeldsen M, Holmstrup P, Bendtzen K. Marginal periodontitis and cytokines: a review of the literature. J Periodontol 1993: 64: 1013-1022.
    • (1993) J Periodontol , vol.64 , pp. 1013-1022
    • Kjeldsen, M.1    Holmstrup, P.2    Bendtzen, K.3
  • 174
    • 0030813996 scopus 로고    scopus 로고
    • The proteinase-antiproteinase theory of emphysema: A speculative analysis of recent advances into the pathogenesis of emphysema
    • Knight KR, Burdon JG, Cook L, Brenton S, Ayad M, Janus ED. The proteinase-antiproteinase theory of emphysema: a speculative analysis of recent advances into the pathogenesis of emphysema. Respirology 1997: 2: 91-95.
    • (1997) Respirology , vol.2 , pp. 91-95
    • Knight, K.R.1    Burdon, J.G.2    Cook, L.3    Brenton, S.4    Ayad, M.5    Janus, E.D.6
  • 175
    • 0030020420 scopus 로고    scopus 로고
    • Cysteine protease of Porphyromonas gingivalis 381 enhances binding of fimbriae to cultured human fibroblasts and matrix proteins
    • Kontani M, Ono H, Shibata H, Okamura Y, Tanaka T, Fujiwara T, Kimura S, Hamada S. Cysteine protease of Porphyromonas gingivalis 381 enhances binding of fimbriae to cultured human fibroblasts and matrix proteins. Infect Immun 1996: 64: 756-762.
    • (1996) Infect Immun , vol.64 , pp. 756-762
    • Kontani, M.1    Ono, H.2    Shibata, H.3    Okamura, Y.4    Tanaka, T.5    Fujiwara, T.6    Kimura, S.7    Hamada, S.8
  • 176
    • 0030834088 scopus 로고    scopus 로고
    • Adherence of Porphyromonas gingivalis to matrix proteins via a fimbrial cryptic receptor exposed by its own arginine-specific protease
    • Kontani M, Kimura S, Nakagawa I, Hamada S. Adherence of Porphyromonas gingivalis to matrix proteins via a fimbrial cryptic receptor exposed by its own arginine-specific protease. Mol Microbiol 1997: 24: 1179-1187.
    • (1997) Mol Microbiol , vol.24 , pp. 1179-1187
    • Kontani, M.1    Kimura, S.2    Nakagawa, I.3    Hamada, S.4
  • 177
    • 0031152001 scopus 로고    scopus 로고
    • The host response to the microbial challenge in periodontitis: Assembling the players
    • Kornman KS, Page RC, Tonetti MS. The host response to the microbial challenge in periodontitis: assembling the players. Periodontol 2000 1997: 14: 33-53.
    • (1997) Periodontol 2000 , vol.14 , pp. 33-53
    • Kornman, K.S.1    Page, R.C.2    Tonetti, M.S.3
  • 178
    • 0031711572 scopus 로고    scopus 로고
    • The number of direct repeats in hagA is variable among Porphyromonas gingivalis strains
    • Kozarov E, Whitlock J, Dong H, Carrasco E, Progulske-Fox A. The number of direct repeats in hagA is variable among Porphyromonas gingivalis strains. Infect Immun 1998: 66: 4721-4725.
    • (1998) Infect Immun , vol.66 , pp. 4721-4725
    • Kozarov, E.1    Whitlock, J.2    Dong, H.3    Carrasco, E.4    Progulske-Fox, A.5
  • 179
  • 180
    • 0025306916 scopus 로고
    • Cathepsins B, H and L activities in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects
    • Kunimatsu K, Yamamoto K, Ichimaru E, Kato Y, Kato I. Cathepsins B, H and L activities in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects. J Periodontal Res 1990: 25: 69-73.
    • (1990) J Periodontal Res , vol.25 , pp. 69-73
    • Kunimatsu, K.1    Yamamoto, K.2    Ichimaru, E.3    Kato, Y.4    Kato, I.5
  • 181
    • 0029141081 scopus 로고
    • Identification and possible function of cathepsin G in gingival crevicular fluid from chronic adult periodontitis patients and from experimental gingivitis subjects
    • Kunimatsu K, Mine N, Muraoka Y, Kato I, Hase T, Aoki Y, Yamamoto K. Identification and possible function of cathepsin G in gingival crevicular fluid from chronic adult periodontitis patients and from experimental gingivitis subjects. J Periodontal Res 1995: 30: 51-57.
    • (1995) J Periodontal Res , vol.30 , pp. 51-57
    • Kunimatsu, K.1    Mine, N.2    Muraoka, Y.3    Kato, I.4    Hase, T.5    Aoki, Y.6    Yamamoto, K.7
  • 182
    • 0032189067 scopus 로고    scopus 로고
    • Proteases of Porphyromonas gingivalis: What don't they do?
    • Kuramitsu HK. Proteases of Porphyromonas gingivalis: what don't they do? Oral Microbiol Immunol 1998: 13: 263-270.
    • (1998) Oral Microbiol Immunol , vol.13 , pp. 263-270
    • Kuramitsu, H.K.1
  • 183
    • 0029247619 scopus 로고
    • Proteases and collagenases of Porphyromonas gingivalis
    • Kuramitsu HK, Yoneda M, Madden T. Proteases and collagenases of Porphyromonas gingivalis. Adv Dent Res 1995: 9: 37-40.
    • (1995) Adv Dent Res , vol.9 , pp. 37-40
    • Kuramitsu, H.K.1    Yoneda, M.2    Madden, T.3
  • 184
    • 0028305420 scopus 로고
    • Porphyromonas gingivalis trypsin-like protease: A possible natural ligand for the neutrophil formyl peptide receptor
    • Lala A, Amano A, Sojar HT, Radel SJ, De Nardin E. Porphyromonas gingivalis trypsin-like protease: a possible natural ligand for the neutrophil formyl peptide receptor. Biochem Biophys Res Commun 1994: 199: 1489-1496.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1489-1496
    • Lala, A.1    Amano, A.2    Sojar, H.T.3    Radel, S.J.4    De Nardin, E.5
  • 186
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont RJ, Jenkinson HF. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol Mol Biol Rev 1998: 62: 1244-1263.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 188
    • 0025089133 scopus 로고
    • Absence of bleeding on probing. An indicator of periodontal stability
    • Lang NP, Adler R, Joss A, Nyman S. Absence of bleeding on probing. An indicator of periodontal stability. J Clin Periodontol 1990: 17: 714-721.
    • (1990) J Clin Periodontol , vol.17 , pp. 714-721
    • Lang, N.P.1    Adler, R.2    Joss, A.3    Nyman, S.4
  • 190
    • 0025915038 scopus 로고
    • Identification of Porphyromonas gingivalis components that mediate its interactions with fibronectin
    • Lantz MS, Allen RD, Duck LW, Blume JL, Switalski LM, Hook M. Identification of Porphyromonas gingivalis components that mediate its interactions with fibronectin. J Bacteriol 1991: 173: 4263-4270.
    • (1991) J Bacteriol , vol.173 , pp. 4263-4270
    • Lantz, M.S.1    Allen, R.D.2    Duck, L.W.3    Blume, J.L.4    Switalski, L.M.5    Hook, M.6
  • 191
    • 0026164308 scopus 로고
    • Porphyromonas gingivalis surface components bind and degrade connective-tissue proteins
    • Lantz MS, Allen RD, Duck LW, Switalski LM, Hook M. Porphyromonas gingivalis surface components bind and degrade connective-tissue proteins. J Periodontal Res 1991: 26: 283-285.
    • (1991) J Periodontal Res , vol.26 , pp. 283-285
    • Lantz, M.S.1    Allen, R.D.2    Duck, L.W.3    Switalski, L.M.4    Hook, M.5
  • 192
    • 0026020589 scopus 로고
    • Specific cell components of Bacteroides gingivalis mediate binding and degradation of human fibrinogen
    • Lantz MS, Allen RD, Vail TA, Hook, M. Specific cell components of Bacteroides gingivalis mediate binding and degradation of human fibrinogen. J Bacteriol 1991: 173: 495-504.
    • (1991) J Bacteriol , vol.173 , pp. 495-504
    • Lantz, M.S.1    Allen, R.D.2    Vail, T.A.3    Hook, M.4
  • 193
    • 0026566498 scopus 로고
    • Biochemical characterization of Porphyromonas (Bacteroides) gingivalis collagenase
    • Lawson DA, Meyer TF. Biochemical characterization of Porphyromonas (Bacteroides) gingivalis collagenase. Infect Immun 1992: 60: 1524-1529.
    • (1992) Infect Immun , vol.60 , pp. 1524-1529
    • Lawson, D.A.1    Meyer, T.F.2
  • 194
    • 0025968113 scopus 로고
    • Porphyromonas (Bacteroides) gingivalis fimbrillin: Size, amino-terminal sequence, and antigenic heterogeneity
    • Lee JY, Sojar HT, Bedi GS, Genco RJ. Porphyromonas (Bacteroides) gingivalis fimbrillin: size, amino-terminal sequence, and antigenic heterogeneity. Infect Immun 1991: 59: 383-389.
    • (1991) Infect Immun , vol.59 , pp. 383-389
    • Lee, J.Y.1    Sojar, H.T.2    Bedi, G.S.3    Genco, R.J.4
  • 195
    • 0026049102 scopus 로고
    • Collagenase activity in recurrent periodontitis: Relationship to disease progression and doxycycline therapy
    • Lee W, Aitken S, Kulkarni G, Birek P, Overall CM, Sodek J, McCulloch CA. Collagenase activity in recurrent periodontitis: relationship to disease progression and doxycycline therapy. J Periodontal Res 1991: 26: 479-485.
    • (1991) J Periodontal Res , vol.26 , pp. 479-485
    • Lee, W.1    Aitken, S.2    Kulkarni, G.3    Birek, P.4    Overall, C.M.5    Sodek, J.6    McCulloch, C.A.7
  • 196
    • 0029141399 scopus 로고
    • Evidence of a direct relationship between neutrophil collagenase activity and peripdontal tissue destruction in vivo: Role of active enzyme in human periodontitis
    • Lee W, Aitken S, Sodek J, McCulloch CA. Evidence of a direct relationship between neutrophil collagenase activity and peripdontal tissue destruction in vivo: role of active enzyme in human periodontitis. J Periodontal Res 1995: 30: 23-33.
    • (1995) J Periodontal Res , vol.30 , pp. 23-33
    • Lee, W.1    Aitken, S.2    Sodek, J.3    McCulloch, C.A.4
  • 198
    • 0032922566 scopus 로고    scopus 로고
    • A potential role of an intracellular signaling defect in neutrophil functional abnormalities and promotion of tissue damage in patients with localized juvenile periodontitis
    • Leino L, Hurttia H. A potential role of an intracellular signaling defect in neutrophil functional abnormalities and promotion of tissue damage in patients with localized juvenile periodontitis. Clin Chem Lab Med 1999: 37: 215-222.
    • (1999) Clin Chem Lab Med , vol.37 , pp. 215-222
    • Leino, L.1    Hurttia, H.2
  • 200
    • 0028526427 scopus 로고
    • Regulation of bone metabolism by the kallikrein-kinin system, the coagulation cascade, and the acute-phase reactants
    • Lerner UH. Regulation of bone metabolism by the kallikrein-kinin system, the coagulation cascade, and the acute-phase reactants. Oral Surg Oral Med Oral Pathol Oral Radiol Endod 1994: 78; 481-493.
    • (1994) Oral Surg Oral Med Oral Pathol Oral Radiol Endod , vol.78 , pp. 481-493
    • Lerner, U.H.1
  • 201
    • 0031842401 scopus 로고    scopus 로고
    • IS195, an insertion sequence-like element associated with protease genes in Porphyromonas gingivalis
    • Levis JP, Macrina FL. IS195, an insertion sequence-like element associated with protease genes in Porphyromonas gingivalis. Infect Immun 1998: 66: 3035-3042.
    • (1998) Infect Immun , vol.66 , pp. 3035-3042
    • Levis, J.P.1    Macrina, F.L.2
  • 203
    • 12644298687 scopus 로고    scopus 로고
    • Effect of oral bacteria on peripheral blood leukocyte interleukin-6 and soluble interleukin-6 receptor production
    • Lindemann RA, Kinde Haake SA, Kjeldsen M, Avanessian AB. Effect of oral bacteria on peripheral blood leukocyte interleukin-6 and soluble interleukin-6 receptor production. Oral Microbiol Immunol 1996: 11: 332-336.
    • (1996) Oral Microbiol Immunol , vol.11 , pp. 332-336
    • Lindemann, R.A.1    Kinde Haake, S.A.2    Kjeldsen, M.3    Avanessian, A.B.4
  • 204
    • 0020320840 scopus 로고
    • The bacteriology of acute necrotizing ulcerative gingivitis
    • Loesche WJ, Syed SA, Laughon BE, Stoll J. The bacteriology of acute necrotizing ulcerative gingivitis. J Periodontol 1982: 53: 223-230.
    • (1982) J Periodontol , vol.53 , pp. 223-230
    • Loesche, W.J.1    Syed, S.A.2    Laughon, B.E.3    Stoll, J.4
  • 205
    • 0025296789 scopus 로고
    • Development of a diagnostic test for anaerobic periodontal infections based on plaque hydrolysis of benzoyl-DL-arginine-naphthylamide
    • Loesche WJ, Bretz WA, Kerschensteiner D, Stoll J, Socransky SS, Hujoel P, Lopatin DE. Development of a diagnostic test for anaerobic periodontal infections based on plaque hydrolysis of benzoyl-DL-arginine-naphthylamide. J Clin Microbiol 1990: 28: 1551-1559.
    • (1990) J Clin Microbiol , vol.28 , pp. 1551-1559
    • Loesche, W.J.1    Bretz, W.A.2    Kerschensteiner, D.3    Stoll, J.4    Socransky, S.S.5    Hujoel, P.6    Lopatin, D.E.7
  • 207
    • 0032508557 scopus 로고    scopus 로고
    • Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis
    • Lourbakos A, Chinni C, Thompson P, Potempa J, Travis J, Mackie EJ, Pike RN. Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis. FEBS Lett 1998: 435: 45-48.
    • (1998) FEBS Lett , vol.435 , pp. 45-48
    • Lourbakos, A.1    Chinni, C.2    Thompson, P.3    Potempa, J.4    Travis, J.5    Mackie, E.J.6    Pike, R.N.7
  • 208
    • 0032425627 scopus 로고    scopus 로고
    • Expression of the tpr protease gene of Porphyromonas gingivalis is regulated by peptide nutrients
    • Lu B, McBride BC. Expression of the tpr protease gene of Porphyromonas gingivalis is regulated by peptide nutrients. Infect Immunol 1998: 66: 5147-5156.
    • (1998) Infect Immunol , vol.66 , pp. 5147-5156
    • Lu, B.1    McBride, B.C.2
  • 209
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains
    • Lukomski S, Sreevatsan S, Amberg C, Reichardt W, Woischnik M, Podbielski A, Musser JM. Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J Clin Invest 1997: 99: 2574-2580.
    • (1997) J Clin Invest , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, C.3    Reichardt, W.4    Woischnik, M.5    Podbielski, A.6    Musser, J.M.7
  • 210
    • 0028878078 scopus 로고
    • Revised sequence of the Porphyromonas gingivalis prtT cysteine protease/ hemagglutinin gene: Homology with streptococcal pyrogenic exotoxin B/streptococcal proteinase
    • Madden TE, Clark VL, Kuramitsu HK. Revised sequence of the Porphyromonas gingivalis prtT cysteine protease/ hemagglutinin gene: homology with streptococcal pyrogenic exotoxin B/streptococcal proteinase. Infect Immun 1995: 63: 238-247.
    • (1995) Infect Immun , vol.63 , pp. 238-247
    • Madden, T.E.1    Clark, V.L.2    Kuramitsu, H.K.3
  • 211
    • 0026786952 scopus 로고
    • Microbial proteinases as an universal trigger of kinin generation in microbial infections
    • Maeda H, Maruo K, Akaike T, Kaminishi H, Hagiwara Y. Microbial proteinases as an universal trigger of kinin generation in microbial infections. Agents Actions 1992: 38(suppl): 362-369.
    • (1992) Agents Actions , vol.38 , Issue.SUPPL. , pp. 362-369
    • Maeda, H.1    Maruo, K.2    Akaike, T.3    Kaminishi, H.4    Hagiwara, Y.5
  • 212
    • 0029879578 scopus 로고    scopus 로고
    • Pathogenic mechanisms induced by microbial proteases in microbial infections
    • Maeda H, Yamamoto T. Pathogenic mechanisms induced by microbial proteases in microbial infections. Biol Chem Hoppe Seyler 1996: 377: 217-226.
    • (1996) Biol Chem Hoppe Seyler , vol.377 , pp. 217-226
    • Maeda, H.1    Yamamoto, T.2
  • 213
    • 0026629301 scopus 로고
    • Purification and substrate specificity of an endopeptidase from the human oral spirochete Treponema denticola ATCC 35405, active on furylacryloyl-Leu-Gly-Pro-Ala and bradykinin
    • Makinen KK, Makinen PL, Syed SA. Purification and substrate specificity of an endopeptidase from the human oral spirochete Treponema denticola ATCC 35405, active on furylacryloyl-Leu-Gly-Pro-Ala and bradykinin. J Biol Chem 1992: 267: 14285-14293.
    • (1992) J Biol Chem , vol.267 , pp. 14285-14293
    • Makinen, K.K.1    Makinen, P.L.2    Syed, S.A.3
  • 214
    • 0027959709 scopus 로고
    • An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: Evidence of hydrolysis of human bioactive peptides
    • Makinen PL, Makinen KK, Syed SA. An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides. Infect Immun 1994: 62: 4938-4947.
    • (1994) Infect Immun , vol.62 , pp. 4938-4947
    • Makinen, P.L.1    Makinen, K.K.2    Syed, S.A.3
  • 215
    • 0028911526 scopus 로고
    • Purification and general properties of an oligopeptidase from Treponema denticola ATCC 35405 - A human oral spirochete
    • Makinen KK, Makinen PL, Loesche WJ, Syed SA. Purification and general properties of an oligopeptidase from Treponema denticola ATCC 35405 - a human oral spirochete. Arch Biochem Biophys 1995: 316: 689-698.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 689-698
    • Makinen, K.K.1    Makinen, P.L.2    Loesche, W.J.3    Syed, S.A.4
  • 216
    • 0029162741 scopus 로고
    • Role of the chymotrypsin-like membrane-associated proteinase from Treponema denticola ATCC 35405 in inactivation of bioactive peptides
    • Makinen PL, Makinen KK, Syed SA. Role of the chymotrypsin-like membrane-associated proteinase from Treponema denticola ATCC 35405 in inactivation of bioactive peptides. Infect Immun 1995: 63: 3567-3575.
    • (1995) Infect Immun , vol.63 , pp. 3567-3575
    • Makinen, P.L.1    Makinen, K.K.2    Syed, S.A.3
  • 217
    • 0030021821 scopus 로고    scopus 로고
    • Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405
    • Makinen KK, Chen CY, Makinen PL. Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405. Infect Immun 1996: 64: 702-708.
    • (1996) Infect Immun , vol.64 , pp. 702-708
    • Makinen, K.K.1    Chen, C.Y.2    Makinen, P.L.3
  • 218
    • 0028456252 scopus 로고
    • Bradykinin and thrombin stimulate release of arachidonic acid and formation of prostanoids in human periodontal ligament cells
    • Marklund M, Lerner UH, Persson M, Ransjo M. Bradykinin and thrombin stimulate release of arachidonic acid and formation of prostanoids in human periodontal ligament cells. Eur J Orthod 1994: 16: 213-221.
    • (1994) Eur J Orthod , vol.16 , pp. 213-221
    • Marklund, M.1    Lerner, U.H.2    Persson, M.3    Ransjo, M.4
  • 219
    • 0028204138 scopus 로고
    • The effect of growth rate and haemin on the virulence and proteolytic activity of Porphyromonas gingivalis W50
    • Marsh PD, McDermid AS, McKee AS, Baskerville A. The effect of growth rate and haemin on the virulence and proteolytic activity of Porphyromonas gingivalis W50. Microbiology 1994: 140: 861-865.
    • (1994) Microbiology , vol.140 , pp. 861-865
    • Marsh, P.D.1    McDermid, A.S.2    McKee, A.S.3    Baskerville, A.4
  • 221
    • 0021881749 scopus 로고
    • Detection of collagenase activity in oral bacteria
    • Mayrand D, Grenier D. Detection of collagenase activity in oral bacteria. Can J Microbiol 1985: 31: 134-138.
    • (1985) Can J Microbiol , vol.31 , pp. 134-138
    • Mayrand, D.1    Grenier, D.2
  • 222
    • 0019256413 scopus 로고
    • Characterization of Bacteroides asaccharolyticus and B. melaninogenicus oral isolates
    • Mayrand D, McBride BC, Edwards T, Jensen S. Characterization of Bacteroides asaccharolyticus and B. melaninogenicus oral isolates. Can J Microbiol 1980: 26: 1178-1183.
    • (1980) Can J Microbiol , vol.26 , pp. 1178-1183
    • Mayrand, D.1    McBride, B.C.2    Edwards, T.3    Jensen, S.4
  • 223
    • 0010523023 scopus 로고
    • The complement system
    • Sim RB, ed. Dordrecht: Kluwer Academic Publishers
    • McAleer MA, Sim RB. The complement system. In: Sim RB, ed. Activators and inhibitors of complement. Dordrecht: Kluwer Academic Publishers, 1993: 1-15.
    • (1993) Activators and Inhibitors of Complement , pp. 1-15
    • McAleer, M.A.1    Sim, R.B.2
  • 224
    • 0023916164 scopus 로고
    • Effect of environmental pH on enzyme activity and growth of Bacteroides gingivalis W50
    • McDermid AS, McKee AS, Marsh PD. Effect of environmental pH on enzyme activity and growth of Bacteroides gingivalis W50. Infect Immun 1988: 56: 1096-1100.
    • (1988) Infect Immun , vol.56 , pp. 1096-1100
    • McDermid, A.S.1    McKee, A.S.2    Marsh, P.D.3
  • 225
    • 0032133349 scopus 로고    scopus 로고
    • The relationship between concentrations of proinflammatory cytokines within gingiva and the adjacent sulcular depth
    • McGee JM, Tucci MA, Edmundson TP, Serio CL, Johnson RB. The relationship between concentrations of proinflammatory cytokines within gingiva and the adjacent sulcular depth. J Periodontol 1998: 69: 865-871.
    • (1998) J Periodontol , vol.69 , pp. 865-871
    • McGee, J.M.1    Tucci, M.A.2    Edmundson, T.P.3    Serio, C.L.4    Johnson, R.B.5
  • 227
    • 0023785284 scopus 로고
    • Isolation of colonial variants of Bacteroides gingivalis W50 with a reduced virulence
    • McKee AS, McDermid AS, Wait R, Baskerville A, Marsh PD. Isolation of colonial variants of Bacteroides gingivalis W50 with a reduced virulence. J Med Microbiol 1988: 27: 59-64.
    • (1988) J Med Microbiol , vol.27 , pp. 59-64
    • McKee, A.S.1    McDermid, A.S.2    Wait, R.3    Baskerville, A.4    Marsh, P.D.5
  • 228
    • 0031094022 scopus 로고    scopus 로고
    • Active and alpha-1 proteinase inhibitor complexed leukocyte elastase levels in crevicular fluid from patients with periodontal diseases
    • Meyer J, Guessous F, Huynh C, Godeau G, Hornebeck W, Giroud JP, Roch-Arveiller M. Active and alpha-1 proteinase inhibitor complexed leukocyte elastase levels in crevicular fluid from patients with periodontal diseases. J Periodontol 1997: 68: 256-261.
    • (1997) J Periodontol , vol.68 , pp. 256-261
    • Meyer, J.1    Guessous, F.2    Huynh, C.3    Godeau, G.4    Hornebeck, W.5    Giroud, J.P.6    Roch-Arveiller, M.7
  • 229
    • 0026855860 scopus 로고
    • Influence of oral hygiene on elastase concentration of gingival crevicular fluid
    • Meyle J, Zell S, Brecx M, Heller W. Influence of oral hygiene on elastase concentration of gingival crevicular fluid. J Periodontal Res 1992: 27: 226-231.
    • (1992) J Periodontal Res , vol.27 , pp. 226-231
    • Meyle, J.1    Zell, S.2    Brecx, M.3    Heller, W.4
  • 230
    • 0028521284 scopus 로고
    • Leukocyte adhesion deficiency and prepubertal periodontitis
    • Meyle J. Leukocyte adhesion deficiency and prepubertal periodontitis. Periodontol 2000 1994: 6: 26-36.
    • (1994) Periodontol 2000 , vol.6 , pp. 26-36
    • Meyle, J.1
  • 231
    • 0031951529 scopus 로고    scopus 로고
    • Genetic variations of Porphyromonas gingivalis genes encoding gingipains, cysteine proteinases with arginine or lysine specificity
    • Mikolajczyk-Pawlinska J, Kordula T, Pavloff N, Pemberton PA, Kiefer MC, Travis J, Potempa J. Genetic variations of Porphyromonas gingivalis genes encoding gingipains, cysteine proteinases with arginine or lysine specificity. Biol Chem 1998: 237: 205-211.
    • (1998) Biol Chem , vol.237 , pp. 205-211
    • Mikolajczyk-Pawlinska, J.1    Kordula, T.2    Pavloff, N.3    Pemberton, P.A.4    Kiefer, M.C.5    Travis, J.6    Potempa, J.7
  • 232
    • 0032407820 scopus 로고    scopus 로고
    • Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: Implications for pathogenicity of periodontal disease
    • Mikolajczyk-Pawlinska J, Travis J, Potempa J. Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease. FEBS Lett 1998: 4: 282-286.
    • (1998) FEBS Lett , vol.4 , pp. 282-286
    • Mikolajczyk-Pawlinska, J.1    Travis, J.2    Potempa, J.3
  • 233
    • 0027737771 scopus 로고
    • The influence of haemin levels on growth and enzyme production by Porphyromonas gingivalis in continuous culture
    • Minhas T, Greenman J, Schaffer AG. The influence of haemin levels on growth and enzyme production by Porphyromonas gingivalis in continuous culture. Microbios 1993: 76: 105-114.
    • (1993) Microbios , vol.76 , pp. 105-114
    • Minhas, T.1    Greenman, J.2    Schaffer, A.G.3
  • 234
    • 0030963690 scopus 로고    scopus 로고
    • Porphyromonas gingivalis lipopolysaccharide-stimulated bone resorption via CD14 is inhibited by broad-spectrum antibiotics
    • Miyata Y, Takeda H, Kitano S, Hanazawa S. Porphyromonas gingivalis lipopolysaccharide-stimulated bone resorption via CD14 is inhibited by broad-spectrum antibiotics. Infect Immun 1997: 65: 3513-3519.
    • (1997) Infect Immun , vol.65 , pp. 3513-3519
    • Miyata, Y.1    Takeda, H.2    Kitano, S.3    Hanazawa, S.4
  • 235
    • 0026275042 scopus 로고
    • The neutrophil: Mechanisms of controlling periodontal bacteria
    • Miyasaki KT. The neutrophil: mechanisms of controlling periodontal bacteria. J Periodontol 1991: 62: 761-774.
    • (1991) J Periodontol , vol.62 , pp. 761-774
    • Miyasaki, K.T.1
  • 236
    • 0031284855 scopus 로고    scopus 로고
    • Loss of Fc gamma receptor and impaired phagocytosis of polymorphonuclear leukocytes in gingival crevicular fluid
    • Miyazaki A, Kobayashi T, Suzuki T, Yoshie H, Hara K. Loss of Fc gamma receptor and impaired phagocytosis of polymorphonuclear leukocytes in gingival crevicular fluid. J Periodontal Res 1997: 32: 439-446.
    • (1997) J Periodontal Res , vol.32 , pp. 439-446
    • Miyazaki, A.1    Kobayashi, T.2    Suzuki, T.3    Yoshie, H.4    Hara, K.5
  • 237
    • 0024833375 scopus 로고
    • Purification and characterization of glycylprolyl aminopeptidase from Bacteroides gingivalis
    • Miyauchi T, Hayakawa M, Abiko Y. Purification and characterization of glycylprolyl aminopeptidase from Bacteroides gingivalis. Oral Microbiol Immunol 1989: 4: 222-226.
    • (1989) Oral Microbiol Immunol , vol.4 , pp. 222-226
    • Miyauchi, T.1    Hayakawa, M.2    Abiko, Y.3
  • 238
    • 0032086731 scopus 로고    scopus 로고
    • Immunization with Porphyromonas gingivalis cysteine protease: Effects on experimental gingivitis and ligature-induced periodontitis in Macaca fascicularis
    • Moritz AJ, Cappelli D, Lantz MS, Holt SC, Ebersole JL. Immunization with Porphyromonas gingivalis cysteine protease: effects on experimental gingivitis and ligature-induced periodontitis in Macaca fascicularis. J Periodontol 1998: 69: 686-697.
    • (1998) J Periodontol , vol.69 , pp. 686-697
    • Moritz, A.J.1    Cappelli, D.2    Lantz, M.S.3    Holt, S.C.4    Ebersole, J.L.5
  • 239
    • 0019464127 scopus 로고
    • Serum antibodies to oral Bacteroides asaccharolyticus (Bacteroides gingivalis): Relationship to age and periodontal disease
    • Mouton C, Hammond PG, Slots J, Genco RJ. Serum antibodies to oral Bacteroides asaccharolyticus (Bacteroides gingivalis): relationship to age and periodontal disease. Infect Immun 1981: 31: 182-192.
    • (1981) Infect Immun , vol.31 , pp. 182-192
    • Mouton, C.1    Hammond, P.G.2    Slots, J.3    Genco, R.J.4
  • 240
    • 0021227718 scopus 로고
    • Immunoglobulin G response to subgingival gram-negative bacteria in human subjects
    • Naito Y, Okuda K, Takazoe I. Immunoglobulin G response to subgingival gram-negative bacteria in human subjects. Infect Immun 1984: 45: 47-51.
    • (1984) Infect Immun , vol.45 , pp. 47-51
    • Naito, Y.1    Okuda, K.2    Takazoe, I.3
  • 241
    • 0028839251 scopus 로고
    • Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis - Evidence for significant contribution of arg-gingipain to virulence
    • Nakayama K, Kadowaki T, Okamoto K, Yamamoto Y. Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis - evidence for significant contribution of arg-gingipain to virulence. J Biol Chem 1995: 270: 23619-23626.
    • (1995) J Biol Chem , vol.270 , pp. 23619-23626
    • Nakayama, K.1    Kadowaki, T.2    Okamoto, K.3    Yamamoto, Y.4
  • 242
    • 0029917103 scopus 로고    scopus 로고
    • Involvement of arginine-specific cysteine proteinase (ArgGingipain) in fimbriation of Porphyromonas gingivalis
    • Nakayama K, Yoshimura F, Kadowaki T, Yamamoto K. Involvement of arginine-specific cysteine proteinase (ArgGingipain) in fimbriation of Porphyromonas gingivalis. J Bacteriol 1996: 178: 2818-2824.
    • (1996) J Bacteriol , vol.178 , pp. 2818-2824
    • Nakayama, K.1    Yoshimura, F.2    Kadowaki, T.3    Yamamoto, K.4
  • 243
    • 0030891894 scopus 로고    scopus 로고
    • Domain-specific rearrangement between the two Arg-gingipain-encoding genes in Porphyromonas gingivalis: Possible involvement on nonreciprocal recombination
    • Nakayama K. Domain-specific rearrangement between the two Arg-gingipain-encoding genes in Porphyromonas gingivalis: possible involvement on nonreciprocal recombination. Microbiol Immunol 1997: 41: 185-196.
    • (1997) Microbiol Immunol , vol.41 , pp. 185-196
    • Nakayama, K.1
  • 244
    • 0031962568 scopus 로고    scopus 로고
    • Haemoglobin receptor protein is intergenically encoded by the cysteine proteinase-encoding genes and the hemagglutinin-encoding gene of Porphyromonas gingivalis
    • Nakayama K, Ratnayake DB, Tsukuba T, Kadowaki T, Yamamoto K, Fujimura S. Haemoglobin receptor protein is intergenically encoded by the cysteine proteinase-encoding genes and the hemagglutinin-encoding gene of Porphyromonas gingivalis. Mol Microbiol 1998: 27: 51-61.
    • (1998) Mol Microbiol , vol.27 , pp. 51-61
    • Nakayama, K.1    Ratnayake, D.B.2    Tsukuba, T.3    Kadowaki, T.4    Yamamoto, K.5    Fujimura, S.6
  • 245
    • 0023029313 scopus 로고
    • Implication of thrombin formation on the endothelial cell surface
    • Nawroth PP, Stern DM. Implication of thrombin formation on the endothelial cell surface. Semin Thromb Hemost 1986: 12: 197-199.
    • (1986) Semin Thromb Hemost , vol.12 , pp. 197-199
    • Nawroth, P.P.1    Stern, D.M.2
  • 246
    • 0032113805 scopus 로고    scopus 로고
    • Inactivation of alphal-proteinase inhibitor as a broad screen for detecting proteolytic activities in unknown samples
    • Nelson D, Potempa J, Travis J. Inactivation of alphal-proteinase inhibitor as a broad screen for detecting proteolytic activities in unknown samples. Anal Biochem 1998: 260: 230-236.
    • (1998) Anal Biochem , vol.260 , pp. 230-236
    • Nelson, D.1    Potempa, J.2    Travis, J.3
  • 248
    • 0025807827 scopus 로고
    • Characterization of Porphyromonas (Bacteroides) gingivalis hemagglutinin as a protease
    • Nishikata M, Yoshimura F. Characterization of Porphyromonas (Bacteroides) gingivalis hemagglutinin as a protease. Biochem Biophys Res Commun 1991: 178: 336-342.
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 336-342
    • Nishikata, M.1    Yoshimura, F.2
  • 249
    • 0029555645 scopus 로고
    • Active site structure of a haemagglutinating protease from Porphyromonas gingivalis: Similarity to clostripain
    • Nishikata M, Yoshimura F. Active site structure of a haemagglutinating protease from Porphyromonas gingivalis: similarity to clostripain. Biochem Mol Biol Int 1995: 37: 547-553.
    • (1995) Biochem Mol Biol Int , vol.37 , pp. 547-553
    • Nishikata, M.1    Yoshimura, F.2
  • 250
    • 0024582551 scopus 로고
    • Possibility of Bacteroides gingivalis hemagglutinin possessing protease activity revealed by inhibition studies
    • Nishikata M, Yoshimura F, Nodasaka Y. Possibility of Bacteroides gingivalis hemagglutinin possessing protease activity revealed by inhibition studies. Microbiol Immunol 1989: 33: 75-80.
    • (1989) Microbiol Immunol , vol.33 , pp. 75-80
    • Nishikata, M.1    Yoshimura, F.2    Nodasaka, Y.3
  • 251
    • 0025962890 scopus 로고
    • Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis
    • Nishikata M, Kanehira T, Oh H, Tani H, Tazaki M, Kuboki Y. Salivary histatin as an inhibitor of a protease produced by the oral bacterium Bacteroides gingivalis. Biochem Biophys Res Commun 1991: 74: 625-630.
    • (1991) Biochem Biophys Res Commun , vol.74 , pp. 625-630
    • Nishikata, M.1    Kanehira, T.2    Oh, H.3    Tani, H.4    Tazaki, M.5    Kuboki, Y.6
  • 252
    • 0021315626 scopus 로고
    • Crevicular fluid prostaglandin e levels as a measure of the periodontal disease status of adult and juvenile periodontitis patients
    • Offenbacher S, Odle BM, Gray RC, Van Dyke TE. Crevicular fluid prostaglandin E levels as a measure of the periodontal disease status of adult and juvenile periodontitis patients. J Periodontal Res 1984: 19: 1-13.
    • (1984) J Periodontal Res , vol.19 , pp. 1-13
    • Offenbacher, S.1    Odle, B.M.2    Gray, R.C.3    Van Dyke, T.E.4
  • 254
    • 0028360859 scopus 로고
    • Molecular cloning and characterization of the genes encoding the immunoreactive major cell-surface proteins of Porphyromonas gingivalis
    • Ogawa T, Mori H, Yasuda K, Hasegawa M. Molecular cloning and characterization of the genes encoding the immunoreactive major cell-surface proteins of Porphyromonas gingivalis. FEMS Microbiol Lett 1994: 120: 23-30.
    • (1994) FEMS Microbiol Lett , vol.120 , pp. 23-30
    • Ogawa, T.1    Mori, H.2    Yasuda, K.3    Hasegawa, M.4
  • 256
    • 0022477095 scopus 로고
    • Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates
    • Ohta K, Makinen KK, Loesche WJ. Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates. Infect Immun 1986: 53: 213-220.
    • (1986) Infect Immun , vol.53 , pp. 213-220
    • Ohta, K.1    Makinen, K.K.2    Loesche, W.J.3
  • 257
    • 0023837944 scopus 로고
    • Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases
    • Okada Y, Watanabe S, Nakanishi I, Kishi J, Hayakawa T, Watorek W, Travis J, Nagase H. Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases. FEBS Lett 1988: 229: 157-160.
    • (1988) FEBS Lett , vol.229 , pp. 157-160
    • Okada, Y.1    Watanabe, S.2    Nakanishi, I.3    Kishi, J.4    Hayakawa, T.5    Watorek, W.6    Travis, J.7    Nagase, H.8
  • 258
    • 0016064983 scopus 로고
    • Hemagglutinating activity of Bacteroides melaninogenicus
    • Okuda K, Takazoe I. Hemagglutinating activity of Bacteroides melaninogenicus. Arch Oral Biol 1974: 19: 415-416.
    • (1974) Arch Oral Biol , vol.19 , pp. 415-416
    • Okuda, K.1    Takazoe, I.2
  • 259
    • 0028931990 scopus 로고
    • Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogen from Porphyromonas gingivalis
    • Okamoto K, Misumi Y, Kadowaki T, Yoneda M, Yamamoto K, Ikehara Y. Structural characterization of argingipain, a novel arginine-specific cysteine proteinase as a major periodontal pathogen from Porphyromonas gingivalis. Arch Biochem Biophys 1995: 316: 917-925.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 917-925
    • Okamoto, K.1    Misumi, Y.2    Kadowaki, T.3    Yoneda, M.4    Yamamoto, K.5    Ikehara, Y.6
  • 260
    • 0029684438 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: Structural relationship with the arginine-specific cysteine proteinase (Arg-gingipain)
    • Okamoto K, Kadowaki T, Nakayama K, Yamamoto K. Cloning and sequencing of the gene encoding a novel lysine-specific cysteine proteinase (Lys-gingipain) in Porphyromonas gingivalis: structural relationship with the arginine-specific cysteine proteinase (Arg-gingipain). J Biochem 1996: 120: 398-406.
    • (1996) J Biochem , vol.120 , pp. 398-406
    • Okamoto, K.1    Kadowaki, T.2    Nakayama, K.3    Yamamoto, K.4
  • 261
    • 0032516926 scopus 로고    scopus 로고
    • Involvement of a lysine-specific cysteine proteinase in hemoglobin adsorption and heme accumulation by Porphyromonas gingivalis
    • Okamoto K, Nakayama K, Kadowaki T, Abe N, Ratnayake DB, Yamamoto K. Involvement of a lysine-specific cysteine proteinase in hemoglobin adsorption and heme accumulation by Porphyromonas gingivalis. J Biol Chem 1998: 273: 21225-21231.
    • (1998) J Biol Chem , vol.273 , pp. 21225-21231
    • Okamoto, K.1    Nakayama, K.2    Kadowaki, T.3    Abe, N.4    Ratnayake, D.B.5    Yamamoto, K.6
  • 262
    • 0024278452 scopus 로고
    • Characterization of a protein C activator from the venom of Agkistrodon contortrix contortrix
    • Orthner CL, Bhattacharya P, Strickland DK. Characterization of a protein C activator from the venom of Agkistrodon contortrix contortrix. Biochemistry 1988: 27: 2558-2564.
    • (1988) Biochemistry , vol.27 , pp. 2558-2564
    • Orthner, C.L.1    Bhattacharya, P.2    Strickland, D.K.3
  • 263
    • 0027498179 scopus 로고
    • Isolation and characterization of the Porphyromonas gingivalis prtT gene, coding for protease activity
    • Otogoto J, Kuramitsu HK. Isolation and characterization of the Porphyromonas gingivalis prtT gene, coding for protease activity. Infect Immun 1993: 61: 117-123.
    • (1993) Infect Immun , vol.61 , pp. 117-123
    • Otogoto, J.1    Kuramitsu, H.K.2
  • 264
    • 0023600976 scopus 로고
    • Isolation and characterization of protease from culture supernatant of Bacteroides gingivalis
    • Otsuka M, Endo J, Hinode D, Nagata A, Maehara R, Sato M, Nakamura R. Isolation and characterization of protease from culture supernatant of Bacteroides gingivalis. J Periodontal Res 1987: 22: 49149-49158.
    • (1987) J Periodontal Res , vol.22 , pp. 49149-49158
    • Otsuka, M.1    Endo, J.2    Hinode, D.3    Nagata, A.4    Maehara, R.5    Sato, M.6    Nakamura, R.7
  • 265
    • 0025746338 scopus 로고
    • Evidence for polymorphonuclear leukocyte collagenase and 92-kilodalton gelatinase in gingival crevicular fluid
    • Overall CM, Sodek J, McCulloch CA, Birek P. Evidence for polymorphonuclear leukocyte collagenase and 92-kilodalton gelatinase in gingival crevicular fluid. Infect Immun 1991: 59: 4687-4692.
    • (1991) Infect Immun , vol.59 , pp. 4687-4692
    • Overall, C.M.1    Sodek, J.2    McCulloch, C.A.3    Birek, P.4
  • 266
    • 0032112772 scopus 로고    scopus 로고
    • The pathobiology of periodontal diseases may affect systemic diseases: Inversion of a paradigm
    • Page RC. The pathobiology of periodontal diseases may affect systemic diseases: inversion of a paradigm. Ann Periodontol 1998: 3: 108-120.
    • (1998) Ann Periodontol , vol.3 , pp. 108-120
    • Page, R.C.1
  • 268
    • 0026856207 scopus 로고
    • Cloning of a Porphyromonas (Bacteroides) gingivalis protease gene and characterization of its product
    • Park Y, McBride BC. Cloning of a Porphyromonas (Bacteroides) gingivalis protease gene and characterization of its product. FEMS Microbiol Lett 1992: 71: 273-278.
    • (1992) FEMS Microbiol Lett , vol.71 , pp. 273-278
    • Park, Y.1    McBride, B.C.2
  • 269
    • 0027381557 scopus 로고
    • Characterization of the tpr gene product and isolation of a specific protease-deficient mutant of Porphyromonas gingivalis W83
    • Park Y, McBride BC. Characterization of the tpr gene product and isolation of a specific protease-deficient mutant of Porphyromonas gingivalis W83. Infect Immun 1993: 61: 4139-4146.
    • (1993) Infect Immun , vol.61 , pp. 4139-4146
    • Park, Y.1    McBride, B.C.2
  • 270
    • 0031018704 scopus 로고    scopus 로고
    • Inducible expression of a Porphyromonas gingivalis W83 membrane-associated protease
    • Park Y, Lu B, Mazur C, McBride BC. Inducible expression of a Porphyromonas gingivalis W83 membrane-associated protease. Infect Immun 1997: 65: 1101-1104.
    • (1997) Infect Immun , vol.65 , pp. 1101-1104
    • Park, Y.1    Lu, B.2    Mazur, C.3    McBride, B.C.4
  • 271
    • 0020407848 scopus 로고
    • Serum antibodies to Bacteroides species in human periodontitis
    • Patters MR, Kornman KS. Serum antibodies to Bacteroides species in human periodontitis. J Periodontal Res 1982: 17: 474-477.
    • (1982) J Periodontal Res , vol.17 , pp. 474-477
    • Patters, M.R.1    Kornman, K.S.2
  • 272
  • 273
    • 0028840005 scopus 로고
    • Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis
    • Pavloff N, Potempa J, Pike NR, Prochazka V, Kiefer MC, Travis J, Barr P. Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. J Biol Chem 1995: 270: 1007-1010.
    • (1995) J Biol Chem , vol.270 , pp. 1007-1010
    • Pavloff, N.1    Potempa, J.2    Pike, N.R.3    Prochazka, V.4    Kiefer, M.C.5    Travis, J.6    Barr, P.7
  • 274
    • 0031018358 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Porphyromonas gingivalis Lysgingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases
    • Pavloff N, Pemberton PA, Potempa J, Chen WCA, Pike NR, Prochazka V, Kiefer MC, Travis J, Barr P. Molecular cloning and characterization of Porphyromonas gingivalis Lysgingipain. A new member of an emerging family of pathogenic bacterial cysteine proteinases. J Biol Chem 1997: 272: 1595-1600.
    • (1997) J Biol Chem , vol.272 , pp. 1595-1600
    • Pavloff, N.1    Pemberton, P.A.2    Potempa, J.3    Chen, W.C.A.4    Pike, N.R.5    Prochazka, V.6    Kiefer, M.C.7    Travis, J.8    Barr, P.9
  • 276
    • 0025876725 scopus 로고
    • Defective polymorphonuclear leukocyte formyl peptide receptor(s) in juvenile periodontitis
    • Perez HD, Kelly E, Elfman F, Armitage G, Winkler J. Defective polymorphonuclear leukocyte formyl peptide receptor(s) in juvenile periodontitis. J Clin Invest 1991: 87: 971-976.
    • (1991) J Clin Invest , vol.87 , pp. 971-976
    • Perez, H.D.1    Kelly, E.2    Elfman, F.3    Armitage, G.4    Winkler, J.5
  • 277
    • 0028013159 scopus 로고
    • Lysine- and arginine-specific proteinases from Porphyromonas gingivalis: Isolation and evidence for the existence of complexes with hemagglutinins
    • Pike R, McGraw W, Potempa J, Travis J. Lysine-and arginine-specific proteinases from Porphyromonas gingivalis: isolation and evidence for the existence of complexes with hemagglutinins. J Biol Chem 1994: 269: 406-411.
    • (1994) J Biol Chem , vol.269 , pp. 406-411
    • Pike, R.1    McGraw, W.2    Potempa, J.3    Travis, J.4
  • 278
    • 0029913412 scopus 로고    scopus 로고
    • Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis
    • Pike RN, Potempa J, McGraw W, Coetzer HT, Travis J. Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis. J Bacteriol 1996: 178: 2876-2882.
    • (1996) J Bacteriol , vol.178 , pp. 2876-2882
    • Pike, R.N.1    Potempa, J.2    McGraw, W.3    Coetzer, H.T.4    Travis, J.5
  • 279
    • 0028873378 scopus 로고
    • Influence of inflammatory bowel-disease on the distribution and concentration of pancreatic secretory trypsin-inhibitor within the colon
    • Playford RJ, Hanby AM, Patel K, Calam J. Influence of inflammatory bowel-disease on the distribution and concentration of pancreatic secretory trypsin-inhibitor within the colon. Am J Pathol 1993: 146: 310-316.
    • (1993) Am J Pathol , vol.146 , pp. 310-316
    • Playford, R.J.1    Hanby, A.M.2    Patel, K.3    Calam, J.4
  • 280
    • 0032212994 scopus 로고    scopus 로고
    • Membrane-type metalloproteinases in tumor invasion
    • Polette M, Birembaut P. Membrane-type metalloproteinases in tumor invasion. Int J Biochem Cell Biol 1998: 30: 1195-1202.
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 1195-1202
    • Polette, M.1    Birembaut, P.2
  • 281
    • 0030338378 scopus 로고    scopus 로고
    • Porphyromonas gingivalis proteinases in periodontitis, a review
    • Potempa J, Travis J. Porphyromonas gingivalis proteinases in periodontitis, a review. Acta Biochim Pol 1996: 43: 455-465.
    • (1996) Acta Biochim Pol , vol.43 , pp. 455-465
    • Potempa, J.1    Travis, J.2
  • 282
    • 0023031993 scopus 로고
    • 1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • 1-proteinase inhibitor by proteinases from Staphylococcus aureus. J Biol Chem 1986: 261: 14330-14334.
    • (1986) J Biol Chem , vol.261 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 283
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J. The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J Biol Chem 1994: 269: 15957-15960.
    • (1994) J Biol Chem , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 284
    • 0028885730 scopus 로고
    • Porphyromonas gingivalis: A proteinase/gene accounting audit
    • Potempa J, Pavloff N, Travis J. Porphyromonas gingivalis: a proteinase/gene accounting audit. Trends Microbiol 1995: 3: 430-434.
    • (1995) Trends Microbiol , vol.3 , pp. 430-434
    • Potempa, J.1    Pavloff, N.2    Travis, J.3
  • 285
    • 0028942506 scopus 로고
    • The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
    • Potempa J, Pike R, Travis J. The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain. Infect Immun 1995: 63: 1176-1182.
    • (1995) Infect Immun , vol.63 , pp. 1176-1182
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 286
    • 34249772781 scopus 로고
    • Host and Porphyromonas gingivalis proteinases in periodontitis: A biochemical model of infection and tissue destruction
    • Potempa J, Pike R, Travis J. Host and Porphyromonas gingivalis proteinases in periodontitis: a biochemical model of infection and tissue destruction. Prospect Drug Discovery Design 1995: 2: 445-458.
    • (1995) Prospect Drug Discovery Design , vol.2 , pp. 445-458
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 287
    • 0031008093 scopus 로고    scopus 로고
    • Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes
    • Potempa J, Pike R, Travis J. Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes. Biol Chem 1997: 378: 223-230.
    • (1997) Biol Chem , vol.378 , pp. 223-230
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 288
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipain Rs), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa I, Mikolajczyk-Pawlinska J, Brassel D, Nelson D, Thogersen IB, Enghild JJ, Travis J. Comparative properties of two cysteine proteinases (gingipain Rs), the products of two related but individual genes of Porphyromonas gingivalis. J Biol Chem 1998: 273: 21648-21657.
    • (1998) J Biol Chem , vol.273 , pp. 21648-21657
    • Potempa, I.1    Mikolajczyk-Pawlinska, J.2    Brassel, D.3    Nelson, D.4    Thogersen, I.B.5    Enghild, J.J.6    Travis, J.7
  • 289
    • 0002491655 scopus 로고    scopus 로고
    • Gingipain R and gingipain K
    • Barrett AJ, Rawlings ND, Woessner F, ed. Amsterdam: Academic Press
    • Potempa J, Travis J. Gingipain R and gingipain K. In: Barrett AJ, Rawlings ND, Woessner F, ed. Handbook on proteinases. Amsterdam: Academic Press, 1998: 762-768.
    • (1998) Handbook on Proteinases , pp. 762-768
    • Potempa, J.1    Travis, J.2
  • 290
    • 0025256081 scopus 로고
    • Interaction of heparin cofactor II with neutrophil elastase and cathepsin G
    • Pratt CW, Tobin RB, Church FC. Interaction of heparin cofactor II with neutrophil elastase and cathepsin G. J Biol Chem 1990: 265: 6092-6097.
    • (1990) J Biol Chem , vol.265 , pp. 6092-6097
    • Pratt, C.W.1    Tobin, R.B.2    Church, F.C.3
  • 291
    • 0021114931 scopus 로고
    • The physical significance of Km in the prothrombinase reaction
    • Pusey ML, Nelsestuen GL. The physical significance of Km in the prothrombinase reaction. Biochem Biophys Res Commun 1983: 114: 526-532.
    • (1983) Biochem Biophys Res Commun , vol.114 , pp. 526-532
    • Pusey, M.L.1    Nelsestuen, G.L.2
  • 292
    • 0025614975 scopus 로고
    • Isolation and characterization of the Treponema denticola prtA gene coding for the chymotrypsinlike protease activity and detection of closely linked gene encoding PZ-PLGPA-hydrolyzing activity
    • Que XC, Kuramitsu HK. Isolation and characterization of the Treponema denticola prtA gene coding for the chymotrypsinlike protease activity and detection of closely linked gene encoding PZ-PLGPA-hydrolyzing activity. Infect Immun 1990: 58: 4099-4105.
    • (1990) Infect Immun , vol.58 , pp. 4099-4105
    • Que, X.C.1    Kuramitsu, H.K.2
  • 294
    • 0031036570 scopus 로고    scopus 로고
    • The prpR1 and the prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes
    • Rangarajan M, Aduse-Opoku J, Slanet JM, Young KA, Curtis MA. The prpR1 and the prR2 arginine-specific protease genes of Porphyromonas gingivalis W50 produce five biochemically distinct enzymes. Mol Microbiol 1997: 23: 855-965.
    • (1997) Mol Microbiol , vol.23 , pp. 855-965
    • Rangarajan, M.1    Aduse-Opoku, J.2    Slanet, J.M.3    Young, K.A.4    Curtis, M.A.5
  • 295
    • 0030925556 scopus 로고    scopus 로고
    • Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor
    • Rangarajan M, Smith SJ, U S, Curtis MA. Biochemical characterization of the arginine-specific proteases of Porphyromonas gingivalis W50 suggests a common precursor. Biochem J 1997: 323: 701-709.
    • (1997) Biochem J , vol.323 , pp. 701-709
    • Rangarajan, M.1    Smith, S.J.2    U., S.3    Curtis, M.A.4
  • 296
    • 0032052598 scopus 로고    scopus 로고
    • Synergistic interactions of bradykinin, thrombin, interleukin 1 and tumor necrosis factor on prostanoid biosynthesis in human periodontal-ligament cells
    • Ransjo M, Marklund M, Persson M, Lerner UH. Synergistic interactions of bradykinin, thrombin, interleukin 1 and tumor necrosis factor on prostanoid biosynthesis in human periodontal-ligament cells. Arch Oral Biol 1998: 43: 253-260.
    • (1998) Arch Oral Biol , vol.43 , pp. 253-260
    • Ransjo, M.1    Marklund, M.2    Persson, M.3    Lerner, U.H.4
  • 297
  • 298
    • 0029310597 scopus 로고
    • Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease
    • Ries C, Petrides PE. Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease. Biol Chem Hoppe Seyler 1995: 376: 345-355.
    • (1995) Biol Chem Hoppe Seyler , vol.376 , pp. 345-355
    • Ries, C.1    Petrides, P.E.2
  • 300
    • 0031824976 scopus 로고    scopus 로고
    • An aminopeptidase nutritionally important to Fusobacterium nucleatum
    • Rogers AH, Gunadi A, Gully NJ, Zilm PS. An aminopeptidase nutritionally important to Fusobacterium nucleatum. Microbiology 1998: 144: 1807-1813.
    • (1998) Microbiology , vol.144 , pp. 1807-1813
    • Rogers, A.H.1    Gunadi, A.2    Gully, N.J.3    Zilm, P.S.4
  • 302
    • 0029394815 scopus 로고
    • Elevated conversion of alpha-2-macroglobulin to the complexed form in gingival crevicular fluid from adult periodontitis patients
    • Rosin M, Benjamin P, Rogers P, Gibson M, Van Leuven F, Johnson NW, Curtis M. Elevated conversion of alpha-2-macroglobulin to the complexed form in gingival crevicular fluid from adult periodontitis patients. J Periodontal Res 1995: 30: 436-444.
    • (1995) J Periodontal Res , vol.30 , pp. 436-444
    • Rosin, M.1    Benjamin, P.2    Rogers, P.3    Gibson, M.4    Van Leuven, F.5    Johnson, N.W.6    Curtis, M.7
  • 303
    • 0030781216 scopus 로고    scopus 로고
    • Cloning, expression and sequencing of a protease gene from Bacteroides forsythus ATCC 43037
    • Saito T, Ishihara K, Kato T, Okuda K. Cloning, expression and sequencing of a protease gene from Bacteroides forsythus ATCC 43037. Infect Immun 1997: 65: 4888-4891.
    • (1997) Infect Immun , vol.65 , pp. 4888-4891
    • Saito, T.1    Ishihara, K.2    Kato, T.3    Okuda, K.4
  • 304
    • 0029943570 scopus 로고    scopus 로고
    • Bradykinin generation triggered by Pseudomonas proteases facilitates invasion of the systemic circulation by Pseudomonas aeruginosa
    • Sakata Y, Akaike T, Suga M, Ijiri S, Ando M, Maeda H. Bradykinin generation triggered by Pseudomonas proteases facilitates invasion of the systemic circulation by Pseudomonas aeruginosa. Microbiol Immunol 1996: 40: 415-423.
    • (1996) Microbiol Immunol , vol.40 , pp. 415-423
    • Sakata, Y.1    Akaike, T.2    Suga, M.3    Ijiri, S.4    Ando, M.5    Maeda, H.6
  • 305
    • 0021171446 scopus 로고
    • Isolation and characterization of thrombomodulin from human placenta
    • Salem HH, Maruyama I, Ishii H, Majerus PW. Isolation and characterization of thrombomodulin from human placenta. J Biol Chem 1984: 259: 12246-12251.
    • (1984) J Biol Chem , vol.259 , pp. 12246-12251
    • Salem, H.H.1    Maruyama, I.2    Ishii, H.3    Majerus, P.W.4
  • 306
    • 0031973470 scopus 로고    scopus 로고
    • Serial alternations of glomerular matrix-degrading metalloproteinase activity in antithymocyte-induced glomerulonephritis in rats
    • Sato Y, Fujimoto S, Eto T. Serial alternations of glomerular matrix-degrading metalloproteinase activity in antithymocyte-induced glomerulonephritis in rats. Nephron 1998: 72: 195-200.
    • (1998) Nephron , vol.72 , pp. 195-200
    • Sato, Y.1    Fujimoto, S.2    Eto, T.3
  • 307
    • 0023885740 scopus 로고
    • The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system
    • Schenkein HA. The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system. J Periodontal Res 1988: 23: 187-192.
    • (1988) J Periodontal Res , vol.23 , pp. 187-192
    • Schenkein, H.A.1
  • 308
    • 0024564504 scopus 로고
    • Failure of Bacteroides gingivalis W83 to accumulate bound C3 following opsonization with serum
    • Schenkein HA. Failure of Bacteroides gingivalis W83 to accumulate bound C3 following opsonization with serum. J Periodontal Res 1989: 24: 20-27.
    • (1989) J Periodontal Res , vol.24 , pp. 20-27
    • Schenkein, H.A.1
  • 309
    • 0026202116 scopus 로고
    • Complement factor D-like activity of Porphyromonas gingivalis W83
    • Schenkein HA. Complement factor D-like activity of Porphyromonas gingivalis W83. Oral Microbiol Immunol 1991: 6: 216-220.
    • (1991) Oral Microbiol Immunol , vol.6 , pp. 216-220
    • Schenkein, H.A.1
  • 310
    • 0028521267 scopus 로고
    • Early-onset periodontitis: Systemic aspects of etiology and pathogenesis
    • Schenkein HA, Van Dyke TE. Early-onset periodontitis: systemic aspects of etiology and pathogenesis. Periodontol 2000 1994: 6: 7-25.
    • (1994) Periodontol 2000 , vol.6 , pp. 7-25
    • Schenkein, H.A.1    Van Dyke, T.E.2
  • 311
    • 0029013679 scopus 로고
    • Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins
    • Schenkein HA, Fletcher HM, Bodnar M, Macrina FL. Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins. J Immunol 1995: 154: 5331-5337.
    • (1995) J Immunol , vol.154 , pp. 5331-5337
    • Schenkein, H.A.1    Fletcher, H.M.2    Bodnar, M.3    Macrina, F.L.4
  • 312
    • 0018464356 scopus 로고
    • Relationship of bacteremia to toothbrushing in clinically healthy patients
    • Sconyers JR, Albers DD, Kelly R. Relationship of bacteremia to toothbrushing in clinically healthy patients. Gen Dent 1979: 27: 51-52.
    • (1979) Gen Dent , vol.27 , pp. 51-52
    • Sconyers, J.R.1    Albers, D.D.2    Kelly, R.3
  • 313
    • 0027413558 scopus 로고
    • Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen
    • Scott CF, Whitaker EJ, Hammond BF, Colman RW. Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen. J Biol Chem 1993: 268: 7935-79342.
    • (1993) J Biol Chem , vol.268 , pp. 7935-79342
    • Scott, C.F.1    Whitaker, E.J.2    Hammond, B.F.3    Colman, R.W.4
  • 314
    • 0033068080 scopus 로고    scopus 로고
    • Targeted disruption of fibronectin-integrin interactions in human gingival fibroblasts by the RI protease of Porphyromonas gingivalis W50
    • Scragg MA, Cannon SJ, Rangarajan M, Williams DM, Curtis MA. Targeted disruption of fibronectin-integrin interactions in human gingival fibroblasts by the RI protease of Porphyromonas gingivalis W50. Infect Immun 1999: 67: 1837-1843.
    • (1999) Infect Immun , vol.67 , pp. 1837-1843
    • Scragg, M.A.1    Cannon, S.J.2    Rangarajan, M.3    Williams, D.M.4    Curtis, M.A.5
  • 315
    • 0027328927 scopus 로고
    • Treatment of ulcerative-colitis with camostat mesilate a serine-protease inhibitor
    • Senda S, Fujiyama Y, Bamba T, Hosoda S. Treatment of ulcerative-colitis with camostat mesilate a serine-protease inhibitor. Intern Med 1993: 32: 350-354.
    • (1993) Intern Med , vol.32 , pp. 350-354
    • Senda, S.1    Fujiyama, Y.2    Bamba, T.3    Hosoda, S.4
  • 316
    • 0023860712 scopus 로고
    • Immunohistological analysis of experimental gingivitis in humans
    • Seymour GJ, Gemmell E, Walsh LJ, Powell RN. Immunohistological analysis of experimental gingivitis in humans. Clin Exp Immunol 1988: 71: 132-137.
    • (1988) Clin Exp Immunol , vol.71 , pp. 132-137
    • Seymour, G.J.1    Gemmell, E.2    Walsh, L.J.3    Powell, R.N.4
  • 317
    • 0027689798 scopus 로고
    • Immunopathogenesis of chronic inflammatory periodontal disease: Cellular and molecular mechanisms
    • Seymour GJ, Gemmell E, Reinhardt RA, Eastcott J, Taubman MA. Immunopathogenesis of chronic inflammatory periodontal disease: cellular and molecular mechanisms. J Periodontal Res 1993: 28: 478-486.
    • (1993) J Periodontal Res , vol.28 , pp. 478-486
    • Seymour, G.J.1    Gemmell, E.2    Reinhardt, R.A.3    Eastcott, J.4    Taubman, M.A.5
  • 318
    • 0024623692 scopus 로고
    • Studies on the virulence properties and metabolism of pleiotropic mutants of Porphyromonas gingivalis (Bacteroides gingivalis) W50
    • Shah HN, Seddon SV, Gharbia SE. Studies on the virulence properties and metabolism of pleiotropic mutants of Porphyromonas gingivalis (Bacteroides gingivalis) W50. Oral Microbiol Immunol 1989: 4: 19-23.
    • (1989) Oral Microbiol Immunol , vol.4 , pp. 19-23
    • Shah, H.N.1    Seddon, S.V.2    Gharbia, S.E.3
  • 319
    • 0025074338 scopus 로고
    • Isolation and characterization of gingivain, a cysteine proteinase from Porphyromonas gingivalis strain W83
    • Shah HN, Gharbia SE, Kowlessur D, Wilkie E, Brocklehurst K. Isolation and characterization of gingivain, a cysteine proteinase from Porphyromonas gingivalis strain W83. Biochem Soc Trans 1990: 18: 578-579.
    • (1990) Biochem Soc Trans , vol.18 , pp. 578-579
    • Shah, H.N.1    Gharbia, S.E.2    Kowlessur, D.3    Wilkie, E.4    Brocklehurst, K.5
  • 320
    • 0026723949 scopus 로고
    • Evidence for independent molecular identity and functional interaction of the hemagglutinin and cysteine proteinase (gingivain) of Porphyromonas-gingivalis
    • Shah HN, Gharbia SE, Progulske-Fox A, Brocklehurst K. Evidence for independent molecular identity and functional interaction of the hemagglutinin and cysteine proteinase (gingivain) of Porphyromonas-gingivalis. J Med Microbiol 1992: 36: 239-244.
    • (1992) J Med Microbiol , vol.36 , pp. 239-244
    • Shah, H.N.1    Gharbia, S.E.2    Progulske-Fox, A.3    Brocklehurst, K.4
  • 321
    • 0033580821 scopus 로고    scopus 로고
    • Genetic analyses of proteolysis, hemoglobin finding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA
    • Shi Y, Ratnayake DB, Okamoto K, Abe N, Yamamoto K, Nakayama K. Genetic analyses of proteolysis, hemoglobin finding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA. J Biol Chem 1999: 274: 17955-17960.
    • (1999) J Biol Chem , vol.274 , pp. 17955-17960
    • Shi, Y.1    Ratnayake, D.B.2    Okamoto, K.3    Abe, N.4    Yamamoto, K.5    Nakayama, K.6
  • 322
    • 0033582413 scopus 로고    scopus 로고
    • Determination and characterization of the hemagglutinin-associated short motifs found in Porphyromonas gingivalis gene products
    • Shibata Y, Hayakawa M, Takiguchi H, Shiroza T, Abiko Y. Determination and characterization of the hemagglutinin-associated short motifs found in Porphyromonas gingivalis gene products. J Biol Chem 1999: 274: 5012-5020.
    • (1999) J Biol Chem , vol.274 , pp. 5012-5020
    • Shibata, Y.1    Hayakawa, M.2    Takiguchi, H.3    Shiroza, T.4    Abiko, Y.5
  • 323
    • 0027163688 scopus 로고
    • Purification and partial characterization of an elastolytic serine protease of Prevotella intermedia
    • Shibata Y, Fujimura S, Nakamura T. Purification and partial characterization of an elastolytic serine protease of Prevotella intermedia. Appl Environ Microbiol 1993: 59: 2107-2111.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2107-2111
    • Shibata, Y.1    Fujimura, S.2    Nakamura, T.3
  • 324
    • 0017383101 scopus 로고
    • Experimental transient bacteraemias in human subjects with varying degrees of plaque accumulation and gingival inflammation
    • Silver JG, Martin AW, McBride BC. Experimental transient bacteraemias in human subjects with varying degrees of plaque accumulation and gingival inflammation. J Clin Periodontol 1977: 4: 92-99.
    • (1977) J Clin Periodontol , vol.4 , pp. 92-99
    • Silver, J.G.1    Martin, A.W.2    McBride, B.C.3
  • 325
    • 0018373827 scopus 로고
    • Experimental transient bacteraemias in human subjects with clinically healthy gingivae
    • Silver JG, Martin AW, McBride BC. Experimental transient bacteraemias in human subjects with clinically healthy gingivae. J Clin Periodontol 1979: 6: 33-36.
    • (1979) J Clin Periodontol , vol.6 , pp. 33-36
    • Silver, J.G.1    Martin, A.W.2    McBride, B.C.3
  • 326
    • 0031800218 scopus 로고    scopus 로고
    • Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesion-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes
    • Slakeski N, Bhogal PS, O'Brien-Simpson NM, Reynolds EC. Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesion-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes. Microbiology 1998: 144: 1583-1592.
    • (1998) Microbiology , vol.144 , pp. 1583-1592
    • Slakeski, N.1    Bhogal, P.S.2    O'Brien-Simpson, N.M.3    Reynolds, E.C.4
  • 327
    • 0033121176 scopus 로고    scopus 로고
    • Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins
    • Slakeski N, Cleal SM, Bhogal PS, Reynolds EC. Characterization of a Porphyromonas gingivalis gene prtK that encodes a lysine-specific cysteine proteinase and three sequence-related adhesins. Oral Microbiol Immunol 1999: 14: 92-97.
    • (1999) Oral Microbiol Immunol , vol.14 , pp. 92-97
    • Slakeski, N.1    Cleal, S.M.2    Bhogal, P.S.3    Reynolds, E.C.4
  • 328
    • 0023674920 scopus 로고
    • The degradation of type I collagen and human plasma fibronectin by the trypsin-like enzyme and extracellular membrane vesicles of Bacteroides gingivalis W50
    • Smalley JW, Birss AJ, Shuttleworth CA. The degradation of type I collagen and human plasma fibronectin by the trypsin-like enzyme and extracellular membrane vesicles of Bacteroides gingivalis W50. Arch Oral Biol 1988: 33: 323-329.
    • (1988) Arch Oral Biol , vol.33 , pp. 323-329
    • Smalley, J.W.1    Birss, A.J.2    Shuttleworth, C.A.3
  • 329
    • 0026426028 scopus 로고
    • Haemin-restriction influences haemin-binding, haemagglutination and protease activity of cells and extracellular membrane vesicles of Porphyromonas gingivalis W50
    • Smalley JW, Birss AJ, McKee AS, Marsh PD. Haemin-restriction influences haemin-binding, haemagglutination and protease activity of cells and extracellular membrane vesicles of Porphyromonas gingivalis W50. FEMS Microbiol Lett 1991: 69: 63-67.
    • (1991) FEMS Microbiol Lett , vol.69 , pp. 63-67
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 330
    • 0027358741 scopus 로고
    • Haemin-binding proteins of Porphyromonas gingivalis W50 grown in a chemostat under haemin-limitation
    • Smalley JW, Birss AJ, McKee AS, Marsh PD. Haemin-binding proteins of Porphyromonas gingivalis W50 grown in a chemostat under haemin-limitation. J Gen Microbiol 1993: 139: 2145-2150.
    • (1993) J Gen Microbiol , vol.139 , pp. 2145-2150
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 331
    • 0030586255 scopus 로고    scopus 로고
    • Haemin binding as a factor in the virulence of Porphyromonas gingivalis
    • Smalley JW, Birss AJ, McKee AS, Marsh PD. Haemin binding as a factor in the virulence of Porphyromonas gingivalis. FEMS Microbiol Lett 1996: 141: 65-70.
    • (1996) FEMS Microbiol Lett , vol.141 , pp. 65-70
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 332
    • 0027158451 scopus 로고
    • Purification and characterization of a protease from Porphyromonas gingivalis capable of degrading salt-solubilized collagen
    • Sojar HT, Lee JY, Bedi GS, Genco RJ. Purification and characterization of a protease from Porphyromonas gingivalis capable of degrading salt-solubilized collagen. Infect Immun 1993: 61: 2369-2376.
    • (1993) Infect Immun , vol.61 , pp. 2369-2376
    • Sojar, H.T.1    Lee, J.Y.2    Bedi, G.S.3    Genco, R.J.4
  • 333
    • 0026495127 scopus 로고
    • Identification of proteases from periodontopathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases
    • Sorsa T, Ingman T, Suomalainen K, Haapasalo M, Konttinen YT, Lindy O, Saari H, Uitto VJ. Identification of proteases from periodontopathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases. Infect Immun 1992: 60: 4491-5492.
    • (1992) Infect Immun , vol.60 , pp. 4491-5492
    • Sorsa, T.1    Ingman, T.2    Suomalainen, K.3    Haapasalo, M.4    Konttinen, Y.T.5    Lindy, O.6    Saari, H.7    Uitto, V.J.8
  • 334
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: Common themes and variations in architecture and assembly
    • Soto GE, Hultgren SJ. Bacterial adhesins: common themes and variations in architecture and assembly. J Bacteriol 1999: 181: 1059-1071.
    • (1999) J Bacteriol , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 335
    • 0022904908 scopus 로고
    • Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake)
    • Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J. Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake). J Biol Chem 1986: 261: 13258-13267.
    • (1986) J Biol Chem , vol.261 , pp. 13258-13267
    • Speijer, H.1    Govers-Riemslag, J.W.2    Zwaal, R.F.3    Rosing, J.4
  • 336
    • 0029416989 scopus 로고
    • Capnocytophaga gingivalis aminopeptidase: A potential virulence factor
    • Spratt DA, Greenman J, Schaffer AG. Capnocytophaga gingivalis aminopeptidase: a potential virulence factor. Microbiology 1995: 141: 3087-3093.
    • (1995) Microbiology , vol.141 , pp. 3087-3093
    • Spratt, D.A.1    Greenman, J.2    Schaffer, A.G.3
  • 337
    • 0029903248 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor invasion: From correlation and causality to the clinic
    • Stetler-Stevenson WG, Hewitt R, Corcoran M. Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic. Semin Cancer Biol 1996: 7: 147-154.
    • (1996) Semin Cancer Biol , vol.7 , pp. 147-154
    • Stetler-Stevenson, W.G.1    Hewitt, R.2    Corcoran, M.3
  • 338
    • 84985825807 scopus 로고
    • Degradation in vivo of the C3 protein of guinea-pig complement by a pathogenic strain of Bacteroides gingivalis
    • Sundqvist GK, Carlsson J, Herrmann BF, Hofling JF, Vaatainen A. Degradation in vivo of the C3 protein of guinea-pig complement by a pathogenic strain of Bacteroides gingivalis. Scand J Dent Res 1984: 92: 14-24.
    • (1984) Scand J Dent Res , vol.92 , pp. 14-24
    • Sundqvist, G.K.1    Carlsson, J.2    Herrmann, B.F.3    Hofling, J.F.4    Vaatainen, A.5
  • 339
    • 0021924980 scopus 로고
    • Degradation of human immunoglobulins G and M and complement factors C3 and C5 by black-pigmented Bacteroides
    • Sundqvist G, Carlsson J, Herrmann B, Tarnvik A. Degradation of human immunoglobulins G and M and complement factors C3 and C5 by black-pigmented Bacteroides. J Med Microbiol 1985: 19: 85-94.
    • (1985) J Med Microbiol , vol.19 , pp. 85-94
    • Sundqvist, G.1    Carlsson, J.2    Herrmann, B.3    Tarnvik, A.4
  • 340
  • 342
    • 0027198962 scopus 로고
    • Changes in complement and immunoglobulin G receptor expression on neutrophils associated with Porphyromonas gingivalis-induced inhibition of phagocytosis
    • Tai H, Kobayashi T, Hara K. Changes in complement and immunoglobulin G receptor expression on neutrophils associated with Porphyromonas gingivalis-induced inhibition of phagocytosis. Infect Immun 1993: 61: 3533-5353.
    • (1993) Infect Immun , vol.61 , pp. 3533-5353
    • Tai, H.1    Kobayashi, T.2    Hara, K.3
  • 343
    • 0026425927 scopus 로고
    • Isolation and preliminary characterization of the Porphyromonas gingivalis prtC gene expressing collagenase activity
    • Takahashi N, Kato T, Kuramitsu HK. Isolation and preliminary characterization of the Porphyromonas gingivalis prtC gene expressing collagenase activity. FEMS Microbiol Lett 1991: 68: 135-138.
    • (1991) FEMS Microbiol Lett , vol.68 , pp. 135-138
    • Takahashi, N.1    Kato, T.2    Kuramitsu, H.K.3
  • 344
  • 346
    • 0022389597 scopus 로고
    • Purification and properties of a prothrombin activator from the venom of Notechis scutatus scutatus
    • Tans G, Govers-Riemslag JW, van Rijn JL, Rosing J. Purification and properties of a prothrombin activator from the venom of Notechis scutatus scutatus. J Biol Chem 1985: 260: 9366-9372.
    • (1985) J Biol Chem , vol.260 , pp. 9366-9372
    • Tans, G.1    Govers-Riemslag, J.W.2    Van Rijn, J.L.3    Rosing, J.4
  • 347
    • 0002823788 scopus 로고
    • Resistance of bacteria to complement
    • Roth JA, Bolin CA, Brogden KA, Minion FS, Wannemuehler MJ, ed. Washington, DC: ASM Press
    • Taylor PW. Resistance of bacteria to complement. In: Roth JA, Bolin CA, Brogden KA, Minion FS, Wannemuehler MJ, ed. Virulence mechanisms of bacterial pathogens. Washington, DC: ASM Press, 1995: 49-64.
    • (1995) Virulence Mechanisms of Bacterial Pathogens , pp. 49-64
    • Taylor, P.W.1
  • 350
    • 0029847260 scopus 로고    scopus 로고
    • Role of the Porphyromonas gingivalis protease activity in colonization of oral surfaces
    • Tokuda M, Duncan M, Cho MI, Kuramitsu HK. Role of the Porphyromonas gingivalis protease activity in colonization of oral surfaces. Infect Immun 1996: 64: 4067-4073.
    • (1996) Infect Immun , vol.64 , pp. 4067-4073
    • Tokuda, M.1    Duncan, M.2    Cho, M.I.3    Kuramitsu, H.K.4
  • 351
    • 0032443225 scopus 로고    scopus 로고
    • Regulation of protease expression in Porphyromonas gingivalis
    • Tokuda M, Chen W, Karunakaran T, Kuramitsu HK. Regulation of protease expression in Porphyromonas gingivalis. Infect Immun 1998: 66: 5232-5237.
    • (1998) Infect Immun , vol.66 , pp. 5232-5237
    • Tokuda, M.1    Chen, W.2    Karunakaran, T.3    Kuramitsu, H.K.4
  • 352
    • 0028142785 scopus 로고
    • Localized expression of mRNA for phagocyte-specific chemotactic cytokines in human periodontal infections
    • Tonetti MS, Imboden MA, Gerber L, Lang NP, Laissue J, Mueller C. Localized expression of mRNA for phagocyte-specific chemotactic cytokines in human periodontal infections. Infect Immun 1994: 62: 4005-4014.
    • (1994) Infect Immun , vol.62 , pp. 4005-4014
    • Tonetti, M.S.1    Imboden, M.A.2    Gerber, L.3    Lang, N.P.4    Laissue, J.5    Mueller, C.6
  • 354
    • 0023130990 scopus 로고
    • Purification and characterization of a protease from Bacteroides gingivalis 381
    • Tsutsui H, Kinouchi T, Wakano Y, Ohnishi Y. Purification and characterization of a protease from Bacteroides gingivalis 381. Infect Immun 1987: 55: 420-427.
    • (1987) Infect Immun , vol.55 , pp. 420-427
    • Tsutsui, H.1    Kinouchi, T.2    Wakano, Y.3    Ohnishi, Y.4
  • 355
    • 0023791265 scopus 로고
    • Isolation of a chymotrypsinlike enzyme from Treponema denticola
    • Uitto VJ, Grenier D, Chan EC, McBride BC. Isolation of a chymotrypsinlike enzyme from Treponema denticola. Infect Immun 1988: 56: 2717-2722.
    • (1988) Infect Immun , vol.56 , pp. 2717-2722
    • Uitto, V.J.1    Grenier, D.2    Chan, E.C.3    McBride, B.C.4
  • 356
    • 0024533254 scopus 로고
    • A protease of Bacteroides gingivalis degrades cell surface and matrix glycoproteins of cultured gingival fibroblasts and induces secretion of collagenase and plasminogen activator
    • Uitto VJ, Larjava H, Heino J, Sorsa T. A protease of Bacteroides gingivalis degrades cell surface and matrix glycoproteins of cultured gingival fibroblasts and induces secretion of collagenase and plasminogen activator. Infect Immun 1989: 57: 213-218.
    • (1989) Infect Immun , vol.57 , pp. 213-218
    • Uitto, V.J.1    Larjava, H.2    Heino, J.3    Sorsa, T.4
  • 357
    • 0025349101 scopus 로고
    • Salivary collagenase. Origin, characteristics and relationship to periodontal health
    • Uitto VJ, Suomalainen K, Sorsa T. Salivary collagenase. Origin, characteristics and relationship to periodontal health. J Periodontal Res 1990: 25: 135-142.
    • (1990) J Periodontal Res , vol.25 , pp. 135-142
    • Uitto, V.J.1    Suomalainen, K.2    Sorsa, T.3
  • 358
    • 0029112596 scopus 로고
    • Cytopathic effects of Treponema denticola chymotrypsin-like proteinase on migrating and stratified epithelial cells
    • Uittp VJ, Pan YM, Leung WK, Larjava H, Ellen RP, Finlay BB, McBride BC. Cytopathic effects of Treponema denticola chymotrypsin-like proteinase on migrating and stratified epithelial cells. Infect Immun 1995: 63: 3401-3410.
    • (1995) Infect Immun , vol.63 , pp. 3401-3410
    • Uittp, V.J.1    Pan, Y.M.2    Leung, W.K.3    Larjava, H.4    Ellen, R.P.5    Finlay, B.B.6    McBride, B.C.7
  • 361
    • 0022109396 scopus 로고
    • Reaction of human sera from juvenile periodontitis, rapidly progressive periodontitis, and adult periodontitis patients with selected periodontopathogens
    • Vincent AV, Suzuki JB, Falkler WA Jr, Cornett WC. Reaction of human sera from juvenile periodontitis, rapidly progressive periodontitis, and adult periodontitis patients with selected periodontopathogens. J Periodontol 1985: 56: 464-169.
    • (1985) J Periodontol , vol.56 , pp. 464-1169
    • Vincent, A.V.1    Suzuki, J.B.2    Falkler Jr., W.A.3    Cornett, W.C.4
  • 362
    • 0033111019 scopus 로고    scopus 로고
    • Purification and characterization of a trypsin-like protease from the culture supernatant of Actinobacillus actinomycetemcomitans Y4
    • Wang PL, Shirasu S, Shinohara M, Daito M, Fujii T, Kowashi Y, Ohura K. Purification and characterization of a trypsin-like protease from the culture supernatant of Actinobacillus actinomycetemcomitans Y4. Eur J Oral Sci 1999: 107: 147-153.
    • (1999) Eur J Oral Sci , vol.107 , pp. 147-153
    • Wang, P.L.1    Shirasu, S.2    Shinohara, M.3    Daito, M.4    Fujii, T.5    Kowashi, Y.6    Ohura, K.7
  • 363
    • 0026847646 scopus 로고
    • Molecular cloning and expression of a major surface protein (the 75-kDa protein) of Porphyromonas (Bacteroides) gingivalis in Escherichia coli
    • Watanabe K, Takasawa T, Yoshimura F, Ozeki M, Kawanami M, Kato H. Molecular cloning and expression of a major surface protein (the 75-kDa protein) of Porphyromonas (Bacteroides) gingivalis in Escherichia coli. FEMS Microbiol Lett 1992: 71: 47-55.
    • (1992) FEMS Microbiol Lett , vol.71 , pp. 47-55
    • Watanabe, K.1    Takasawa, T.2    Yoshimura, F.3    Ozeki, M.4    Kawanami, M.5    Kato, H.6
  • 364
    • 0026643426 scopus 로고
    • Effect of a metalloproteinase inhibitor on established corneal ulcers after an alkali burn
    • Wentworth JS, Paterson CA, Gray RD. Effect of a metalloproteinase inhibitor on established corneal ulcers after an alkali burn. Invest Ophthamol Visual Sci 1992: 33: 2174-2179.
    • (1992) Invest Ophthamol Visual Sci , vol.33 , pp. 2174-2179
    • Wentworth, J.S.1    Paterson, C.A.2    Gray, R.D.3
  • 365
    • 0018242325 scopus 로고
    • Stimulation of endothelial cell prostacyclin production by thrombin, trypsin, and the ionophore A 23187
    • Weksler BB, Ley CW, Jaffe EA. Stimulation of endothelial cell prostacyclin production by thrombin, trypsin, and the ionophore A 23187. J Clin Invest 1978: 62: 923-930.
    • (1978) J Clin Invest , vol.62 , pp. 923-930
    • Weksler, B.B.1    Ley, C.W.2    Jaffe, E.A.3
  • 366
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb Z, Tremble PM, Behrendtsen O, Crowley E, Damsky CH. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J Cell Biol 1989: 109: 877-889.
    • (1989) J Cell Biol , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 367
    • 0027292986 scopus 로고
    • Bacterial proteins binding to the mammalian extracellular matrix
    • Westerlund B, Korhonen TK. Bacterial proteins binding to the mammalian extracellular matrix. Mol Microbiol 1993: 9: 687-694.
    • (1993) Mol Microbiol , vol.9 , pp. 687-694
    • Westerlund, B.1    Korhonen, T.K.2
  • 368
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J, Kahari VM. Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J 1999: 13: 781-792.
    • (1999) FASEB J , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.M.2
  • 369
    • 0026650853 scopus 로고
    • Serum immunoglobulin G antibody to Porphyromonas gingivalis in rapidly progressive periodontitis: Titer, avidity, and subclass distribution
    • Whitney C, Ant J, Moncla B, Johnson B, Page RC, Engel D. Serum immunoglobulin G antibody to Porphyromonas gingivalis in rapidly progressive periodontitis: titer, avidity, and subclass distribution. Infect Immun 1992: 60: 2194-2200.
    • (1992) Infect Immun , vol.60 , pp. 2194-2200
    • Whitney, C.1    Ant, J.2    Moncla, B.3    Johnson, B.4    Page, R.C.5    Engel, D.6
  • 370
    • 0022644002 scopus 로고
    • Ability of oral bacteria to degrade fibronectin
    • Wikström M, Linde A. Ability of oral bacteria to degrade fibronectin. Infect Immun 1986: 51: 707-711.
    • (1986) Infect Immun , vol.51 , pp. 707-711
    • Wikström, M.1    Linde, A.2
  • 371
    • 0028219412 scopus 로고
    • Detection of Porphyromonas gingivalis in gingival exudate by a dipeptide-enhanced trypsin-like activity
    • Wikström M, Potempa J, Polanowski A, Travis J, Renvert S. Detection of Porphyromonas gingivalis in gingival exudate by a dipeptide-enhanced trypsin-like activity. J Periodontol 1994: 65: 47-55.
    • (1994) J Periodontol , vol.65 , pp. 47-55
    • Wikström, M.1    Potempa, J.2    Polanowski, A.3    Travis, J.4    Renvert, S.5
  • 372
    • 0031812582 scopus 로고    scopus 로고
    • Bacterial perturbation of cytokine networks
    • Wilson M, Seymour R, Henderson B. Bacterial perturbation of cytokine networks. Infect Immun 1998: 66: 2401-2409.
    • (1998) Infect Immun , vol.66 , pp. 2401-2409
    • Wilson, M.1    Seymour, R.2    Henderson, B.3
  • 373
    • 0026725842 scopus 로고
    • Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis
    • Wingrove JA, DiScipio RG, Chen Z, Potempa J, Travis J, Hugli TE. Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis. J Biol Chem 1992: 267: 18902-18907.
    • (1992) J Biol Chem , vol.267 , pp. 18902-18907
    • Wingrove, J.A.1    DiScipio, R.G.2    Chen, Z.3    Potempa, J.4    Travis, J.5    Hugli, T.E.6
  • 374
    • 0030330678 scopus 로고    scopus 로고
    • Structure and function of a novel arginine-specific cysteine proteinase (argingipain) as a major periodontal pathogenic factor from Porphyromonas gingivalis
    • Yamamoto K, Kadowaki T, Okamoto K, Yoneda M, Nakayama K, Misumi Y, Ikehara Y. Structure and function of a novel arginine-specific cysteine proteinase (argingipain) as a major periodontal pathogenic factor from Porphyromonas gingivalis. Adv Exp Med Biol 1996: 389: 33-42.
    • (1996) Adv Exp Med Biol , vol.389 , pp. 33-42
    • Yamamoto, K.1    Kadowaki, T.2    Okamoto, K.3    Yoneda, M.4    Nakayama, K.5    Misumi, Y.6    Ikehara, Y.7
  • 375
    • 0025122339 scopus 로고
    • Suppression of bactericidal activity of human polymorphonuclear leukocytes by Bacteroides gingivalis
    • Yoneda M, Maeda K, Aono M. Suppression of bactericidal activity of human polymorphonuclear leukocytes by Bacteroides gingivalis. Infect Immun 1990: 58: 406-411.
    • (1990) Infect Immun , vol.58 , pp. 406-411
    • Yoneda, M.1    Maeda, K.2    Aono, M.3
  • 376
    • 0021678531 scopus 로고
    • Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis
    • Yoshimura F, Takahashi K, Nodasaka Y, Suzuki T. Purification and characterization of a novel type of fimbriae from the oral anaerobe Bacteroides gingivalis. J Bacteriol 1984: 160: 949-957.
    • (1984) J Bacteriol , vol.160 , pp. 949-957
    • Yoshimura, F.1    Takahashi, K.2    Nodasaka, Y.3    Suzuki, T.4
  • 377
    • 0021154449 scopus 로고
    • Characterization of a trypsin-like protease from the bacterium Bacteroides gingivalis isolated from human dental plaque
    • Yoshimura F, Nishikata M, Suzuki T, Hoover CI, Newbrun E. Characterization of a trypsin-like protease from the bacterium Bacteroides gingivalis isolated from human dental plaque. Arch Oral Biol 1984: 29: 559-564.
    • (1984) Arch Oral Biol , vol.29 , pp. 559-564
    • Yoshimura, F.1    Nishikata, M.2    Suzuki, T.3    Hoover, C.I.4    Newbrun, E.5
  • 378
    • 0031114710 scopus 로고    scopus 로고
    • Secretion of IL-1β, TNF-α, IL-8 and IL-1ra by human polymorphonuclear leukocytes in response to Iipopolysaccharides from periodontopathic bacteria
    • Yoshimura A, Hara Y, Kaneko T, Kato I. Secretion of IL-1β, TNF-α, IL-8 and IL-1ra by human polymorphonuclear leukocytes in response to Iipopolysaccharides from periodontopathic bacteria. J Periodontal Res 1997: 32: 279-286.
    • (1997) J Periodontal Res , vol.32 , pp. 279-286
    • Yoshimura, A.1    Hara, Y.2    Kaneko, T.3    Kato, I.4
  • 379
    • 0032984684 scopus 로고    scopus 로고
    • Modulation of major histocompatibility complex protein expression by human gamma interferon mediated by cysteine proteinase-adhesin polyproteins of Porphyromonas gingivalis
    • Yun PL, DeCarlo AA, Hunter N. Modulation of major histocompatibility complex protein expression by human gamma interferon mediated by cysteine proteinase-adhesin polyproteins of Porphyromonas gingivalis. Infect Immun 1999: 67: 2986-2995.
    • (1999) Infect Immun , vol.67 , pp. 2986-2995
    • Yun, P.L.1    DeCarlo, A.A.2    Hunter, N.3
  • 381
    • 0033135922 scopus 로고    scopus 로고
    • IL-8 degradation by Porphyromonas gingivalis proteases
    • Zhang J, Dong H, Kashket S, Duncan MJ. IL-8 degradation by Porphyromonas gingivalis proteases. Microb Pathog 1999: 26: 275-280.
    • (1999) Microb Pathog , vol.26 , pp. 275-280
    • Zhang, J.1    Dong, H.2    Kashket, S.3    Duncan, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.