[1]
Fry, B.G. From genome to “venome”: Molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res., 2005, 15(3), 403-420.
[2]
Koh, C.Y.; Modahl, C.M.; Kulkarni, N.; Kini, R.M. Toxins are an excellent source of therapeutic agents against cardiovascular diseases. Semin. Thromb. Hemost., 2018, 44(7), 691-706.
[3]
Koh, C.Y.; Kini, R.M. Molecular diversity of anticoagulants from haematophagous animals. Thromb. Haemost., 2009, 102(3), 437-453.
[5]
Vink, S.; Jin, A.H.; Poth, K.J.; Head, G.A.; Alewood, P.F. Natriuretic peptide drug leads from snake venom. Toxicon, 2012, 59(4), 434-445.
[6]
Ichiki, T.; Dzhoyashvili, N.; Burnett, J.C., Jr Natriuretic peptide based therapeutics for heart failure: Cenderitide: A novel first-in-class designer natriuretic peptide. Int. J. Cardiol., 2019, 281, 166-171.
[8]
Campbell, I.D.; Humphries, M.J. Integrin structure, activation, and interactions. Cold Spring Harb. Perspect. Biol., 2011, 3(3), pii: a004994.
[9]
Perchuc, A.M.; Wilmer, M. In Toxins and Hemostasis: From Bench to Bedside; Kini, R.M.; Clemetson, K.J.; Markland, F.S.; McLane, M.A.; Morita, T., Eds.; Springer Netherlands: Dordrecht, 2010, pp. 747-766.
[10]
Lee, C.J.; Ansell, J.E. Direct thrombin inhibitors. Br. J. Clin. Pharmacol., 2011, 72(4), 581-592.
[11]
Erlinge, D.; Omerovic, E.; Frobert, O.; Linder, R.; Danielewicz, M.; Hamid, M.; Swahn, E.; Henareh, L.; Wagner, H.; Hardhammar, P.; Sjogren, I.; Stewart, J.; Grimfjard, P.; Jensen, J.; Aasa, M.; Robertsson, L.; Lindroos, P.; Haupt, J.; Wikstrom, H.; Ulvenstam, A.; Bhiladvala, P.; Lindvall, B.; Lundin, A.; Todt, T.; Ioanes, D.; Ramunddal, T.; Kellerth, T.; Zagozdzon, L.; Gotberg, M.; Andersson, J.; Angeras, O.; Ostlund, O.; Lagerqvist, B.; Held, C.; Wallentin, L.; Schersten, F.; Eriksson, P.; Koul, S.; James, S. Bivalirudin versus Heparin monotherapy in myocardial infarction. N. Engl. J. Med., 2017, 377(12), 1132-1142.
[12]
Stassens, P.; Bergum, P.W.; Gansemans, Y.; Jespers, L.; Laroche, Y.; Huang, S.; Maki, S.; Messens, J.; Lauwereys, M.; Cappello, M.; Hotez, P.J.; Lasters, I.; Vlasuk, G.P. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc. Natl. Acad. Sci. USA, 1996, 93(5), 2149-2154.
[13]
Giugliano, R.P.; Wiviott, S.D.; Stone, P.H.; Simon, D.I.; Schweiger, M.J.; Bouchard, A.; Leesar, M.A.; Goulder, M.A.; Deitcher, S.R.; McCabe, C.H.; Braunwald, E. Investigators, A.-T.-. Recombinant nematode anticoagulant protein c2 in patients with non-ST-segment elevation acute coronary syndrome: the ANTHEM-TIMI-32 trial. J. Am. Coll. Cardiol., 2007, 49(25), 2398-2407.
[14]
Moons, A.H.; Peters, R.J.; Bijsterveld, N.R.; Piek, J.J.; Prins, M.H.; Vlasuk, G.P.; Rote, W.E.; Buller, H.R. Recombinant nematode anticoagulant protein c2, an inhibitor of the tissue factor/factor VIIa complex, in patients undergoing elective coronary angioplasty. J. Am. Coll. Cardiol., 2003, 41(12), 2147-2153.
[15]
Lee, A.; Agnelli, G.; Buller, H.; Ginsberg, J.; Heit, J.; Rote, W.; Vlasuk, G.; Costantini, L.; Julian, J.; Comp, P.; van Der Meer, J.; Piovella, F.; Raskob, G.; Gent, M. Dose-response study of recombinant factor VIIa/tissue factor inhibitor recombinant nematode anticoagulant protein c2 in prevention of postoperative venous thromboembolism in patients undergoing total knee replacement. Circulation, 2001, 104(1), 74-78.
[16]
Levy, D.E.; del Zoppo, G.J.; Demaerschalk, B.M.; Demchuk, A.M.; Diener, H.C.; Howard, G.; Kaste, M.; Pancioli, A.M.; Ringelstein, E.B.; Spatareanu, C.; Wasiewski, W.W. Ancrod in acute ischemic stroke: results of 500 subjects beginning treatment within 6 hours of stroke onset in the ancrod stroke program. Stroke, 2009, 40(12), 3796-3803.
[17]
Yamada, D.; Morita, T. CA-1 method, a novel assay for quantification of normal prothrombin using a Ca2+ -dependent prothrombin activator, carinactivase-1. Thromb. Res., 1999, 94(4), 221-226.
[18]
Medcalf, R.L. Desmoteplase: Discovery, insights and opportunities for ischaemic stroke. Br. J. Pharmacol., 2012, 165(1), 75-89.
[19]
Albers, G.W.; von Kummer, R.; Truelsen, T.; Jensen, J.K.; Ravn, G.M.; Gronning, B.A.; Chabriat, H.; Chang, K.C.; Davalos, A.E.; Ford, G.A.; Grotta, J.; Kaste, M.; Schwamm, L.H.; Shuaib, A.; Investigators, D. Safety and efficacy of desmoteplase given 3-9 h after ischaemic stroke in patients with occlusion or high-grade stenosis in major cerebral arteries (DIAS-3): a double-blind, randomised, placebo-controlled phase 3 trial. Lancet Neurol., 2015, 14(6), 575-584.
[20]
Markland, F.S.; Swenson, S. Fibrolase: Trials and tribulations. Toxins (Basel), 2010, 2(4), 793-808.
[21]
Brahma, R.K.; McCleary, R.J.; Kini, R.M.; Doley, R. Venom gland transcriptomics for identifying, cataloging, and characterizing venom proteins in snakes. Toxicon, 2015, 93, 1-10.
[22]
Wang, Y.; Gao, H.; Shi, C.; Erhardt, P.W.; Pavlovsky, A. D, A.S.; Bledzka, K.; Ustinov, V.; Zhu, L.; Qin, J.; Munday, A.D.; Lopez, J.; Plow, E.; Simon, D.I. Leukocyte integrin Mac-1 regulates thrombosis via interaction with platelet GPIbalpha. Nat. Commun., 2017, 8, 15559.
[23]
Coelho, A.L.; De Freitas, M.S.; Mariano-Oliveira, A.; Rapozo, D.C.; Pinto, L.F.; Niewiarowski, S.; Zingali, R.B.; Marcinkiewicz, C.; Barja-Fidalgo, C. RGD- and MLD-disintegrins, jarastatin and EC3, activate integrin-mediated signaling modulating the human neutrophils chemotaxis, apoptosis and IL-8 gene expression. Exp. Cell Res., 2004, 292(2), 371-384.
[24]
Moyle, M.; Foster, D.L.; McGrath, D.E.; Brown, S.M.; Laroche, Y.; De Meutter, J.; Stanssens, P.; Bogowitz, C.A.; Fried, V.A.; Ely, J.A. et al. A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18. J. Biol. Chem., 1994, 269(13), 10008-10015.
[25]
O’Bryant, Z.; Vann, K.T.; Xiong, Z.G. Translational strategies for neuroprotection in ischemic stroke--focusing on acid-sensing ion channel 1a. Transl. Stroke Res., 2014, 5(1), 59-68.
[26]
Chassagnon, I.R.; McCarthy, C.A.; Chin, Y.K.; Pineda, S.S.; Keramidas, A.; Mobli, M.; Pham, V.; De Silva, T.M.; Lynch, J.W.; Widdop, R.E.; Rash, L.D.; King, G.F. Potent neuroprotection after stroke afforded by a double-knot spider-venom peptide that inhibits acid-sensing ion channel 1a. Proc. Natl. Acad. Sci. USA, 2017, 114(14), 3750-3755.
[27]
Sridharan, S.; Kini, R.M. Decoding the molecular switches of natriuretic peptides which differentiate its vascular and renal functions. Biochem. J., 2018, 475(2), 399-413.
[28]
Ferreira, S.H. A Bradykinin-potentiating factor (bpf) present in the venom of bothrops jararca. Br. J. Pharmacol. Chemother., 1965, 24, 163-169.
[29]
Ferreira, S.H.; Bartelt, D.C.; Greene, L.J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry, 1970, 9(13), 2583-2593.
[30]
Gan, Z.R.; Gould, R.J.; Jacobs, J.W.; Friedman, P.A.; Polokoff, M.A. Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus. J. Biol. Chem., 1988, 263(36), 19827-19832.
[31]
Egbertson, M.S.; Chang, C.T.; Duggan, M.E.; Gould, R.J.; Halczenko, W.; Hartman, G.D.; Laswell, W.L.; Lynch, J.J., Jr; Lynch, R.J.; Manno, P.D. et al., Non-peptide fibrinogen receptor antagonists. 2. Optimization of a tyrosine template as a mimic for Arg-Gly-Asp. J. Med. Chem., 1994, 37(16), 2537-2551.
[32]
Scarborough, R.M.; Naughton, M.A.; Teng, W.; Rose, J.W.; Phillips, D.R.; Nannizzi, L.; Arfsten, A.; Campbell, A.M.; Charo, I.F. Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa. J. Biol. Chem., 1993, 268(2), 1066-1073.
[33]
Scarborough, R.M.; Rose, J.W.; Hsu, M.A.; Phillips, D.R.; Fried, V.A.; Campbell, A.M.; Nannizzi, L.; Charo, I.F. Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri. J. Biol. Chem., 1991, 266(15), 9359-9362.
[34]
Markwardt, F. The development of hirudin as an antithrombotic drug. Thromb. Res., 1994, 74(1), 1-23.
[35]
Maraganore, J.M.; Bourdon, P.; Jablonski, J.; Ramachandran, K.L.; Fenton, J.W., 2nd Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry, 1990, 29(30), 7095-7101.
[36]
Fox, I.; Dawson, A.; Loynds, P.; Eisner, J.; Findlen, K.; Levin, E.; Hanson, D.; Mant, T.; Wagner, J.; Maraganore, J. Anticoagulant activity of Hirulog, a direct thrombin inhibitor, in humans. Thromb. Haemost., 1993, 69(2), 157-163.
[37]
Lisy, O.; Huntley, B.K.; McCormick, D.J.; Kurlansky, P.A.; Burnett, J.C., Jr Design, synthesis, and actions of a novel chimeric natriuretic peptide: CD-NP. J. Am. Coll. Cardiol., 2008, 52(1), 60-68.
[38]
Schweitz, H.; Vigne, P.; Moinier, D.; Frelin, C.; Lazdunski, M. A new member of the natriuretic peptide family is present in the venom of the green mamba (Dendroaspis angusticeps). J. Biol. Chem., 1992, 267(20), 13928-13932.
[39]
Cappello, M.; Vlasuk, G.P.; Bergum, P.W.; Huang, S.; Hotez, P.J. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa. Proc. Natl. Acad. Sci. USA, 1995, 92(13), 6152-6156.
[40]
Sherman, D.G.; Atkinson, R.P.; Chippendale, T.; Levin, K.A.; Ng, K.; Futrell, N.; Hsu, C.Y.; Levy, D.E. Intravenous ancrod for treatment of acute ischemic stroke: the STAT study: a randomized controlled trial. Stroke Treatment with Ancrod Trial. JAMA, 2000, 283(18), 2395-2403.
[41]
Kratzschmar, J.; Haendler, B.; Langer, G.; Boidol, W.; Bringmann, P.; Alagon, A.; Donner, P.; Schleuning, W.D. The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: cloning and expression. Gene, 1991, 105(2), 229-237.
[42]
Gardell, S.J.; Duong, L.T.; Diehl, R.E.; York, J.D.; Hare, T.R.; Register, R.B.; Jacobs, J.W.; Dixon, R.A.; Friedman, P.A. Isolation, characterization, and cDNA cloning of a vampire bat salivary plasminogen activator. J. Biol. Chem., 1989, 264(30), 17947-17952.
[43]
Bajwa, S.S.; Kirakossian, H.; Reddy, K.N.; Markland, F.S. Thrombin-like and fibrinolytic enzymes in the venoms from the Gaboon viper (Bitis gabonica), eastern cottonmouth moccasin (Agkistrodon p. piscivorus) and southern copperhead (Agkistrodon c. contortrix) snakes. Toxicon, 1982, 20(2), 427-432.
[44]
Randolph, A.; Chamberlain, S.H.; Chu, H.L.; Retzios, A.D.; Markland, F.S., Jr; Masiarz, F.R. Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom. Protein Sci., 1992, 1(5), 590-600.
[45]
Brinkhous, K.M.; Barnes, D.S.; Potter, J.Y.; Read, M.S. Von Willebrand syndrome induced by a Bothrops venom factor: bioassay for venom coagglutinin. Proc. Natl. Acad. Sci. USA, 1981, 78(5), 3230-3234.
[46]
Polgar, J.; Clemetson, J.M.; Kehrel, B.E.; Wiedemann, M.; Magnenat, E.M.; Wells, T.N.; Clemetson, K.J. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J. Biol. Chem., 1997, 272(21), 13576-13583.
Article Metrics
28
3