메뉴 건너뛰기




Volumn 4, Issue 5, 2012, Pages 296-322

Disintegrins from hematophagous sources

Author keywords

Angiogenesis; Bloodsucking; Disintegrins; Hematophagy; Platelet aggregation; Proteome; Salivary; Sialogenins; Sialome; Snake venom; Thrombus; Transcriptome

Indexed keywords

ANGIOGENESIS INHIBITOR; ANTICOAGULANT AGENT; ANTINEOPLASTIC AGENT; ANTITHROMBOCYTIC AGENT; CONTORTROSTATIN; DECORSIN; DISAGREGIN; DISINTEGRIN; INTEGRIN; IXODEGRIN; JERDOSTATIN; MONOGRIN; OBTUSTATIN; ORNATIN; SAVIGNYGRIN; SIALOGENIN; TABINHIBITIN; TABLYSIN 15; TRIFLAVIN; UNCLASSIFIED DRUG; VARIABILIN;

EID: 84861498404     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins4050296     Document Type: Article
Times cited : (37)

References (76)
  • 2
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood, J.D.; Cheresh, D.A. Role of integrins in cell invasion and migration. Nat. Rev. Cancer 2002, 2, 91-100.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 4
    • 0031814234 scopus 로고    scopus 로고
    • What have snakes taught us about integrins?
    • Huang, T.F. What have snakes taught us about integrins? Cell. Mol. Life Sci. 1998, 54, 527-540.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 527-540
    • Huang, T.F.1
  • 5
    • 52049111824 scopus 로고    scopus 로고
    • Disintegrins in health and disease
    • McLane, M.A.; Joerger, T.; Mahmoud, A. Disintegrins in health and disease. Front Biosci. 2008, 13, 6617-6637.
    • (2008) Front Biosci , vol.13 , pp. 6617-6637
    • McLane, M.A.1    Joerger, T.2    Mahmoud, A.3
  • 6
    • 44349151718 scopus 로고    scopus 로고
    • Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
    • Fox, J.W.; Serrano, S.M. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 2008, 275, 3016-3030.
    • (2008) FEBS J , vol.275 , pp. 3016-3030
    • Fox, J.W.1    Serrano, S.M.2
  • 7
    • 0026506731 scopus 로고
    • Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor
    • Kini, R.M.; Evans, H.J. Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon 1992, 30, 265-293.
    • (1992) Toxicon , vol.30 , pp. 265-293
    • Kini, R.M.1    Evans, H.J.2
  • 8
    • 79960075940 scopus 로고    scopus 로고
    • Brief history and molecular determinants of snake venom disintegrin evolution
    • Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA
    • Calvete, J.J. Brief history and molecular determinants of snake venom disintegrin evolution. In Toxins and Hemostasis from Bench to Bedside; Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA, 2010; pp. 285-300.
    • (2010) Toxins and Hemostasis From Bench to Bedside , pp. 285-300
    • Calvete, J.J.1
  • 9
    • 80052407252 scopus 로고    scopus 로고
    • Non-RGD-containing snake venom disintegrins, functional and structural relations
    • Walsh, E.M.; Marcinkiewicz, C. Non-RGD-containing snake venom disintegrins, functional and structural relations. Toxicon 2011, 58, 355-362.
    • (2011) Toxicon , vol.58 , pp. 355-362
    • Walsh, E.M.1    Marcinkiewicz, C.2
  • 10
    • 77957900996 scopus 로고    scopus 로고
    • Platelet aggregation inhibitors from hematophagous animals
    • Francischetti, I.M. Platelet aggregation inhibitors from hematophagous animals. Toxicon 2010, 56, 1130-1144.
    • (2010) Toxicon , vol.56 , pp. 1130-1144
    • Francischetti, I.M.1
  • 11
    • 84861488229 scopus 로고    scopus 로고
    • Anti-Angiogenesis and disintegrins
    • Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA
    • Swenson, S.; Minea, R.; Zidovetzki, S.; Helchowski, C.; Costa, F.; Markland, F.S. Anti-Angiogenesis and disintegrins. In Toxins and Hemostasis from Bench to Bedside; Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA, 2010; pp. 301-329.
    • (2010) Toxins and Hemostasis From Bench to Bedside , pp. 301-329
    • Swenson, S.1    Minea, R.2    Zidovetzki, S.3    Helchowski, C.4    Costa, F.5    Markland, F.S.6
  • 12
    • 77952549971 scopus 로고    scopus 로고
    • Matrix biology meets toxinology
    • Eble, J.A. Matrix biology meets toxinology. Matrix Biol. 2010, 29, 239-247.
    • (2010) Matrix Biol , vol.29 , pp. 239-247
    • Eble, J.A.1
  • 14
    • 38449122195 scopus 로고    scopus 로고
    • Anti-Angiogenesis and RGD-containing snake venom disintegrins
    • Swenson, S.; Ramu, S.; Markland, F.S. Anti-Angiogenesis and RGD-containing snake venom disintegrins. Curr. Pharm. Des. 2007, 13, 2860-2871.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2860-2871
    • Swenson, S.1    Ramu, S.2    Markland, F.S.3
  • 16
    • 28844477790 scopus 로고    scopus 로고
    • cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha1beta1 integrin
    • Sanz, L.; Chen, R.Q.; Perez, A.; Hilario, R.; Juarez, P.; Marcinkiewicz, C.; Monleon, D.; Celda, B.; Xiong, Y.L.; Perez-Paya, E.; Calvete, J.J. cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the alpha1beta1 integrin. J. Biol. Chem. 2005, 280, 40714-40722.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40714-40722
    • Sanz, L.1    Chen, R.Q.2    Perez, A.3    Hilario, R.4    Juarez, P.5    Marcinkiewicz, C.6    Monleon, D.7    Celda, B.8    Xiong, Y.L.9    Perez-Paya, E.10    Calvete, J.J.11
  • 19
    • 84861494829 scopus 로고    scopus 로고
    • The discovery of disintegrins
    • Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA
    • Huang, T.F. The discovery of disintegrins. In Toxins and Hemostasis from Bench to Bedside; Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA, 2010; pp. 269-284.
    • (2010) Toxins and Hemostasis From Bench to Bedside , pp. 269-284
    • Huang, T.F.1
  • 22
    • 0023639428 scopus 로고
    • A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex
    • Huang, T.F.; Holt, J.C.; Lukasiewicz, H.; Niewiarowski, S.T. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. J. Biol. Chem. 1987, 262, 16157-16163.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16157-16163
    • Huang, T.F.1    Holt, J.C.2    Lukasiewicz, H.3    Niewiarowski, S.T.4
  • 23
    • 84920166193 scopus 로고    scopus 로고
    • Introduction
    • Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA
    • Clemetson, K.J.; Kini, R.M. Introduction. In Toxins and Hemostasis from Bench to Bedside; Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA, 2010; pp. 1-8.
    • (2010) Toxins and Hemostasis From Bench to Bedside , pp. 1-8
    • Clemetson, K.J.1    Kini, R.M.2
  • 24
    • 0001278780 scopus 로고    scopus 로고
    • Contortrostatin, a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits angiogenesis
    • Zhou, Q.; Nakada, M.T.; Arnold, C.; Shieh, K.Y.; Markland, F.S.J. Contortrostatin, a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits angiogenesis. Angiogenesis 1999, 3, 259-269.
    • (1999) Angiogenesis , vol.3 , pp. 259-269
    • Zhou, Q.1    Nakada, M.T.2    Arnold, C.3    Shieh, K.Y.4    Markland, F.S.J.5
  • 27
    • 22144494698 scopus 로고    scopus 로고
    • Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis
    • Francischetti, I.M.; Mather, T.N.; Ribeiro, J.M. Tick saliva is a potent inhibitor of endothelial cell proliferation and angiogenesis. Thromb. Haemost. 2005, 94, 167-174.
    • (2005) Thromb. Haemost. , vol.94 , pp. 167-174
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 28
    • 71049174810 scopus 로고    scopus 로고
    • Anti-Thrombosis repertoire of blood-feeding horsefly salivary glands
    • Ma, D.; Wang, Y.; Yang, H.; Wu, J.; An, S.; Gao, L.; Xu, X.; Lai, R. Anti-Thrombosis repertoire of blood-feeding horsefly salivary glands. Mol. Cell Proteomics 2009, 8, 2071-2079.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2071-2079
    • Ma, D.1    Wang, Y.2    Yang, H.3    Wu, J.4    An, S.5    Gao, L.6    Xu, X.7    Lai, R.8
  • 29
    • 79958217683 scopus 로고    scopus 로고
    • A novel family of RGD-containing disintegrins (Tablysin-15) from the salivary gland of the horsefly Tabanus yao targets alphaIIbbeta3 or alphaVbeta3 and inhibits platelet aggregation and angiogenesis
    • Ma, D.; Xu, X.; An, S.; Liu, H.; Yang, X.; Andersen, J.F.; Wang, Y.; Tokumasu, F.; Ribeiro, J.M.; Francischetti, I.M.; Lai, R. A novel family of RGD-containing disintegrins (Tablysin-15) from the salivary gland of the horsefly Tabanus yao targets alphaIIbbeta3 or alphaVbeta3 and inhibits platelet aggregation and angiogenesis. Thromb. Haemost. 2011, 105, 1032-1045.
    • (2011) Thromb. Haemost. , vol.105 , pp. 1032-1045
    • Ma, D.1    Xu, X.2    An, S.3    Liu, H.4    Yang, X.5    Andersen, J.F.6    Wang, Y.7    Tokumasu, F.8    Ribeiro, J.M.9    Francischetti, I.M.10    Lai, R.11
  • 30
    • 70649086232 scopus 로고    scopus 로고
    • A horsefly saliva antigen 5-like protein containing RTS motif is an angiogenesis inhibitor
    • Ma, D.; Gao, L.; An, S.; Song, Y.; Wu, J.; Xu, X.; Lai, R. A horsefly saliva antigen 5-like protein containing RTS motif is an angiogenesis inhibitor. Toxicon 2010, 55, 45-51.
    • (2010) Toxicon , vol.55 , pp. 45-51
    • Ma, D.1    Gao, L.2    An, S.3    Song, Y.4    Wu, J.5    Xu, X.6    Lai, R.7
  • 31
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • Ribeiro, J.M.; Francischetti, I.M. Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives. Annu. Rev. Entomol. 2003, 48, 73-88.
    • (2003) Annu. Rev. Entomol. , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 33
    • 29944446610 scopus 로고    scopus 로고
    • Proteins in the saliva of the Ixodida (ticks): Pharmacological features and biological significance
    • Steen, N.A.; Barker, S.C.; Alewood, P.F. Proteins in the saliva of the Ixodida (ticks): Pharmacological features and biological significance. Toxicon 2006, 47, 1-20.
    • (2006) Toxicon , vol.47 , pp. 1-20
    • Steen, N.A.1    Barker, S.C.2    Alewood, P.F.3
  • 34
    • 84894440711 scopus 로고    scopus 로고
    • Sialomic perspectives on the evolution of blood-feeding behavior in arthropods: Future therapeutics by natural design
    • Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA
    • Mans, B.J.; Francischetti, I.M.B. Sialomic perspectives on the evolution of blood-feeding behavior in arthropods: Future therapeutics by natural design. In Toxins and Hemostasis from Bench to Bedside; Kini, R.M., Clemetson, K., Markland, F.S., McLane, M.A., Morita, T., Eds.; Springer: New York, NY, USA, 2010; pp. 21-44.
    • (2010) Toxins and Hemostasis From Bench to Bedside , pp. 21-44
    • Mans, B.J.1    Francischetti, I.M.B.2
  • 36
    • 0029898540 scopus 로고    scopus 로고
    • Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis
    • Wang, X.; Coons, L.B.; Taylor, D.B.; Stevens, S.E.J.; Gartner, T.K. Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis. J. Biol. Chem. 1996, 271, 17785-17790.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17785-17790
    • Wang, X.1    Coons, L.B.2    Taylor, D.B.3    Stevens, S.E.J.4    Gartner, T.K.5
  • 38
    • 36749092203 scopus 로고    scopus 로고
    • Characterization of anti-hemostatic factors in the argasid, Argas monolakensis: Implications for the evolution of blood-feeding in the soft tick family
    • Mans, B.J.; Andersen, J.F.; Schwan, T.G.; Ribeiro, J.M. Characterization of anti-hemostatic factors in the argasid, Argas monolakensis: Implications for the evolution of blood-feeding in the soft tick family. Insect Biochem. Mol. Biol. 2008, 38, 22-41.
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 22-41
    • Mans, B.J.1    Andersen, J.F.2    Schwan, T.G.3    Ribeiro, J.M.4
  • 39
    • 0028986726 scopus 로고
    • An inhibitor from the argasid tick Ornithodoros moubata of cell adhesion to collagen
    • Karczewski, J.; Waxman, L.; Endris, R.G.; Connolly, T.M. An inhibitor from the argasid tick Ornithodoros moubata of cell adhesion to collagen. Biochem. Biophys. Res. Commun. 1995, 208, 532-541.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 532-541
    • Karczewski, J.1    Waxman, L.2    Endris, R.G.3    Connolly, T.M.4
  • 40
    • 0028217639 scopus 로고
    • Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata
    • Karczewski, J.; Endris, R.; Connolly, T.M. Disagregin is a fibrinogen receptor antagonist lacking the Arg-Gly-Asp sequence from the tick, Ornithodoros moubata. J. Biol. Chem. 1994, 269, 6702-6708.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6702-6708
    • Karczewski, J.1    Endris, R.2    Connolly, T.M.3
  • 42
    • 0037077268 scopus 로고    scopus 로고
    • Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold
    • Mans, B.J.; Louw, A.I.; Neitz, A.W. Savignygrin, a platelet aggregation inhibitor from the soft tick Ornithodoros savignyi, presents the RGD integrin recognition motif on the Kunitz-BPTI fold. J. Biol. Chem. 2002, 277, 21371-21378.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21371-21378
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 43
    • 0025329916 scopus 로고
    • A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
    • Seymour, J.L.; Henzel, W.J.; Nevins, B.; Stults, J.T.; Lazarus, R.A. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J. Biol. Chem. 1990, 265, 10143-10147.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10143-10147
    • Seymour, J.L.1    Henzel, W.J.2    Nevins, B.3    Stults, J.T.4    Lazarus, R.A.5
  • 44
    • 0026331936 scopus 로고
    • Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata
    • Mazur, P.; Henzel, W.J.; Seymour, J.L.; Lazarus, R.A. Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur. J. Biochem. 1991, 202, 1073-1082.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1073-1082
    • Mazur, P.1    Henzel, W.J.2    Seymour, J.L.3    Lazarus, R.A.4
  • 45
    • 0038015446 scopus 로고    scopus 로고
    • Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum
    • Del Valle, A.; Jones, B.F.; Harrison, L.M.; Chadderdon, R.C.; Cappello, M. Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum. Mol. Biochem. Parasitol. 2003, 129, 167-177.
    • (2003) Mol. Biochem. Parasitol. , vol.129 , pp. 167-177
    • del Valle, A.1    Jones, B.F.2    Harrison, L.M.3    Chadderdon, R.C.4    Cappello, M.5
  • 47
    • 0031590846 scopus 로고    scopus 로고
    • The interaction of disagregin with the platelet fibrinogen receptor, glycoprotein IIb-IIIa
    • Karczewski, J.; Connolly, T.M. The interaction of disagregin with the platelet fibrinogen receptor, glycoprotein IIb-IIIa. Biochem. Biophys. Res. Commun. 1997, 241, 744-748.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 744-748
    • Karczewski, J.1    Connolly, T.M.2
  • 48
  • 50
    • 84859499792 scopus 로고    scopus 로고
    • Structure of a protein having inhibitory disintegrin and leukotriene scavenging functions contained in a single domain
    • in press
    • Xu, X.; Francischetti, I.M.; Lai, R.; Ribeiro, J.M.; Andersen, J.F. Structure of a protein having inhibitory disintegrin and leukotriene scavenging functions contained in a single domain. J. Biol. Chem. 2012, in press.
    • (2012) J. Biol. Chem.
    • Xu, X.1    Francischetti, I.M.2    Lai, R.3    Ribeiro, J.M.4    Andersen, J.F.5
  • 51
    • 78650433241 scopus 로고    scopus 로고
    • Salivary transcriptome of the North American medicinal leech, Macrobdella decora
    • Min, G.S.; Sarkar, I.N.; Siddall, M.E. Salivary transcriptome of the North American medicinal leech, Macrobdella decora. J. Parasitol. 2010, 96, 1211-1221.
    • (2010) J. Parasitol. , vol.96 , pp. 1211-1221
    • Min, G.S.1    Sarkar, I.N.2    Siddall, M.E.3
  • 52
    • 0028017504 scopus 로고
    • Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting
    • Krezel, A.M.; Wagner, G.; Seymour-Ulmer, J.; Lazarus, R.A. Structure of the RGD protein decorsin: Conserved motif and distinct function in leech proteins that affect blood clotting. Science 1994, 264, 1944-1947.
    • (1994) Science , vol.264 , pp. 1944-1947
    • Krezel, A.M.1    Wagner, G.2    Seymour-Ulmer, J.3    Lazarus, R.A.4
  • 53
    • 0027650728 scopus 로고
    • Expression, purification, and characterization of recombinant ornatin E, a potent glycoprotein IIb-IIIa antagonist
    • Mazur, P.; Dennis, M.S.; Seymour, J.L.; Lazarus, R.A. Expression, purification, and characterization of recombinant ornatin E, a potent glycoprotein IIb-IIIa antagonist. Protein Expr. Purif. 1993, 4, 282-289.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 282-289
    • Mazur, P.1    Dennis, M.S.2    Seymour, J.L.3    Lazarus, R.A.4
  • 54
    • 0028020563 scopus 로고
    • Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18
    • Muchowski, P.J.; Zhang, L.; Chang, E.R.; Soule, H.R.; Plow, E.F.; Moyle, M. Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18. J. Biol. Chem. 1994, 269, 26419-26423.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26419-26423
    • Muchowski, P.J.1    Zhang, L.2    Chang, E.R.3    Soule, H.R.4    Plow, E.F.5    Moyle, M.6
  • 55
    • 0028557171 scopus 로고
    • The A-domain of beta 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF
    • Rieu, P.; Ueda, T.; Haruta, I.; Sharma, C.P.; Arnaout, M.A. The A-domain of beta 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF. J. Cell Biol. 1994, 127, 2081-2091.
    • (1994) J. Cell Biol. , vol.127 , pp. 2081-2091
    • Rieu, P.1    Ueda, T.2    Haruta, I.3    Sharma, C.P.4    Arnaout, M.A.5
  • 56
    • 0032103369 scopus 로고    scopus 로고
    • In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism
    • Zhou, M.Y.; Lo, S.K.; Bergenfeldt, M.; Tiruppathi, C.; Jaffe, A.; Xu, N.; Malik, A.B. In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism. J. Clin. Invest. 1998, 101, 2427-2437.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2427-2437
    • Zhou, M.Y.1    Lo, S.K.2    Bergenfeldt, M.3    Tiruppathi, C.4    Jaffe, A.5    Xu, N.6    Malik, A.B.7
  • 57
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen, H.; Brunak, S.; von Heijne, G. Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Protein Eng. 1999, 12, 3-9.
    • (1999) Protein Eng , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    von Heijne, G.3
  • 62
    • 0036671719 scopus 로고    scopus 로고
    • Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae
    • Francischetti, I.M.; Valenzuela, J.G.; Pham, V.M.; Garfield, M.K.; Ribeiro, J.M. Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae. J. Exp. Biol. 2002, 205, 2429-2451.
    • (2002) J. Exp. Biol. , vol.205 , pp. 2429-2451
    • Francischetti, I.M.1    Valenzuela, J.G.2    Pham, V.M.3    Garfield, M.K.4    Ribeiro, J.M.5
  • 65
    • 77957914111 scopus 로고    scopus 로고
    • Structure and mechanism in salivary proteins from blood-feeding arthropods
    • Andersen, J.F. Structure and mechanism in salivary proteins from blood-feeding arthropods. Toxicon 2010, 56, 1120-1129.
    • (2010) Toxicon , vol.56 , pp. 1120-1129
    • Andersen, J.F.1
  • 67
    • 34547737945 scopus 로고    scopus 로고
    • Identification and characterization of plasma kallikrein-kinin system inhibitors from salivary glands of the blood-sucking insect Triatoma infestans
    • Isawa, H.; Orito, Y.; Jingushi, N.; Iwanaga, S.; Morita, A.; Chinzei, Y.; Yuda, M. Identification and characterization of plasma kallikrein-kinin system inhibitors from salivary glands of the blood-sucking insect Triatoma infestans. FEBS J. 2007, 274, 4271-4286.
    • (2007) FEBS J , vol.274 , pp. 4271-4286
    • Isawa, H.1    Orito, Y.2    Jingushi, N.3    Iwanaga, S.4    Morita, A.5    Chinzei, Y.6    Yuda, M.7
  • 69
    • 0025941687 scopus 로고
    • Vaccination with -concealed{norm of matrix} antigens: Myth or reality?
    • Willadsen, P.; McKenna, R.V. Vaccination with -concealed{norm of matrix} antigens: Myth or reality? Parasite Immunol. 1991, 13, 605-616.
    • (1991) Parasite Immunol , vol.13 , pp. 605-616
    • Willadsen, P.1    McKenna, R.V.2
  • 70
    • 75649105755 scopus 로고    scopus 로고
    • The immunosuppresive tick salivary protein, Salp15
    • Juncadella, I.J.; Anguita, J. The immunosuppresive tick salivary protein, Salp15. Adv. Exp. Med. Biol. 2009, 666, 121-131.
    • (2009) Adv. Exp. Med. Biol. , vol.666 , pp. 121-131
    • Juncadella, I.J.1    Anguita, J.2
  • 75
    • 4344607978 scopus 로고    scopus 로고
    • Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 A resolution
    • Bilgrami, S.; Tomar, S.; Yadav, S.; Kaur, P.; Kumar, J.; Jabeen, T.; Sharma, S.; Singh, T.P. Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 A resolution. J. Mol. Biol. 2004, 341, 829-837.
    • (2004) J. Mol. Biol. , vol.341 , pp. 829-837
    • Bilgrami, S.1    Tomar, S.2    Yadav, S.3    Kaur, P.4    Kumar, J.5    Jabeen, T.6    Sharma, S.7    Singh, T.P.8
  • 76
    • 0042887427 scopus 로고    scopus 로고
    • Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD
    • Fujii, Y.; Okuda, D.; Fujimoto, Z.; Horii, K.; Morita, T.; Mizuno, H. Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD. J. Mol. Biol. 2003, 332, 1115-1122.
    • (2003) J. Mol. Biol. , vol.332 , pp. 1115-1122
    • Fujii, Y.1    Okuda, D.2    Fujimoto, Z.3    Horii, K.4    Morita, T.5    Mizuno, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.