메뉴 건너뛰기




Volumn 3, Issue 3, 2012, Pages 117-127

The role of cystatins in tick physiology and blood feeding

Author keywords

Blood feeding; Cystatin; Cysteine proteases; Immunomodulators; Midgut; Physiology; Tick

Indexed keywords

BMCYSTATIN; CATHEPSIN S; CYSTATIN; CYSTEINE PROTEINASE; LEGUMAIN; PAPAIN LIKE CYSTEINE PROTEINASE; PROTEIN HLCYST 2; PROTEIN HLSC 1; SALIVA PROTEIN; SIALOSTATIN L2; UNCLASSIFIED DRUG;

EID: 84864769112     PISSN: 1877959X     EISSN: 18779603     Source Type: Journal    
DOI: 10.1016/j.ttbdis.2012.03.004     Document Type: Short Survey
Times cited : (68)

References (86)
  • 2
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • Adkison A.M., Raptis S.Z., Kelley D.G., Pham C.T. Dipeptidyl peptidase activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J. Clin. Invest. 2002, 109:363-371.
    • (2002) J. Clin. Invest. , vol.109 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.4
  • 4
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain, induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • Alim M.A., Tsuji N., Miyoshi T., Islam M.K., Huang X., Motobu M., Fujisaki K. Characterization of asparaginyl endopeptidase, legumain, induced by blood feeding in the ixodid tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 2007, 37:911-922.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 911-922
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Huang, X.5    Motobu, M.6    Fujisaki, K.7
  • 5
    • 40849104745 scopus 로고    scopus 로고
    • HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion
    • Alim M.A., Tsuji N., Miyoshi T., Islam M.K., Huang X., Hatta T., Fujisaki K. HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion. J. Insect Physiol. 2008, 54:573-585.
    • (2008) J. Insect Physiol. , vol.54 , pp. 573-585
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Huang, X.5    Hatta, T.6    Fujisaki, K.7
  • 6
    • 57549087068 scopus 로고    scopus 로고
    • Legumains from the hard tick Haemaphysalis longicornis play modulatory roles in blood feeding and gut cellular remodelling and impact on embryogenesis
    • Alim M.A., Tsuji N., Miyoshi T., Islam M.K., Hatta T., Fujisaki K. Legumains from the hard tick Haemaphysalis longicornis play modulatory roles in blood feeding and gut cellular remodelling and impact on embryogenesis. Int. J. Parasitol. 2009, 39:97-107.
    • (2009) Int. J. Parasitol. , vol.39 , pp. 97-107
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3    Islam, M.K.4    Hatta, T.5    Fujisaki, K.6
  • 8
    • 60849099047 scopus 로고    scopus 로고
    • Exploring the mialome of ticks: an annotated catalogue of midgut transcripts from the hard tick, Dermacentor variabilis (Acari: Ixodidae)
    • Anderson J.M., Sonenshine D.E., Valenzuela J.G. Exploring the mialome of ticks: an annotated catalogue of midgut transcripts from the hard tick, Dermacentor variabilis (Acari: Ixodidae). BMC Genomics 2008, 9:552.
    • (2008) BMC Genomics , vol.9 , pp. 552
    • Anderson, J.M.1    Sonenshine, D.E.2    Valenzuela, J.G.3
  • 9
    • 77957034551 scopus 로고
    • Cystatin, the egg white inhibitor of cysteine proteinases
    • Barrett A.J. Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymol. 1981, 80:771-778.
    • (1981) Methods Enzymol. , vol.80 , pp. 771-778
    • Barrett, A.J.1
  • 10
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 1997, 272:20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 11
    • 0029776802 scopus 로고    scopus 로고
    • The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases
    • Björk I., Brieditis I., Raub-Segall E., Pol E., Håkansson K., Abrahamson M. The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases. Biochemistry 1996, 35:10720-10726.
    • (1996) Biochemistry , vol.35 , pp. 10720-10726
    • Björk, I.1    Brieditis, I.2    Raub-Segall, E.3    Pol, E.4    Håkansson, K.5    Abrahamson, M.6
  • 12
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily - new members and their evolution
    • Brown W.M., Dziegielewska K.M. Friends and relations of the cystatin superfamily - new members and their evolution. Protein Sci. 1997, 6:5-12.
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 13
    • 0021053487 scopus 로고
    • Protein inhibitors of cysteine proteinases: I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes
    • Brzin J., Kopitar M., Turk V., Machleidt W. Protein inhibitors of cysteine proteinases: I. Isolation and characterization of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z. Physiol. Chem. 1983, 364:1475-1480.
    • (1983) Hoppe-Seyler's Z. Physiol. Chem. , vol.364 , pp. 1475-1480
    • Brzin, J.1    Kopitar, M.2    Turk, V.3    Machleidt, W.4
  • 14
    • 30044444910 scopus 로고    scopus 로고
    • Endosomal proteases in antigen presentation
    • Chapman H.A. Endosomal proteases in antigen presentation. Curr. Opin. Immunol. 2006, 18:78-84.
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 78-84
    • Chapman, H.A.1
  • 15
    • 3242698093 scopus 로고    scopus 로고
    • An attempt to elucidate the increased incidence of tick-borne encephalitis and its spread to higher altitudes in the Czech Republic
    • Daniel M., Danielová V., KříŽ B., Kott I. An attempt to elucidate the increased incidence of tick-borne encephalitis and its spread to higher altitudes in the Czech Republic. Int. J. Med. Microbiol. 2004, 293(Suppl. 37):55-62.
    • (2004) Int. J. Med. Microbiol. , vol.293 , Issue.SUPPL. 37 , pp. 55-62
    • Daniel, M.1    Danielová, V.2    Kříž, B.3    Kott, I.4
  • 16
    • 0030849487 scopus 로고    scopus 로고
    • Sustainable tick and tickborne disease control in livestock improvement in developing countries
    • de Castro J.J. Sustainable tick and tickborne disease control in livestock improvement in developing countries. Vet. Parasitol. 1997, 71:77-97.
    • (1997) Vet. Parasitol. , vol.71 , pp. 77-97
    • de Castro, J.J.1
  • 17
    • 33745654531 scopus 로고    scopus 로고
    • Strategies for development of vaccines for control of ixodid tick species
    • de la Fuente J., Kocan K.M. Strategies for development of vaccines for control of ixodid tick species. Parasite Immunol. 2006, 28:275-283.
    • (2006) Parasite Immunol. , vol.28 , pp. 275-283
    • de la Fuente, J.1    Kocan, K.M.2
  • 18
    • 34547830937 scopus 로고    scopus 로고
    • Tick vaccines and the transmission of tick-borne pathogens
    • de la Fuente J., Kocan K.M., Blouin E.F. Tick vaccines and the transmission of tick-borne pathogens. Vet. Res. Commun. 2007, 31(Suppl. 1):85-90.
    • (2007) Vet. Res. Commun. , vol.31 , Issue.SUPPL. 1 , pp. 85-90
    • de la Fuente, J.1    Kocan, K.M.2    Blouin, E.F.3
  • 19
    • 0036357785 scopus 로고    scopus 로고
    • Salivary (SD-type) cystatins: over one billion years in the making - but to what purpose?
    • Dickinson D.P. Salivary (SD-type) cystatins: over one billion years in the making - but to what purpose?. Crit. Rev. Oral Biol. Med. 2002, 13:485-508.
    • (2002) Crit. Rev. Oral Biol. Med. , vol.13 , pp. 485-508
    • Dickinson, D.P.1
  • 20
    • 0014278378 scopus 로고
    • Ficin and papain inhibitor from chicken egg white
    • Fossum K., Whitaker J.R. Ficin and papain inhibitor from chicken egg white. Arch. Biochem. Biophys. 1968, 125:367-375.
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 367-375
    • Fossum, K.1    Whitaker, J.R.2
  • 23
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics and biochemical information
    • Gabb H.A., Jackson R.M., Sternberg M.J.E. Modelling protein docking using shape complementarity, electrostatics and biochemical information. J. Mol. Biol. 1997, 272:106-120.
    • (1997) J. Mol. Biol. , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.E.3
  • 24
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity
    • Grunclová L., Horn M., Vancová M., Sojka D., Franta Z., Mares M., Kopácek P. Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. Biol. Chem. 2006, 387:1635-1644.
    • (2006) Biol. Chem. , vol.387 , pp. 1635-1644
    • Grunclová, L.1    Horn, M.2    Vancová, M.3    Sojka, D.4    Franta, Z.5    Mares, M.6    Kopácek, P.7
  • 27
    • 0042825912 scopus 로고    scopus 로고
    • Modulation of host immune responses by nematode cystatins
    • Hartmann S., Lucius R. Modulation of host immune responses by nematode cystatins. Int. J. Parasitol. 2003, 33:1291-1302.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 1291-1302
    • Hartmann, S.1    Lucius, R.2
  • 28
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K., Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 2003, 3:472-482.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 30
  • 31
    • 23044433357 scopus 로고    scopus 로고
    • RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding
    • Karim S., Miller N.J., Valenzuela J.G., Sauer J.R., Mather T.N. RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding. Biochem. Biophys. Res. Commun. 2005, 334:1336-1342.
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 1336-1342
    • Karim, S.1    Miller, N.J.2    Valenzuela, J.G.3    Sauer, J.R.4    Mather, T.N.5
  • 32
    • 0016611551 scopus 로고
    • Inhibition of cathepsin C by papain inhibitor from chicken egg white and by complex with cathepsin B1
    • Keilová H., Tomásek V. Inhibition of cathepsin C by papain inhibitor from chicken egg white and by complex with cathepsin B1. Collect. Czech. Chem. Commun. 1975, 40:218-224.
    • (1975) Collect. Czech. Chem. Commun. , vol.40 , pp. 218-224
    • Keilová, H.1    Tomásek, V.2
  • 33
    • 33748746599 scopus 로고    scopus 로고
    • Antiinflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis
    • Kotsyfakis M., Sá-Nunes A., Francischetti I.M., Mather T.N., Andersen J.F., Ribeiro J.M. Antiinflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis. J. Biol. Chem. 2006, 281:26298-26307.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26298-26307
    • Kotsyfakis, M.1    Sá-Nunes, A.2    Francischetti, I.M.3    Mather, T.N.4    Andersen, J.F.5    Ribeiro, J.M.6
  • 34
    • 35748942888 scopus 로고    scopus 로고
    • Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis
    • Kotsyfakis M., Karim S., Andersen J.F., Mather T.N., Ribeiro J.M. Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis. J. Biol. Chem. 2007, 282:29256-29263.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29256-29263
    • Kotsyfakis, M.1    Karim, S.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 36
    • 77954378928 scopus 로고    scopus 로고
    • The crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model
    • Kotsyfakis M., Horka H., Salat J., Andersen J.F. The crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model. Mol. Microbiol. 2010, 77:456-470.
    • (2010) Mol. Microbiol. , vol.77 , pp. 456-470
    • Kotsyfakis, M.1    Horka, H.2    Salat, J.3    Andersen, J.F.4
  • 38
    • 3042704064 scopus 로고    scopus 로고
    • Transcriptomic analysis in the leech Theromyzon tessulatum: involvement of cystatin B in innate immunity
    • Lefebvre C., Cocquerelle C., Vandenbulcke F., Hot D., Huot L., Lemoine Y., Salzet M. Transcriptomic analysis in the leech Theromyzon tessulatum: involvement of cystatin B in innate immunity. Biochem. J. 2004, 380:617-625.
    • (2004) Biochem. J. , vol.380 , pp. 617-625
    • Lefebvre, C.1    Cocquerelle, C.2    Vandenbulcke, F.3    Hot, D.4    Huot, L.5    Lemoine, Y.6    Salzet, M.7
  • 40
    • 33745746366 scopus 로고    scopus 로고
    • Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus
    • Lima C.A., Sasaki S.D., Tanaka A.S. Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus. Biochem. Biophys. Res. Commun. 2006, 347:44-50.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 44-50
    • Lima, C.A.1    Sasaki, S.D.2    Tanaka, A.S.3
  • 42
    • 0026020716 scopus 로고
    • Characterization of an Onchocerca volvulus cDNA clone encoding a genus specific antigen present in infective larvae and adult worms
    • Lustigman S., Brotman B., Huima T., Prince A.M. Characterization of an Onchocerca volvulus cDNA clone encoding a genus specific antigen present in infective larvae and adult worms. Mol. Biochem. Parasitol. 1991, 45:65-75.
    • (1991) Mol. Biochem. Parasitol. , vol.45 , pp. 65-75
    • Lustigman, S.1    Brotman, B.2    Huima, T.3    Prince, A.M.4
  • 43
    • 0026804645 scopus 로고
    • Molecular cloning and characterization of onchocystatin, a cysteine proteinase inhibitor of Onchocerca volvulus
    • Lustigman S., Brotman B., Huima T., Prince A.M., McKerrow J.H. Molecular cloning and characterization of onchocystatin, a cysteine proteinase inhibitor of Onchocerca volvulus. J. Biol. Chem. 1992, 267:17339-17346.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17339-17346
    • Lustigman, S.1    Brotman, B.2    Huima, T.3    Prince, A.M.4    McKerrow, J.H.5
  • 44
    • 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. Protein inhibitors of cysteine proteinases: II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z. Physiol. Chem. 1983, 364:1481-1486.
    • (1983) Hoppe-Seyler's Z. Physiol. Chem. , vol.364 , pp. 1481-1486
    • Machleidt, W.1    Borchart, U.2    Fritz, H.3    Brzin, J.4    Ritonja, A.5    Turk, V.6
  • 45
    • 1642431664 scopus 로고    scopus 로고
    • The N-terminus moiety of the cystatin SmCys from Schistosoma mansoni regulates its inhibitory activity in vitro and in vivo
    • Morales F.C., Furtado D.R., Rumjanek F.D. The N-terminus moiety of the cystatin SmCys from Schistosoma mansoni regulates its inhibitory activity in vitro and in vivo. Mol. Biochem. Parasitol. 2004, 134:65-73.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 65-73
    • Morales, F.C.1    Furtado, D.R.2    Rumjanek, F.D.3
  • 47
    • 0021876151 scopus 로고
    • Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data
    • Müller-Esterl W., Fritz H., Machleidt W., Ritonja A., Brzin J., Kotnik M., Turk V., Kellermann J., Lottspeich F. Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data. FEBS Lett. 1985, 182:310-314.
    • (1985) FEBS Lett. , vol.182 , pp. 310-314
    • Müller-Esterl, W.1    Fritz, H.2    Machleidt, W.3    Ritonja, A.4    Brzin, J.5    Kotnik, M.6    Turk, V.7    Kellermann, J.8    Lottspeich, F.9
  • 48
    • 0021676017 scopus 로고
    • Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen
    • Ohkubo I., Kurachi K., Takasawa T., Shiokawa H., Sasaki M. Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 1984, 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
  • 49
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham C.T., Ley T.J. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:8627-8632.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 50
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre P., Mellman I. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 1998, 93:1135-1145.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 51
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings N.D., Barrett A.J. Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 1990, 30:60-71.
    • (1990) J. Mol. Evol. , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barrett, A.J.2
  • 54
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy V.Y., Zhang Q.Y., Weiss S.J. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:3849-3853.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 57
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver
    • Ritonja A., Machleidt W., Barrett A.J. Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver. Biochem. Biophys. Res. Commun. 1985, 131:1187-1192.
    • (1985) Biochem. Biophys. Res. Commun. , vol.131 , pp. 1187-1192
    • Ritonja, A.1    Machleidt, W.2    Barrett, A.J.3
  • 60
    • 34447341756 scopus 로고    scopus 로고
    • Kininogens coordinate adaptive immunity through the proteolytic release of bradykinin, an endogenous danger signal driving dendritic cell maturation
    • Scharfstein J., Schmitz V., Svensjö E., Granato A., Monteiro A.C. Kininogens coordinate adaptive immunity through the proteolytic release of bradykinin, an endogenous danger signal driving dendritic cell maturation. Scand. J. Immunol. 2007, 66:128-136.
    • (2007) Scand. J. Immunol. , vol.66 , pp. 128-136
    • Scharfstein, J.1    Schmitz, V.2    Svensjö, E.3    Granato, A.4    Monteiro, A.C.5
  • 61
    • 0035884985 scopus 로고    scopus 로고
    • Modulation of human T cell responses and macrophage functions by onchocystatin, a secreted protein of the filarial nematode Onchocerca volvulus
    • Schönemeyer A., Lucius R., Sonnenburg B., Brattig N., Sabat R., Schilling K., Bradley J., Hartmann S. Modulation of human T cell responses and macrophage functions by onchocystatin, a secreted protein of the filarial nematode Onchocerca volvulus. J. Immunol. 2001, 167:3207-3215.
    • (2001) J. Immunol. , vol.167 , pp. 3207-3215
    • Schönemeyer, A.1    Lucius, R.2    Sonnenburg, B.3    Brattig, N.4    Sabat, R.5    Schilling, K.6    Bradley, J.7    Hartmann, S.8
  • 63
    • 57449094299 scopus 로고    scopus 로고
    • Analysis of the distribution of the tick Ixodes ricinus L. (Acari: Ixodidae) in a nature reserve of western Germany using Geographic Information Systems
    • Schwarz A., Maier W.A., Kistemann T., Kampen H. Analysis of the distribution of the tick Ixodes ricinus L. (Acari: Ixodidae) in a nature reserve of western Germany using Geographic Information Systems. Int. J. Hyg. Environ. Health 2009, 212:87-96.
    • (2009) Int. J. Hyg. Environ. Health , vol.212 , pp. 87-96
    • Schwarz, A.1    Maier, W.A.2    Kistemann, T.3    Kampen, H.4
  • 64
    • 0015857449 scopus 로고
    • Some properties of a ficin-papain inhibitor from avian egg white
    • Sen L.C., Whitaker J.R. Some properties of a ficin-papain inhibitor from avian egg white. Arch. Biochem. Biophys. 1973, 158:623-632.
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 623-632
    • Sen, L.C.1    Whitaker, J.R.2
  • 66
    • 0031030180 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer
    • Sotiropoulou G., Anisonowicz A., Sager R. Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. J. Biol. Chem. 1997, 272:903-910.
    • (1997) J. Biol. Chem. , vol.272 , pp. 903-910
    • Sotiropoulou, G.1    Anisonowicz, A.2    Sager, R.3
  • 67
    • 0025301658 scopus 로고
    • The refined 2.4A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction
    • Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V. The refined 2.4A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 1990, 9:1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 68
    • 67650364778 scopus 로고    scopus 로고
    • Type I cystatin (stefin) is a major component of Fasciola gigantica excretion/secretion product
    • Tarasuk M., Vichasri Grams S., Viyanant V., Grams R. Type I cystatin (stefin) is a major component of Fasciola gigantica excretion/secretion product. Mol. Biochem. Parasitol. 2009, 167:60-71.
    • (2009) Mol. Biochem. Parasitol. , vol.167 , pp. 60-71
    • Tarasuk, M.1    Vichasri Grams, S.2    Viyanant, V.3    Grams, R.4
  • 69
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 70
  • 71
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: biochemical and structural properties, and medical relevance
    • Turk V., Stoka V., Turk D. Cystatins: biochemical and structural properties, and medical relevance. Front. Biosci. 2008, 13:5406-5420.
    • (2008) Front. Biosci. , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 74
    • 34347349183 scopus 로고    scopus 로고
    • Ectoparasites: future challenges in a changing world
    • Wall R. Ectoparasites: future challenges in a changing world. Vet. Parasitol. 2007, 148:62-74.
    • (2007) Vet. Parasitol. , vol.148 , pp. 62-74
    • Wall, R.1
  • 75
    • 0030607410 scopus 로고    scopus 로고
    • Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo
    • Wasilewski M.M., Lim K.C., Phillips J., McKerrow J.H. Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo. Mol. Biochem. Parasitol. 1996, 81:179-189.
    • (1996) Mol. Biochem. Parasitol. , vol.81 , pp. 179-189
    • Wasilewski, M.M.1    Lim, K.C.2    Phillips, J.3    McKerrow, J.H.4
  • 77
    • 33646367410 scopus 로고    scopus 로고
    • Tick control: thoughts on a research agenda
    • Willadsen P. Tick control: thoughts on a research agenda. Vet. Parasitol. 2006, 138:161-168.
    • (2006) Vet. Parasitol. , vol.138 , pp. 161-168
    • Willadsen, P.1
  • 82
    • 33646513917 scopus 로고    scopus 로고
    • Cysteine cathepsins in the immune response
    • Zavasnik-Bergant T., Turk B. Cysteine cathepsins in the immune response. Tissue Antigens 2006, 67:349-355.
    • (2006) Tissue Antigens , vol.67 , pp. 349-355
    • Zavasnik-Bergant, T.1    Turk, B.2
  • 83
    • 42549100331 scopus 로고    scopus 로고
    • Cystatin protease inhibitors and immune functions
    • Zavasnik-Bergant T. Cystatin protease inhibitors and immune functions. Front. Biosci. 2008, 13:4625-4637.
    • (2008) Front. Biosci. , vol.13 , pp. 4625-4637
    • Zavasnik-Bergant, T.1
  • 84
    • 33745713839 scopus 로고    scopus 로고
    • A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity
    • Zhou J., Ueda M., Umemiya R., Battsetseg B., Boldbaatar D., Xuan X., Fujisaki K. A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity. Insect Biochem. Mol. Biol. 2006, 36:527-535.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 527-535
    • Zhou, J.1    Ueda, M.2    Umemiya, R.3    Battsetseg, B.4    Boldbaatar, D.5    Xuan, X.6    Fujisaki, K.7
  • 85
    • 59649083646 scopus 로고    scopus 로고
    • Characterization of an intracellular cystatin homolog from the tick Haemaphysalis longicornis
    • Zhou J., Liao M., Ueda M., Gong H., Xuan X., Fujisaki K. Characterization of an intracellular cystatin homolog from the tick Haemaphysalis longicornis. Vet. Parasitol. 2009, 160:180-183.
    • (2009) Vet. Parasitol. , vol.160 , pp. 180-183
    • Zhou, J.1    Liao, M.2    Ueda, M.3    Gong, H.4    Xuan, X.5    Fujisaki, K.6
  • 86
    • 77954428098 scopus 로고    scopus 로고
    • Characterization of Hlcyst-3 as a member of cystatins from the tick Haemaphysalis longicornis
    • Zhou J., Liao M., Gong H., Xuan X., Fujisaki K. Characterization of Hlcyst-3 as a member of cystatins from the tick Haemaphysalis longicornis. Exp. Appl. Acarol. 2010, 51:327-333.
    • (2010) Exp. Appl. Acarol. , vol.51 , pp. 327-333
    • Zhou, J.1    Liao, M.2    Gong, H.3    Xuan, X.4    Fujisaki, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.