{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T02:33:47Z","timestamp":1793846027247,"version":"4.6.1"},"reference-count":217,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2016,9,29]],"date-time":"2016-09-29T00:00:00Z","timestamp":1475107200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Snake venom metalloproteases, in addition to their contribution to the digestion of the prey, affect various physiological functions by cleaving specific proteins. They exhibit their activities through activation of zymogens of coagulation factors, and precursors of integrins or receptors. Based on their structure\u2013function relationships and mechanism of action, we have defined classification and nomenclature of functional sites of proteases. These metalloproteases are useful as research tools and in diagnosis and treatment of various thrombotic and hemostatic conditions. They also contribute to our understanding of molecular details in the activation of specific factors involved in coagulation, platelet aggregation and matrix biology. This review provides a ready reference for metalloproteases that interfere in blood coagulation, fibrinolysis and platelet aggregation.<\/jats:p>","DOI":"10.3390\/toxins8100284","type":"journal-article","created":{"date-parts":[[2016,9,29]],"date-time":"2016-09-29T09:54:50Z","timestamp":1475142890000},"page":"284","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":178,"title":["Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6100-3251","authenticated-orcid":false,"given":"R.","family":"Kini","sequence":"first","affiliation":[{"name":"Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, 14 Science Drive 4, National University of Singapore, Singapore 117543, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0002-4603","authenticated-orcid":false,"given":"Cho","family":"Koh","sequence":"additional","affiliation":[{"name":"Protein Science Laboratory, Department of Biological Sciences, Faculty of Science, 14 Science Drive 4, National University of Singapore, Singapore 117543, Singapore"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2016,9,29]]},"reference":[{"key":"ref_1","unstructured":"Harvey, A.L. (1991). Snake Toxins, Pergamon."},{"key":"ref_2","unstructured":"Tu, A.T. (1991). Reptile Venoms and Toxins, Marcel Decker."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/S0041-0101(02)00102-2","article-title":"Snake venom l-amino acid oxidases","volume":"40","author":"Du","year":"2002","journal-title":"Toxicon"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.toxicon.2005.02.012","article-title":"Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases","volume":"45","author":"Fox","year":"2005","journal-title":"Toxicon"},{"key":"ref_5","unstructured":"MEROPS The Peptidase Database. Available online: http:\/\/merops.sanger.ac.uk\/."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1159\/000092424","article-title":"Serine proteinases affecting blood coagulation and fibrinolysis from snake venom","volume":"34","author":"Kini","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2012.09.003","article-title":"The long road of research on snake venom serine proteinases","volume":"62","author":"Serrano","year":"2013","journal-title":"Toxicon"},{"key":"ref_8","unstructured":"Bailey, G.S. (1998). Enzymes from Snake Venom, Alaken Inc."},{"key":"ref_9","first-page":"225","article-title":"Snake venom activators of factor X: An overview","volume":"31","author":"Tans","year":"2001","journal-title":"Haemostasis"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1021\/bi00667a023","article-title":"Factor X activating enzyme from Russell\u2019s viper venom: Isolation and characterization","volume":"15","author":"Kisiel","year":"1976","journal-title":"Biochemistry"},{"key":"ref_11","first-page":"186","article-title":"Purification and properties of an activating enzyme of blood clotting factor X from the venom of Cerastes cerastes","volume":"747","author":"Franssen","year":"1983","journal-title":"Biochem. Biophys. Acta"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1021\/bi00377a019","article-title":"Blood coagulation induced by the venom of Bothrops atrox. Identification, purification and properties of two factor X activators","volume":"26","author":"Hofmann","year":"1987","journal-title":"Biochemistry"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/0041-0101(94)90209-7","article-title":"Characterization of OhSl, an arginine\/lysine amidase from the venom of king cobra (Ophiophagus hannah)","volume":"32","author":"Zhang","year":"1994","journal-title":"Toxicon"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1016\/0041-0101(95)00070-3","article-title":"An activator of blood coagulation factor X from the venom of B. fasciatus","volume":"33","author":"Zhang","year":"1995","journal-title":"Toxicon"},{"key":"ref_15","first-page":"772","article-title":"Biochemical characterization of a factor X activator protein purified from Walterinnesia aegyptia venom","volume":"26","author":"Khan","year":"2015","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"5290","DOI":"10.1021\/bi00723a006","article-title":"The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways","volume":"13","author":"Fujikawa","year":"1974","journal-title":"Biochemistry"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"14109","DOI":"10.1016\/S0021-9258(19)49685-3","article-title":"Coagulation factor X activating enzyme from Russell\u2019s viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains","volume":"267","author":"Takeya","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1038\/sj.emboj.7601131","article-title":"Crystal structures of VAP1 reveal ADAMs\u2019 MDC domain architecture and its unique C-shaped scaffold","volume":"25","author":"Takeda","year":"2006","journal-title":"EMBO J."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"5859","DOI":"10.1016\/j.febslet.2007.11.062","article-title":"Crystal structure of RVV-X: An example of evolutionary gain of specificity by ADAM proteinases","volume":"581","author":"Takeda","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/j.febslet.2007.04.057","article-title":"Crystal structures of catrocollastatin\/VAP2B reveal a dynamic, modular architecture of ADAM\/adamalysin\/reprolysin family proteins","volume":"581","author":"Igarashi","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.toxicon.2008.08.021","article-title":"The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: Insights for a new classification of snake venom metalloprotease subgroups","volume":"52","author":"Muniz","year":"2008","journal-title":"Toxicon"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.jsb.2009.11.009","article-title":"Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins","volume":"169","author":"Guan","year":"2009","journal-title":"J. Struct. Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.bbrc.2009.06.004","article-title":"Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM\/reprolysin family proteins","volume":"386","author":"Zhu","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"4151","DOI":"10.1002\/j.1460-2075.1993.tb06099.x","article-title":"First structure of a snake venom metalloproteinase: A prototype for matrix metalloproteinases\/collagenases","volume":"12","author":"Kress","year":"1993","journal-title":"EMBO J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1006\/jmbi.1994.1392","article-title":"Refined 2.0 \u00c5 X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin","volume":"239","author":"Kress","year":"1994","journal-title":"J. Mol. Biol."},{"key":"ref_26","first-page":"49","article-title":"Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis","volume":"119","author":"Kumasaka","year":"1996","journal-title":"Biochemistry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S0014-5793(97)01401-4","article-title":"2 \u00c5 X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode","volume":"418","author":"Cirilli","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1006\/jmbi.1998.2110","article-title":"Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus","volume":"283","author":"Gong","year":"1998","journal-title":"J. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.1107\/S0907444999010306","article-title":"Structure of acutolysin-C, a haemorrhagic toxin from the venom of Agkistrodon acutus, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases","volume":"55","author":"Zhu","year":"1999","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1110\/ps.03102403","article-title":"Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities","volume":"12","author":"Watanabe","year":"2003","journal-title":"Protein Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.jsb.2005.09.006","article-title":"Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus","volume":"152","author":"Lou","year":"2005","journal-title":"J. Struct. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"6166","DOI":"10.1021\/bi9002315","article-title":"High-resolution crystal structure of the snake venom metalloproteinase BaP1 complexed with a peptidomimetic: Insight into inhibitor binding","volume":"48","author":"Lingott","year":"2009","journal-title":"Biochemistry"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.toxicon.2009.08.013","article-title":"Structural studies of BmooMPalph\u03b1-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom","volume":"55","author":"Akao","year":"2010","journal-title":"Toxicon"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.toxicon.2013.05.009","article-title":"Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors","volume":"71","author":"Chou","year":"2013","journal-title":"Toxicon"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1107\/S090744490100614X","article-title":"Crystallization and preliminary X-ray analysis of jararhagin, a metalloproteinase\/disintegrin from Bothrops jararaca snake venom","volume":"57","author":"Souza","year":"2001","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1021\/jp808182y","article-title":"Determination of the structure form of the fourth ligand of zinc in Acutolysin A using combined quantum mechanical and molecular mechanical simulation","volume":"113","author":"Wu","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/S0022-2836(03)00991-4","article-title":"Crystal structure of trimestatin, a disintegrin containing a cell adhesion recognition motif RGD","volume":"332","author":"Fujii","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1111\/j.1742-4658.2008.06466.x","article-title":"Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity","volume":"275","author":"Fox","year":"2008","journal-title":"FEBS J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"7230","DOI":"10.1073\/pnas.131179698","article-title":"Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X","volume":"98","author":"Mizuno","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1055\/s-0038-1648201","article-title":"Inventory of exogenous prothrombin activators","volume":"65","author":"Rosing","year":"1991","journal-title":"Thromb. Haemost."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1016\/0041-0101(92)90023-X","article-title":"Structural and functional properties of snake venom prothrombin activators","volume":"30","author":"Rosing","year":"1992","journal-title":"Toxicon"},{"key":"ref_42","first-page":"155","article-title":"Prothrombin activation by snake venom proteases","volume":"12","author":"Tans","year":"1993","journal-title":"J. Toxicol."},{"key":"ref_43","unstructured":"Bailey, G.S. (1998). Enzymes from Snake Venom, Alaken Inc."},{"key":"ref_44","unstructured":"M\u00e8nez, A. (2002). Perspectives in Molecular Toxinology, John Wiley."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"397","DOI":"10.2174\/1568006043335781","article-title":"Snake venom prothrombin activators similar to blood coagulation factor Xa","volume":"4","author":"Joseph","year":"2004","journal-title":"Curr. Drug Targets Cardiovasc. Haematol. Dis."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1016\/j.toxicon.2005.02.019","article-title":"The intriguing world of prothrombin activators from snake venoms","volume":"45","author":"Kini","year":"2005","journal-title":"Toxicon"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5200","DOI":"10.1074\/jbc.271.9.5200","article-title":"Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism","volume":"271","author":"Yamada","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_48","first-page":"710","article-title":"Classification and nomenclature of prothrombin activators isolated from snake venoms","volume":"85","author":"Kini","year":"2001","journal-title":"Thromb. Haemost."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/0049-3848(75)90150-4","article-title":"Prothrombin activation induced by Ecarin-a prothrombin converting enzyme from Echis carinatus venom","volume":"6","author":"Kornalik","year":"1975","journal-title":"Thromb. Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1021\/bi00005a034","article-title":"cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom","volume":"34","author":"Nishida","year":"1995","journal-title":"Biochemistry"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1021\/bi00377a018","article-title":"Blood coagulation induced by the venom of Bothrops atrox. 1. Identification, purification, and properties of a prothrombin activator","volume":"26","author":"Hofmann","year":"1987","journal-title":"Biochemistry"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"13258","DOI":"10.1016\/S0021-9258(18)69299-3","article-title":"Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake)","volume":"261","author":"Speijer","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1182\/blood.V94.2.621","article-title":"Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: Its structural similarity to coagulation factor Xa","volume":"94","author":"Joseph","year":"1999","journal-title":"Blood"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1042\/bj20020889","article-title":"Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa","volume":"369","author":"Rao","year":"2003","journal-title":"Biochem. J."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1055\/s-0037-1613264","article-title":"Pseutarin C, a prothrombin activator from Pseudonaja textilis venom: Its structural and functional similarity to mammalian coagulation factor Xa-Va complex","volume":"88","author":"Rao","year":"2002","journal-title":"Thromb. Haemost."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"14903","DOI":"10.1016\/S0021-9258(18)98563-7","article-title":"The primary structure of coagulation factor IX\/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E.","volume":"266","author":"Atoda","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0049-3848(98)00212-6","article-title":"CA-1 method, a novel assay for quantification of normal prothrombin using a Ca2+-dependent prothrombin activator, carinactivase-1","volume":"94","author":"Yamada","year":"1999","journal-title":"Thromb. Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1093\/oxfordjournals.jbchem.a021862","article-title":"Purification and characterization of a Ca2+-dependent prothrombin activator, multactivase, from the venom of Echis multisquamatus","volume":"122","author":"Yamada","year":"1997","journal-title":"J. Biochem."},{"key":"ref_59","first-page":"1","article-title":"Comparison of the actions of thrombin and the thrombin-like venom enzymes ancrod and batroxobin","volume":"36","author":"Aronson","year":"1976","journal-title":"Thromb. Haemost."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"18","DOI":"10.2165\/00003495-199700543-00005","article-title":"Defibrinogenating enzymes","volume":"54","author":"Bell","year":"1997","journal-title":"Drugs"},{"key":"ref_61","first-page":"444","article-title":"Thrombin-like enzymes from snake venoms; an inventory","volume":"65","author":"Pirkle","year":"1991","journal-title":"Thromb. Haemost."},{"key":"ref_62","unstructured":"Bailey, G.S. (1998). Enzymes from Snake Venom, Alaken Inc."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/0268-960X(93)90004-N","article-title":"Action of snake venom components on the haemostatic system","volume":"7","author":"Hutton","year":"1993","journal-title":"Blood Rev."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1016\/0005-2744(77)90295-9","article-title":"Physicochemical properties of \u03b1- and \u03b2-fibrinogenases of Trimeresurus mucrosquamatus venom","volume":"481","author":"Ouyang","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0005-2744(79)90097-4","article-title":"\u03b1 and \u03b2-fibrinogenases from Trimeresurus gramineus snake venom","volume":"571","author":"Ouyang","year":"1979","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0041-0101(83)90046-6","article-title":"\u03b1-Fibrinogenase from Agkistrodon rhodostoma (Malayan pit viper) snake venom","volume":"21","author":"Ouyang","year":"1983","journal-title":"Toxicon"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1007\/978-1-4613-0361-9_36","article-title":"Fibrolase, an active thrombolytic enzyme in arterial and venous thrombosis model systems","volume":"391","author":"Markland","year":"1996","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1295","DOI":"10.1016\/S0041-0101(96)00106-7","article-title":"Biochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme","volume":"34","author":"Tu","year":"1996","journal-title":"Toxicon"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1093\/oxfordjournals.jbchem.a022269","article-title":"Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom","volume":"125","author":"Terada","year":"1999","journal-title":"J. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1159\/000092426","article-title":"Vipera lebetina venom contains all types of snake venom metalloproteases","volume":"34","author":"Siigur","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"417","DOI":"10.2174\/1568006043335754","article-title":"\u03b1-Fibrinogenases","volume":"4","author":"Swenson","year":"2004","journal-title":"Curr. Drug Targets Cardiovasc. Haematol. Disord."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Kini, R.M., Clemetson, K.J., Markland, F.S., McLane, M.A., and Morita, T. (2010). Toxins and Hemostasis: From Bench to Bedside, Springer.","DOI":"10.1007\/978-90-481-9295-3"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0041-0101(79)90290-3","article-title":"Properties of fibrinogen degradation products produced by \u03b1- and \u03b2- fibrinogenases of Trimeresurus mucrosquamatus snake venom","volume":"17","author":"Ouyang","year":"1979","journal-title":"Toxicon"},{"key":"ref_74","first-page":"1197","article-title":"Inhibition of rabbit platelet aggregation by alpha-fibrinogenase purified from Calloselasma rhodostoma (Malayan pit viper) venom","volume":"84","author":"Ouyang","year":"1985","journal-title":"J. Formos. Med. Assoc. (Taiwan Yi Xue Hui Za Zhi)"},{"key":"ref_75","first-page":"31","article-title":"The effects of brinolase (fibrinolytic enzyme from Aspergillus Oryzae) on platelet aggregation of dog and man","volume":"28","author":"Roschlau","year":"1972","journal-title":"Thromb. Diath. Haemorrh."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/0304-4165(74)90013-0","article-title":"Correlations between the enzymatic activities and the factors active on blood coagulation and platelet aggregation from the venom of Vipera aspis","volume":"354","author":"Boffa","year":"1974","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_77","first-page":"286","article-title":"Plasmin inhibition of thrombin-induced platelet aggregation","volume":"33","author":"Miller","year":"1975","journal-title":"Thromb. Diath. Haemorrh."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0167-4889(91)90073-7","article-title":"Inhibition of platelet aggregation by a fibrinogenase from Naja nigricollis venom is independent of fibrinogen degradation","volume":"1095","author":"Kini","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/0167-4838(92)90086-S","article-title":"A novel \u03b1-type fibrinogenase from Agkistrodon rhodostoma snake venom","volume":"1160","author":"Huang","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0304-4165(93)90028-7","article-title":"Antiplatelet protease, kistomin, selectively cleaves human platelet glycoprotein Ib","volume":"1158","author":"Huang","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1124\/mol.107.038018","article-title":"Antithrombotic effect of a protein-type I class snake venom metalloproteinase, kistomin, is mediated by affecting glycoprotein Ib-von Willebrand factor interaction","volume":"72","author":"Hsu","year":"2007","journal-title":"Mol. Pharmacol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1578","DOI":"10.1111\/j.1538-7836.2008.03071.x","article-title":"A snake venom metalloproteinase, kistomin, cleaves platelet glycoprotein VI and impairs platelet functions","volume":"6","author":"Hsu","year":"2008","journal-title":"J. Thromb. Haemost."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1055\/s-0037-1616755","article-title":"Crotalin, a vWF and GP Ib cleaving metalloproteinase from venom of Crotalus atrox","volume":"86","author":"Wu","year":"2001","journal-title":"Thromb. Haemost."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"4929","DOI":"10.1021\/bi952456c","article-title":"Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ib\u03b1. Identification of the sulfated tyrosine\/anionic sequence Tyr-276-Glu-282 of glycoprotein Ib\u03b1 as a binding site for von Willebrand factor and \u03b1-thrombin","volume":"35","author":"Ward","year":"1996","journal-title":"Biochemistry"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"26734","DOI":"10.1074\/jbc.270.45.26734","article-title":"A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature N terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding","volume":"270","author":"Dunlop","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1016\/0041-0101(96)00115-8","article-title":"Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other Elapidae venoms","volume":"34","author":"Ward","year":"1996","journal-title":"Toxicon"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1016\/j.toxicon.2007.07.006","article-title":"Fractionation of snake venom metalloproteinases by metal ion affinity: A purified cobra metalloproteinase, Nk, from Naja kaouthia binds Ni2+-agarose","volume":"50","author":"Wijeyewickrema","year":"2007","journal-title":"Toxicon"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"11793","DOI":"10.1074\/jbc.M110.100479","article-title":"Nerve growth factor inhibits metalloproteinase-disintegrins and blocks ectodomain shedding of platelet glycoprotein VI","volume":"285","author":"Wijeyewickrema","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1007\/s00277-010-1103-1","article-title":"The metalloprotease, NN-PF3 from Naja naja venom inhibits platelet aggregation primarily by affecting \u03b12\u03b21 integrin","volume":"90","author":"Kumar","year":"2011","journal-title":"Ann. Hematol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"22869","DOI":"10.1016\/S0021-9258(18)50027-2","article-title":"Purification, cloning and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin-like gene family","volume":"267","author":"Paine","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1055\/s-0038-1648847","article-title":"Properties of fibrinogen cleaved by jararhagin, a metalloproteinase from the venom of Bothrops jararaca","volume":"72","author":"Kamiguti","year":"1994","journal-title":"Thromb. Haemost."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/0041-0101(96)00017-7","article-title":"Insights into the mechanism of hemorrhage caused by the snake venom metalloproteinases","volume":"34","author":"Kamiguti","year":"1996","journal-title":"Toxicon"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"3513","DOI":"10.1074\/jbc.274.6.3513","article-title":"A peptide inhibiting the collagen binding function of integrin \u03b12I domain","volume":"274","author":"Ivaska","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"31493","DOI":"10.1074\/jbc.274.44.31493","article-title":"\u201cRKKH\u201d peptides from the snake venom metalloproteinase of Bothrops jararaca bind near the metal ion-dependent adhesion site of the human integrin \u03b12I-domain","volume":"274","author":"Pentikainen","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"16665","DOI":"10.1074\/jbc.M710483200","article-title":"Competitive interactions of collagen and a jararhagin-derived disintegrin peptide with the integrin \u03b12-I domain","volume":"283","author":"Lambert","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1042\/bj3200635","article-title":"Inhibition of collagen-induced platelet aggregation as the result of cleavage of \u03b12\u03b21-integrin by the snake venom metalloproteinase jarararhagin","volume":"320","author":"Kamiguti","year":"1996","journal-title":"Biochem. J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1006\/bbrc.1995.1081","article-title":"Jararhagin and jaracetin: Novel snake venom inhibitors of the integrin collagen receptor, \u03b12\u03b21","volume":"206","author":"Ward","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"32599","DOI":"10.1074\/jbc.272.51.32599","article-title":"Proteolytic cleavage of the \u03b21 subunit of platelet \u03b12\u03b21 integrin by the metalloproteinase jararhagin compromises collagen-stimulated phosphorylation of pp72syk","volume":"272","author":"Kamiguti","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/j.toxicon.2009.12.010","article-title":"Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to \u03b12\u03b21 integrin and collagen","volume":"55","author":"Tanjoni","year":"2010","journal-title":"Toxicon"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"13094","DOI":"10.1074\/jbc.272.20.13094","article-title":"Function of disintegrin-like\/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists","volume":"272","author":"Jia","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1042\/bj3070411","article-title":"Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen","volume":"307","author":"Zhou","year":"1995","journal-title":"Biochem. J."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1006\/abbi.1996.9787","article-title":"Crovidisin, a collagen-binding protein isolated from snake venom of Crotalus viridis, prevents platelet-collagen interaction","volume":"337","author":"Liu","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1006\/abbi.2000.2120","article-title":"The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits \u03b12\u03b21 integrin-mediated cell adhesion","volume":"384","author":"Souza","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/j.biochi.2005.06.002","article-title":"Primary structure and antiplatelet mechanism of a snake venom metalloproteinase, acurhagin, from Agkistrodon acutus venom","volume":"87","author":"Wang","year":"2005","journal-title":"Biochimie"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/j.bbrc.2003.08.049","article-title":"A novel disintegrin-like domain of a high molecular weight metalloprotease inhibits platelet aggregation","volume":"309","author":"You","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1055\/s-0037-1615236","article-title":"Purification and characterization of kaouthiagin, a von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom","volume":"80","author":"Hamako","year":"1998","journal-title":"Thromb. Haemost."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/j.bbagen.2015.12.021","article-title":"A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops barnetti (Barnett\u00b4s pitviper) snake venom with anti-platelet properties","volume":"1860","author":"Sanchez","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"28092","DOI":"10.1074\/jbc.M011352200","article-title":"A novel viper venom metalloproteinase, alborhagin, is an agonist at the platelet collagen receptor GPVI","volume":"276","author":"Andrews","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"27035","DOI":"10.1074\/jbc.272.43.27035","article-title":"Adhesion and activation of human platelets induced by convulxin involve glycoprotein VI and integrin \u03b12\u03b21","volume":"272","author":"Lagrue","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"13576","DOI":"10.1074\/jbc.272.21.13576","article-title":"Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62\/GPVI collagen receptor","volume":"272","author":"Polgar","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1042\/bj3330389","article-title":"Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from Crotalus durissus terrificus venom","volume":"333","author":"Leduc","year":"1998","journal-title":"Biochem. J."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1160\/TH07-06-0402","article-title":"Snake venom metalloproteinases, crotarhagin and alborhagin, induce ectodomain shedding of the platelet collagen receptor, glycoprotein VI","volume":"98","author":"Wijeyewickrema","year":"2007","journal-title":"Thromb. Haemost."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0041-0101(92)90869-7","article-title":"Structural domains in venom proteins: Evidence that metalloproteinases and nonenzymatic aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor","volume":"30","author":"Kini","year":"1992","journal-title":"Toxicon"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0167-4781(93)90190-O","article-title":"Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom","volume":"1173","author":"Au","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1006\/bbrc.1994.1706","article-title":"A 28 kDa-protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen- and ADP-induced platelet aggregation","volume":"201","author":"Usami","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1006\/abbi.1997.0133","article-title":"Sequence and biological activity of catrocollastatin-C: A disintegrin-like\/cysteine-rich two-domain protein from Crotalus atrox venom","volume":"343","author":"Shimokawa","year":"1997","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.matbio.2009.09.009","article-title":"Leberagin-C, A disintegrin-like\/cysteine-rich protein from Macrovipera lebetina transmediterranea venom, inhibits \u03b1v\u03b23 integrin-mediated cell adhesion","volume":"29","author":"Limam","year":"2010","journal-title":"Matrix Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"16157","DOI":"10.1016\/S0021-9258(18)47710-1","article-title":"Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex","volume":"262","author":"Huang","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"19827","DOI":"10.1016\/S0021-9258(19)77710-2","article-title":"Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus","volume":"263","author":"Gan","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1021\/bi00428a037","article-title":"Trigramin: Primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb\/IIIa complex on human platelets","volume":"28","author":"Huang","year":"1989","journal-title":"Biochemistry"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1016\/S0021-9258(18)54041-2","article-title":"Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms","volume":"268","author":"Scarborough","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"168","DOI":"10.3181\/00379727-195-43129B","article-title":"Disintegrins: A family of integrin inhibitory proteins from viper venoms","volume":"195","author":"Gould","year":"1990","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"2471","DOI":"10.1073\/pnas.87.7.2471","article-title":"Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: Evidence for a family of platelet-aggregation inhibitors","volume":"87","author":"Dennis","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_124","first-page":"289","article-title":"Disintegrins and other naturally antagonists of platelet fibrinogen receptors","volume":"31","author":"Niewiarowski","year":"1994","journal-title":"Semin. Hematol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1126\/science.1862345","article-title":"Solution structure of kistrin, a potent platelet aggregation inhibitor and GPIIb\u2013IIIa antagonist","volume":"253","author":"Adler","year":"1991","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"7369","DOI":"10.1021\/bi00244a003","article-title":"Three-dimensional structure of echistatin, the smallest active RGD protein","volume":"30","author":"Saudek","year":"1991","journal-title":"Biochemistry"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1002\/prot.340150308","article-title":"Binding interactions of kistrin with platelet glycoprotein IIb-IIIa: Analysis by site-directed mutagenesis","volume":"15","author":"Dennis","year":"1993","journal-title":"Proteins"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/0958-1669(93)90009-L","article-title":"Structural and functional aspects of RGD-containing protein antagonists of glycoprotein IIb-IIIa","volume":"4","author":"Lazarus","year":"1993","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1182\/blood.V90.4.1565","article-title":"Significance of the RGD loop and C-terminal domain of echistatin for recognition of \u03b1IIb\u03b23 and \u03b1v\u03b23 integrins and expression of ligand-induced binding sites","volume":"90","author":"Marcinkiewicz","year":"1997","journal-title":"Blood"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"9359","DOI":"10.1016\/S0021-9258(18)92826-7","article-title":"Barbourin. A GPIIb\u2013IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri","volume":"266","author":"Scarborough","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1042\/bj20021739","article-title":"Snake venom disintegrins: Novel dimeric disintegrins and structural diversification by disulphide bond engineering","volume":"372","author":"Calvete","year":"2003","journal-title":"Biochem. J."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2860","DOI":"10.2174\/138161207782023793","article-title":"Anti-angiogenesis and RGD-containing snake venom disintegrins","volume":"13","author":"Swenson","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"6617","DOI":"10.2741\/3177","article-title":"Disintegrins in health and disease","volume":"13","author":"McLane","year":"2008","journal-title":"Front. Biosci."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"2606","DOI":"10.3390\/toxins2112606","article-title":"Snake venom disintegrins and cell migration","volume":"2","author":"Pontes","year":"2010","journal-title":"Toxins"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1974","DOI":"10.1016\/j.biocel.2013.06.009","article-title":"Applications of snake venom components to modulate integrin activities in cell-matrix interactions","volume":"45","author":"Marcinkiewicz","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.toxicon.2012.09.005","article-title":"The continuing saga of snake venom disintegrins","volume":"62","author":"Calvete","year":"2013","journal-title":"Toxicon"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"532","DOI":"10.2174\/1389203716666150515125002","article-title":"Disintegrins from snake venoms and their applications in cancer research and therapy","volume":"16","author":"Fox","year":"2015","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1006\/bbrc.1996.0301","article-title":"The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregation by binding to collagen via its disintegrin-like domain","volume":"219","author":"Zhou","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1006\/abbi.1999.1372","article-title":"Jararhagin ECD-disintegrin-like domain: Expression in Escherichia coli and inhibition of the platelet-collagen interaction","volume":"369","author":"Kamiguti","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0304-4165(96)00140-7","article-title":"Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin","volume":"1335","author":"Kamiguti","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1006\/abbi.1999.1517","article-title":"Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A","volume":"373","author":"Jia","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0014-5793(03)00799-3","article-title":"Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function","volume":"549","author":"Kamiguti","year":"2003","journal-title":"FEBS Lett."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.abb.2006.10.010","article-title":"Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain","volume":"457","author":"Pinto","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1042\/BJ20050483","article-title":"Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: Targeting adhesion proteins collagen I and von Willebrand factor","volume":"391","author":"Serrano","year":"2005","journal-title":"Biochem. J."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"39746","DOI":"10.1074\/jbc.M604855200","article-title":"The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: Role in substrate targeting","volume":"281","author":"Serrano","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1111\/j.1742-4658.2007.05895.x","article-title":"Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation","volume":"274","author":"Serrano","year":"2007","journal-title":"FEBS J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"3232","DOI":"10.1182\/blood-2003-03-0908","article-title":"ADAMTS-13 cysteine-rich\/spacer domains are functionally essential for von Willebrand factor cleavage","volume":"102","author":"Soejima","year":"2003","journal-title":"Blood"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0968-0004(98)01254-7","article-title":"Catalytic triads and their relatives","volume":"23","author":"Dodson","year":"1998","journal-title":"Trends Biochem. Sci."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.jprot.2010.12.002","article-title":"High resolution analysis of snake venom metalloproteinase (SVMP) peptide bond cleavage specificity using proteome based peptide libraries and mass spectrometry","volume":"74","author":"Escalante","year":"2011","journal-title":"J. Proteom."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1111\/j.1538-7836.2005.01363.x","article-title":"Molecular recognition mechanisms of thrombin","volume":"3","author":"Huntington","year":"2005","journal-title":"J. Thromb. Haemost."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1055\/s-2006-939551","article-title":"The structure of thrombin: A janus-headed proteinase","volume":"32","author":"Bode","year":"2006","journal-title":"Semin. Thromb. Hemost."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Kini, R.M., Clemetson, K.J., Markland, F.S., McLane, M.A., and Morita, T. (2010). Toxins and Hemostasis: From Bench to Bedside, Springer.","DOI":"10.1007\/978-90-481-9295-3"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"7095","DOI":"10.1021\/bi00482a021","article-title":"Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin","volume":"29","author":"Maraganore","year":"1990","journal-title":"Biochemistry"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1016\/0022-2836(91)90939-4","article-title":"Structure of the hirugen and hirulog 1 complexes of \u03b1-thrombin","volume":"221","author":"Carperos","year":"1991","journal-title":"J. Mol. Biol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"29101","DOI":"10.1074\/jbc.M705600200","article-title":"Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick","volume":"282","author":"Koh","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/j.matbio.2015.01.002","article-title":"New strategies for targeting matrix metalloproteinases","volume":"44\u201346","author":"Fields","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"4357","DOI":"10.1021\/acs.jmedchem.5b00278","article-title":"Design of highly potent urea-based, exosite-binding inhibitors selective for glutamate carboxypeptidase II","volume":"58","author":"Tykvart","year":"2015","journal-title":"J. Med. Chem."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1021\/bi500950x","article-title":"Probing BoNT\/A protease exosites: Implications for inhibitor design and light chain longevity","volume":"53","author":"Xue","year":"2014","journal-title":"Biochemistry"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/bmb.2005.494033032470","article-title":"Allosteric Modulation of Monomeric Proteins","volume":"33","author":"Ascenzi","year":"2005","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.bpc.2010.03.001","article-title":"Allostery in a monomeric protein: The case of human serum albumin","volume":"148","author":"Ascenzi","year":"2010","journal-title":"Biophys. Chem."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1016\/j.bbapap.2013.02.012","article-title":"Non-covalent and covalent modifications modulate the reactivity of monomeric mammalian globins","volume":"1834","author":"Ascenzi","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1016\/j.jmb.2013.04.009","article-title":"Unraveling hidden regulatory sites in structurally homologous metalloproteases","volume":"425","author":"Udi","year":"2013","journal-title":"J. Mol. Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1038\/nrd746","article-title":"Allosteric binding sites on cell-surface receptors: Novel targets for drug discovery","volume":"1","author":"Christopoulos","year":"2002","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1039\/b819720b","article-title":"Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms","volume":"5","author":"Tsai","year":"2009","journal-title":"Mol. Biosyst."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jchromb.2005.10.002","article-title":"Receptor-ligand binding assays: Technologies and applications","volume":"829","author":"Uges","year":"2005","journal-title":"J. Chromatogr. B"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1111\/j.1476-5381.2009.00604.x","article-title":"Ligand binding assays at equilibrium: Validation and interpretation","volume":"161","author":"Hulme","year":"2010","journal-title":"Br. J. Pharmacol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1007\/978-3-642-66913-2_14","article-title":"Hemorrhagic, necrotizing and edema-forming effects of snake venoms","volume":"Volume 52","author":"Lee","year":"1979","journal-title":"Handbook of Experimental Pharmacology"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/0163-7258(94)90049-3","article-title":"Hemorrhagic metalloproteinases from snake venoms","volume":"62","author":"Bjarnason","year":"1994","journal-title":"Pharmacol. Ther."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1538-7836.2011.04279.x","article-title":"Toxins in thrombosis and haemostasis: Potential beyond imagination","volume":"9","author":"Kini","year":"2011","journal-title":"J. Thromb. Haemost."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.thromres.2013.09.031","article-title":"Snake bites and hemostasis\/thrombosis","volume":"132","author":"McCleary","year":"2013","journal-title":"Thromb. Res."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.tmrv.2014.09.005","article-title":"Hematologic effects and complications of snake envenoming","volume":"29","author":"Berling","year":"2015","journal-title":"Transfus. Med. Rev."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1016\/S0041-0101(98)00126-3","article-title":"Snake venoms and the hemostatic system","volume":"36","author":"Markland","year":"1998","journal-title":"Toxicon"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"570","DOI":"10.3181\/00379727-93-22823","article-title":"Effect of Russell\u2019s viper venom (Stypven) on Stuart clotting defect","volume":"98","author":"Hougie","year":"1956","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1182\/blood.V68.4.869.869","article-title":"The use of the dilute Russell viper venom time for the diagnosis of lupus anticoagulants","volume":"68","author":"Thiagarajan","year":"1986","journal-title":"Blood"},{"key":"ref_175","first-page":"287","article-title":"Lupus anticoagulants: Pathogenesis and laboratory diagnosis","volume":"54","author":"Court","year":"1997","journal-title":"Br. J. Biomed. Sci."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1159\/000081505","article-title":"The ecarin clotting time, a universal method to quantify direct thrombin inhibitors","volume":"33","author":"Nowak","year":"2003","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1159\/000081506","article-title":"Ecarin chromogenic assay--a new method for quantitative determination of direct thrombin inhibitors like hirudin","volume":"33","author":"Lange","year":"2003","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.toxicon.2005.02.016","article-title":"Practical applications of snake venom toxins in haemostasis","volume":"45","author":"Marsh","year":"2005","journal-title":"Toxicon"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1159\/000092430","article-title":"The use of snake venom-derived compounds for new functional diagnostic test kits in the field of haemostasis","volume":"34","author":"Schoni","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.cbpb.2009.03.002","article-title":"VGD and MLD motifs containing heterodimeric disintegrin viplebedin-2 from Vipera lebetina snake venom. Purification and cDNA cloning","volume":"153","author":"Vija","year":"2009","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"14248","DOI":"10.1021\/bi025876s","article-title":"A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region","volume":"41","author":"Okuda","year":"2002","journal-title":"Biochemistry"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"4223","DOI":"10.1002\/pmic.200402024","article-title":"Snake venomics: Comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina","volume":"5","author":"Bazaa","year":"2005","journal-title":"Proteomics"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.toxicon.2011.07.004","article-title":"Non-RGD-containing snake venom disintegrins, functional and structural relations","volume":"58","author":"Walsh","year":"2011","journal-title":"Toxicon"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.febslet.2004.10.050","article-title":"Structural determinants of the selectivity of KTS-disintegrins for the \u03b11\u03b21 integrin","volume":"577","author":"Kisiel","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"815","DOI":"10.2174\/1381612053381765","article-title":"Functional characteristic of snake venom disintegrins: Potential therapeutic implication","volume":"11","author":"Marcinkiewicz","year":"2005","journal-title":"Curr. Pharm. Des."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1038\/labinvest.3700350","article-title":"Lebestatin, a disintegrin from Macrovipera venom, inhibits integrin-mediated cell adhesion, migration and angiogenesis","volume":"85","author":"Olfa","year":"2005","journal-title":"Lab. Investig."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"40714","DOI":"10.1074\/jbc.M509738200","article-title":"cDNA cloning and functional expression of jerdostatin, a novel RTS-disintegrin from Trimeresurus jerdonii and a specific antagonist of the \u03b11\u03b21 integrin","volume":"208","author":"Sanz","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1042\/BJ20081403","article-title":"Structural requirements of KTS-disintegrins for inhibition of \u03b11\u03b21 integrin","volume":"417","author":"Brown","year":"2009","journal-title":"Biochem. J."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.2174\/138161207782023766","article-title":"KTS and RTS-disintegrins: Anti-angiogenic viper venom peptides specifically targeting the alpha 1 beta 1 integrin","volume":"13","author":"Calvete","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/j.toxicon.2005.02.024","article-title":"Snake venom disintegrins: Evolution of structure and function","volume":"45","author":"Calvete","year":"2005","journal-title":"Toxicon"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1161\/01.RES.88.3.352","article-title":"Regional differences in integrin expression: Role of \u03b15\u03b21 in regulating smooth muscle cell functions","volume":"88","author":"Davenpeck","year":"2001","journal-title":"Circ. Res."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1210\/me.2004-0481","article-title":"\u03b1v\u03b23 integrins and Pyk2 mediate insulin-like growth factor I activation of Src and mitogen-activated protein kinase in 3T3-L1 cells","volume":"19","author":"Sekimoto","year":"2005","journal-title":"Mol. Endocrinol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.phrs.2004.08.004","article-title":"Differential effects of echistatin and thrombin on collagen production and prolidase activity in human dermal fibroblasts and their possible implication in \u03b21-integrin-mediated signaling","volume":"51","author":"Surazynski","year":"2005","journal-title":"Pharmacol. Res."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"12898","DOI":"10.1074\/jbc.M708226200","article-title":"Transforming growth factor \u03b21 induces \u03b1v\u03b23 integrin expression in human lung fibroblasts via a \u03b23 integrin-, c-Src-, and p38 MAPK-dependent pathway","volume":"283","author":"Pechkovsky","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.ejcb.2005.06.002","article-title":"Modulation of chondrocyte adhesion to collagen by echistatin","volume":"8410","author":"Belisario","year":"2005","journal-title":"Eur. J. Cell Biol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"2948","DOI":"10.1002\/jbmr.511","article-title":"Skeletal unloading induced insulin-like growth factor 1 (IGF-1) nonresponsiveness is not shared by platelet-derived growth factor: The selective role of integrins in IGF-1 signaling","volume":"26","author":"Long","year":"2011","journal-title":"J. Bone Miner. Res."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/s12031-009-9211-x","article-title":"Integrins contribute to initial morphological development and process outgrowth in rat adult hippocampal progenitor cells","volume":"40","author":"Harper","year":"2010","journal-title":"J. Mol. Neurosci."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/j.atherosclerosis.2015.09.026","article-title":"\u03b11\u03b21 and integrin-linked kinase interact and modulate angiotensin II effects in vascular smooth muscle cells","volume":"243","author":"Moraes","year":"2015","journal-title":"Atherosclerosis"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.dib.2015.11.053","article-title":"Data in support of \u03b11\u03b21 and integrin-linked kinase interact and modulate angiotensin II effects in vascular smooth muscle cells","volume":"6","author":"Moraes","year":"2015","journal-title":"Data Brief"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1111\/j.1527-3466.2007.00022.x","article-title":"A review of clinical trials with eptifibatide in cardiology","volume":"25","author":"Zeymer","year":"2007","journal-title":"Cardiovasc. Drug Rev."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"637","DOI":"10.2147\/VHRM.S2691","article-title":"Antiplatelet drugs in cardiological practice: Established strategies and new developments","volume":"4","author":"Krotz","year":"2008","journal-title":"Vasc. Health Risk Manag."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1023\/A:1009059210733","article-title":"Contortrostatin, a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits angiogenesis","volume":"3","author":"Zhou","year":"1999","journal-title":"Angiogenesis"},{"key":"ref_203","first-page":"183","article-title":"Novel snake venom disintegrin that inhibits human ovarian cancer dissemination and angiogenesis in an orthotopic nude mouse model","volume":"31","author":"Markland","year":"2001","journal-title":"Haemostasis"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1159\/000092418","article-title":"Contortrostatin, a snake venom disintegrin with anti-angiogenic and anti-tumor activity","volume":"34","author":"Swenson","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1158\/1535-7163.499.3.4","article-title":"Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression","volume":"3","author":"Swenson","year":"2004","journal-title":"Mol. Cancer Ther."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Minea, R.O., Helchowski, C.M., Zidovetzki, S.J., Costa, F.K., Swenson, S.D., and Markland, F.S. (2010). Vicrostatin\u2014An anti-invasive multi-integrin targeting chimeric disintegrin with tumor anti-angiogenic and pro-apoptotic activities. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010929"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1124\/jpet.114.214643","article-title":"Vimocin and vidapin, cyclic KTS peptides, are dual antagonists of \u03b11\u03b21\/\u03b12\u03b21 integrins with antiangiogenic activity","volume":"350","author":"Momic","year":"2014","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_208","first-page":"291","article-title":"Vipegitide: A folded peptidomimetic partial antagonist of \u03b12\u03b21 integrin with antiplatelet aggregation activity","volume":"9","author":"Momic","year":"2015","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1016\/j.toxicon.2005.02.025","article-title":"Snake venom probes of platelet adhesion receptors and their ligands","volume":"45","author":"Wijeyewickrema","year":"2005","journal-title":"Toxicon"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1016\/j.toxicon.2005.02.026","article-title":"Platelets as targets of snake venom metalloproteinases","volume":"45","author":"Kamiguti","year":"2005","journal-title":"Toxicon"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1002\/pro.5560010505","article-title":"Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom","volume":"1","author":"Randolph","year":"1992","journal-title":"Protein Sci."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"2448","DOI":"10.1161\/01.CIR.90.5.2448","article-title":"Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis","volume":"90","author":"Markland","year":"1994","journal-title":"Circulation"},{"key":"ref_213","first-page":"141","article-title":"Alfimeprase: Pharmacology of a novel fibrinolytic metalloproteinase for thrombolysis","volume":"31","author":"Toombs","year":"2001","journal-title":"Haemostasis"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1097\/01.RVI.0000167863.10122.2A","article-title":"A phase I trial of alfimeprase for peripheral arterial thrombolysis","volume":"16","author":"Ouriel","year":"2005","journal-title":"J. Vasc. Interv. Radiol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"3056","DOI":"10.1200\/JCO.2006.05.8438","article-title":"Phase II trial of alfimeprase, a novel-acting fibrin degradation agent, for occluded central venous access devices","volume":"24","author":"Moll","year":"2006","journal-title":"J. Clin. Oncol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"793","DOI":"10.3390\/toxins2040793","article-title":"Fibrolase: Trials and tribulations","volume":"2","author":"Markland","year":"2010","journal-title":"Toxins"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1097\/FJC.0b013e31827aadbc","article-title":"Hirudin and S18886 maintain luminal patency after thrombolysis with alfimeprase","volume":"61","author":"Lee","year":"2013","journal-title":"J. Cardiovasc. Pharmacol."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/8\/10\/284\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:32:04Z","timestamp":1760211124000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/8\/10\/284"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,9,29]]},"references-count":217,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2016,10]]}},"alternative-id":["toxins8100284"],"URL":"https:\/\/doi.org\/10.3390\/toxins8100284","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,9,29]]}}}