{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T06:37:36Z","timestamp":1774852656021,"version":"3.50.1"},"reference-count":39,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81260494"],"award-info":[{"award-number":["81260494"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["U1812403"],"award-info":[{"award-number":["U1812403"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004001","name":"Guizhou Science and Technology Department","doi-asserted-by":"publisher","award":["2019-5702"],"award-info":[{"award-number":["2019-5702"]}],"id":[{"id":"10.13039\/501100004001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004001","name":"Guizhou Science and Technology Department","doi-asserted-by":"publisher","award":["QKHPTRC 2016-5625"],"award-info":[{"award-number":["QKHPTRC 2016-5625"]}],"id":[{"id":"10.13039\/501100004001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004001","name":"Guizhou Science and Technology Department","doi-asserted-by":"publisher","award":["QKHRC 2016-4018"],"award-info":[{"award-number":["QKHRC 2016-4018"]}],"id":[{"id":"10.13039\/501100004001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004001","name":"Guizhou Science and Technology Department","doi-asserted-by":"publisher","award":["QKHZC 2018-2828"],"award-info":[{"award-number":["QKHZC 2018-2828"]}],"id":[{"id":"10.13039\/501100004001","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1016\/j.toxicon.2020.09.009","type":"journal-article","created":{"date-parts":[[2020,9,21]],"date-time":"2020-09-21T12:58:28Z","timestamp":1600693108000},"page":"223-231","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"special_numbering":"C","title":["Inhibition of platelet aggregation and blood coagulation by a P-III class metalloproteinase purified from Naja atra venom"],"prefix":"10.1016","volume":"187","author":[{"given":"Qian-Yun","family":"Sun","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cai-E","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ya-Nan","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Juan","family":"Bao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2020.09.009_bib1","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/0076-6879(95)48023-4","article-title":"Snake venom metalloendopeptidases: reprolysins","volume":"248","author":"Bjarnason","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib2","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1113\/jphysiol.1963.sp007185","article-title":"The aggregation of blood platelets","volume":"168","author":"Born","year":"1963","journal-title":"J. Physiol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib3","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/S0300-9084(00)01178-0","article-title":"Snake venom proteins acting on hemostasis","volume":"82","author":"Braud","year":"2000","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2020.09.009_bib4","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1055\/s-0038-1657230","article-title":"Bleeding time in rats: a comparison of different experimental conditions","volume":"48","author":"Dejana","year":"1982","journal-title":"Thromb. Haemostasis"},{"key":"10.1016\/j.toxicon.2020.09.009_bib5","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.toxicon.2017.04.013","article-title":"The role of platelets in hemostasis and the effects of snake venom toxins on platelet function","volume":"133","author":"de Queiroz","year":"2017","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib6","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0304-4165(84)90032-1","article-title":"Purification and properties of a fibrinogenase from the venom of Naja nigricollis","volume":"802","author":"Evans","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2020.09.009_bib7","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":"10.1016\/j.toxicon.2020.09.009_bib8","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":"10.1016\/j.toxicon.2020.09.009_bib9","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":"10.1016\/j.toxicon.2020.09.009_bib10","first-page":"778","article-title":"Current epidemiological study of snakebites in China","volume":"21","author":"Gong","year":"2012","journal-title":"J. Emerg. Tradit. Chin. Med."},{"key":"10.1016\/j.toxicon.2020.09.009_bib11","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":"2010","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib12","doi-asserted-by":"crossref","first-page":"304","DOI":"10.3390\/toxins8100304","article-title":"A comprehensive view of the structural and functional alterations of extracellular matrix by snake venom metalloproteinases (SVMPs): novel perspectives on the pathophysiology of envenoming","volume":"8","author":"Guti\u00e9rrez","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2020.09.009_bib13","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0300-9084(00)01163-9","article-title":"Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage","volume":"82","author":"Guti\u00e9rrez","year":"2000","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2020.09.009_bib14","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. Haemostasis"},{"key":"10.1016\/j.toxicon.2020.09.009_bib15","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1021\/bi00377a019","article-title":"Blood coagulation induced by the venom of Bothrops atrox. 2. Identification, purification and properties of two factor X activators","volume":"26","author":"Hofmann","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2020.09.009_bib16","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/S0041-0101(01)00216-1","article-title":"A non-toxic anticoagulant metalloprotease: purification and characterization from India cobra (Naja naja naja) venom","volume":"40","author":"Jagadeesha","year":"2002","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib17","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":"10.1016\/j.toxicon.2020.09.009_bib18","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":"10.1016\/j.toxicon.2020.09.009_bib19","doi-asserted-by":"crossref","first-page":"284","DOI":"10.3390\/toxins8100284","article-title":"Metalloproteases affecting blood coagulation, fibrinolysis and platelet aggregation from snake venoms: definition and nomenclature of interaction sites","volume":"8","author":"Kini","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2020.09.009_bib20","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 platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor","volume":"30","author":"Kini","year":"1992","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib21","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1021\/bi00667a023","article-title":"Factor X activating enzyme from Russell's viper venom: isolation and characterization","volume":"15","author":"Kisiel","year":"1976","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2020.09.009_bib22","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":"10.1016\/j.toxicon.2020.09.009_bib23","first-page":"1653","article-title":"Investigation on change regulation of blood coagulation function before and after treatment of snake bite patients","volume":"36","author":"Liang","year":"2015","journal-title":"Internet J. Lab. Med."},{"key":"10.1016\/j.toxicon.2020.09.009_bib24","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","article-title":"Snake venom metalloproteinases","volume":"62","author":"Markland","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib25","first-page":"589","article-title":"Insularinase A, a prothrombin activator from Bothrops insularis venom, is a metalloprotease derived from a gene encoding protease and disintegrin domains","volume":"386","author":"Modesto","year":"2005","journal-title":"Biol. Chem."},{"key":"10.1016\/j.toxicon.2020.09.009_bib26","doi-asserted-by":"crossref","first-page":"183","DOI":"10.3390\/toxins8060183","article-title":"Processing of snake venom metalloproteinases: generation of toxin diversity and enzyme inactivation","volume":"8","author":"Moura-da-Silva","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2020.09.009_bib27","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.toxicon.2012.03.026","article-title":"Jararhagin, a hemorrhagic snake venom metalloproteinase from Bothrops jararaca","volume":"60","author":"Moura-da-Silva","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib28","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. Haemostasis"},{"key":"10.1016\/j.toxicon.2020.09.009_bib29","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":"10.1016\/j.toxicon.2020.09.009_bib30","doi-asserted-by":"crossref","first-page":"392","DOI":"10.3390\/toxins9120392","article-title":"Direct fibrinolytic snake venom metalloproteinases affecting hemostasis: structural, biochemical features and therapeutic potential","volume":"9","author":"Sanchez","year":"2017","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2020.09.009_bib31","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1016\/j.molimm.2004.11.009","article-title":"Oxiagin from the Naja oxiana cobra venom is the first reprolysin inhibiting the classical pathway of complement","volume":"42","author":"Shoibonov","year":"2005","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib32","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/S0304-4165(01)00206-9","article-title":"Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity","volume":"1568","author":"Siigur","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2020.09.009_bib33","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1016\/j.toxicon.2010.08.013","article-title":"Purification, cloning and characterization of a metalloproteinase from Naja atra venom","volume":"56","author":"Sun","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2020.09.009_bib34","first-page":"835","article-title":"Purification and characterization of a metalloproteinase with weak fibrinogenolytic activity from Naja atra venom","volume":"23","author":"Sun","year":"2007","journal-title":"Chin. J. Biochem. Mol. Biol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib35","doi-asserted-by":"crossref","first-page":"4929","DOI":"10.1021\/bi952456c","volume":"35","author":"Ward","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2020.09.009_bib36","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":"10.1016\/j.toxicon.2020.09.009_bib37","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.biocel.2005.10.011","article-title":"Potent histamine-releasing activity of atrahagin, a novel snake venom metalloproteinase","volume":"38","author":"Wei","year":"2006","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.toxicon.2020.09.009_bib38","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":"10.1016\/j.toxicon.2020.09.009_bib39","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"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010120303913?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010120303913?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:18:24Z","timestamp":1758575904000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010120303913"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11]]},"references-count":39,"alternative-id":["S0041010120303913"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2020.09.009","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2020,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Inhibition of platelet aggregation and blood coagulation by a P-III class metalloproteinase purified from Naja atra venom","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2020.09.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}