메뉴 건너뛰기




Volumn 377, Issue 2, 1996, Pages 71-86

Cystatins in health disease

Author keywords

Cystatins; Cysteine proteinases; Inflammation; Inhibitors; Pathological processes

Indexed keywords

CYSTATIN; CYSTEINE PROTEINASE; PROTEINASE; PROTEINASE INHIBITOR;

EID: 0029913216     PISSN: 01773593     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (218)

References (193)
  • 1
    • 0023024774 scopus 로고
    • Isolation of six proteinase inhibitors from human urine. Their physicochemical enzyme kinetic properties concentrations in biological fluids
    • Abrahamson, M., Salvesen, G., Barrett, A.J., Grubb, A. (1986). Isolation of six proteinase inhibitors from human urine. Their physicochemical enzyme kinetic properties concentrations in biological fluids. J. Biol. Chem. 261, 11282-11289.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11282-11289
    • Abrahamson, M.1    Salvesen, G.2    Barrett, A.J.3    Grubb, A.4
  • 2
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C chicken cystatin
    • Abrahamson, M., Ritonja, A., Brown, M.A., Grubb, A., Machleidt, W., Barrett, A.J. (1987a). Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C chicken cystatin. J. Biol. Chem. 262, 9688-9694.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3    Grubb, A.4    Machleidt, W.5    Barrett, A.J.6
  • 3
    • 0023229953 scopus 로고
    • Molecular cloning sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C
    • Abrahamson, M., Grubb, A., Olafsson, I., Lundwall, A. (1987b). Molecular cloning sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett. 216,229-233.
    • (1987) FEBS Lett. , vol.216 , pp. 229-233
    • Abrahamson, M.1    Grubb, A.2    Olafsson, I.3    Lundwall, A.4
  • 4
    • 0023684074 scopus 로고
    • Efficient production of native, biologically active human cystatin C by Escherichia coli
    • Abrahamson, M., Dalboge, H., Olafsson, I., Carlsen, S., Grubb, A. (1988). Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett. 236, 14-18.
    • (1988) FEBS Lett. , vol.236 , pp. 14-18
    • Abrahamson, M.1    Dalboge, H.2    Olafsson, I.3    Carlsen, S.4    Grubb, A.5
  • 5
    • 0024338979 scopus 로고
    • The human cystatin C gene (CST3), mutated in hereditary cystatin C amyloid angiopathy, is located on chromosome 20
    • Abrahamson, M., Islam, M.W., Szpirer, J., Szpirer, C., Levan, G. (1989). The human cystatin C gene (CST3), mutated in hereditary cystatin C amyloid angiopathy, is located on chromosome 20. Hum. Genet. 82,223-226.
    • (1989) Hum. Genet. , vol.82 , pp. 223-226
    • Abrahamson, M.1    Islam, M.W.2    Szpirer, J.3    Szpirer, C.4    Levan, G.5
  • 8
    • 0026718486 scopus 로고
    • Hereditary cystatin C amyloid angiopathy, identification of the disease-causing mutation specific diagnosis by polymerase chain reaction based analysis
    • Abrahamson, M., Jonsdottir, S., Olafsson, I., Jensson, O., Grubb, A. (1992). Hereditary cystatin C amyloid angiopathy, identification of the disease-causing mutation specific diagnosis by polymerase chain reaction based analysis. Hum. Genet. 89,377-380.
    • (1992) Hum. Genet. , vol.89 , pp. 377-380
    • Abrahamson, M.1    Jonsdottir, S.2    Olafsson, I.3    Jensson, O.4    Grubb, A.5
  • 9
    • 0004571537 scopus 로고
    • Cystatins-Proteinase inhibitors of papain-like cysteine proteinases
    • Abrahamson, M. (1993). Cystatins-Proteinase inhibitors of papain-like cysteine proteinases. J. Braz. Assoc. Adv. Sc. 45, 299-304.
    • (1993) J. Braz. Assoc. Adv. Sc. , vol.45 , pp. 299-304
    • Abrahamson, M.1
  • 10
    • 0027976996 scopus 로고
    • Increased body temperature accelerates aggregation of the Leu-68 -Gin mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
    • Abrahamson, M., Grubb, A. (1994a). Increased body temperature accelerates aggregation of the Leu-68 -Gin mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy. Proc. Natl. Acad. Sei. USA. 91,1 -5.
    • (1994) Proc. Natl. Acad. Sei. USA. , vol.91 , pp. 1-5
    • Abrahamson, M.1    Grubb, A.2
  • 14
    • 0023944901 scopus 로고
    • Purification, molecular cloning sequencing of salivary cystatin SA-I
    • AI-Hashimi, I., Dickinson, D., Levine, M.J. (1988). Purification, molecular cloning sequencing of salivary cystatin SA-I. J. Biol. Chem. 263,9381 -9387.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9381-9387
    • Ai-Hashimi, I.1    Dickinson, D.2    Levine, M.J.3
  • 15
    • 0028367702 scopus 로고
    • Induction of synthesis of the rat cystatin S protein by the submibular gl during the acute phase of experimental chagas disease
    • Alves, J.B., Alves, M.S.D., Naito, Y. (1994). Induction of synthesis of the rat cystatin S protein by the submibular gl during the acute phase of experimental chagas disease. Mem. Inst. Oswaldo Cruz, Rio Janero. 89,81 -85.
    • (1994) Mem. Inst. Oswaldo Cruz, Rio Janero. , vol.89 , pp. 81-85
    • Alves, J.B.1    Alves, M.S.D.2    Naito, Y.3
  • 16
    • 0028916483 scopus 로고
    • Antiviral effect of oryzacystatin, a proteinase inhibitor in rice, against herpes simplex virus type I in vitro in vivo
    • Aoki, H., Akaike, T., Abe, K., Kuroda, M., Arai, S., Okamura, R.-l., Negi, A., Maeda, H. (1995). Antiviral effect of oryzacystatin, a proteinase inhibitor in rice, against herpes simplex virus type I in vitro in vivo. Antimicrob. Agents Chemother. 39, 846-849.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 846-849
    • Aoki, H.1    Akaike, T.2    Abe, K.3    Kuroda, M.4    Arai, S.5    Okamura, R.-L.6    Negi, A.7    Maeda, H.8
  • 20
    • 0026637990 scopus 로고
    • Cysteine proteinase inhibitor in cultured human medullary thyroid carcinoma cells
    • Barka, T., Noen, van der H., Patil, S. (1992). Cysteine proteinase inhibitor in cultured human medullary thyroid carcinoma cells. Lab. Invest. 66,691 -700.
    • (1992) Lab. Invest. , vol.66 , pp. 691-700
    • Barka, T.1    Van Noen Der, H.2    Patil, S.3
  • 21
    • 0019765848 scopus 로고
    • Cathepsin, B, cathepsin H cathepsin L
    • Barrett, A.J., Kirschke, H. (1981). Cathepsin, B, cathepsin H cathepsin L. Methods Enzymol. 80,535-561.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 22
    • 0021236724 scopus 로고
    • The place of human -y-trace (cystatin C) amongst the cysteine proteinase inhibitors
    • Barrett, A.J., Davies, M.E., Grubb, A. (1984). The place of human -y-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem. Biophys. Res. Commun. 120,631 -636.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 631-636
    • Barrett, A.J.1    Davies, M.E.2    Grubb, A.3
  • 24
    • 0002486962 scopus 로고
    • Cysteine proteinase inhibitors of the cystatin superfamily
    • A.J. Barrett G. Salvesen, eds. Amsterdam, The Netherls: Elsevier Science Publishers
    • Barrett, A.J., Rawlings, N.D., Davies, M.E., Machleidt, W., Salvesen, G., Turk, V. (1986b). Cysteine proteinase inhibitors of the cystatin superfamily. In: Proteinase Inhibitors, A.J. Barrett G. Salvesen, eds. (Amsterdam, The Netherls: Elsevier Science Publishers), pp. 515-569.
    • (1986) Proteinase Inhibitors , pp. 515-569
    • Barrett, A.J.1    Rawlings, N.D.2    Davies, M.E.3    Machleidt, W.4    Salvesen, G.5    Turk, V.6
  • 26
    • 0024600478 scopus 로고
    • Purification characterization of an inducible cysteine proteinase inhibitor from submibular gls of isoproterenol-treated rats
    • Bedi, G.S.'(1989a). Purification characterization of an inducible cysteine proteinase inhibitor from submibular gls of isoproterenol-treated rats. Archs. Biochem. Biophys. 270, 335-343.
    • (1989) Archs. Biochem. Biophys. , vol.270 , pp. 335-343
    • Bedi, G.S.1
  • 27
    • 0024371672 scopus 로고
    • Amino acid sequence of an inducible cysteine proteinase inhibitor (cystatin) from submibular gls of isoproterenol-treated rats
    • Bedi, G.S. (1989b). Amino acid sequence of an inducible cysteine proteinase inhibitor (cystatin) from submibular gls of isoproterenol-treated rats. Archs. Biochem. Biophys. 273, 245-253.
    • (1989) Archs. Biochem. Biophys. , vol.273 , pp. 245-253
    • Bedi, G.S.1
  • 28
    • 0025216092 scopus 로고
    • A rapid radioimmunoassay for inducible rat submibular gl cysteine proteinase inhibitor (cystatin)
    • Bedi, G.S. (1990). A rapid radioimmunoassay for inducible rat submibular gl cysteine proteinase inhibitor (cystatin). Immunol. Invest. 19,199-208.
    • (1990) Immunol. Invest. , vol.19 , pp. 199-208
    • Bedi, G.S.1
  • 29
    • 0025765945 scopus 로고
    • The effects of autonomie drugs on the concentration of kallikrein-like proteases cysteine-proteinase inhibitor (cystatin) in rat whole saliva
    • Bedi, G.S. (1991 a). The effects of autonomie drugs on the concentration of kallikrein-like proteases cysteine-proteinase inhibitor (cystatin) in rat whole saliva. J. Dent. Res. 70, 924-930.
    • (1991) J. Dent. Res. , vol.70 , pp. 924-930
    • Bedi, G.S.1
  • 30
    • 0026293739 scopus 로고
    • The effects of adrenergic agonists antagonists on cysteine-proteinase inhibitor (cystatin) in rat saliva
    • Bedi, G.S. (1991 b). The effects of adrenergic agonists antagonists on cysteine-proteinase inhibitor (cystatin) in rat saliva. Archs. Oral. Biol. 36,611 -618.
    • (1991) Archs. Oral. Biol. , vol.36 , pp. 611-618
    • Bedi, G.S.1
  • 31
    • 0024814554 scopus 로고
    • Dementia with non-hereditary cystatin C angiopathy
    • M. Roth L.L. Iversen, eds. (Edinburgh, UK: Churchill Livingstone)
    • Benedikz, E., Blöndal, H., Jöhannesson, G., Gudmundsson, G. (1989). Dementia with non-hereditary cystatin C angiopathy. In: Alzheimer's Disease Related Disorders. M. Roth L.L. Iversen, eds. (Edinburgh, UK: Churchill Livingstone), pp. 517-522.
    • (1989) Alzheimer's Disease Related Disorders , pp. 517-522
    • Benedikz, E.1    Blöndal, H.2    Jöhannesson, G.3    Gudmundsson, G.4
  • 32
    • 0024546648 scopus 로고
    • Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
    • Björck, L, Akesson, P., Bohus, M., Trojnar, J., Abrahamson, M., Olafsson, I., Grubb, A. (1989). Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337,387-388.
    • (1989) Nature , vol.337 , pp. 387-388
    • Björck, L.1    Akesson, P.2    Bohus, M.3    Trojnar, J.4    Abrahamson, M.5    Olafsson, I.6    Grubb, A.7
  • 33
    • 0025177313 scopus 로고
    • Cystatin C, a proteinase inhibitor, blocks replication of herpes simplex virus
    • Björck, L, Grubb, A., Kjellen, L. (1990). Cystatin C, a proteinase inhibitor, blocks replication of herpes simplex virus. J. Virol. 64,385-386.
    • (1990) J. Virol. , vol.64 , pp. 385-386
    • Björck, L.1    Grubb, A.2    Kjellen, L.3
  • 34
    • 0026670859 scopus 로고
    • Different roles of the two disulfide bonds of the cysteine proteinase inhibitor chicken cystatin, for the conformation of the active protein
    • Björk, I., Ylinenjärvi, K. (1992). Different roles of the two disulfide bonds of the cysteine proteinase inhibitor chicken cystatin, for the conformation of the active protein. Biochemistry 31, 8597-8602.
    • (1992) Biochemistry , vol.31 , pp. 8597-8602
    • Björk, I.1    Ylinenjärvi, K.2
  • 35
    • 0025814769 scopus 로고
    • Human salivay cystatin S. Cloning, sequence analyses, hybridization in situ immunocytochemistry
    • Bobek, LA, Aguirre, A., Levine, M.J. (1991). Human salivay cystatin S. Cloning, sequence analyses, hybridization in situ immunocytochemistry. Biochem. J. 278, 627-635.
    • (1991) Biochem. J. , vol.278 , pp. 627-635
    • Bobek, L.A.1    Aguirre, A.2    Levine, M.J.3
  • 37
    • 0028587077 scopus 로고
    • Biological activities secondary structures of variant forms of human salivary cystatin SN produced
    • Bobek, LA., Ramasubbu, N., Wang, X., Weaver, T.R., Levine, M.J. (1994). Biological activities secondary structures of variant forms of human salivary cystatin SN produced in Escherichia coli. Gene. 151,303-308.
    • (1994) Escherichia Coli. Gene. , vol.151 , pp. 303-308
    • Bobek, L.A.1    Ramasubbu, N.2    Wang, X.3    Weaver, T.R.4    Levine, M.J.5
  • 38
    • 84955841443 scopus 로고
    • Cystatin C, alias post-y-globulin: A marker for multiple sclerosis
    • Bollengier, F. (1987). Cystatin C, alias post-y-globulin: a marker for multiple sclerosis. J. Clin. Chem. Biochem. 25,589-593.
    • (1987) J. Clin. Chem. Biochem. , vol.25 , pp. 589-593
    • Bollengier, F.1
  • 39
    • 0020025542 scopus 로고
    • An endogenous inhibitor of cysteine serine proteinases from spleen
    • Brzin, J., Kopitar, M., Locnikar, P., Turk, V. (1982). An endogenous inhibitor of cysteine serine proteinases from spleen. FEBS Lett. 138,193-197.
    • (1982) FEBS Lett. , vol.138 , pp. 193-197
    • Brzin, J.1    Kopitar, M.2    Locnikar, P.3    Turk, V.4
  • 41
    • 0021343788 scopus 로고
    • Human cystatin, a new protein inhibitor of cysteine proteinases
    • Brzin, J., Popovic, T., Turk, V. (1984). Human cystatin, a new protein inhibitor of cysteine proteinases. Biochem. Biophys. Res. Commun. 118,103-109.
    • (1984) Biochem. Biophys. Res. Commun. , vol.118 , pp. 103-109
    • Brzin, J.1    Popovic, T.2    Turk, V.3
  • 42
    • 0026575258 scopus 로고
    • Degradation of extracellular matrix proteins by human cathepsin B from normal tumour tissues
    • Buck, M.R., Karustic, D.G., Day, NA, Jonn, K.V., Sloane, B.F. (1992). Degradation of extracellular matrix proteins by human cathepsin B from normal tumour tissues. Biochem. J. 252, 273-278.
    • (1992) Biochem. J. , vol.252 , pp. 273-278
    • Buck, M.R.1    Karustic, D.G.2    Day3    Jonn4    Sloane, B.F.5
  • 43
    • 0028939165 scopus 로고
    • Synthesis secretion of procathepsin B cystatin C by human bronchial epithelial cells in vitro: Modulation of cathepsin a activity by neutrophil elastase
    • Burnett, D., Abrahamson, M., Devalia, J.L, Sapsford, R.J., Davies, R.J., Buttle, D.J. (1995). Synthesis secretion of procathepsin B cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin A activity by neutrophil elastase. Archs. Biochim. Biophys. 377,305-310.
    • (1995) Archs. Biochim. Biophys. , vol.377 , pp. 305-310
    • Burnett, D.1    Abrahamson, M.2    Devalia3    Sapsford4    Davies, R.J.5    Buttle, D.J.6
  • 44
    • 0023764678 scopus 로고
    • A catalytically active high-Mr form of human cathepsin B from sputum
    • Buttle, D.J., Bonner, B.C., Burnett, D., Barrett, A.J. (1988). A catalytically active high-Mr form of human cathepsin B from sputum. Biochem. J. 254,693-699.
    • (1988) Biochem. J. , vol.254 , pp. 693-699
    • Buttle, D.J.1    Bonner, B.C.2    Burnett, D.3    Barrett, A.J.4
  • 45
    • 0025105872 scopus 로고
    • Levels of neutrophil elastase cathepsin B activities, cystatins in human sputum, relationship to inflammation
    • Buttle, D.J., Burnett, D., Abrahamson, M. (1990). Levels of neutrophil elastase cathepsin B activities, cystatins in human sputum, relationship to inflammation. Sc. J. Clin. Lab. Invest. 50,509-516.
    • (1990) Sc. J. Clin. Lab. Invest. , vol.50 , pp. 509-516
    • Buttle, D.J.1    Burnett, D.2    Abrahamson, M.3
  • 46
    • 0025848068 scopus 로고
    • Human sputum cathepsin B degrades proteoglycan, is inhibited by aa-macroglobulin is modulated by neutrophil elastase cleavage of cathepsin B precursor cystatin C
    • Buttle, D.J., Abrahamson, M., Burnett, D., Mort, J.S., Barrett, A.J., Do, P.M., Hill, S.L. (1991). Human sputum cathepsin B degrades proteoglycan, is inhibited by aa-macroglobulin is modulated by neutrophil elastase cleavage of cathepsin B precursor cystatin C. Biochem. J. 276,325-331.
    • (1991) Biochem. J. , vol.276 , pp. 325-331
    • Buttle, D.J.1    Abrahamson, M.2    Burnett, D.3    Mort, J.S.4    Barrett, A.J.5    Do, P.M.6    Hill, S.L.7
  • 47
    • 0025320213 scopus 로고
    • Identification of cystatin C, a cysteine proteinase inhibitor, as a major secretory product of human alveolar macrophages in vitro
    • Chapman, H.A., Reilly, J.J., Yee, R., Grubb, A. (1990). Identification of cystatin C, a cysteine proteinase inhibitor, as a major secretory product of human alveolar macrophages in vitro. Am. Rev. Respir. Dis. 141,698-705.
    • (1990) Am. Rev. Respir. Dis. , vol.141 , pp. 698-705
    • Chapman, H.A.1    Reilly, J.J.2    Yee, R.3    Grubb, A.4
  • 49
    • 0000806552 scopus 로고
    • Clausen, J. Proteins in normal ceresbrospinal fluid not found in serum. (1961). Proc. Soc. Exp. Biol. Med. 707,170-172.
    • (1961) Proc. Soc. Exp. Biol. Med. , vol.707 , pp. 170-172
  • 50
    • 33746455657 scopus 로고
    • Induction of type 2 cystatin with systemically administered drugs
    • Cohen, R.E., Bedi, G.S., Neiders, M.E. (1989). Induction of type 2 cystatin with systemically administered drugs. J. Dent. Res. 69,167 (abstract 470).
    • (1989) J. Dent. Res. , vol.69 , Issue.167 , pp. 470
    • Cohen, R.E.1    Bedi, G.S.2    Neiders, M.E.3
  • 51
    • 0025256413 scopus 로고
    • Tissue distribution of an inducible cystatin in isoproterenol-treated rats
    • Cohen, R.E., Bedi, G.S., Neiders, M.E. (1990). Tissue distribution of an inducible cystatin in isoproterenol-treated rats. Lab. Invest. 62,452-458.
    • (1990) Lab. Invest. , vol.62 , pp. 452-458
    • Cohen, R.E.1    Bedi, G.S.2    Neiders, M.E.3
  • 52
    • 0010014006 scopus 로고
    • Anticarcinogenic activities of naturally occurring cysteine proteinase inhibitors
    • W. Troll A.R. Kennedy, eds. (New York: Plenum Press)
    • Colella, R., Chambers, A.F., Denhardt, D.T. (1993). Anticarcinogenic activities of naturally occurring cysteine proteinase inhibitors. In: Protease Inhibitors as Cancer Chemopreventive Agents. W. Troll A.R. Kennedy, eds. (New York: Plenum Press), pp. 199-216.
    • (1993) Protease Inhibitors as Cancer Chemopreventive Agents , pp. 199-216
    • Colella, R.1    Chambers, A.F.2    Denhardt, D.T.3
  • 53
    • 0017104823 scopus 로고
    • Occurrence of s-microglobulin post-y-globulin in human semen
    • Collé, A., Guinet, R., Leclerq, M., Manuel, Y. (1976). Occurrence of s-microglobulin post-y-globulin in human semen. Clin. Chim. Acta. 67,93-97.
    • (1976) Clin. Chim. Acta. , vol.67 , pp. 93-97
    • Collé, A.1    Guinet, R.2    Leclerq, M.3    Manuel, Y.4
  • 54
    • 0026063144 scopus 로고
    • Inhibitory effects of recombinant human cystatin C on human coronaviruses
    • Collins, A.R., Grubb, A. (1991). Inhibitory effects of recombinant human cystatin C on human coronaviruses. Antimicrobial Agents Chemotherapy 35,2444-2446.
    • (1991) Antimicrobial Agents Chemotherapy , vol.35 , pp. 2444-2446
    • Collins, A.R.1    Grubb, A.2
  • 55
    • 0026779586 scopus 로고
    • Cystatin C cathepsin B in human colon carcinoma: Expression by cell lines matrix degradation
    • Corticchiato, O., Cajot, J.-R, Abrahamson, M., Chan, S.J., Keppler, D. (1992). Cystatin C cathepsin B in human colon carcinoma: expression by cell lines matrix degradation. Int. J. Cancer. 52,645-652.
    • (1992) Int. J. Cancer. , vol.52 , pp. 645-652
    • Corticchiato, O.1    Cajot, J.-R.2    Abrahamson, M.3    Chan, S.J.4    Keppler, D.5
  • 56
    • 0023504662 scopus 로고
    • Preliminary studies on cysteine serine proteinase activities in inflamed human gingiva using different 7-amino-4-trifluoromethyl coumarin substrates protease inhibitors
    • Cox, S.W., Eley, B.M. (1987). Preliminary studies on cysteine serine proteinase activities in inflamed human gingiva using different 7-amino-4-trifluoromethyl coumarin substrates protease inhibitors. Archs. Oral Biol. 32,599-605.
    • (1987) Archs. Oral Biol. , vol.32 , pp. 599-605
    • Cox, S.W.1    Eley, B.M.2
  • 57
    • 0024820274 scopus 로고
    • Detection of cathepsin B- L-, elastase-, tryptase-, trypsin- dipeptidyl peptidase IVlike activities in crevicular fluid from gingivitis periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin
    • Cox, S.W., Eley, B.M. (1989). Detection of cathepsin B- L-, elastase-, tryptase-, trypsin- dipeptidyl peptidase IVlike activities in crevicular fluid from gingivitis periodontitis patients with peptidyl derivatives of 7-amino-4-trifluoromethyl coumarin. J. Periodont. Res. 24,353-361.
    • (1989) J. Periodont. Res. , vol.24 , pp. 353-361
    • Cox, S.W.1    Eley, B.M.2
  • 59
    • 0021251392 scopus 로고
    • Immunolocalization of human cystatins in neutrophils lymfocytes
    • Davies, M.E., Barrett, A.J. (1984). Immunolocalization of human cystatins in neutrophils lymfocytes. Histochemistry 50,373-377.
    • (1984) Histochemistry , vol.50 , pp. 373-377
    • Davies, M.E.1    Barrett, A.J.2
  • 60
    • 0020804419 scopus 로고
    • Identification of a cathepsin B-like protease in the crevicular fluid of gingivitis patients
    • Elsenhower, O.A., Hutchinson, R., Javed, T., McDonald, J.K. (1983). Identification of a cathepsin B-like protease in the crevicular fluid of gingivitis patients. J. Dent. Res. 62,917-921.
    • (1983) J. Dent. Res. , vol.62 , pp. 917-921
    • Elsenhower, O.A.1    Hutchinson, R.2    Javed, T.3    McDonald, J.K.4
  • 61
    • 0026478425 scopus 로고
    • Cathepsin B/L-, elastase-, tryptase-, trypsin- Dipeptidyl peptidase IV-like activities in gingival crevicular fluid, Correlation with clinical parameters in untreated chronic periodontitis patients
    • Eley, B.M., Cox, S.W. (1992a). Cathepsin B/L-, elastase-, tryptase-, trypsin- dipeptidyl peptidase IV-like activities in gingival crevicular fluid, Correlation with clinical parameters in untreated chronic periodontitis patients. J. Periodont. Res. 27, 62-69.
    • (1992) J. Periodont. Res. , vol.27 , pp. 62-69
    • Eley, B.M.1    Cox, S.W.2
  • 62
    • 0026863493 scopus 로고
    • Cathepsin B/L-, elastase-, tryptase-, trypsin- Dipeptidyl peptidase IV-like activities in gingival crevicular fluid, a comparison of levels before after periodontal surgery in chronic periodontitis patients
    • Eley, B.M., Cox, S.W. (1992b). Cathepsin B/L-, elastase-, tryptase-, trypsin- dipeptidyl peptidase IV-like activities in gingival crevicular fluid, a comparison of levels before after periodontal surgery in chronic periodontitis patients. J. Periodontol. 63,412-417.
    • (1992) J. Periodontol. , vol.63 , pp. 412-417
    • Eley, B.M.1    Cox, S.W.2
  • 65
    • 0025757378 scopus 로고
    • Structure expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor
    • Freije, J.P., Abrahamson, M., Olafsson, I., Velasco, G., Grubb, A., Lôpez-Otin, C. (1991). Structure expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor. J. Biol. Chem. 266,20538-20543.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20538-20543
    • Freije, J.P.1    Abrahamson, M.2    Olafsson, I.3    Velasco, G.4    Grubb, A.5    Lôpez-Otin, C.6
  • 67
    • 0027242118 scopus 로고
    • Human cystatin D. cDNA cloning, characterization of the Escherichia coli expressed inhibitor, identification of the native protein in saliva
    • Freije, J.P., Balbîn, M., Abrahamson, M., Velasco, G., Dalboge, H., Grubb, A., Lôpez-Otin, C. (1993b). Human cystatin D. cDNA cloning, characterization of the Escherichia coli expressed inhibitor, identification of the native protein in saliva. J. Biol. Chem. 268,15737-15744.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15737-15744
    • Freije, J.P.1    Balbîn, M.2    Abrahamson, M.3    Velasco, G.4    Dalboge, H.5    Grubb, A.6    Lôpez-Otin, C.7
  • 68
    • 0023009152 scopus 로고
    • Components of saliva inactivate human immunodeficiency virus
    • Fultz, P.N. (1986). Components of saliva inactivate human immunodeficiency virus. Lancet. //, 1215.
    • (1986) Lancet , vol.1215
    • Fultz, P.N.1
  • 69
  • 70
    • 0011766298 scopus 로고
    • Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelic type is a variant of gamma-trace basic protein (cystatin C)
    • Ghiso, J., Jensson, O., Frangione, B. (1986). Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelic type is a variant of gamma-trace basic protein (cystatin C). Proc. Natl. Acad. Sei. USA. 83,2974-2978.
    • (1986) Proc. Natl. Acad. Sei. USA. , vol.83 , pp. 2974-2978
    • Ghiso, J.1    Jensson, O.2    Frangione, B.3
  • 71
    • 0025063904 scopus 로고
    • Binding of cystatin C to C4, the importance of senseantisense peptides in their interaction
    • Ghiso, J., Saball, E., Leoni, J., Rostagno, A., Frangione, B. (1990). Binding of cystatin C to C4, the importance of senseantisense peptides in their interaction. Proc. Natl. Acad. Sei. USA. 87,1288-1291.
    • (1990) Proc. Natl. Acad. Sei. USA. , vol.87 , pp. 1288-1291
    • Ghiso, J.1    Saball, E.2    Leoni, J.3    Rostagno, A.4    Frangione, B.5
  • 72
    • 0021346826 scopus 로고
    • Cystatin-like cysteine proteinase inhibitors from human liver
    • Green, G.D.J., Kembhavi, A.A., Davies, M.E., Barrett, A.J. (1984). Cystatin-like cysteine proteinase inhibitors from human liver. Biochem. J. 218,939-946.
    • (1984) Biochem. J. , vol.218 , pp. 939-946
    • Green, G.D.J.1    Kembhavi, A.A.2    Davies, M.E.3    Barrett, A.J.4
  • 74
    • 0027058414 scopus 로고
    • Diagnostic value of analysis of cystatin C protein HC in biological fluids
    • Grubb, A. (1992). Diagnostic value of analysis of cystatin C protein HC in biological fluids. Clin. Nephr. 38, S20-S27.
    • (1992) Clin. Nephr. , vol.38
    • Grubb, A.1
  • 75
    • 0040635025 scopus 로고
    • Human -y-trace, a basic microprotein, amino acid sequence presence in the adenohypophysis
    • Grubb, A., Löfberg, H. (1982). Human -y-trace, a basic microprotein, amino acid sequence presence in the adenohypophysis. Proc. Natl. Acad. Sei. USA 79,3024-3027.
    • (1982) Proc. Natl. Acad. Sei. USA , vol.79 , pp. 3024-3027
    • Grubb, A.1    Löfberg, H.2
  • 76
    • 0020609588 scopus 로고
    • The -y-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma
    • Grubb, A., Weiber, H., Löfberg, H. (1983). The -y-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma. Sc. J. Clin. Lab. Invest. 43,421 -425.
    • (1983) Sc. J. Clin. Lab. Invest. , vol.43 , pp. 421-425
    • Grubb, A.1    Weiber, H.2    Löfberg, H.3
  • 78
    • 0022396733 scopus 로고
    • Serum concentration of cystatin C, Factor D 2-microglobulin as a measure of glomerular filtration rate
    • Grubb, A., Simonsen, O., Sturfelt, L., Truedsson, L., Thysell, H. (1985). Serum concentration of cystatin C, Factor D 2-microglobulin as a measure of glomerular filtration rate. Acta Med. Sc. 218,499-503.
    • (1985) Acta Med. Sc. , vol.218 , pp. 499-503
    • Grubb, A.1    Simonsen, O.2    Sturfelt, L.3    Truedsson, L.4    Thysell, H.5
  • 80
    • 0027329828 scopus 로고
    • In vitro study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like L
    • Guinée, N., Dalet-Fumeron, V., Pagano, M. (1993). In vitro study of basement membrane degradation by the cysteine proteinases, cathepsins B, B-like L. Biol. Chem. HoppeSeyler. 374,1135-1146.
    • (1993) Biol. Chem. HoppeSeyler. , vol.374 , pp. 1135-1146
    • Guinée, N.1    Dalet-Fumeron, V.2    Pagano, M.3
  • 81
    • 0026070511 scopus 로고
    • A specific inhibitor of cysteine proteinase impairs a Vif-dependent modification of human immunodeficiency virus typel Env protein
    • Guy B., Geist, M., Dott, K., Spehner, D., Kieny, M.-R, Lecocq, J.-R (1991). A specific inhibitor of cysteine proteinase impairs a Vif-dependent modification of human immunodeficiency virus typel Env protein. J. Viral. 65,1325-1331.
    • (1991) J. Viral. , vol.65 , pp. 1325-1331
    • Guy, B.1    Geist, M.2    Dott, K.3    Spehner, D.4    Kieny, M.-R.5    Lecocq, J.-R.6
  • 83
    • 0027408783 scopus 로고
    • Importance of the evolutionary conserved glycin residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition
    • Hall, A., Dalboge, H., Grubb, A., Abrahamson, M. (1993). Importance of the evolutionary conserved glycin residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition. Biochem. J. 297,123-129,
    • (1993) Biochem. J. , vol.297 , pp. 123-129
    • Hall, A.1    Dalboge, H.2    Grubb, A.3    Abrahamson, M.4
  • 84
    • 0024256223 scopus 로고
    • Molecular cloning of mouse epidermal cystatin a detection of regulated expression in differentiation tumorigenesis
    • Hawley-Nelson, P., Roop, D.H., Cheng, C.K., Krieg, T.M., Yuspa, S.H. (1988). Molecular cloning of mouse epidermal cystatin A detection of regulated expression in differentiation tumorigenesis. Mol. Carcinogen. 1,202-211.
    • (1988) Mol. Carcinogen. , vol.1 , pp. 202-211
    • Hawley-Nelson, P.1    Roop, D.H.2    Cheng, C.K.3    Krieg, T.M.4    Yuspa, S.H.5
  • 85
    • 0027355946 scopus 로고
    • Protein, albumin cystatin concentrations in saliva of healthy subjects of patients with gingivitis or periodontitis
    • Henskens, Y.M.C., Van der Velden, U., Veerman, E.C.I., Nieuw Amerongen, A.V. (1993a). Protein, albumin cystatin concentrations in saliva of healthy subjects of patients with gingivitis or periodontitis. J. Periodont. Res. 28,43-48.
    • (1993) J. Periodont. Res. , vol.28 , pp. 43-48
    • Henskens, Y.M.C.1    Van Der Velden, U.2    Veerman, E.C.I.3    Nieuw Amerongen, A.V.4
  • 90
    • 33746444288 scopus 로고
    • Trace proteins in ceresbrospinal fluid other biological fluids. I. Effect of various fractionation procedures on -trace -y-trace proteins methods for isolation of both proteins
    • Hochwald, G.M., Thorbecke, G.J. (1963). Trace proteins in ceresbrospinal fluid other biological fluids. I. Effect of various fractionation procedures on -trace -y-trace proteins methods for isolation of both proteins. Archs. Biochem. Biophys. 101,325-334.
    • (1963) Archs. Biochem. Biophys. , vol.101 , pp. 325-334
    • Hochwald, G.M.1    Thorbecke, G.J.2
  • 91
    • 0014061584 scopus 로고
    • Trace proteins in biological fluids. IV. Physicochemical properties sites of formation of -y-trace -trace proteins
    • Hochwald, G.M., Pepe, A.J., Thorbecke, G.J. (1967). Trace proteins in biological fluids. IV. Physicochemical properties sites of formation of -y-trace -trace proteins. Proc. Soc. Exp. Biol. Med. 124, 961 -966.
    • (1967) Proc. Soc. Exp. Biol. Med. , vol.124 , pp. 961-966
    • Hochwald, G.M.1    Pepe, A.J.2    Thorbecke, G.J.3
  • 92
    • 0020532195 scopus 로고
    • Separation of cysteine proteinase inhibitors from psoriatic scale
    • Hopsu-Havu, V, Järvinen, M., Rinne, A. (1983). Separation of cysteine proteinase inhibitors from psoriatic scale. Brit. J. Dermatol. 709,77-85.
    • (1983) Brit. J. Dermatol. , vol.709 , pp. 77-85
    • Hopsu-Havu, V.1    Järvinen, M.2    Rinne, A.3
  • 93
    • 0021882035 scopus 로고
    • The distribution of cathepsin B in human tissues
    • Howie, A.J., Burnett, D., Crocker, J. (1985). The distribution of cathepsin B in human tissues. J. Pathol. 145,307-314.
    • (1985) J. Pathol. , vol.145 , pp. 307-314
    • Howie, A.J.1    Burnett, D.2    Crocker, J.3
  • 94
    • 0025970993 scopus 로고
    • Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21
    • Hsieh, W.-T, Fong, D., Sloane, B.F., Golembieski, W., Smith, D.I. (1991). Mapping of the gene for human cysteine proteinase inhibitor stefin A, STF1, to chromosome 3cen-q21. Genomics. 9,207-209.
    • (1991) Genomics. , vol.9 , pp. 207-209
    • Hsieh, W.-T.1    Fong, D.2    Sloane, B.F.3    Golembieski, W.4    Smith, D.I.5
  • 95
    • 0026829596 scopus 로고
    • Cystatin activity in gingival crevicular fluid from periodontal disease patients measured by a new quantitative analysis method
    • Ichimaru, E., Imura, K., Hara, Y, Kato, Y, Kato, I. (1992). Cystatin activity in gingival crevicular fluid from periodontal disease patients measured by a new quantitative analysis method. J. Periodont. Res. 27,119-125.
    • (1992) J. Periodont. Res. , vol.27 , pp. 119-125
    • Ichimaru, E.1    Imura, K.2    Hara, Y.3    Kato, Y.4    Kato, I.5
  • 96
    • 0021152013 scopus 로고
    • Isolation amino acid sequence of SAP-1, an acidic protein of human whole saliva, sequence homology with human -y-trace
    • Isemura, S., Saitoh, E., Sanada, K. (1984a). Isolation amino acid sequence of SAP-1, an acidic protein of human whole saliva, sequence homology with human -y-trace. J. Biochem. 96,489-498.
    • (1984) J. Biochem. , vol.96 , pp. 489-498
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 97
    • 0021134636 scopus 로고
    • Cystatin-S, a cysteine proteinase inhibitor of human whole saliva, J
    • Isemura, S., Saitoh, E., Ito, S., Isemura, M., Sanada, K. (1984b). Cystatin-S, A cysteine proteinase inhibitor of human whole saliva, J. Biochem. 96,1311 -1314.
    • (1984) Biochem. , vol.96 , pp. 1311-1314
    • Isemura, S.1    Saitoh, E.2    Ito, S.3    Isemura, M.4    Sanada, K.5
  • 98
    • 0022444892 scopus 로고
    • Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S
    • Isemura, S., Saitoh, E., Sanada, K. (1986). Characterization of a new cysteine proteinase inhibitor of human saliva, cystatin SN, which is immunologically related to cystatin S. FEBS Lett. 795,145-149.
    • (1986) FEBS Lett. , vol.795 , pp. 145-149
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 99
    • 0023433543 scopus 로고
    • Characterization amino acid sequence of a new acidic cysteine proteinase inhibitor (Cystatin SA) structurally closely related to cystatin S, from human saliva
    • Isemura, S., Saitoh, E., Sanada, K. (1987). Characterization amino acid sequence of a new acidic cysteine proteinase inhibitor (Cystatin SA) structurally closely related to cystatin S, from human saliva. J. Biochem. 102, 693-704.
    • (1987) J. Biochem. , vol.102 , pp. 693-704
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3
  • 100
    • 0026010564 scopus 로고
    • Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, two phosphorylated forms of cystatin S) in human whole saliva determination of phosphorylation sites of cystatin S
    • Isemura, S., Saitoh, E., Sanada, K., Minakata, K. (1991 ). Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, two phosphorylated forms of cystatin S) in human whole saliva determination of phosphorylation sites of cystatin S. J. Biochem. 110, 648-654.
    • (1991) J. Biochem. , vol.110 , pp. 648-654
    • Isemura, S.1    Saitoh, E.2    Sanada, K.3    Minakata, K.4
  • 101
    • 0029041438 scopus 로고
    • Transthyretin cystatin C are catabolized in proximal tubular epithelial cells the proteins are not useful as markers for renal cell carcinomas
    • Jacobsson, B., Lignelid, H., Bergerheim, U.S.R. (1995). Transthyretin cystatin C are catabolized in proximal tubular epithelial cells the proteins are not useful as markers for renal cell carcinomas. Histopathol. 26,559-564.
    • (1995) Histopathol. , vol.26 , pp. 559-564
    • Jacobsson, B.1    Lignelid, H.2    Bergerheim, U.S.R.3
  • 102
    • 0018175625 scopus 로고
    • Purification some characteristics of the human epidermal SH-protease inhibitor
    • Järvinen, M. (1978). Purification some characteristics of the human epidermal SH-protease inhibitor. J. Invest. Dermatol. 77,114-118.
    • (1978) J. Invest. Dermatol. , vol.77 , pp. 114-118
    • Järvinen, M.1
  • 103
    • 0343745748 scopus 로고
    • Human cystatins in normal diseased tissues-A review
    • Järvinen, M., Rinne, A., Hopsu-Havu, V.K. (1987). Human cystatins in normal diseased tissues-A review. Acta Histochem. 02,5-18.
    • (1987) Acta Histochem. , vol.2 , pp. 5-18
    • Järvinen, M.1    Rinne, A.2    Hopsu-Havu, V.K.3
  • 104
    • 0027222966 scopus 로고
    • Molecular diagnosis of hereditary cystatin C amyloid angiopathy
    • Jonsdottir, S., Palsdottir, A. (1993). Molecular diagnosis of hereditary cystatin C amyloid angiopathy. Biochem. Med. Met. Biol. 49,117-123.
    • (1993) Biochem. Med. Met. Biol. , vol.49 , pp. 117-123
    • Jonsdottir, S.1    Palsdottir, A.2
  • 105
    • 0018651320 scopus 로고
    • Isolation partial characterization of three acidic proteins from human submibu-lar saliva
    • Juriaanse, A.C., Booij, M. (1979a). Isolation partial characterization of three acidic proteins from human submibu-lar saliva. Archs. Oral Biol. 24,621 -625.
    • (1979) Archs. Oral Biol. , vol.24 , pp. 621-625
    • Juriaanse, A.C.1    Booij, M.2
  • 106
    • 0018651328 scopus 로고
    • Isolation characterization of the main neutral protein from human submibular saliva
    • Juriaanse, A.C., Booij, M. (1979b). Isolation characterization of the main neutral protein from human submibular saliva. Archs. Oral Biol. 24,825-828.
    • (1979) Archs. Oral Biol. , vol.24 , pp. 825-828
    • Juriaanse, A.C.1    Booij, M.2
  • 107
    • 0028245396 scopus 로고
    • Determinants of the serum concentrations of low molecular weight proteins in patients on maintenance hemodialysis
    • Kaba, A., Jadoul, M., Pochet, J.M., Lauwerys, R., Van Ypersele de Strihou, C., Bernard, A. (1994). Determinants of the serum concentrations of low molecular weight proteins in patients on maintenance hemodialysis. Kidney. Int. 45, 1689-1696.
    • (1994) Kidney. Int. , vol.45 , pp. 1689-1696
    • Kaba, A.1    Jadoul, M.2    Pochet, J.M.3    Lauwerys, R.4    Bernard, A.5
  • 110
    • 0025017237 scopus 로고
    • Viral proteinases, weakness strength
    • Kay, J., Dünn, B.M. (1990). Viral proteinases, weakness strength. Biochim. Biophys. Acta. 1048,1-18.
    • (1990) Biochim. Biophys. Acta. , vol.1048 , pp. 1-18
    • Kay, J.1    Dünn, B.M.2
  • 111
    • 0028356053 scopus 로고
    • Latency of cathepsin B secreted by human colon carcinoma cells is not secretion of cystatin C is relieved by neutrophil elastase
    • Keppler, D., Waridel, R, Abrahamson, M., Bachmann, D., Berdoz, J., Sordat, B. (1994). Latency of cathepsin B secreted by human colon carcinoma cells is not secretion of cystatin C is relieved by neutrophil elastase. Biochim. Biophys. Acta 7226,117-128.
    • (1994) Biochim. Biophys. Acta , vol.7226 , pp. 117-128
    • Keppler, D.1    Waridel, R.2    Abrahamson, M.3    Bachmann, D.4    Berdoz, J.5    Sordat, B.6
  • 112
    • 0025895698 scopus 로고
    • The selective role of cathepsins B D in the lysosomal degradation of endogenous exogenous proteins
    • Kominami, E., Ueno.T., Muno, D., Katunuma, N. (1991). The selective role of cathepsins B D in the lysosomal degradation of endogenous exogenous proteins. FEES Lett. 287, 189-192.
    • (1991) FEES Lett. , vol.287 , pp. 189-192
    • Kominami, E.1    Ueno, T.2    Muno, D.3    Katunuma, N.4
  • 113
    • 0026505938 scopus 로고
    • Inhibitory effect of oryzacystatins a truncation mutant on the replication of poliovirus in infected Vero cells
    • Kondo, H., Ijjri, S., Abe, K., Maeda, H., Aral, S. (1992). Inhibitory effect of oryzacystatins a truncation mutant on the replication of poliovirus in infected Vero cells. FEBS Lett. 299, 48-50.
    • (1992) FEBS Lett. , vol.299 , pp. 48-50
    • Kondo, H.1    Ijjri, S.2    Abe, K.3    Maeda, H.4    Aral, S.5
  • 114
    • 0021844663 scopus 로고
    • Cystatin, a protein inhibitor of cysteine proteinases alters viral protein cleavages in infected human cells
    • Korant, B.D., Brzin, J., Turk, V. (1985). Cystatin, a protein inhibitor of cysteine proteinases alters viral protein cleavages in infected human cells. Biochem. Biophys. Res. Commun. 727, 1072-1076.
    • (1985) Biochem. Biophys. Res. Commun. , vol.727 , pp. 1072-1076
    • Korant, B.D.1    Brzin, J.2    Turk, V.3
  • 117
    • 0028339254 scopus 로고
    • Imbalance between cathepsin B cysteine proteinase inhibitors is of prognostic significance in human lung cancer
    • Knoch, H., Werle, B., Ebert, W., Spiess, E. (1994). Imbalance between cathepsin B cysteine proteinase inhibitors is of prognostic significance in human lung cancer. Int. J. Oncol. 5, 77-85.
    • (1994) Int. J. Oncol. , vol.5 , pp. 77-85
    • Knoch, H.1    Werle, B.2    Ebert, W.3    Spiess, E.4
  • 120
    • 0025002175 scopus 로고
    • Cysteine proteinase inhibitors in human cancerous tissues fluids
    • Lah, T.T., Kokalj-Kunovar, M., Turk, V. (1990). Cysteine proteinase inhibitors in human cancerous tissues fluids. Biol. Chem. Hoppe-Seyler. 377,199-203.
    • (1990) Biol. Chem. Hoppe-Seyler. , vol.377 , pp. 199-203
    • Lah, T.T.1    Kokalj-Kunovar, M.2    Turk, V.3
  • 125
    • 33746455656 scopus 로고
    • A note of proteins apparently "specific" for ceresbrospinal fluid
    • Laterre, B.C., Heremans, J.F. 1963. A note of proteins apparently "specific" for ceresbrospinal fluid. Clin. Chim. Acta 8, 220-226.
    • (1963) Clin. Chim. Acta , vol.8 , pp. 220-226
    • Laterre, B.C.1    Heremans, J.F.2
  • 128
    • 0026587183 scopus 로고
    • Human cystatin C, a cysteine proteinase inhibitor, inhibits bone résorption in vitro stimulated by parathyroid hormone parathyroid hormone-related peptide of malignancy
    • Lerner, U.H., Grubb, A. (1992). Human cystatin C, a cysteine proteinase inhibitor, inhibits bone résorption in vitro stimulated by parathyroid hormone parathyroid hormone-related peptide of malignancy. J. Bone Min. Res. 7,433-440.
    • (1992) J. Bone Min. Res. , vol.7 , pp. 433-440
    • Lerner, U.H.1    Grubb, A.2
  • 129
    • 0025218056 scopus 로고
    • Modulation of phagocytosis-associated respiratory burst by human cystatin C, role of the N-terminal tetrapeptide Lys-Pra-Pro-Arg
    • Leung-Tack, J., Tavera, C., Gensac, M.C., Martinez, J., Colle, A. (1990a). Modulation of phagocytosis-associated respiratory burst by human cystatin C, role of the N-terminal tetrapeptide Lys-Pra-Pro-Arg. Exp. Cell Res. 188,16-22.
    • (1990) Exp. Cell Res. , vol.188 , pp. 16-22
    • Leung-Tack, J.1    Tavera, C.2    Gensac, M.C.3    Martinez, J.4    Colle, A.5
  • 130
    • 0025306567 scopus 로고
    • Neutrophil chemotactic activity is modulated by human cystatin C, an inhibitor of cysteine proteinases
    • Leung-Tack, J., Tavera, C., Martinez, J., Colle, A. (1990b). Neutrophil chemotactic activity is modulated by human cystatin C, an inhibitor of cysteine proteinases. Inflammation. 14, 247-258.
    • (1990) Inflammation. , vol.14 , pp. 247-258
    • Leung-Tack, J.1    Tavera, C.2    Martinez, J.3    Colle, A.4
  • 131
    • 0024504095 scopus 로고
    • Stroke in Icelic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteinases
    • Levy, E., Lopez-Otin, C., Ghiso, J., Geltner, D., Frangione, B. (1989). Stroke in Icelic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteinases. J. Exp. Med. 169,1771-1778.
    • (1989) J. Exp. Med. , vol.169 , pp. 1771-1778
    • Levy, E.1    Lopez-Otin, C.2    Ghiso, J.3    Geltner, D.4    Frangione, B.5
  • 132
    • 0027378622 scopus 로고
    • Abnormal distribution of cathepsin proteinases endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam senile dementia in the aged
    • Li, K., Ito, H., Kominami, E., Hirano, A. (1993). Abnormal distribution of cathepsin proteinases endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam senile dementia in the aged. Virchows Archs. A. Pathol. Anat. 423,185-194.
    • (1993) Virchows Archs. A. Pathol. Anat. , vol.423 , pp. 185-194
    • Li, K.1    Ito, H.2    Kominami, E.3    Hirano, A.4
  • 133
    • 0027053955 scopus 로고
    • Cystatin C in the human pancreas gut: An immunohistochemical study of normal neoplastic tissues
    • Lignelid, H., Jacobsson, B. (1992). Cystatin C in the human pancreas gut: an immunohistochemical study of normal neoplastic tissues. Virchows Archiv. A. Pathol. Anat. 421, 491-495.
    • (1992) Virchows Archiv. A. Pathol. Anat. , vol.421 , pp. 491-495
    • Lignelid, H.1    Jacobsson, B.2
  • 134
    • 0023801371 scopus 로고
    • Interaction of the cysteine proteinase inhibitor chicken cystatin with papain
    • Lindahl, P., Alriksson, E., Jörnwall, Björk, I. (1988). Interaction of the cysteine proteinase inhibitor chicken cystatin with papain. Biochemistry 27,5074-5082.
    • (1988) Biochemistry , vol.27 , pp. 5074-5082
    • Lindahl, P.1    Alriksson, E.2    Jörnwall3    Björk, I.4
  • 135
    • 0026570448 scopus 로고
    • Interaction of recombinant human cystatin C with cysteine proteinases papain actinidin
    • Lindahl, P., Abrahamson, M., Björk, I. (1992). Interaction of recombinant human cystatin C with cysteine proteinases papain actinidin. Biochem. J. 281,49-55.
    • (1992) Biochem. J. , vol.281 , pp. 49-55
    • Lindahl, P.1    Abrahamson, M.2    Björk, I.3
  • 136
    • 0018718823 scopus 로고
    • Quantification of gamma-trace in human biological fluids, indication for production in the central nervous system
    • Löfberg, H., Grubb, A. (1979). Quantification of gamma-trace in human biological fluids, indication for production in the central nervous system. Sc. J. Clin. Lab. Invest. 39,619-626.
    • (1979) Sc. J. Clin. Lab. Invest. , vol.39 , pp. 619-626
    • Löfberg, H.1    Grubb, A.2
  • 137
    • 0018904393 scopus 로고
    • The cerebrospinal fluid plasma concentrations of gammatrace beta2-microglobulin at various ages in neurological disorders
    • Löfberg, H., Grubb, A., Sveger, T., Olsson, J.E. (1980). The cerebrospinal fluid plasma concentrations of gammatrace beta2-microglobulin at various ages in neurological disorders. J. Neural. 223,159-170.
    • (1980) J. Neural. , vol.223 , pp. 159-170
    • Löfberg, H.1    Grubb, A.2    Sveger, T.3    Olsson, J.E.4
  • 139
    • 0023159948 scopus 로고
    • Immunohistochemical characterization of the amyloid deposits quantitation of pertinent cerebrospinal hemorrhage with amyloidosis
    • Löfberg, H., Grubb, A., Nilsson, E.K., Jensson, O., Gudmundsson, G., Blöndal, H., Arnason, A., Thorsteinsson, L. (1987). Immunohistochemical characterization of the amyloid deposits quantitation of pertinent cerebrospinal hemorrhage with amyloidosis. Stroke 18,431 -440.
    • (1987) Stroke , vol.18 , pp. 431-440
    • Löfberg, H.1    Grubb, A.2    Nilsson, E.K.3    Jensson, O.4    Gudmundsson, G.5    Blöndal, H.6    Arnason, A.7    Thorsteinsson, L.8
  • 140
    • 0021080396 scopus 로고
    • Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Machleidt, W., Borchart, U., Fritz, H., Brzin, J., Ritonja, A., Turk, V. (1983). Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Biol. Chem. Hoppe-Seyler. 364, S1481-S1486.
    • (1983) Biol. Chem. Hoppe-Seyler , vol.364
    • Machleidt, W.1    Borchart, U.2    Fritz, H.3    Brzin, J.4    Ritonja, A.5    Turk, V.6
  • 142
    • 0025918732 scopus 로고
    • Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: Kinetic studies with natural recombinant variants of cystatins stefins
    • Machleidt, W., Thiele, U., Assfalg-Machleidt, I., Forger, D., Auerswald, E.A. (1991). Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural recombinant variants of cystatins stefins. Biomed. Biochim. Acta. 50,613-620.
    • (1991) Biomed. Biochim. Acta. , vol.50 , pp. 613-620
    • Machleidt, W.1    Thiele, U.2    Assfalg-Machleidt, I.3    Forger, D.4    Auerswald, E.A.5
  • 143
    • 0027217252 scopus 로고
    • HIV in the oral cavity, virus, viral inhibitory activity antiviral antibodies, a review
    • Malamud, D., Friedman, H.M. (1993). HIV in the oral cavity, virus, viral inhibitory activity antiviral antibodies, a review. Crit. Rev. Oral. Biol. Med. 4,461 -466.
    • (1993) Crit. Rev. Oral. Biol. Med. , vol.4 , pp. 461-466
    • Malamud, D.1    Friedman, H.M.2
  • 144
    • 0026667617 scopus 로고
    • Characterization of amyloid fibril protein from a case of cerebral amyloid angiopathy showing immunohistochemical reactivity for both beta protein cystatin C
    • Maruyama, K., Kametani, F., Ikeda, S., Ishihara, T., Yanagisawa, N. (1992). Characterization of amyloid fibril protein from a case of cerebral amyloid angiopathy showing immunohistochemical reactivity for both beta protein cystatin C. Neurosci. Lett. 144,38-42.
    • (1992) Neurosci. Lett. , vol.144 , pp. 38-42
    • Maruyama, K.1    Kametani, F.2    Ikeda, S.3    Ishihara, T.4    Yanagisawa, N.5
  • 145
    • 0027428152 scopus 로고    scopus 로고
    • McKerrow, J.H. The proteases pathogenicity of parasitic protozoa. Annu. Rev. Microbiol. 47,821 -853.
    • , vol.47 , pp. 821-853
    • The Proteases, M.J.H.1
  • 146
    • 0006321271 scopus 로고
    • Quantitative estimation of the-yc-globulin in normal pathological cerebrospinal fluids by an immunochemical method
    • McPherson, C.F.C. (1965). Quantitative estimation of the-yc-globulin in normal pathological cerebrospinal fluids by an immunochemical method. Clin. Chim. Acta 11,298-309.
    • (1965) Clin. Chim. Acta , vol.11 , pp. 298-309
    • McPherson, C.F.C.1
  • 147
    • 0021257265 scopus 로고
    • New protein inhibitors of cysteine proteinases in human saliva salivary gls
    • Minakata, K., Asano, M. (1984). New protein inhibitors of cysteine proteinases in human saliva salivary gls. Biol. Chem. Hoppe-Seyler. 365,399-403.
    • (1984) Biol. Chem. Hoppe-Seyler. , vol.365 , pp. 399-403
    • Minakata, K.1    Asano, M.2
  • 151
    • 0026752356 scopus 로고
    • Induction of cystatin S in rat submibular gls by papain
    • Naito, Y, Suzuki, I., Hasegawa, S. (1992). Induction of cystatin S in rat submibular gls by papain. Comp. Biochem. Physiol. 102B, 861 -865.
    • (1992) Comp. Biochem. Physiol. , vol.102 B , pp. 861-865
    • Naito, Y.1    Suzuki, I.2    Hasegawa, S.3
  • 153
    • 0028934503 scopus 로고
    • Serum cystatin C measured by automated immunoassay: A more sensitive marker of changes in GFR than serum creatinine
    • Newman, D.J., Thakkar, H., Edwards, R.G., Wilkie, M., White, T., Grubb, A., Price, C.P. (1995). Serum cystatin C measured by automated immunoassay: a more sensitive marker of changes in GFR than serum creatinine. Kidney. Int. 47,312-318.
    • (1995) Kidney. Int. , vol.47 , pp. 312-318
    • Newman, D.J.1    Thakkar, H.2    Edwards, R.G.3    Wilkie, M.4    White, T.5    Grubb, A.6    Price, C.P.7
  • 154
    • 0021191980 scopus 로고
    • Athiol protease inhibitor released from cultured human malignant melanoma cells
    • Nishida, Y, Sumi, H., Mihara, H. (1984). Athiol protease inhibitor released from cultured human malignant melanoma cells. Cancer Res. 44,3324-3329.
    • (1984) Cancer Res. , vol.44 , pp. 3324-3329
    • Nishida, Y.1    Sumi, H.2    Mihara, H.3
  • 155
    • 0021676017 scopus 로고
    • Isolation of a human cDNA for a2-thiol proteinases inhibitor its identity with Low Molecular Weight Kininogen
    • Ohkubo, I., Kurachi, K., Takasawa, T., Shiokawa, H., Sasaki, M. (1984). Isolation of a human cDNA for a2-thiol proteinases inhibitor its identity with Low Molecular Weight Kininogen. Biochemistry 23,5691 -5697.
    • (1984) Biochemistry , vol.23 , pp. 5691-5697
    • Ohkubo, I.1    Kurachi, K.2    Takasawa, T.3    Shiokawa, H.4    Sasaki, M.5
  • 156
    • 0020039346 scopus 로고
    • Biochemical properties of thiol proteinase inhibitors purified from psoriatic scales
    • Othani, O., Fukuyama, K., Epstein, W.L. (1982). Biochemical properties of thiol proteinase inhibitors purified from psoriatic scales. J. Invest. Dermatol. 82,280-284.
    • (1982) J. Invest. Dermatol. , vol.82 , pp. 280-284
    • Othani, O.1    Fukuyama, K.2    Epstein, W.L.3
  • 158
    • 0006367748 scopus 로고
    • Trace proteins in biological fluids III. Quantitation of -y-trace major spinal fluid proteins including -trace
    • Pepe, A.J., Hochwald, G.M. (1967). Trace proteins in biological fluids III. Quantitation of -y-trace major spinal fluid proteins including -trace. Proc. Soc. Exp. Biol. Med. 126, 630-633.
    • (1967) Proc. Soc. Exp. Biol. Med. , vol.126 , pp. 630-633
    • Pepe, A.J.1    Hochwald, G.M.2
  • 159
    • 0026018131 scopus 로고
    • Largescale purification characterization of the major phosphoproteins mucins of human submibular-sublingual saliva
    • Ramasubbu, N., Reddy, M.S., Bergey, E.J., Haraszthy, G., Soni, S.-D., Levine, M.J. (1991). Largescale purification characterization of the major phosphoproteins mucins of human submibular-sublingual saliva. Biochem. J. 280, 341-352.
    • (1991) Biochem. J. , vol.280 , pp. 341-352
    • Ramasubbu, N.1    Reddy, M.S.2    Bergey, E.J.3    Haraszthy, G.4    Soni, S.-D.5    Levine, M.J.6
  • 160
    • 0025392051 scopus 로고
    • Comparison of a salivary 14 kD protein displaying cysteine proteinase inhibitory activity with other salivary cystatins
    • Rathman, W.M., Van Zeyl, M.J., Van den Keijbus, P.A.M., Veerman, E.C.I., Nieuw Amerongen, A.V. (1990a). Comparison of a salivary 14 kD protein displaying cysteine proteinase inhibitory activity with other salivary cystatins. J. Biol. Buc. 18, 9-18.
    • (1990) J. Biol. Buc. , vol.18 , pp. 9-18
    • Rathman, W.M.1    Van Zeyl, M.J.2    Van Den Keijbus, P.A.M.3    Veerman, E.C.I.4    Nieuw Amerongen, A.V.5
  • 161
    • 0025395696 scopus 로고
    • Characterization of monoclonal antibodies to human salivary (glyco)proteins. Cellular localization of mucin, cystatin-like 14 kD protein 20 kD glycoprotein in the human submibular
    • Rathman, W.M., Van den Keijbus, P.A.M., Van Zeyl, M.J., Döpp, E.A., Veerman, E.C.I., Nieuw Amerongen, A.V. (1990b). Characterization of monoclonal antibodies to human salivary (glyco)proteins. Cellular localization of mucin, cystatin-like 14 kD protein 20 kD glycoprotein in the human submibular gl. J. Biol. Buc. 18,19-27.
    • (1990) Gl. J. Biol. Buc. , vol.18 , pp. 19-27
    • Rathman, W.M.1    Van Den Keijbus, P.A.M.2    Van Zeyl, M.J.3    Döpp, E.A.4    Veerman, E.C.I.5    Nieuw Amerongen, A.V.6
  • 162
    • 0004924526 scopus 로고
    • In: Minor proteins from human mucous salivary gls
    • Thesis, Amsterdam, Free University
    • Rathman, W.M. (1990c). In: Minor proteins from human mucous salivary gls. A biochemical immunological approach. Thesis, Amsterdam, Free University, pp. 105-120.
    • (1990) A Biochemical Immunological Approach , pp. 105-120
    • Rathman, W.M.1
  • 163
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings, N.D., Barre, A.J. (1990). Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 30,60-71.
    • (1990) J. Mol. Evol. , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barre, A.J.2
  • 164
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human rat liver
    • Ritonja, A., Machleidt, W., Barrett, A.J. (1985). Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human rat liver. Biochem. Biophys. Res. Commun. 131,1187-1192.
    • (1985) Biochem. Biophys. Res. Commun. , pp. 131
    • Ritonja, A.1    Machleidt, W.2    Barrett, A.J.3
  • 166
    • 0024692293 scopus 로고
    • Tissue distribution of RNAs for cystatins, histatins, statherin proline-rich salivary proteins in humans macaques
    • Sabatini, L.M., Warner, T.F., Saitoh, E., Azen, E.A. (1989). Tissue distribution of RNAs for cystatins, histatins, statherin proline-rich salivary proteins in humans macaques. J. Dent. Res. 68,1138-1145.
    • (1989) J. Dent. Res. , vol.68 , pp. 1138-1145
    • Sabatini, L.M.1    Warner, T.F.2    Saitoh, E.3    Azen, E.A.4
  • 167
    • 0023888506 scopus 로고
    • Cystatin superfamily. Evidence that family II cystatin genes are evolutionary related to family III cystatin genes
    • Saitoh, E., Isemura, S., Sanada, K., Hyung-Suk, K., Smithies, O., Maeda, N. (1988). Cystatin superfamily. Evidence that family II cystatin genes are evolutionary related to family III cystatin genes. Biol. Chem. Hoppe-Seyler. 369,191-197.
    • (1988) Biol. Chem. Hoppe-Seyler. , pp. 191-197
    • Saitoh, E.1    Isemura, S.2    Sanada, K.3    Hyung-Suk, K.4    Smithies, O.5    Maeda, N.6
  • 168
  • 169
    • 0026006656 scopus 로고
    • The human cystatin gene family, cloning of three members evolutionary relationship between cystatins Bowman-Birk type proteinase inhibitors
    • Saitoh, E., Isemura, S., Sanada, K., Ohnishi, K. (1991). The human cystatin gene family, cloning of three members evolutionary relationship between cystatins Bowman-Birk type proteinase inhibitors. Biomed. Biochim. Acta. 50, 599-605.
    • (1991) Biomed. Biochim. Acta. , vol.50 , pp. 599-605
    • Saitoh, E.1    Isemura, S.2    Sanada, K.3    Ohnishi, K.4
  • 170
    • 0022555509 scopus 로고
    • Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure in inhibitory activity for cysteine proteinase
    • Salvesen, G., Parkes, C., Abrahamson, M., Grubb, A., Barrett, A.J. (1989). Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure in inhibitory activity for cysteine proteinase. Biochem. J. 234, 429-434.
    • (1989) Biochem. J. , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 172
    • 0019421064 scopus 로고
    • Multi-molecular forms of thiol proteinase inhibitor in human plasma
    • Sasaki, M., Taniguchi, K., Minakata, K. (1981). Multi-molecular forms of thiol proteinase inhibitor in human plasma. J. Biochem. 59,169-177.
    • (1981) J. Biochem. , vol.59 , pp. 169-177
    • Sasaki, M.1    Taniguchi, K.2    Minakata, K.3
  • 173
    • 0027724935 scopus 로고
    • Characterization of cysteine proteases their endogenous inhibitors in MCF-7 adriamycin-resistant MCF-7 human breast cancer cells
    • Scaddan, P.B., Dufresne, M.J. (1993). Characterization of cysteine proteases their endogenous inhibitors in MCF-7 adriamycin-resistant MCF-7 human breast cancer cells, invasion Metastasis. 13,301-313.
    • (1993) Invasion Metastasis , vol.13 , pp. 301-313
    • Scaddan, P.B.1    Dufresne, M.J.2
  • 174
    • 0027210445 scopus 로고
    • Cystatin C (CST3), the cidate gene for hereditary cystatin C amyloid angiopathy (HCCAA) other members of the cystatin gene family are clustered on chromosome 20p11.2
    • Schnittger, S., Rao, G., Abrahamson, M., Hansmann, I. (1993). Cystatin C (CST3), the cidate gene for hereditary cystatin C amyloid angiopathy (HCCAA) other members of the cystatin gene family are clustered on chromosome 20p11.2. Genomics. 76,50-55.
    • (1993) Genomics. , vol.76 , pp. 50-55
    • Schnittger, S.1    Rao, G.2    Abrahamson, M.3    Hansmann, I.4
  • 175
    • 0024272955 scopus 로고
    • Cloning sequencing of cDNA encoding a rat salivary cysteine proteinase inhibitor inducible by beta-adrenergic agonists
    • Shaw, P.A., Cox, J.L., Barka, T., Naito, Y. (1988). Cloning sequencing of cDNA encoding a rat salivary cysteine proteinase inhibitor inducible by beta-adrenergic agonists. J. Biol. Chem. 263,18133-18137.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18133-18137
    • Shaw, P.A.1    Cox, J.L.2    Barka, T.3    Naito, Y.4
  • 176
    • 33746432113 scopus 로고
    • Beta-adrenergic induction of a cysteine-proteinase-inhibitor mRNA in rat salivary gls
    • Shaw, P.A., Barka, T. (1989). Beta-adrenergic induction of a cysteine-proteinase-inhibitor mRNA in rat salivary gls. Biochem. J. 257,695-689.
    • (1989) Biochem. J. , vol.257 , pp. 695-1689
    • Shaw, P.A.1    Barka, T.2
  • 177
    • 0020093847 scopus 로고
    • Properties of cysteine-containing phosphoproteins from human submibular-sublingual saliva
    • Shomers, J.P., Tabak, LA., Levine, M.J., Mel, I.D., Hay, D.J. (1982a). Properties of cysteine-containing phosphoproteins from human submibular-sublingual saliva. J. Dent. Res. 67,397-399.
    • (1982) J. Dent. Res. , vol.67 , pp. 397-399
    • Shomers, J.P.1    Tabak, L.A.2    Levine, M.J.3    Mel, I.D.4    Hay, D.J.5
  • 178
    • 0020144053 scopus 로고
    • Characterization of cysteine-containing phosphoproteins from human submibular-sublingual saliva
    • Shomers, J.P., Tabak, L.A., Levine, M.J., Mel, I.D., Ellison, S.A. (1982b). Characterization of cysteine-containing phosphoproteins from human submibular-sublingual saliva. J. Dent. Res. 61, 764-767.
    • (1982) J. Dent. Res. , vol.61 , pp. 764-767
    • Shomers, J.P.1    Tabak, L.A.2    Levine, M.J.3    Mel, I.D.4    Ellison, S.A.5
  • 179
    • 0020174087 scopus 로고
    • The isolation of a family of cysteine-containing phosphoproteins from human submibular-sublingual saliva
    • Shomers, J.P., Tabak, L.A., Levine, M.J., Mel, l.D., Ellison, S.A. (1982c). The isolation of a family of cysteine-containing phosphoproteins from human submibular-sublingual saliva. J. Dent. Res. 61,973-977.
    • (1982) J. Dent. Res. , pp. 973-977
    • Shomers, J.P.1    Tabak, L.A.2    Levine, M.J.3    Mel, L.D.4    Ellison, S.A.5
  • 180
    • 0021964955 scopus 로고
    • The blood serum concentration of cystatin C (-y-trace) as a measure of the glomerular filtration rate
    • Simonsen, O., Grubb, A., Thysell, H. (1985). The blood serum concentration of cystatin C (-y-trace) as a measure of the glomerular filtration rate. Sc. J. Clin. Lab. Invest. 45, 97-101.
    • (1985) Sc. J. Clin. Lab. Invest. , vol.45 , pp. 97-101
    • Simonsen, O.1    Grubb, A.2    Thysell, H.3
  • 181
    • 0024821880 scopus 로고
    • Immunochemical quantitation of cysteine proteinase inhibitor cystatin C of inflamed human gingiva
    • Skaleric, U., Babnik, J., Curin, V., Lah, T., Turk, V. (1989). Immunochemical quantitation of cysteine proteinase inhibitor cystatin C of inflamed human gingiva. Archs. Oral Biol. 34, 301-305.
    • (1989) Archs. Oral Biol. , vol.34 , pp. 301-305
    • Skaleric, U.1    Babnik, J.2    Curin, V.3    Lah, T.4    Turk, V.5
  • 184
    • 0029049091 scopus 로고
    • Expression of acid cysteine proteinase inhibitor (ACPI) in the normal human prostate, benign prostatic hyperplasia adenocarcinoma
    • Söderström, K.-O., Laato, M., Wu, P., Hopsu-Havu, V.K., Nurmi, M., Rinne, A. (1995). Expression of acid cysteine proteinase inhibitor (ACPI) in the normal human prostate, benign prostatic hyperplasia adenocarcinoma. Int. J. Cancer 62, 1-4.
    • (1995) Int. J. Cancer , vol.62 , pp. 1-4
    • Söderström, K.-O.1    Laato, M.2    Wu, P.3    Hopsu-Havu, V.K.4    Nurmi, M.5    Rinne, A.6
  • 185
    • 0022002505 scopus 로고
    • A new function of kininogens as thiol-proteinase inhibitors, inhibition of papain, cathepsin B, H L by bovine, rat human plasma kininogens
    • Sueyoshi, T., Enjvoji, K., Shimada, T., Kalo, H., Iwanaga, S., Banod, Y, Koninami, E., Katunuma, N. (1985). A new function of kininogens as thiol-proteinase inhibitors, inhibition of papain, cathepsin B, H L by bovine, rat human plasma kininogens. FEBSLett. 182,193-195.
    • (1985) FEBSLett. , vol.182 , pp. 193-195
    • Sueyoshi, T.1    Enjvoji, K.2    Shimada, T.3    Kalo, H.4    Iwanaga, S.5    Banod, Y.6    Koninami, E.7    Katunuma, N.8
  • 186
    • 0027973629 scopus 로고
    • Inhibition of growth cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin a in skin cornified envelope
    • Takahashi, M., Tezuka, T., Katunuma, N. (1994). Inhibition of growth cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin a in skin cornified envelope. FEBS Lett. 355,275-278.
    • (1994) FEBS Lett. , vol.355 , pp. 275-278
    • Takahashi, M.1    Tezuka, T.2    Katunuma, N.3
  • 187
    • 0026552528 scopus 로고
    • On the role of monocytes/macrophages in the pathogenesis of central nervous system lesions in hereditary cystatin C amyloid angiopathy
    • Thorsteinsson, L, Georgesson, G., Asgeirsson, B., Bjarnadôttir, M., Olafsson, I., Jensson, O., Gudmundsson, G. (1992). On the role of monocytes/macrophages in the pathogenesis of central nervous system lesions in hereditary cystatin C amyloid angiopathy. J. Neural. Sei. 108,121 -128.
    • (1992) J. Neural. Sei. , vol.108 , pp. 121-128
    • Thorsteinsson, L.1    Georgesson, G.2    Asgeirsson, B.3    Bjarnadôttir, M.4    Olafsson, I.5    Jensson, O.6    Gudmundsson, G.7
  • 188
    • 0028082364 scopus 로고
    • Cida albicans aspartic proteinase cleaves inactivates human epidermal cysteine proteinase inhibitor
    • Tsushima, H., Mine, H., Kawakami, Y, Hyodoh, F., Ueki, A. (1994). Cida albicans aspartic proteinase cleaves inactivates human epidermal cysteine proteinase inhibitor, cystatin A. Microbiol. 740,167-171.
    • (1994) Cystatin A. Microbiol. , vol.740 , pp. 167-171
    • Tsushima, H.1    Mine, H.2    Kawakami, Y.3    Hyodoh, F.4    Ueki, A.5
  • 190
    • 0023471335 scopus 로고
    • Constitutive secretion of cystatin C fr-trace by monocytes macrophages its down regulation after stimulation
    • Warfei, A.H., Zucker-Franklin, D., Frangione, B., Ghiso, J. (1987). Constitutive secretion of cystatin C fr-trace) by monocytes macrophages its down regulation after stimulation. J. Exp. Med. 166,1912-1917.
    • (1987) J. Exp. Med. , vol.166 , pp. 1912-1917
    • Warfei, A.H.1    Zucker-Franklin, D.2    Frangione, B.3    Ghiso, J.4
  • 191
    • 0026062068 scopus 로고
    • Cystatin C cathepsin'B production by alveolar macrophages from smokers nonsmokers
    • Warfel, A.H., Cardozo, C., Yoo, O.H., Zucker-Franklin, D. (1991). Cystatin C cathepsin'B production by alveolar macrophages from smokers nonsmokers. J. Leukocyte Biol. 49,41 -47.
    • (1991) J. Leukocyte Biol. , vol.49 , pp. 41-47
    • Warfel, A.H.1    Cardozo, C.2    Yoo, O.H.3    Zucker-Franklin, D.4
  • 193
    • 0023003550 scopus 로고
    • Induction of a specific (LM) protein in the submibular gl of the rat by repeated amputation of the lower incisor teeth
    • Yagil, C., Barkam, T. (1986). Induction of a specific (LM) protein in the submibular gl of the rat by repeated amputation of the lower incisor teeth. Am. J. Anat. J 77,513-518.
    • (1986) Am. J. Anat. J , vol.77 , pp. 513-518
    • Yagil, C.1    Barkam, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.