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Volumn 1477, Issue 1-2, 2000, Pages 35-50

Bacterial proteinases as targets for the development of second-generation antibiotics

Author keywords

Bacterial pathogen; Pathogenicity; Proteinase inhibitor; Proteolytic enzyme

Indexed keywords

CELL SURFACE RECEPTOR; PROTEINASE; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR;

EID: 0034615573     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00278-2     Document Type: Review
Times cited : (152)

References (145)
  • 1
    • 0030825663 scopus 로고    scopus 로고
    • The HIV protease and therapies for AIDS
    • Korant B.D., Rizzo C.J. The HIV protease and therapies for AIDS. Adv. Exp. Med. Biol. 421:1997;279-284.
    • (1997) Adv. Exp. Med. Biol. , vol.421 , pp. 279-284
    • Korant, B.D.1    Rizzo, C.J.2
  • 2
    • 0032580479 scopus 로고    scopus 로고
    • HIV-protease inhibitors
    • Flexner C. HIV-protease inhibitors. N. Engl. J. Med. 338:1998;1281-1292.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 1281-1292
    • Flexner, C.1
  • 3
    • 0016904389 scopus 로고
    • Peptides and micro-organisms
    • Payne J.W. Peptides and micro-organisms. Adv. Microb. Physiol. 13:1976;55-113.
    • (1976) Adv. Microb. Physiol. , vol.13 , pp. 55-113
    • Payne, J.W.1
  • 4
    • 0028783299 scopus 로고
    • Are bacterial proteinases pathogenic factors?
    • Travis J., Potempa J., Maeda H. Are bacterial proteinases pathogenic factors? Trends Microbiol. 3:1995;405-407.
    • (1995) Trends Microbiol. , vol.3 , pp. 405-407
    • Travis, J.1    Potempa, J.2    Maeda, H.3
  • 5
    • 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. 377:1996;217-226.
    • (1996) Biol. Chem. Hoppe Seyler , vol.377 , pp. 217-226
    • Maeda, H.1    Yamamoto, T.2
  • 6
    • 0029907110 scopus 로고    scopus 로고
    • Role of microbial proteases in pathogenesis
    • Maeda H. Role of microbial proteases in pathogenesis. Microbiol. Immunol. 40:1996;685-699.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 685-699
    • Maeda, H.1
  • 8
    • 0027076834 scopus 로고
    • Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics
    • Borth W. Alpha 2-macroglobulin, a multifunctional binding protein with targeting characteristics. FASEB J. 15:1992;3345-3353.
    • (1992) FASEB J. , vol.15 , pp. 3345-3353
    • Borth, W.1
  • 9
  • 10
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont R.J., Jenkinson H.F. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62:1998;1244-1263.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 11
    • 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. 3:1995;430-434.
    • (1995) Trends Microbiol. , vol.3 , pp. 430-434
    • Potempa, J.1    Pavloff, N.2    Travis, J.3
  • 12
    • 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. 43:1996;455-465.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 455-465
    • Potempa, J.1    Travis, J.2
  • 13
    • 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. 269:1994;15957-15960.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 14
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive-loop conformations by proteolytic cleavage
    • Chang W.S., Wardell M.R., Lomas D.A., Carrell R.W. Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314:1996;647-653.
    • (1996) Biochem. J. , vol.314 , pp. 647-653
    • Chang, W.S.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 16
    • 0028116127 scopus 로고
    • Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3
    • Pei D., Majmudar G., Weiss S.J. Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J. Biol. Chem. 269:1994;25849-25855.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25849-25855
    • Pei, D.1    Majmudar, G.2    Weiss, S.J.3
  • 17
    • 0025991867 scopus 로고
    • Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity
    • Desrochers P.E., Jeffrey J.J., Weiss S.J. Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity. J. Clin. Invest. 87:1991;2258-2265.
    • (1991) J. Clin. Invest. , vol.87 , pp. 2258-2265
    • Desrochers, P.E.1    Jeffrey, J.J.2    Weiss, S.J.3
  • 18
    • 0025997534 scopus 로고
    • 1-anti-chymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin)
    • 1-anti-chymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J. Biol. Chem. 266:1991;15810-15816.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15810-15816
    • Mast, A.E.1    Enghild, J.J.2    Nagase, H.3    Suzuki, K.4    Pizzo, S.V.5    Salvesen, G.6
  • 19
    • 0025270792 scopus 로고
    • 1-proteinase inhibitor by human PMN leucocyte collagenase
    • 1-proteinase inhibitor by human PMN leucocyte collagenase. FEBS Lett. 263:1990;355-357.
    • (1990) FEBS Lett. , vol.263 , pp. 355-357
    • Knauper, V.1    Reinke, H.2    Tschesche, H.3
  • 22
    • 0023031993 scopus 로고
    • 1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • 1-proteinase inhibitor by proteinases from Staphylococcus aureus. J. Biol. Chem. 261:1986;14330-14334.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 25
    • 0022843745 scopus 로고
    • 1-proteinase inhibitor by cleavage in the reactive site region
    • 1-proteinase inhibitor by cleavage in the reactive site region. J. Biol. Chem. 261:1986;14748-14751.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14748-14751
    • Johnson, D.A.1    Barrett, A.J.2    Mason, R.W.3
  • 29
    • 10244251626 scopus 로고    scopus 로고
    • Purification and characterization of a novel endopeptidase in ragweed (Ambrosia artemisiifolia) pollen
    • Bagarozzi D.A. Jr., Pike R., Potempa J., Travis J. Purification and characterization of a novel endopeptidase in ragweed (Ambrosia artemisiifolia) pollen. J. Biol. Chem. 271:1996;26227-26232.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26227-26232
    • Bagarozzi D.A., Jr.1    Pike, R.2    Potempa, J.3    Travis, J.4
  • 31
    • 0019140674 scopus 로고
    • Enzymatic inactivation of human antithrombin III. Limited proteolysis of the inhibitor by snake venom proteinases in the presence of heparin
    • Kress L.F., Catanese J. Enzymatic inactivation of human antithrombin III. Limited proteolysis of the inhibitor by snake venom proteinases in the presence of heparin. Biochim. Biophys. Acta. 615:1980;178-186.
    • (1980) Biochim. Biophys. Acta , vol.615 , pp. 178-186
    • Kress, L.F.1    Catanese, J.2
  • 32
    • 0022395406 scopus 로고
    • 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis
    • 1-antitrypsin, antithrombin and the mechanism of inflammatory thrombosis. Nature. 317:1985;730-732.
    • (1985) Nature , vol.317 , pp. 730-732
    • Carrell, R.W.1    Owen, M.C.2
  • 33
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell R.W., Evans D.L., Stein P.E. Mobile reactive centre of serpins and the control of thrombosis. Nature. 352:1991;576-578.
    • (1991) Nature , vol.352 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.E.3
  • 35
    • 0025886117 scopus 로고
    • Inactivation of human plasma C1-inhibitor by human PMN leucocyte matrix metalloproteinases
    • Knauper V., Triebel S., Reinke H., Tschesche H. Inactivation of human plasma C1-inhibitor by human PMN leucocyte matrix metalloproteinases. FEBS Lett. 290:1991;99-102.
    • (1991) FEBS Lett. , vol.290 , pp. 99-102
    • Knauper, V.1    Triebel, S.2    Reinke, H.3    Tschesche, H.4
  • 36
    • 0025256081 scopus 로고
    • Interaction of heparin cofactor II with neutrophil elastase and cathepsin G
    • Pratt C.W., Tobin R.B., Church F.C. Interaction of heparin cofactor II with neutrophil elastase and cathepsin G. J. Biol. Chem. 265:1990;6092-6097.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6092-6097
    • Pratt, C.W.1    Tobin, R.B.2    Church, F.C.3
  • 38
  • 40
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa J., Mikolajczyk-Pawlinska J., Brassell D., Nelson D., Thogersen I.B., Enghild J.J., Travis J. Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis. J. Biol. Chem. 273:1998;21648-21657.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21648-21657
    • Potempa, J.1    Mikolajczyk-Pawlinska, J.2    Brassell, D.3    Nelson, D.4    Thogersen, I.B.5    Enghild, J.J.6    Travis, J.7
  • 41
    • 0028114835 scopus 로고
    • The role of proteolytic enzymes in the development of pulmonary emphysema and periodontal disease
    • Travis J., Pike R., Imamura T., Potempa J. The role of proteolytic enzymes in the development of pulmonary emphysema and periodontal disease. Am. J. Respir. Crit. Care Med. 150:1994;S143-S146.
    • (1994) Am. J. Respir. Crit. Care Med. , vol.150
    • Travis, J.1    Pike, R.2    Imamura, T.3    Potempa, J.4
  • 43
    • 0031884829 scopus 로고    scopus 로고
    • Human matrix metalloprotease activation by insults of bacterial infection involving proteases and free radicals
    • Maeda H., Okamoto T., Akaike T. Human matrix metalloprotease activation by insults of bacterial infection involving proteases and free radicals. Biol. Chem. 379:1998;193-200.
    • (1998) Biol. Chem. , vol.379 , pp. 193-200
    • Maeda, H.1    Okamoto, T.2    Akaike, T.3
  • 44
    • 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 Y.T., Lindy O., Saari H., Uitto V.I. Identification of proteases from periodontopathogenic bacteria as activators of latent human neutrophil and fibroblast-type interstitial collagenases. Infect. Immun. 60:1992;4491-4495.
    • (1992) Infect. Immun. , vol.60 , pp. 4491-4495
    • Sorsa, T.1    Ingman, T.2    Suomalainen, K.3    Haapasalo, M.4    Konttinen, Y.T.5    Lindy, O.6    Saari, H.7    Uitto, V.I.8
  • 45
    • 0031158475 scopus 로고    scopus 로고
    • Activation and novel processing of matrix metalloproteinases by a thiol-proteinase from the oral anaerobe Porphyromonas gingivalis
    • DeCarlo A.A. Jr., Windsor L.J., Bodden M.K., Harber G.J., 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. 76:1997;1260-1270.
    • (1997) J. Dent. Res. , vol.76 , pp. 1260-1270
    • Decarlo A.A., Jr.1    Windsor, L.J.2    Bodden, M.K.3    Harber, G.J.4    Birkedal-Hansen, B.5    Birkedal-Hansen, H.6
  • 46
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle M.D., Lottenberg R. Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77:1997;1-10.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2
  • 47
    • 0028089206 scopus 로고
    • Capturing host plasmin(ogen): A common mechanism for invasive pathogens?
    • Lottenberg R., Minning-Wenz D., Boyle M.D. Capturing host plasmin(ogen): a common mechanism for invasive pathogens? Trends Microbiol. 2:1994;20-24.
    • (1994) Trends Microbiol. , vol.2 , pp. 20-24
    • Lottenberg, R.1    Minning-Wenz, D.2    Boyle, M.D.3
  • 48
    • 0032769770 scopus 로고    scopus 로고
    • Plasmin-coated Borrelia burgdorferi degrades soluble and insoluble components of the mammalian extracellular matrix
    • Coleman J.L., Roemer E.J., Benach J.L. Plasmin-coated Borrelia burgdorferi degrades soluble and insoluble components of the mammalian extracellular matrix. Infect. Immun. 67:1999;3929-3936.
    • (1999) Infect. Immun. , vol.67 , pp. 3929-3936
    • Coleman, J.L.1    Roemer, E.J.2    Benach, J.L.3
  • 49
    • 0023691251 scopus 로고
    • Production of chemotactic factors for neutrophils following the interaction of Bacteroides gingivalis with purified C5
    • Schenkein H.A., Berry C.R. Production of chemotactic factors for neutrophils following the interaction of Bacteroides gingivalis with purified C5. J. Periodontal Res. 23:1988;308-312.
    • (1988) J. Periodontal Res. , vol.23 , pp. 308-312
    • Schenkein, H.A.1    Berry, C.R.2
  • 50
    • 0023885740 scopus 로고
    • The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system
    • Schenkein H.A. The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system. J. Periodontal Res. 23:1988;187-192.
    • (1988) J. Periodontal Res. , vol.23 , pp. 187-192
    • Schenkein, H.A.1
  • 51
    • 0025761240 scopus 로고
    • The role of complement in periodontal diseases
    • Schenkein H.A. The role of complement in periodontal diseases. Crit. Rev. Oral Biol. Med. 2:1991;65-81.
    • (1991) Crit. Rev. Oral Biol. Med. , vol.2 , pp. 65-81
    • Schenkein, H.A.1
  • 52
    • 0026725842 scopus 로고
    • Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis
    • Wingrove J.A., DiScipio R.G., Chen Z., Potempa J., Travis J., Hugli T.E. Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis. J. Biol. Chem. 267:1992;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
  • 53
    • 0016390788 scopus 로고
    • Collagenases (first of three parts)
    • Harris E.D. Jr., Krane S.M. Collagenases (first of three parts). N. Engl. J. Med. 291:1974;557-563.
    • (1974) N. Engl. J. Med. , vol.291 , pp. 557-563
    • Harris E.D., Jr.1    Krane, S.M.2
  • 55
    • 0027140429 scopus 로고
    • Bacterial extracellular zinc-containing metalloproteases
    • Hase C.C., Finkelstein R.A. Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57:1993;823-837.
    • (1993) Microbiol. Rev. , vol.57 , pp. 823-837
    • Hase, C.C.1    Finkelstein, R.A.2
  • 56
    • 0023932283 scopus 로고
    • Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases
    • Kilian M., Mestecky J., Russell M.W. Defense mechanisms involving Fc-dependent functions of immunoglobulin A and their subversion by bacterial immunoglobulin A proteases. Microbiol. Rev. 52:1988;296-303.
    • (1988) Microbiol. Rev. , vol.52 , pp. 296-303
    • Kilian, M.1    Mestecky, J.2    Russell, M.W.3
  • 57
    • 0032610769 scopus 로고    scopus 로고
    • Bacterial degradation of immunoglobulin A1 in relation to periodontal diseases
    • Gronbaek-Frandsen E.V. Bacterial degradation of immunoglobulin A1 in relation to periodontal diseases. APMIS. 87:1999;1-54.
    • (1999) APMIS , vol.87 , pp. 1-54
    • Gronbaek-Frandsen, E.V.1
  • 58
    • 0020656366 scopus 로고
    • The IgA1 proteases of pathogenic bacteria
    • Plaut A.G. The IgA1 proteases of pathogenic bacteria. Annu. Rev. Microbiol. 37:1983;603-622.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 603-622
    • Plaut, A.G.1
  • 59
    • 0030014069 scopus 로고    scopus 로고
    • Biological significance of IgA1 proteases in bacterial colonization and pathogenesis critical evaluation of experimental evidence
    • Kilian M., Reinholdt J., Lomholt H., Poulsen K., Frandsen E.V. Biological significance of IgA1 proteases in bacterial colonization and pathogenesis critical evaluation of experimental evidence. APMIS. 104:(5):1996;321-338.
    • (1996) APMIS , vol.104 , Issue.5 , pp. 321-338
    • Kilian, M.1    Reinholdt, J.2    Lomholt, H.3    Poulsen, K.4    Frandsen, E.V.5
  • 60
    • 0027240039 scopus 로고
    • The cleavage of immunoglobulin G in vitro and in vivo by a proteinase secreted by the urinary tract pathogen Proteus mirabilis
    • Loomes L.M., Kerr M.A., Senior B.W. The cleavage of immunoglobulin G in vitro and in vivo by a proteinase secreted by the urinary tract pathogen Proteus mirabilis. J. Med. Microbiol. 39:1993;225-232.
    • (1993) J. Med. Microbiol. , vol.39 , pp. 225-232
    • Loomes, L.M.1    Kerr, M.A.2    Senior, B.W.3
  • 61
    • 0025326902 scopus 로고
    • A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2, and IgG isotypes
    • Loomes L.M., Senior B.W., Kerr M.A. A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2, and IgG isotypes. Infect. Immun. 58:1990;1979-1985.
    • (1990) Infect. Immun. , vol.58 , pp. 1979-1985
    • Loomes, L.M.1    Senior, B.W.2    Kerr, M.A.3
  • 62
    • 0026201464 scopus 로고
    • Degradation of plasma proteins by the trypsin-like enzyme of Porphyromonas gingivalis and inhibition of protease activity by a serine protease inhibitor of human plasma
    • Fishburn C.S., Slaney J.M., Carman R.J., Curtis M.A. Degradation of plasma proteins by the trypsin-like enzyme of Porphyromonas gingivalis and inhibition of protease activity by a serine protease inhibitor of human plasma. Oral Microbiol. Immunol. 6:1991;209-215.
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 209-215
    • Fishburn, C.S.1    Slaney, J.M.2    Carman, R.J.3    Curtis, M.A.4
  • 63
    • 0021673570 scopus 로고
    • Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: Elastase, an IgG protease
    • Holder I.A., Wheeler R. Experimental studies of the pathogenesis of infections owing to Pseudomonas aeruginosa: elastase, an IgG protease. Can. J. Microbiol. 30:1984;1118-1124.
    • (1984) Can. J. Microbiol. , vol.30 , pp. 1118-1124
    • Holder, I.A.1    Wheeler, R.2
  • 66
    • 0024797909 scopus 로고
    • Functional importance of cystic fibrosis immunoglobulin G fragments generated by Pseudomonas aeruginosa elastase
    • Bainbridge T., Fick R.B. Jr. Functional importance of cystic fibrosis immunoglobulin G fragments generated by Pseudomonas aeruginosa elastase. J. Lab. Clin. Med. 114:1989;728-733.
    • (1989) J. Lab. Clin. Med. , vol.114 , pp. 728-733
    • Bainbridge, T.1    Fick R.B., Jr.2
  • 67
    • 0029311217 scopus 로고
    • Characterization of immunoglobulin G-degrading proteases of Prevotella intermedia and Prevotella nigrescens
    • Jansen H.J., Grenier D., VanderHoeven J.S. Characterization of immunoglobulin G-degrading proteases of Prevotella intermedia and Prevotella nigrescens. Oral Microbiol. Immunol. 10:1995;138-145.
    • (1995) Oral Microbiol. Immunol. , vol.10 , pp. 138-145
    • Jansen, H.J.1    Grenier, D.2    Vanderhoeven, J.S.3
  • 68
    • 0026889494 scopus 로고
    • A 41.7 kDa serine protease from Clostridium perfringens type A: Degradation of purified human serum proteins
    • Wolf U., Bauer D., Traub W.H. A 41.7 kDa serine protease from Clostridium perfringens type A: degradation of purified human serum proteins. Zent.bl. Bakteriol. 277:1992;145-160.
    • (1992) Zent.bl. Bakteriol. , vol.277 , pp. 145-160
    • Wolf, U.1    Bauer, D.2    Traub, W.H.3
  • 69
    • 0030885721 scopus 로고    scopus 로고
    • The intrinsic coagulation/kinin-forming cascade: Assembly in plasma and cell surfaces in inflammation
    • Kaplan A.P., Joseph K., Shibayama Y., Reddigari S., Ghebrehiwet B., Silverberg M. The intrinsic coagulation/kinin-forming cascade: assembly in plasma and cell surfaces in inflammation. Adv. Immunol. 66:1997;225-272.
    • (1997) Adv. Immunol. , vol.66 , pp. 225-272
    • Kaplan, A.P.1    Joseph, K.2    Shibayama, Y.3    Reddigari, S.4    Ghebrehiwet, B.5    Silverberg, M.6
  • 70
    • 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 R.N., 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. 94:1994;361-367.
    • (1994) J. Clin. Invest. , vol.94 , pp. 361-367
    • Imamura, T.1    Pike, R.N.2    Potempa, J.3    Travis, J.4
  • 71
    • 0021847045 scopus 로고
    • A serratial protease causes vascular permeability reaction by activation of the Hageman factor-dependent pathway in guinea pigs
    • Kamata R., Yamamoto T., Matsumoto K., Maeda H. A serratial protease causes vascular permeability reaction by activation of the Hageman factor-dependent pathway in guinea pigs. Infect. Immun. 48:1985;747-753.
    • (1985) Infect. Immun. , vol.48 , pp. 747-753
    • Kamata, R.1    Yamamoto, T.2    Matsumoto, K.3    Maeda, H.4
  • 72
    • 0024340635 scopus 로고
    • Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases
    • Molla A., Yamamoto T., Akaike T., Miyoshi S., Maeda H. Activation of Hageman factor and prekallikrein and generation of kinin by various microbial proteinases. J. Biol. Chem. 264:1989;10589-10594.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10589-10594
    • Molla, A.1    Yamamoto, T.2    Akaike, T.3    Miyoshi, S.4    Maeda, H.5
  • 74
    • 0027305768 scopus 로고
    • Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity
    • Maruo K., Akaike T., Inada Y., Ohkubo I., Ono T., Maeda H. Effect of microbial and mite proteases on low and high molecular weight kininogens. Generation of kinin and inactivation of thiol protease inhibitory activity. J. Biol. Chem. 268:1993;17711-17715.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17711-17715
    • Maruo, K.1    Akaike, T.2    Inada, Y.3    Ohkubo, I.4    Ono, T.5    Maeda, H.6
  • 75
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A virulence mechanism
    • Herwald H., Collin M., Muller-Esterl W., Bjorck L. Streptococcal cysteine proteinase releases kinins: a virulence mechanism. J. Exp. Med. 184:1996;665-673.
    • (1996) J. Exp. Med. , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Muller-Esterl, W.3    Bjorck, L.4
  • 76
    • 0031931098 scopus 로고    scopus 로고
    • Involvement of bradykinin generation in intravascular dissemination of Vibrio vulnificus and prevention of invasion by a bradykinin antagonist
    • Maruo K., Akaike T., Ono T., Maeda H. Involvement of bradykinin generation in intravascular dissemination of Vibrio vulnificus and prevention of invasion by a bradykinin antagonist. Infect. Immun. 66:1998;866-969.
    • (1998) Infect. Immun. , vol.66 , pp. 866-969
    • Maruo, K.1    Akaike, T.2    Ono, T.3    Maeda, H.4
  • 77
    • 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 M. Bradykinin generation triggered by Pseudomonas proteases facilitates invasion of the systemic circulation by Pseudomonas aeruginosa. Microbiol. Immunol. 40:1996;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, M.6
  • 78
    • 0026601820 scopus 로고
    • Effect of Pseudomonas aeruginosa elastase and alkaline protease on serum complement and isolated components C1q and C3
    • Hong Y.Q., Ghebrehiwet B. Effect of Pseudomonas aeruginosa elastase and alkaline protease on serum complement and isolated components C1q and C3. Clin. Immunol. Immunopathol. 62:1992;133-138.
    • (1992) Clin. Immunol. Immunopathol. , vol.62 , pp. 133-138
    • Hong, Y.Q.1    Ghebrehiwet, B.2
  • 79
    • 0016244565 scopus 로고
    • Elastase of Pseudomonas aeruginosa: Inactivation of complement components and complement-derived chemotactic and phagocytic factors
    • Schultz D.R., Miller K.D. Elastase of Pseudomonas aeruginosa: inactivation of complement components and complement-derived chemotactic and phagocytic factors. Infect. Immun. 10:1974;128-135.
    • (1974) Infect. Immun. , vol.10 , pp. 128-135
    • Schultz, D.R.1    Miller, K.D.2
  • 80
    • 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. 19:1985;85-94.
    • (1985) J. Med. Microbiol. , vol.19 , pp. 85-94
    • Sundqvist, G.1    Carlsson, J.2    Herrmann, B.3    Tarnvik, A.4
  • 81
    • 0023885740 scopus 로고
    • The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system
    • Schenkein H.A. The effect of periodontal proteolytic Bacteroides species on proteins of the human complement system. J. Periodontal Res. 23:1988;187-192.
    • (1988) J. Periodontal Res. , vol.23 , pp. 187-192
    • Schenkein, H.A.1
  • 83
    • 0025275204 scopus 로고
    • Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease
    • Oda T., Kojima Y., Akaike T., Ijiri S., Molla A., Maeda H. Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease. Infect. Immun. 58:1990;1269.
    • (1990) Infect. Immun. , vol.58 , pp. 1269
    • Oda, T.1    Kojima, Y.2    Akaike, T.3    Ijiri, S.4    Molla, A.5    Maeda, H.6
  • 86
    • 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. 380:1999;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
  • 87
    • 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. 272:1997;16062-16067.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16062-16067
    • Imamura, T.1    Potempa, J.2    Tanase, S.3    Travis, J.4
  • 88
    • 0030688025 scopus 로고    scopus 로고
    • Subsite specificity studies on the unusual cysteine protease clostripain: Charged residues in the P3 position indicate a narrow subsite region
    • Bordusa F., Ullmann D., Jakubke H.D. Subsite specificity studies on the unusual cysteine protease clostripain: charged residues in the P3 position indicate a narrow subsite region. Biol. Chem. 378:1997;1193-1198.
    • (1997) Biol. Chem. , vol.378 , pp. 1193-1198
    • Bordusa, F.1    Ullmann, D.2    Jakubke, H.D.3
  • 89
    • 0031988026 scopus 로고    scopus 로고
    • Oral pathogens: From dental plaque to cardiac disease
    • Meyer D.H., Fives-Taylor P.M. Oral pathogens: from dental plaque to cardiac disease. Curr. Opin. Microbiol. 1:1998;88-95.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 88-95
    • Meyer, D.H.1    Fives-Taylor, P.M.2
  • 90
    • 0032112772 scopus 로고    scopus 로고
    • The pathobiology of periodontal diseases may affect systemic diseases: Inversion of a paradigm
    • Page R.C. The pathobiology of periodontal diseases may affect systemic diseases: inversion of a paradigm. Ann. Periodontol. 31:1998;108-120.
    • (1998) Ann. Periodontol. , vol.31 , pp. 108-120
    • Page, R.C.1
  • 93
    • 0342981798 scopus 로고    scopus 로고
    • Purification and characterisation of a plasminogen-binding protein from Haemophilus influenzae. Sequence determination reveals identity with aspartase
    • Sjostrom I., Grondahl H., Falk G., Kronvall G., Ullberg M. Purification and characterisation of a plasminogen-binding protein from Haemophilus influenzae. Sequence determination reveals identity with aspartase. Biochim. Biophys. Acta. 1324:1997;182-190.
    • (1997) Biochim. Biophys. Acta , vol.1324 , pp. 182-190
    • Sjostrom, I.1    Grondahl, H.2    Falk, G.3    Kronvall, G.4    Ullberg, M.5
  • 94
    • 0025004988 scopus 로고
    • Receptors for human plasminogen on Gram-negative bacteria
    • Ullberg M., Kronvall G., Karlsson I., Wiman B. Receptors for human plasminogen on Gram-negative bacteria. Infect. Immun. 58:1990;21-25.
    • (1990) Infect. Immun. , vol.58 , pp. 21-25
    • Ullberg, M.1    Kronvall, G.2    Karlsson, I.3    Wiman, B.4
  • 96
    • 0031680277 scopus 로고    scopus 로고
    • Plasminogen binding and activation at the surface of Helicobacter pylori CCUG 17874
    • Pantzar M., Ljungh A., Wadstrom T. Plasminogen binding and activation at the surface of Helicobacter pylori CCUG 17874. Infect. Immun. 66:1998;4976-4980.
    • (1998) Infect. Immun. , vol.66 , pp. 4976-4980
    • Pantzar, M.1    Ljungh, A.2    Wadstrom, T.3
  • 97
    • 0026489197 scopus 로고
    • Binding of plasminogen to Neisseria meningitidis and Neisseria gonorrhoeae and formation of surface-associated plasmin
    • Ullberg M., Kuusela P., Kristiansen B.E., Kronvall G. Binding of plasminogen to Neisseria meningitidis and Neisseria gonorrhoeae and formation of surface-associated plasmin. J. Infect. Dis. 166:1992;1329-1334.
    • (1992) J. Infect. Dis. , vol.166 , pp. 1329-1334
    • Ullberg, M.1    Kuusela, P.2    Kristiansen, B.E.3    Kronvall, G.4
  • 98
    • 0025009728 scopus 로고
    • Binding and activation of plasminogen at the surface of Staphylococcus aureus. Increase in affinity after conversion to the Lys form of the ligand
    • Kuusela P., Saksela O. Binding and activation of plasminogen at the surface of Staphylococcus aureus. Increase in affinity after conversion to the Lys form of the ligand. Eur. J. Biochem. 193:1990;759-765.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 759-765
    • Kuusela, P.1    Saksela, O.2
  • 99
    • 0345120581 scopus 로고    scopus 로고
    • Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo
    • Svensson M.D., Sjobring U., Bessen D.E. Selective distribution of a high-affinity plasminogen-binding site among group A streptococci associated with impetigo. Infect. Immun. 67:1999;3915-3920.
    • (1999) Infect. Immun. , vol.67 , pp. 3915-3920
    • Svensson, M.D.1    Sjobring, U.2    Bessen, D.E.3
  • 100
    • 0033103020 scopus 로고    scopus 로고
    • Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes
    • Eberhard T., Kronvall G., Ullberg M. Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes. Microb. Pathog. 26:1999;175-181.
    • (1999) Microb. Pathog. , vol.26 , pp. 175-181
    • Eberhard, T.1    Kronvall, G.2    Ullberg, M.3
  • 101
    • 0032104441 scopus 로고    scopus 로고
    • Interaction of a group A Streptococcus within human plasma results in assembly of a surface plasminogen activator that contributes to occupancy of surface plasmin-binding structures
    • D'Costa S.S., Boyle M.D. Interaction of a group A Streptococcus within human plasma results in assembly of a surface plasminogen activator that contributes to occupancy of surface plasmin-binding structures. Microb. Pathog. 24:1998;341-349.
    • (1998) Microb. Pathog. , vol.24 , pp. 341-349
    • D'Costa, S.S.1    Boyle, M.D.2
  • 102
    • 0342974425 scopus 로고
    • Activation of plasminogen to plasmin by a protease associated with the outer membrane of Escherichia coli
    • Leytus S.P., Bowles L.K., Konisky J., Mangel W.F. Activation of plasminogen to plasmin by a protease associated with the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA. 78:1981;1485-1485.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1485-1485
    • Leytus, S.P.1    Bowles, L.K.2    Konisky, J.3    Mangel, W.F.4
  • 105
    • 0031769659 scopus 로고    scopus 로고
    • Structural features, physiological roles, and biotechnological applications of the membrane proteases of the OmpT bacterial endopeptidase family: A micro-review
    • Stathopoulos C. Structural features, physiological roles, and biotechnological applications of the membrane proteases of the OmpT bacterial endopeptidase family: a micro-review. Membr. Cell Biol. 12:1998;1-8.
    • (1998) Membr. Cell Biol. , vol.12 , pp. 1-8
    • Stathopoulos, C.1
  • 106
    • 0024563389 scopus 로고
    • Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: Relationship to ompT of Escherichia coli and gene E of Salmonella typhimurium
    • Sodeinde O.A., Goguen J.D. Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: relationship to ompT of Escherichia coli and gene E of Salmonella typhimurium. Infect. Immun. 57:1989;1517-1523.
    • (1989) Infect. Immun. , vol.57 , pp. 1517-1523
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 107
    • 0026939349 scopus 로고
    • Prevalence of ompT among Escherichia coli isolates of human origin
    • Lundrigan M.D., Webb R.M. Prevalence of ompT among Escherichia coli isolates of human origin. FEMS Microbiol. Lett. 76:1992;51-56.
    • (1992) FEMS Microbiol. Lett. , vol.76 , pp. 51-56
    • Lundrigan, M.D.1    Webb, R.M.2
  • 108
    • 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 R.N., Moore J.N., Barton M.H., 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. 63:1995;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
  • 109
    • 0029913412 scopus 로고    scopus 로고
    • Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis
    • Pike R.N., Potempa J., McGraw W., Coetzer T.H., Travis J. Characterization of the binding activities of proteinase-adhesin complexes from Porphyromonas gingivalis. J. Bacteriol. 178:1996;2876-2882.
    • (1996) J. Bacteriol. , vol.178 , pp. 2876-2882
    • Pike, R.N.1    Potempa, J.2    McGraw, W.3    Coetzer, T.H.4    Travis, J.5
  • 110
    • 0028213355 scopus 로고
    • Characterization of fibrinolytic activities of Treponema denticola
    • Rosen G., Naor R., Kutner S., Sela M.N. Characterization of fibrinolytic activities of Treponema denticola. Infect. Immun. 62:1994;1749-1754.
    • (1994) Infect. Immun. , vol.62 , pp. 1749-1754
    • Rosen, G.1    Naor, R.2    Kutner, S.3    Sela, M.N.4
  • 111
    • 0032785373 scopus 로고    scopus 로고
    • Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity
    • Matsuka Y.V., Pillai S., Gubba S., Musser J.M., Olmsted S.B. Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity. Infect. Immun. 67:1999;4326-4333.
    • (1999) Infect. Immun. , vol.67 , pp. 4326-4333
    • Matsuka, Y.V.1    Pillai, S.2    Gubba, S.3    Musser, J.M.4    Olmsted, S.B.5
  • 112
    • 0032786580 scopus 로고    scopus 로고
    • Characterization and purification of an outer membrane metalloproteinase from Pseudomonas aeruginosa with fibrinogenolytic activity
    • Fricke B., Parchmann O., Kruse K., Rucknagel P., Schierhorn A., Menge S. Characterization and purification of an outer membrane metalloproteinase from Pseudomonas aeruginosa with fibrinogenolytic activity. Biochim. Biophys. Acta. 1454:1999;236-250.
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 236-250
    • Fricke, B.1    Parchmann, O.2    Kruse, K.3    Rucknagel, P.4    Schierhorn, A.5    Menge, S.6
  • 114
    • 0032479154 scopus 로고    scopus 로고
    • Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa
    • Engel L.S., Hill J.M., Caballero A.R., Green L.C., O'Callaghan R.J. Protease IV, a unique extracellular protease and virulence factor from Pseudomonas aeruginosa. J. Biol. Chem. 273:1998;16792-16797.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16792-16797
    • Engel, L.S.1    Hill, J.M.2    Caballero, A.R.3    Green, L.C.4    O'Callaghan, R.J.5
  • 115
    • 0027288424 scopus 로고
    • Legionella pneumophila protease inactivates interleukin-2 and cleaves CD4 on human T cells
    • Mintz C.S., Miller R.D., Gutgsell N.S., Malek T. Legionella pneumophila protease inactivates interleukin-2 and cleaves CD4 on human T cells. Infect. Immun. 61:1993;3416-3421.
    • (1993) Infect. Immun. , vol.61 , pp. 3416-3421
    • Mintz, C.S.1    Miller, R.D.2    Gutgsell, N.S.3    Malek, T.4
  • 116
    • 0023738994 scopus 로고
    • Pseudomonas aeruginosa alkaline protease degrades human gamma interferon and inhibits its bioactivity
    • Horvat R.T., Parmely M.J. Pseudomonas aeruginosa alkaline protease degrades human gamma interferon and inhibits its bioactivity. Infect. Immun. 56:1988;2925-2932.
    • (1988) Infect. Immun. , vol.56 , pp. 2925-2932
    • Horvat, R.T.1    Parmely, M.J.2
  • 118
    • 0025170582 scopus 로고
    • Proteolytic inactivation of cytokines by Pseudomonas aeruginosa
    • Parmely M., Gale A., Clabaugh M., Horvat R., Zhou W.W. Proteolytic inactivation of cytokines by Pseudomonas aeruginosa. Infect. Immun. 58:1990;3009-3014.
    • (1990) Infect. Immun. , vol.58 , pp. 3009-3014
    • Parmely, M.1    Gale, A.2    Clabaugh, M.3    Horvat, R.4    Zhou, W.W.5
  • 119
    • 0032549590 scopus 로고    scopus 로고
    • Inactivation of tumor necrosis factor-α By proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion
    • Calkins C.C., Platt K., Potempa J., Travis J. Inactivation of tumor necrosis factor-α by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion. J. Biol. Chem. 273:1998;6611-6614.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6611-6614
    • Calkins, C.C.1    Platt, K.2    Potempa, J.3    Travis, J.4
  • 122
    • 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 P.C., Travis J., Potempa J. Rapid and efficient inactivation of IL-6 gingipains, lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Biochem. Biophys. Res. Commun. 261:1999;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
  • 123
    • 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 P.L., DeCarlo A.A., Hunter N. Modulation of major histocompatibility complex protein expression by human gamma interferon mediated by cysteine proteinase-adhesin polyproteins of Porphyromonas gingivalis. Infect. Immun. 67:1999;2986-2995.
    • (1999) Infect. Immun. , vol.67 , pp. 2986-2995
    • Yun, P.L.1    Decarlo, A.A.2    Hunter, N.3
  • 124
    • 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. 440:1998;282-286.
    • (1998) FEBS Lett. , vol.440 , pp. 282-286
    • Mikolajczyk-Pawlinska, J.1    Travis, J.2    Potempa, J.3
  • 125
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines M., Wolf M., Walz A., Baggiolini M. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352:1994;231-235.
    • (1994) FEBS Lett. , vol.352 , pp. 231-235
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 126
    • 0033135922 scopus 로고    scopus 로고
    • IL-8 degradation by Porphyromonas gingivalis proteases
    • Zhang J., Dong H., Kashket S., Duncan M.J. IL-8 degradation by Porphyromonas gingivalis proteases. Microb. Pathog. 26:1999;275-280.
    • (1999) Microb. Pathog. , vol.26 , pp. 275-280
    • Zhang, J.1    Dong, H.2    Kashket, S.3    Duncan, M.J.4
  • 127
    • 0028032258 scopus 로고
    • Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface
    • Wolf B.B., Gibson C.A., Kapur V., Hussaini I.M., Musser J.M., Gonias S.L. Proteolytically active streptococcal pyrogenic exotoxin B cleaves monocytic cell urokinase receptor and releases an active fragment of the receptor from the cell surface. J. Biol. Chem. 269:1994;30682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30682
    • Wolf, B.B.1    Gibson, C.A.2    Kapur, V.3    Hussaini, I.M.4    Musser, J.M.5    Gonias, S.L.6
  • 128
    • 0029736417 scopus 로고    scopus 로고
    • Novel pathogenic mechanism of microbial metalloproteinases: Liberation of membrane-anchored molecules in biologically active form exemplified by studies with the human interleukin-6 receptor
    • Vollmer P., Walev I., Rose-John S., Bhakdi S. Novel pathogenic mechanism of microbial metalloproteinases: liberation of membrane-anchored molecules in biologically active form exemplified by studies with the human interleukin-6 receptor. Infect. Immun. 64:1996;3646-3651.
    • (1996) Infect. Immun. , vol.64 , pp. 3646-3651
    • Vollmer, P.1    Walev, I.2    Rose-John, S.3    Bhakdi, S.4
  • 129
    • 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 E.J., Pike R.N. Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis. FEBS Lett. 435:1998;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
  • 132
    • 0023136546 scopus 로고
    • Role of Staphylococcus protease in the development of influenza pneumonia
    • Tashiro M., Ciborowski P., Klenk H.D., Pulverer G., Rott R. Role of Staphylococcus protease in the development of influenza pneumonia. Nature. 325:1987;536-537.
    • (1987) Nature , vol.325 , pp. 536-537
    • Tashiro, M.1    Ciborowski, P.2    Klenk, H.D.3    Pulverer, G.4    Rott, R.5
  • 133
    • 0023111155 scopus 로고
    • Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity
    • Tashiro M., Ciborowski P., Reinacher M., Pulverer G., Klenk H.D., Rott R. Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity. Virology. 157:1987;421-430.
    • (1987) Virology , vol.157 , pp. 421-430
    • Tashiro, M.1    Ciborowski, P.2    Reinacher, M.3    Pulverer, G.4    Klenk, H.D.5    Rott, R.6
  • 134
    • 0026706343 scopus 로고
    • Interactions between bacteria and influenza A virus in the development of influenza pneumonia
    • Scheiblauer H., Reinacher M., Tashiro M., Rott R. Interactions between bacteria and influenza A virus in the development of influenza pneumonia. J. Infect. Dis. 166:1992;783-791.
    • (1992) J. Infect. Dis. , vol.166 , pp. 783-791
    • Scheiblauer, H.1    Reinacher, M.2    Tashiro, M.3    Rott, R.4
  • 135
    • 0031152116 scopus 로고    scopus 로고
    • Advances in the pathogenesis of periodontitis summary of developments, clinical implications and future directions
    • Page R.C., Offenbacher S., Schroeder H.E., Seymour G.J., Kornman K.S. Advances in the pathogenesis of periodontitis summary of developments, clinical implications and future directions. Periodontol. 2000. 14:1997;216-248.
    • (1997) Periodontol. 2000 , vol.14 , pp. 216-248
    • Page, R.C.1    Offenbacher, S.2    Schroeder, H.E.3    Seymour, G.J.4    Kornman, K.S.5
  • 137
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: Pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont R.J., Jenkinson H.F. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 62:1998;1244-1263.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 138
    • 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. 43:1996;455-465.
    • (1996) Acta Biochim. Pol. , vol.43 , pp. 455-465
    • Potempa, J.1    Travis, J.2
  • 139
    • 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. 3:1995;430-434.
    • (1995) Trends Microbiol. , vol.3 , pp. 430-434
    • Potempa, J.1    Pavloff, N.2    Travis, J.3
  • 140
    • 0034303490 scopus 로고    scopus 로고
    • Role of bacterial proteinases in matrix destruction and modulation of host responses
    • (in press)
    • J. Potempa, A. Banbula and J. Travis, Role of bacterial proteinases in matrix destruction and modulation of host responses, Periodontol. 2000 (in press).
    • (2000) Periodontol.
    • Potempa, J.1    Banbula, A.2    Travis, J.3
  • 141
    • 0027221467 scopus 로고
    • Adhere today, here tomorrow: Oral bacterial adherence
    • Kolenbrander P.E., London J. Adhere today, here tomorrow: oral bacterial adherence. J. Bacteriol. 175:1993;3247-3252.
    • (1993) J. Bacteriol. , vol.175 , pp. 3247-3252
    • Kolenbrander, P.E.1    London, J.2
  • 142
    • 0027135337 scopus 로고
    • Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis
    • Cutler C.W., Arnold R.R., Schenkein H.A. Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis. J. Immunol. 15:1993;7016-7029.
    • (1993) J. Immunol. , vol.15 , pp. 7016-7029
    • Cutler, C.W.1    Arnold, R.R.2    Schenkein, H.A.3
  • 143
    • 0030004180 scopus 로고    scopus 로고
    • Proteolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis
    • Jagels M.A., Travis J., Potempa J., Pike R., Hugli T.E. Proteolytic inactivation of the leukocyte C5a receptor by proteinases derived from Porphyromonas gingivalis. Infect. Immun. 64:1996;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
  • 144
    • 0028305420 scopus 로고
    • Porphyromonas gingivalis trypsin-like protease: A possible natural ligand for the neutrophil formyl peptide receptor
    • Lala A., Amano A., Sojar H.T., Radel S.J., DeNardin E. Porphyromonas gingivalis trypsin-like protease: a possible natural ligand for the neutrophil formyl peptide receptor. Biochem. Biophys. Res. Commun. 199:1994;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    Denardin, E.5
  • 145
    • 0028909491 scopus 로고
    • Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis
    • Imamura T., Potempa J., Pike R.N., Travis J. Dependence of vascular permeability enhancement on cysteine proteinases in vesicles of Porphyromonas gingivalis. Infect. Immun. 63:1995;1999-2003.
    • (1995) Infect. Immun. , vol.63 , pp. 1999-2003
    • Imamura, T.1    Potempa, J.2    Pike, R.N.3    Travis, J.4


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