{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T21:09:54Z","timestamp":1792789794181,"version":"4.5.0"},"reference-count":266,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2024,10,3]],"date-time":"2024-10-03T00:00:00Z","timestamp":1727913600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"CNPq","award":["422508\/2021-7"],"award-info":[{"award-number":["422508\/2021-7"]}]},{"name":"University of Brasilia and CAPES","award":["422508\/2021-7"],"award-info":[{"award-number":["422508\/2021-7"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey\u2019s hemostatic system. Their actions extend across the coagulation cascade, the kallikrein\u2013kinin system, and platelet activation. Despite their specificity for different substrates, these enzymes are homologous across all toxicoferans and display high sequence similarity. The aim of this review is to compile decades of knowledge about venom serine proteases, showing the diversity of biochemically and biophysically characterized enzymes, their structural characteristics, advances in understanding their origin and evolution, as well as methods of obtaining enzymes and their biotechnological applications.<\/jats:p>","DOI":"10.3390\/toxins16100428","type":"journal-article","created":{"date-parts":[[2024,10,3]],"date-time":"2024-10-03T03:36:03Z","timestamp":1727926563000},"page":"428","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview"],"prefix":"10.3390","volume":"16","author":[{"given":"Julia F. D.","family":"Vidal","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matheus F.","family":"Schwartz","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aisel V.","family":"Garay","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6251-7342","authenticated-orcid":false,"given":"Napole\u00e3o F.","family":"Valadares","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9802-331X","authenticated-orcid":false,"given":"Renata V.","family":"Bueno","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Carolina L.","family":"Monteiro","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7562-4980","authenticated-orcid":false,"given":"S\u00f4nia Maria de","family":"Freitas","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00e3o Alexandre R. G.","family":"Barbosa","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Bras\u00edlia, Asa Norte, Brasilia 70910-900, DF, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,10,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1791","DOI":"10.1111\/j.1538-7836.2005.01358.x","article-title":"Snake Venoms and Hemostasis","volume":"3","author":"Lu","year":"2005","journal-title":"J. Thromb. Haemost."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1016\/j.crvi.2005.10.001","article-title":"The Phylogeny of Squamate Reptiles (Lizards, Snakes, and Amphisbaenians) Inferred from Nine Nuclear Protein-Coding Genes","volume":"328","author":"Vidal","year":"2005","journal-title":"Comptes Rendus Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nature04328","article-title":"Early Evolution of the Venom System in Lizards and Snakes","volume":"439","author":"Fry","year":"2006","journal-title":"Nature"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"8969","DOI":"10.1073\/pnas.0810883106","article-title":"A Central Role for Venom in Predation by Varanus komodoensis (Komodo Dragon) and the Extinct Giant Varanus (Megalania) Priscus","volume":"106","author":"Fry","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","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_6","first-page":"47","article-title":"The Squamate Tree of Life","volume":"163","author":"Pyron","year":"2021","journal-title":"Bull. Mus. Comp. Zool."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"4501","DOI":"10.1021\/cr000033x","article-title":"Serine Protease Mechanism and Specificity","volume":"102","author":"Hedstrom","year":"2002","journal-title":"Chem. Rev."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"D503","DOI":"10.1093\/nar\/gkt953","article-title":"MEROPS: The Database of Proteolytic Enzymes, Their Substrates and Inhibitors","volume":"42","author":"Rawlings","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1084\/jem.164.6.1835","article-title":"Helodermatine, a Kallikrein-like, Hypotensive Enzyme from the Venom of Heloderma horridum horridum (Mexican Beaded Lizard)","volume":"164","author":"Alagon","year":"1986","journal-title":"J. Exp. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"21975","DOI":"10.1016\/S0021-9258(20)80636-X","article-title":"Complete Primary Structure and Biochemical Properties of Gilatoxin, a Serine Protease with Kallikrein-like and Angiotensin-Degrading Activities","volume":"268","author":"Utaisincharoen","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.toxicon.2005.02.020","article-title":"Snake Venom Serine Proteinases: Sequence Homology vs. Substrate Specificity, a Paradox to Be Solved","volume":"45","author":"Serrano","year":"2005","journal-title":"Toxicon"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e2015159118","DOI":"10.1073\/pnas.2015159118","article-title":"Tracking the Recruitment and Evolution of Snake Toxins Using the Evolutionary Context Provided by the Bothrops jararaca Genome","volume":"118","author":"Almeida","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/j.ijbiomac.2018.03.164","article-title":"Thrombin-like Enzymes from Snake Venom: Structural Characterization and Mechanism of Action","volume":"114","author":"Ullah","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1002\/jsfa.4733","article-title":"Isolation and Characterisation of a Kallikrein-like Enzyme from Agkistrodon halys pallas Snake Venom","volume":"92","author":"Zhang","year":"2012","journal-title":"J. Sci. Food Agric."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/0304-4165(94)00216-K","article-title":"Cerastocytin, a New Thrombin-like Platelet Activator from the Venom of the Tunisian Viper Cerastes cerastes","volume":"1244","author":"Marrakchi","year":"1995","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1762","DOI":"10.1016\/j.bbagen.2006.08.023","article-title":"Biochemical Characterization and Molecular Cloning of a Plasminogen Activator Proteinase (LV-PA) from Bushmaster Snake Venom","volume":"1760","author":"Sanchez","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_17","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_18","doi-asserted-by":"crossref","unstructured":"Mukherjee, A.K. (2014). The Pro-Coagulant Fibrinogenolytic Serine Protease Isoenzymes Purified from Daboia russelii russelii Venom Coagulate the Blood through Factor V Activation: Role of Glycosylation on Enzymatic Activity. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0086823"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.biochi.2013.04.006","article-title":"Cotiarinase Is a Novel Prothrombin Activator from the Venom of Bothrops Cotiara","volume":"95","author":"Kitano","year":"2013","journal-title":"Biochimie"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.bbapap.2005.08.003","article-title":"Crystallization and Preliminary X-Ray Crystallographic Studies of Protac, a Commercial Protein C Activator Isolated from Agkistrodon contortrix contortrix Venom","volume":"1752","author":"Murakami","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1073\/pnas.79.6.1688","article-title":"Kallikrein-like Activity of Crotalase, a Snake Venom Enzyme That Clots Fibrinogen","volume":"79","author":"Markland","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/S0167-4838(99)00268-X","article-title":"Snake Venom Proteases Affecting Hemostasis and Thrombosis","volume":"1477","author":"Matsui","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1002\/pro.3290","article-title":"Clustal Omega for Making Accurate Alignments of Many Protein Sequences","volume":"27","author":"Sievers","year":"2018","journal-title":"Protein Sci."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering Key Features in Protein Structures with the New ENDscript Server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_25","unstructured":"Rawlings, N.D., and Salvesen, G. (2013). Chapter 642\u2014Coagulation Factor Xa. Handbook of Proteolytic Enzymes, Academic Press. [3rd ed.]."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/0268-960X(94)90007-8","article-title":"Biochemistry of Factor X","volume":"8","author":"Hertzberg","year":"1994","journal-title":"Blood Rev."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"6293","DOI":"10.1021\/bi002209v","article-title":"Binding of Plasminogen and Tissue Plasminogen Activator to Plasmin-Modulated Factor X and Factor Xa","volume":"40","author":"Grundy","year":"2001","journal-title":"Biochemistry"},{"key":"ref_28","first-page":"225","article-title":"Snake Venom Activators of Factor X: An Overview","volume":"31","author":"Tans","year":"2001","journal-title":"Haemostasis"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/0041-0101(93)90260-P","article-title":"Low Molecular Weight Factor X Activator from Cerastes Vipera (Sahara Sand Viper) Venom","volume":"31","author":"Farid","year":"1993","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Latinovi\u0107, Z., Leonardi, A., Koh, C.Y., Kini, R.M., Trampu\u0161 Bakija, A., Punger\u010dar, J., and Kri\u017eaj, I. (2020). The Procoagulant Snake Venom Serine Protease Potentially Having a Dual, Blood Coagulation Factor V and X-Activating Activity. Toxins, 12.","DOI":"10.3390\/toxins12060358"},{"key":"ref_31","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 Bungarus fasciatus","volume":"33","author":"Zhang","year":"1995","journal-title":"Toxicon"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1016\/0041-0101(95)00077-Y","article-title":"Isolation and Properties of a Blood Coagulation Factor X Activator from the Venom of King Cobra (Ophiophagus hannah)","volume":"33","author":"Lee","year":"1995","journal-title":"Toxicon"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"10294","DOI":"10.1021\/bi000145i","article-title":"A Novel Venombin B from Agkistrodon contortrix contortrix: Evidence for Recognition Properties in the Surface around the Primary Specificity Pocket Different from Thrombin","volume":"39","author":"Amiconi","year":"2000","journal-title":"Biochemistry"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1016\/0041-0101(92)90052-7","article-title":"Activation of Bovine Factor V by an Activator Purified from the Venom of Naja naja oxiana","volume":"30","author":"Gerads","year":"1992","journal-title":"Toxicon"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1016\/j.febslet.2011.08.022","article-title":"Structural Basis of Coagulation Factor V Recognition for Cleavage by RVV-V","volume":"585","author":"Nakayama","year":"2011","journal-title":"FEBS Lett."},{"key":"ref_36","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_37","doi-asserted-by":"crossref","first-page":"17471","DOI":"10.1016\/S0021-9258(19)77860-0","article-title":"The Factor V-Activating Enzyme (RVV-V) from Russell\u2019s Viper Venom. Identification of Isoproteins RVV-V Alpha, -V Beta, and -V Gamma and Their Complete Amino Acid Sequences","volume":"263","author":"Tokunaga","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_38","first-page":"241","article-title":"Factor V Activation and Inactivation by Venom Proteases","volume":"31","author":"Rosing","year":"2001","journal-title":"Haemostasis"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/S0167-4838(98)00232-5","article-title":"Isolation, Properties and N-Terminal Amino Acid Sequence of a Factor V Activator from Vipera lebetina (Levantine Viper) Snake Venom","volume":"1429","author":"Siigur","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_40","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_41","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_42","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1016\/0041-0101(94)90352-2","article-title":"Isolation and Characterization of Textarin, a Prothrombin Activator from Eastern Brown Snake (Pseudonaja textilis) Venom","volume":"32","author":"Stocker","year":"1994","journal-title":"Toxicon"},{"key":"ref_43","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_44","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_45","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1006\/bbrc.1999.0203","article-title":"cDNA Cloning and Expression of Acutin","volume":"255","author":"Pan","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj3540161","article-title":"Serine Protease Isoforms of Deinagkistrodon acutus Venom: Cloning, Sequencing and Phylogenetic Analysis","volume":"354","author":"Wang","year":"2001","journal-title":"Biochem. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1016\/S0041-0101(98)00228-1","article-title":"Purification and Characterization of Two Fibrinogen-Clotting Enzymes from Five-Pace Snake (Agkistrodon acutus) Venom","volume":"37","author":"Huang","year":"1999","journal-title":"Toxicon"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.ejps.2013.02.002","article-title":"Biochemical Properties and Comparative Pharmacology of a Coagulant from Deinagkistrodon acutus Snake Venom","volume":"49","author":"Tang","year":"2013","journal-title":"Eur. J. Pharm. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00018-003-3325-z","article-title":"Snake Venom Thrombin-like Enzymes: From Reptilase to Now","volume":"61","author":"Castro","year":"2004","journal-title":"Cell Mol. Life Sci."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0076-6879(76)45020-6","article-title":"Ancrod, the Coagulating Enzyme from Malayan Pit Viper (Agkistrodon rhodostoma) Venom","volume":"45","author":"Nolan","year":"1976","journal-title":"Methods Enzymol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/0014-5793(92)80559-Y","article-title":"Amino Acid Sequence Determination of Ancrod, the Thrombin-like Alpha-Fibrinogenase from the Venom of Akistrodon rhodostoma","volume":"297","author":"Burkhart","year":"1992","journal-title":"FEBS Lett."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/S0076-6879(76)45021-8","article-title":"The Coagulant Enzyme from Bothrops Atrox Venom (Batroxobin)","volume":"45","author":"Stocker","year":"1976","journal-title":"Methods Enzymol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"16862","DOI":"10.1074\/jbc.M113.464750","article-title":"Batroxobin Binds Fibrin with Higher Affinity and Promotes Clot Expansion to a Greater Extent than Thrombin","volume":"288","author":"Vu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1016\/j.toxicon.2010.02.014","article-title":"Bhalternin: Functional and Structural Characterization of a New Thrombin-like Enzyme from Bothrops Alternatus Snake Venom","volume":"55","author":"Costa","year":"2010","journal-title":"Toxicon"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Torres-Huaco, F.D., Werneck, C.C., Vicente, C.P., Vassequi-Silva, T., Nery-Diez, A.C.C., Mendes, C.B., Antunes, E., Marangoni, S., and Damico, D.C.S. (2013). Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-like\/Gyroxin-like Enzyme from Lachesis muta rhombeata Snake Venom. Biomed. Res. Int., 2013.","DOI":"10.1155\/2013\/903292"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1476","DOI":"10.1016\/j.biochi.2013.03.015","article-title":"Coagulant Thrombin-like Enzyme (Barnettobin) from Bothrops barnetti Venom: Molecular Sequence Analysis of Its cDNA and Biochemical Properties","volume":"95","author":"Sandoval","year":"2013","journal-title":"Biochimie"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1843","DOI":"10.1021\/bi00173a030","article-title":"Purification and Characterization of Bothrombin, a Fibrinogen-Clotting Serine Protease from the Venom of Bothrops jararaca","volume":"33","author":"Nishida","year":"1994","journal-title":"Biochemistry"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.toxicon.2009.05.040","article-title":"Biochemical and Functional Properties of a Thrombin-like Enzyme Isolated from Bothrops pauloensis Snake Venom","volume":"54","author":"Costa","year":"2009","journal-title":"Toxicon"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1093\/oxfordjournals.jbchem.a021319","article-title":"Purification and Molecular Cloning of Calobin, a Thrombin-like Enzyme from Agkistrodon caliginosus (Korean Viper)","volume":"119","author":"Hahn","year":"1996","journal-title":"J. Biochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.toxicon.2012.11.010","article-title":"Biochemical and Biological Characterization of Two Serine Proteinases from Colombian Crotalus durissus cumanensis Snake Venom","volume":"63","author":"Rucavado","year":"2013","journal-title":"Toxicon"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1111\/j.1432-1033.1997.00121.x","article-title":"Cerastotin, a Serine Protease from Cerastes cerastes Venom, with Platelet-Aggregating and Agglutinating Properties","volume":"247","author":"Marrakchi","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1055\/s-0037-1614423","article-title":"Crotalase, a Fibrinogen-Clotting Snake Venom Enzyme: Primary Structure and Evidence for a Fibrinogen Recognition Exosite Different from Thrombin","volume":"81","author":"Theodor","year":"1999","journal-title":"Thromb. Haemost."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Amorim, F.G., Menaldo, D.L., Carone, S.E.I., Silva, T.A., Sartim, M.A., De Pauw, E., Quinton, L., and Sampaio, S.V. (2018). New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom. Toxins, 10.","DOI":"10.3390\/toxins10120500"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0041-0101(02)00363-X","article-title":"Purification and Characterization of a Thrombin like Enzyme, Elegaxobin II, with Lys-Bradykinin Releasing Activity from the Venom of Trimeresurus elegans (Sakishima-Habu)","volume":"41","author":"Oyama","year":"2003","journal-title":"Toxicon"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1046\/j.1365-2567.2002.01490.x","article-title":"Flavoxobin, a Serine Protease from Trimeresurus flavoviridis (Habu Snake) Venom, Independently Cleaves Arg726-Ser727 of Human C3 and Acts as a Novel, Heterologous C3 Convertase","volume":"107","author":"Yamamoto","year":"2002","journal-title":"Immunology"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/0041-0101(88)90260-7","article-title":"Gyroxin, a Toxin from the Venom of Crotalus durissus terrificus, Is a Thrombin-like Enzyme","volume":"26","author":"Alexander","year":"1988","journal-title":"Toxicon"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1016\/S0041-0101(99)00222-6","article-title":"Characterization of a Thrombin-like Enzyme from the Venom of Trimeresurus jerdonii","volume":"38","author":"Lu","year":"2000","journal-title":"Toxicon"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.toxicon.2004.11.006","article-title":"Molecular Characterization of a Weak Fibrinogen-Clotting Enzyme from Trimeresurus jerdonii Venom","volume":"45","author":"Jin","year":"2005","journal-title":"Toxicon"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1046\/j.1432-1327.1998.2510845.x","article-title":"Purification and Characterization of a Kinin-Releasing and Fibrinogen-Clotting Serine Proteinase (KN-BJ) from the Venom of Bothrops jararaca, and Molecular Cloning and Sequence Analysis of Its cDNA","volume":"251","author":"Serrano","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.cbpa.2005.12.033","article-title":"Purification and Properties of a Coagulant Thrombin-like Enzyme from the Venom of Bothrops leucurus","volume":"146","author":"Richardson","year":"2007","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/0014-5793(93)80205-9","article-title":"The Complete Amino Acid Sequence of a Thrombin-like Enzyme\/Gyroxin Analogue from Venom of the Bushmaster Snake (Lachesis muta muta)","volume":"329","author":"Magalhaes","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"3570","DOI":"10.1021\/bi00583a021","article-title":"Thrombocytin, a Serine Protease from Bothrops Atrox Venom. 2. Interaction with Platelets and Plasma-Clotting Factors","volume":"18","author":"Niewiarowski","year":"1979","journal-title":"Biochemistry"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3564","DOI":"10.1021\/bi00583a020","article-title":"Thrombocytin, a Serine Protease from Bothrops Atrox Venom. 1. Purification and Characterization of the Enzyme","volume":"18","author":"Kirby","year":"1979","journal-title":"Biochemistry"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1016\/0041-0101(92)90515-7","article-title":"A Fibrinogen-Clotting Serine Proteinase from Cerastes cerastes (Horned Viper) Venom with Arginine-Esterase and Amidase Activities. Purification, Characterization and Kinetic Parameter Determination","volume":"30","author":"Marchot","year":"1992","journal-title":"Toxicon"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1046\/j.1432-1327.1998.2520569.x","article-title":"Purification and Amino Acid Sequence of Halystase from Snake Venom of Agkistrodon halys Blomhoffii, a Serine Protease That Cleaves Specifically Fibrinogen and Kininogen","volume":"252","author":"Matsui","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1006\/prep.2001.1531","article-title":"Cloning and Functional Expression of the Mucrosobin Protein, a Beta-Fibrinogenase of Trimeresurus mucrosquamatus (Taiwan Habu)","volume":"23","author":"Guo","year":"2001","journal-title":"Protein Expr. Purif."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1016\/j.biochi.2012.07.007","article-title":"Biochemical Characterization and Comparative Analysis of Two Distinct Serine Proteases from Bothrops pirajai Snake Venom","volume":"94","author":"Menaldo","year":"2012","journal-title":"Biochimie"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.toxicon.2007.02.018","article-title":"BJ-48, a Novel Thrombin-like Enzyme from the Bothrops jararacussu Venom with High Selectivity for Arg over Lys in P1: Role of N-Glycosylation in Thermostability and Active Site Accessibility","volume":"50","author":"Guedes","year":"2007","journal-title":"Toxicon"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.bpc.2007.11.002","article-title":"Structural Characterization and Low-Resolution Model of BJ-48, a Thrombin-like Enzyme from Bothrops jararacussu Venom","volume":"132","author":"Guedes","year":"2008","journal-title":"Biophys. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1006\/bbrc.1999.0977","article-title":"Purification and Characterization of Brevinase, a Heterogeneous Two-Chain Fibrinolytic Enzyme from the Venom of Korean Snake, Agkistrodon blomhoffii brevicaudus","volume":"260","author":"Lee","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_81","first-page":"217","article-title":"Cloning, Sequence Analysis and Expression in E. Coli of the cDNA of the Thrombin-like Enzyme (Pallabin) from the Venom of Agkistrodon halys pallas","volume":"47","author":"Fan","year":"1999","journal-title":"Biochem. Mol. Biol. Int."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1111\/j.1432-1033.1995.756_3.x","article-title":"Afa\u00e2cytin, an Alpha Beta-Fibrinogenase from Cerastes cerastes (Horned Viper) Venom, Activates Purified Factor X and Induces Serotonin Release from Human Blood Platelets","volume":"233","author":"Mauco","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.toxicon.2016.09.017","article-title":"Agkihpin, a Novel SVTLE from Gloydius halys pallas, Promotes Platelet Aggregation in Vitro and Inhibits Thrombus Formation in Vivo in Murine Models of Thrombosis","volume":"122","author":"Xie","year":"2016","journal-title":"Toxicon"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0041-0101(93)90144-8","article-title":"Effect of Bilineobin, a Thrombin-like Proteinase from the Venom of Common Cantil (Agkistrodon bilineatus)","volume":"31","author":"Komori","year":"1993","journal-title":"Toxicon"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1006\/abbi.1995.1208","article-title":"Primary Structure of a Coagulant Enzyme, Bilineobin, from Agkistrodon bilineatus Venom","volume":"318","author":"Nikai","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.toxicon.2016.01.055","article-title":"Biochemical and Functional Characterization of BmooSP, a New Serine Protease from Bothrops moojeni Snake Venom","volume":"111","author":"Mamede","year":"2016","journal-title":"Toxicon"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Zaqueo, K.D., Kayano, A.M., Sim\u00f5es-Silva, R., Moreira-Dill, L.S., Fernandes, C.F.C., Fuly, A.L., Maltarollo, V.G., Hon\u00f3rio, K.M., da Silva, S.L., and Acosta, G. (2014). Isolation and Biochemical Characterization of a New Thrombin-like Serine Protease from Bothrops pirajai Snake Venom. Biomed. Res. Int., 2014.","DOI":"10.1155\/2014\/595186"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/0041-0101(96)00006-2","article-title":"Purification and Characterization of a Fibrinogen-Clotting Enzyme from the Venom of Jararacu\u00e7u (Bothrops jararacussu)","volume":"34","author":"Zaganelli","year":"1996","journal-title":"Toxicon"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"8830","DOI":"10.1016\/S0021-9258(19)84456-3","article-title":"Thrombin-like Enzyme from the Venom of Bitis Gabonica. Purification, Properties, and Coagulant Actions","volume":"261","author":"Pirkle","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1016\/j.bbagen.2013.02.007","article-title":"Biochemical and Pharmacological Properties of a New Thrombin-like Serine Protease (Russelobin) from the Venom of Russell\u2019s Viper (Daboia russelii russelii) and Assessment of Its Therapeutic Potential","volume":"1830","author":"Mukherjee","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1021\/bi00427a051","article-title":"Characterization of Cerastobin, a Thrombin-like Enzyme from the Venom of Cerastes vipera (Sahara Sand Viper)","volume":"28","author":"Farid","year":"1989","journal-title":"Biochemistry"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S0041-0101(02)00140-X","article-title":"Purification, Characterization and Crystallization of Jararacussin-I, a Fibrinogen-Clotting Enzyme Isolated from the Venom of Bothrops jararacussu","volume":"40","author":"Bortoleto","year":"2002","journal-title":"Toxicon"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1097\/MBC.0000000000000856","article-title":"Purification and Characterization of a Thrombin-like Enzyme Isolated from Vipera lebetina Venom: Its Interaction with Platelet Receptor","volume":"31","year":"2020","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1002\/jbt.21709","article-title":"Purification and Characterization of a New Serine Protease (VLCII) Isolated from Vipera lebetina Venom: Its Role in Hemostasis","volume":"29","author":"Amel","year":"2015","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/0049-3848(93)90080-8","article-title":"Protein C Activator from the Venom of Agkistrodon blomhoffi ussuriensis Retards Thrombus Formation in the Arterio-Venous Shunt in Rats","volume":"70","author":"Kogan","year":"1993","journal-title":"Thromb. Res."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1097\/00001721-199308000-00012","article-title":"Protein C Activation by an Activator Purified from the Venom of Agkistrodon halys halys","volume":"4","author":"Bakker","year":"1993","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"4175","DOI":"10.1021\/bi00363a001","article-title":"Purification of a Protein C Activator from the Venom of the Southern Copperhead Snake (Agkistrodon contortrix contortrix)","volume":"25","author":"Klein","year":"1986","journal-title":"Biochemistry"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/0049-3848(90)90305-V","article-title":"Isolation and Characterization of a Protein C Activator from Tropical Moccasin Venom","volume":"58","author":"Nakagaki","year":"1990","journal-title":"Thromb. Res."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2965","DOI":"10.1016\/j.febslet.2007.05.047","article-title":"Identification and Characterization of Harobin, a Novel Fibrino(Geno)Lytic Serine Protease from a Sea Snake (Lapemis hardwickii)","volume":"581","author":"He","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/s40409-018-0176-5","article-title":"Kn-Ba: A Novel Serine Protease Isolated from Bitis Arietans Snake Venom with Fibrinogenolytic and Kinin-Releasing Activities","volume":"24","author":"Megale","year":"2018","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/S1046-5928(03)00053-6","article-title":"Kallikrein-like Proteinase from Bushmaster Snake Venom","volume":"30","author":"Felicori","year":"2003","journal-title":"Protein Expr. Purif."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Vaiyapuri, S., Harrison, R.A., Bicknell, A.B., Gibbins, J.M., and Hutchinson, G. (2010). Purification and Functional Characterisation of Rhinocerase, a Novel Serine Protease from the Venom of Bitis gabonica rhinoceros. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0009687"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1006\/bbrc.2001.4452","article-title":"Fibrinogenolytic Proteases Isolated from the Snake Venom of Taiwan Habu: Serine Proteases with Kallikrein-like and Angiotensin-Degrading Activities","volume":"281","author":"Hung","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"3517","DOI":"10.1021\/bi00515a033","article-title":"Biochemical Characterization of the Lizard Toxin Gilatoxin","volume":"20","author":"Hendon","year":"1981","journal-title":"Biochemistry"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"10246","DOI":"10.1074\/jbc.270.17.10246","article-title":"A Novel Plasminogen Activator from Snake Venom. Purification, Characterization, and Molecular Cloning","volume":"270","author":"Zhang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1006\/abbi.2000.1781","article-title":"Isolation of a Proteinase with Plasminogen-Activating Activity from Lachesis muta muta (Bushmaster) Snake Venom","volume":"378","author":"Sanchez","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1016\/S0041-0101(98)00090-7","article-title":"Expression and Characterization of a Novel Plasminogen Activator from Agkistrodon halys Venom","volume":"36","author":"Park","year":"1998","journal-title":"Toxicon"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1182\/blood.V56.6.1020.1020","article-title":"Crotalocytin: Characterization of the Timber Rattlesnake Platelet Activating Protein","volume":"56","author":"Schmaier","year":"1980","journal-title":"Blood"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"7186","DOI":"10.1021\/bi00021a033","article-title":"Purification, Characterization, and Amino Acid Sequence of a Serine Proteinase, PA-BJ, with Platelet-Aggregating Activity from the Venom of Bothrops jararaca","volume":"34","author":"Serrano","year":"1995","journal-title":"Biochemistry"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/0041-0101(93)90182-I","article-title":"Basic Proteinases from Bothrops moojeni (Caissaca) Venom\u2014I. Isolation and Activity of Two Serine Proteinases, MSP 1 and MSP 2, on Synthetic Substrates and on Platelet Aggregation","volume":"31","author":"Serrano","year":"1993","journal-title":"Toxicon"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"6508","DOI":"10.1073\/pnas.86.17.6508","article-title":"Differential Proteolytic Activation of Factor VIII-von Willebrand Factor Complex by Thrombin","volume":"86","author":"Parker","year":"1989","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1016\/0049-3848(77)90144-X","article-title":"Throbocytin-a Novel Platelet Activating Enzyme from Bothrops Atrox Venom","volume":"10","author":"Niewiarowski","year":"1977","journal-title":"Thromb. Res."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1021\/bi00457a004","article-title":"Activation of Human Factor V by Factor Xa and Thrombin","volume":"29","author":"Monkovic","year":"1990","journal-title":"Biochemistry"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3137","DOI":"10.1182\/blood.2021010684","article-title":"Cryo-EM Structures of Human Coagulation Factors V and Va","volume":"137","author":"Ruben","year":"2021","journal-title":"Blood"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"22044","DOI":"10.1016\/S0021-9258(18)45845-0","article-title":"Kinetic Intermediates in Prothrombin Activation. Bovine Prethrombin 1 Conversion to Thrombin by Factor X","volume":"265","author":"Carlisle","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"4224","DOI":"10.1016\/S0021-9258(17)35651-X","article-title":"Formation of Meizothrombin as Intermediate in Factor Xa-Catalyzed Prothrombin Activation","volume":"261","author":"Rosing","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"21864","DOI":"10.1016\/S0021-9258(18)54717-7","article-title":"Meizothrombin Formation during Factor Xa-Catalyzed Prothrombin Activation. Formation in a Purified System and in Plasma","volume":"266","author":"Tans","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"4017","DOI":"10.1016\/S0021-9258(19)67895-6","article-title":"Formation of Meizothrombin as Intermediate in Factor Xa-Catalyzed Prothrombin Activation on Endothelial Cells. The Influence of Thrombin on the Reaction Mechanism","volume":"266","author":"Tijburg","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_119","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_120","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1055\/s-0037-1616108","article-title":"Registry of Exogenous Hemostatic Factors of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis Classification and Nomenclature of Prothrombin Activators Isolated from Snake Venoms","volume":"86","author":"Morita","year":"2001","journal-title":"Thromb. Haemost."},{"key":"ref_121","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_122","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/BF00501003","article-title":"The Prothrombin-Activating Principle from Echis carinatus Venom. II. Coagulation Studies in Vitro and in Vivo","volume":"274","author":"Schieck","year":"1972","journal-title":"Naunyn Schmiedebergs Arch. Pharmacol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S0049-3848(97)00258-2","article-title":"Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom","volume":"88","author":"Petrovan","year":"1997","journal-title":"Thromb. Res."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1021\/bi00546a029","article-title":"Characterization of the Prothrombin Activator from the Venom of Oxyuranus scutellatus scutellatus (Taipan Venom)","volume":"19","author":"Walker","year":"1980","journal-title":"Biochemistry"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1160\/TH04-03-0144","article-title":"The Catalytic Subunit of Pseutarin C, a Group C Prothrombin Activator from the Venom of Pseudonaja textilis, Is Structurally Similar to Mammalian Blood Coagulation Factor Xa","volume":"92","author":"Rao","year":"2004","journal-title":"Thromb. Haemost."},{"key":"ref_126","first-page":"234","article-title":"Snake Venom Prothrombin Activators Homologous to Blood Coagulation Factor Xa","volume":"31","author":"Joseph","year":"2001","journal-title":"Haemostasis"},{"key":"ref_127","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 Venom","volume":"45","author":"Kini","year":"2005","journal-title":"Toxicon"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1182\/blood-2002-12-3839","article-title":"The Nonenzymatic Subunit of Pseutarin C, a Prothrombin Activator from Eastern Brown Snake (Pseudonaja textilis) Venom, Shows Structural Similarity to Mammalian Coagulation Factor V","volume":"102","author":"Rao","year":"2003","journal-title":"Blood"},{"key":"ref_129","first-page":"825","article-title":"Purification and Characterization of a Prothrombin Activator from the Venom of the Australian Brown Snake, Pseudonaja textilis textilis","volume":"17","author":"Masci","year":"1988","journal-title":"Biochem. Int."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Lang, F. (2009). Activated Protein C Resistance. Encyclopedia of Molecular Mechanisms of Disease, Springer.","DOI":"10.1007\/978-3-540-29676-8"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"6567","DOI":"10.1074\/jbc.M308574200","article-title":"Factor Va Is Inactivated by Activated Protein C in the Absence of Cleavage Sites at Arg-306, Arg-506, and Arg-679","volume":"279","author":"Dirven","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1182\/asheducation-2009.1.255","article-title":"Pathogenesis of Thrombosis","volume":"2009","author":"Furie","year":"2009","journal-title":"Hematol. Am. Soc. Hematol. Educ. Program"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.blre.2006.11.001","article-title":"Thrombin Generation and Fibrin Clot Structure","volume":"21","author":"Wolberg","year":"2007","journal-title":"Blood Rev."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.blre.2014.09.003","article-title":"Fibrinolysis and the Control of Blood Coagulation","volume":"29","author":"Chapin","year":"2015","journal-title":"Blood Rev."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.thromres.2011.11.040","article-title":"Factor XIII, Clot Structure, Thrombosis","volume":"129","author":"Bagoly","year":"2012","journal-title":"Thromb. Res."},{"key":"ref_136","first-page":"275","article-title":"Multifunctional Roles of Thrombin","volume":"29","author":"Narayanan","year":"1999","journal-title":"Ann. Clin. Lab. Sci."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1097\/MBC.0000000000001130","article-title":"The Role of Thrombin in Haemostasis","volume":"33","year":"2022","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0065-2423(08)60207-3","article-title":"Current Concepts of Coagulation and Fibrinolysis","volume":"33","author":"Narayanan","year":"1998","journal-title":"Adv. Clin. Chem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.2174\/092986710791233706","article-title":"Regulation of the Protein C Anticoagulant and Antiinflammatory Pathways","volume":"17","author":"Rezaie","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3109\/15569543.2013.852109","article-title":"Snake Venom Thrombin-like Enzymes","volume":"33","author":"Pradniwat","year":"2014","journal-title":"Toxin Rev."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Phillips, D.J., Swenson, S.D., and Markland, F.S. (2010). Thrombin-like Snake Venom Proteinases. Handbook of Venoms and Toxins of Reptiles, CRC Press.","DOI":"10.1201\/9781420008661.ch6"},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Kini, R.M., Clemetson, K.J., Markland, F.S., McLane, M.A., and Morita, T. (2010). Thrombin-Like Enzymes in Snake Venoms. Toxins and Hemostasis: From Bench to Bedside, Springer.","DOI":"10.1007\/978-90-481-9295-3"},{"key":"ref_143","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_144","doi-asserted-by":"crossref","first-page":"913","DOI":"10.2174\/092986609788923293","article-title":"Venom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins","volume":"16","author":"Soares","year":"2009","journal-title":"Protein Pept. Lett."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1107\/S1744309111022548","article-title":"Structure of Saxthrombin, a Thrombin-like Enzyme from Gloydius saxatilis","volume":"67","author":"Huang","year":"2011","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1006\/bbrc.1994.2865","article-title":"Characterization of One Novel Venom Protease with Beta-Fibrinogenase Activity from the Taiwan Habu (Trimeresurus mucrosquamatus): Purification and cDNA Sequence Analysis","volume":"205","author":"Hung","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/S0021-9258(17)33886-3","article-title":"A New Vitamin K-Dependent Protein. Purification from Bovine Plasma and Preliminary Characterization","volume":"251","author":"Stenflo","year":"1976","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1182\/blood.V59.5.1067.1067","article-title":"Mechanism of Action of Human Activated Protein C, a Thrombin-Dependent Anticoagulant Enzyme","volume":"59","author":"Marlar","year":"1982","journal-title":"Blood"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"5548","DOI":"10.1016\/S0021-9258(20)81925-5","article-title":"Proteolytic Formation and Properties of Gamma-Carboxyglutamic Acid-Domainless Protein C","volume":"258","author":"Esmon","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"643","DOI":"10.2174\/0929866525666180619101218","article-title":"Venom Protein C Activators as Diagnostic Agents for Defects of Protein C System","volume":"25","author":"Asmat","year":"2018","journal-title":"Protein Pept. Lett."},{"key":"ref_151","first-page":"266","article-title":"Protein C Activators from Snake Venoms and Their Diagnostic Use","volume":"31","author":"Volz","year":"2001","journal-title":"Haemostasis"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1182\/blood.V96.2.585.014k30_585_593","article-title":"The Autolysis Loop of Activated Protein C Interacts with Factor Va and Differentiates between the Arg506 and Arg306 Cleavage Sites","volume":"96","author":"Gale","year":"2000","journal-title":"Blood"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"16355","DOI":"10.1074\/jbc.M708985200","article-title":"Detailed Mechanisms of the Inactivation of Factor VIIIa by Activated Protein C in the Presence of Its Cofactors, Protein S and Factor V","volume":"283","author":"Gale","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/BJ20060302","article-title":"Anticoagulant Proteins from Snake Venoms: Structure, Function and Mechanism","volume":"397","author":"Kini","year":"2006","journal-title":"Biochem. J."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1016\/0049-3848(91)90381-6","article-title":"Comparative Study of Protein C Activators from the Agkistrodon Snake Venoms","volume":"62","author":"Kogan","year":"1991","journal-title":"Thromb. Res."},{"key":"ref_156","first-page":"124","article-title":"The Kinin System\u2014Bradykinin: Biological Effects and Clinical Implications. Multiple Role of the Kinin System\u2014Bradykinin","volume":"11","author":"Golias","year":"2007","journal-title":"Hippokratia"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/sj.bjp.0705669","article-title":"The Role of Bradykinin, AT2 and Angiotensin 1-7 Receptors in the EDRF-Dependent Vasodilator Effect of Angiotensin II on the Isolated Mesenteric Vascular Bed of the Rat","volume":"141","author":"Resende","year":"2004","journal-title":"Br. J. Pharmacol."},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"P\u00e9terfi, O., Boda, F., Szab\u00f3, Z., Ferencz, E., and B\u00e1ba, L. (2019). Hypotensive Snake Venom Components-A Mini-Review. Molecules, 24.","DOI":"10.3390\/molecules24152778"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.peptides.2018.01.015","article-title":"LmrBPP9: A Synthetic Bradykinin-Potentiating Peptide from Lachesis muta rhombeata Venom That Inhibits the Angiotensin-Converting Enzyme Activity in Vitro and Reduces the Blood Pressure of Hypertensive Rats","volume":"102","author":"Bendhack","year":"2018","journal-title":"Peptides"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"3114","DOI":"10.1182\/blood.V78.12.3114.3114","article-title":"Basic and Clinical Aspects of Fibrinolysis and Thrombolysis","volume":"78","author":"Collen","year":"1991","journal-title":"Blood"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1096\/fasebj.9.10.7615162","article-title":"Gene Targeting and Gene Transfer Studies of the Plasminogen\/Plasmin System: Implications in Thrombosis, Hemostasis, Neointima Formation, and Atherosclerosis","volume":"9","author":"Carmeliet","year":"1995","journal-title":"FASEB J."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1055\/s-0037-1615920","article-title":"Matrix Metalloproteinase System Deficiencies and Matrix Degradation","volume":"82","author":"Lijnen","year":"1999","journal-title":"Thromb. Haemost."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1055\/s-0037-1616232","article-title":"Extracellular Proteolysis and Angiogenesis","volume":"86","author":"Pepper","year":"2001","journal-title":"Thromb. Haemost."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1161\/ATVBAHA.107.140046","article-title":"Vascular Functions of the Plasminogen Activation System","volume":"27","author":"Fay","year":"2007","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"2840","DOI":"10.1007\/s00018-004-4230-9","article-title":"Regulation and Interactions in the Activation of Cell-Associated Plasminogen","volume":"61","author":"Vaheri","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1111\/j.1365-2141.2005.05444.x","article-title":"Molecular Mechanisms of Fibrinolysis","volume":"129","author":"Hajjar","year":"2005","journal-title":"Br. J. Haematol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S0268-9499(99)90079-6","article-title":"Plasminogen and Cell Migration in Vivo","volume":"13","author":"Plow","year":"1999","journal-title":"Fibrinolysis Proteolysis"},{"key":"ref_168","first-page":"1754","article-title":"Plasminogen Receptors: The Sine qua Non of Cell Surface Plasminogen Activation","volume":"10","author":"Miles","year":"2005","journal-title":"Front. Biosci."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.tcm.2004.03.002","article-title":"Plasminogen Activator Inhibitor 1, Fibrin, and the Vascular Response to Injury","volume":"14","author":"Fay","year":"2004","journal-title":"Trends Cardiovasc. Med."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.pep.2013.07.009","article-title":"Expression, Purification and Characterization of Recombinant Plasminogen Activator from Gloydius Brevicaudus Venom in Escherichia Coli","volume":"91","author":"Zhang","year":"2013","journal-title":"Protein Expr. Purif."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1016\/j.toxicon.2005.12.009","article-title":"Interaction of a Plasminogen Activator Proteinase, LV-PA with Human Alpha2-Macroglobulin","volume":"47","author":"Hermogenes","year":"2006","journal-title":"Toxicon"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.toxicon.2011.01.006","article-title":"Haemostatically Active Proteins in Snake Venoms","volume":"57","author":"Sajevic","year":"2011","journal-title":"Toxicon"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.tracli.2012.02.004","article-title":"Platelets and Cytokines: How and Why?","volume":"19","author":"Garraud","year":"2012","journal-title":"Transfus. Clin. Biol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"781857","DOI":"10.1155\/2014\/781857","article-title":"Overview of Platelet Physiology: Its Hemostatic and Nonhemostatic Role in Disease Pathogenesis","volume":"2014","author":"Ghoshal","year":"2014","journal-title":"Sci. World J."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1160\/TH15-02-0179","article-title":"Antiplatelet Drugs in Patients with Enhanced Platelet Turnover: Biomarkers versus Platelet Function Testing","volume":"114","author":"Freynhofer","year":"2015","journal-title":"Thromb. Haemost."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1160\/TH14-12-1067","article-title":"The Role of Platelets in Inflammation","volume":"114","author":"Thomas","year":"2015","journal-title":"Thromb. Haemost."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Yun, S.-H., Sim, E.-H., Goh, R.-Y., Park, J.-I., and Han, J.-Y. (2016). Platelet Activation: The Mechanisms and Potential Biomarkers. Biomed. Res. Int., 2016.","DOI":"10.1155\/2016\/9060143"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1160\/TH09-03-0192","article-title":"Mechanisms of Platelet Activation: Need for New Strategies to Protect against Platelet-Mediated Atherothrombosis","volume":"102","author":"Jennings","year":"2009","journal-title":"Thromb. Haemost."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1152\/physiol.00020.2016","article-title":"New Concepts and Mechanisms of Platelet Activation Signaling","volume":"32","author":"Estevez","year":"2017","journal-title":"Physiology"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.thromres.2011.11.036","article-title":"Platelets and Primary Haemostasis","volume":"129","author":"Clemetson","year":"2012","journal-title":"Thromb. Res."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1111\/jth.12235","article-title":"Platelet Receptors Activated via Mulitmerization: Glycoprotein VI, GPIb-IX-V, and CLEC-2","volume":"11","author":"Ozaki","year":"2013","journal-title":"J. Thromb. Haemost."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1764","DOI":"10.1111\/jth.12730","article-title":"Platelets in Inflammation and Immunity","volume":"12","author":"Herter","year":"2014","journal-title":"J. Thromb. Haemost."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s10930-006-9001-z","article-title":"Characterization of a New Platelet Aggregating Factor from Crotoxin Crotalus durissus cascavella Venom","volume":"25","author":"Fonseca","year":"2006","journal-title":"Protein J."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/s00109-010-0691-5","article-title":"Platelet Receptor Signaling in Thrombus Formation","volume":"89","author":"Stegner","year":"2011","journal-title":"J. Mol. Med."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1055\/s-0038-1642776","article-title":"Comparison of the Platelet Aggregation Induced by Three Thrombin-like Enzymes of Snake Venoms and Thrombin","volume":"59","author":"Teng","year":"1988","journal-title":"Thromb. Haemost."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"10609","DOI":"10.1021\/bi034790b","article-title":"Molecular Cloning and Expression of a Functional Snake Venom Serine Proteinase, with Platelet Aggregating Activity, from the Cerastes cerastes Viper","volume":"42","author":"Dekhil","year":"2003","journal-title":"Biochemistry"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"6165","DOI":"10.1021\/bi00393a033","article-title":"Nucleotide Sequence of the Gene for Human Prothrombin","volume":"26","author":"Degen","year":"1987","journal-title":"Biochemistry"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/S0969-2126(98)00119-1","article-title":"The Crystal Structure of the Novel Snake Venom Plasminogen Activator TSV-PA: A Prototype Structure for Snake Venom Serine Proteinases","volume":"6","author":"Parry","year":"1998","journal-title":"Structure"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"3036","DOI":"10.1093\/emboj\/20.12.3036","article-title":"Molecular Markers of Serine Protease Evolution","volume":"20","author":"Krem","year":"2001","journal-title":"EMBO J."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"10524","DOI":"10.1074\/jbc.M412900200","article-title":"Crystal Structures and Amidolytic Activities of Two Glycosylated Snake Venom Serine Proteinases","volume":"280","author":"Zhu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1007\/s00204-012-0957-5","article-title":"Crystal Structure and Activating Effect on RyRs of AhV_TL-I, a Glycosylated Thrombin-like Enzyme from Agkistrodon halys Snake Venom","volume":"87","author":"Zeng","year":"2013","journal-title":"Arch. Toxicol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1002\/pro.2189","article-title":"Crystal Structure of Jararacussin-I: The Highly Negatively Charged Catalytic Interface Contributes to Macromolecular Selectivity in Snake Venom Thrombin-like Enzymes","volume":"22","author":"Ullah","year":"2013","journal-title":"Protein Sci."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1098\/rstb.1970.0010","article-title":"Homologies in Serine Proteinases","volume":"257","author":"Hartley","year":"1970","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1016\/0006-291X(68)90326-4","article-title":"On the Active Site of Proteases. 3. Mapping the Active Site of Papain; Specific Peptide Inhibitors of Papain","volume":"32","author":"Schechter","year":"1968","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.toxicon.2008.05.013","article-title":"A Unique Group of Inactive Serine Protease Homologues from Snake Venom","volume":"52","author":"Wu","year":"2008","journal-title":"Toxicon"},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Vaiyapuri, S., Wagstaff, S.C., Harrison, R.A., Gibbins, J.M., and Hutchinson, E.G. (2011). Evolutionary Analysis of Novel Serine Proteases in the Venom Gland Transcriptome of Bitis gabonica rhinoceros. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021532"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.toxicon.2013.11.007","article-title":"VaSP1, Catalytically Active Serine Proteinase from Vipera Ammodytes Ammodytes Venom with Unconventional Active Site Triad","volume":"77","author":"Brgles","year":"2014","journal-title":"Toxicon"},{"key":"ref_198","first-page":"310","article-title":"Prediction of Glycosylation across the Human Proteome and the Correlation to Protein Function","volume":"7","author":"Gupta","year":"2002","journal-title":"Pac. Symp. Biocomput."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1093\/oxfordjournals.jbchem.a123867","article-title":"Novel Structure of the N-Acetylgalactosamine Containing N-Glycosidic Carbohydrate Chain of Batroxobin, a Thrombin-like Snake Venom Enzyme","volume":"112","author":"Tanaka","year":"1992","journal-title":"J. Biochem."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbapap.2003.08.001","article-title":"The Unusual High Molecular Mass of Bothrops Protease A, a Trypsin-like Serine Peptidase from the Venom of Bothrops jararaca, Is Due to Its High Carbohydrate Content","volume":"1652","author":"Murayama","year":"2003","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1007\/BF00702206","article-title":"Glycosylation of the Thrombin-like Serine Protease Ancrod from Agkistrodon rhodostoma Venom. Oligosaccharide Substitution Pattern at Each N-Glycosylation Site","volume":"10","author":"Pfeiffer","year":"1993","journal-title":"Glycoconj. J."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1055\/s-0037-1614965","article-title":"Thrombin-like Enzymes from Snake Venoms: An Updated Inventory. Scientific and Standardization Committee\u2019s Registry of Exogenous Hemostatic Factors","volume":"79","author":"Pirkle","year":"1998","journal-title":"Thromb. Haemost."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1111\/j.1432-1033.1995.tb20326.x","article-title":"Carbohydrate Structure Analysis of Batroxobin, a Thrombin-like Serine Protease from Bothrops moojeni Venom","volume":"228","author":"Lochnit","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1111\/j.1432-1033.1992.tb16863.x","article-title":"Carbohydrate Structure of a Thrombin-like Serine Protease from Agkistrodon rhodostoma. Structure Elucidation of Oligosaccharides by Methylation Analysis, Liquid Secondary-Ion Mass Spectrometry and Proton Magnetic Resonance","volume":"205","author":"Pfeiffer","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1101\/gr.3228405","article-title":"From Genome to \u201cVenome\u201d: Molecular Origin and Evolution of the Snake Venom Proteome Inferred from Phylogenetic Analysis of Toxin Sequences and Related Body Proteins","volume":"15","author":"Fry","year":"2005","journal-title":"Genome Res."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M700094-MCP200","article-title":"Evolution of an Arsenal: Structural and Functional Diversification of the Venom System in the Advanced Snakes (Caenophidia)","volume":"7","author":"Fry","year":"2008","journal-title":"Mol. Cell. Proteom."},{"key":"ref_207","doi-asserted-by":"crossref","unstructured":"Koumandou, V.L., and Scorilas, A. (2013). Evolution of the Plasma and Tissue Kallikreins, and Their Alternative Splicing Isoforms. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0068074"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/0003-9969(87)90123-3","article-title":"Temporal Variations of Glandular Kallikrein, Protein and Amylase in Mixed Human Saliva","volume":"32","author":"Jenzano","year":"1987","journal-title":"Arch. Oral Biol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1113\/expphysiol.1987.sp003081","article-title":"Factors Affecting the Secretion of Submandibular Salivary Kallikrein in Cats","volume":"72","author":"Garrett","year":"1987","journal-title":"Q. J. Exp. Physiol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1016\/j.toxicon.2012.02.012","article-title":"Venomous Mammals: A Review","volume":"59","author":"Verli","year":"2012","journal-title":"Toxicon"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"e2021311118","DOI":"10.1073\/pnas.2021311118","article-title":"An Ancient, Conserved Gene Regulatory Network Led to the Rise of Oral Venom Systems","volume":"118","author":"Barua","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"Barua, A., Koludarov, I., and Mikheyev, A.S. (2021). Co-Option of the Same Ancestral Gene Family Gave Rise to Mammalian and Reptilian Toxins. BMC Biol., 19.","DOI":"10.1186\/s12915-021-01191-1"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"2369","DOI":"10.1074\/mcp.M110.001370","article-title":"Functional and Structural Diversification of the Anguimorpha Lizard Venom System","volume":"9","author":"Fry","year":"2010","journal-title":"Mol. Cell Proteom."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1038\/ncomms2065","article-title":"Dynamic Evolution of Venom Proteins in Squamate Reptiles","volume":"3","author":"Casewell","year":"2012","journal-title":"Nat. Commun."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1093\/molbev\/msu337","article-title":"Venom-Related Transcripts from Bothrops jararaca Tissues Provide Novel Molecular Insights into the Production and Evolution of Snake Venom","volume":"32","author":"Bastos","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.toxicon.2014.10.004","article-title":"Testing the Toxicofera: Comparative Transcriptomics Casts Doubt on the Single, Early Evolution of the Reptile Venom System","volume":"92","author":"Hargreaves","year":"2014","journal-title":"Toxicon"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1093\/molbev\/msu294","article-title":"Expression of Venom Gene Homologs in Diverse Python Tissues Suggests a New Model for the Evolution of Snake Venom","volume":"32","author":"Card","year":"2015","journal-title":"Mol. Biol. Evol."},{"key":"ref_218","doi-asserted-by":"crossref","unstructured":"Koludarov, I., Jackson, T.N., Brouw, B.O.d., Dobson, J., Dashevsky, D., Arbuckle, K., Clemente, C.J., Stockdale, E.J., Cochran, C., and Debono, J. (2017). Enter the Dragon: The Dynamic and Multifunctional Evolution of Anguimorpha Lizard Venoms. Toxins, 9.","DOI":"10.3390\/toxins9080242"},{"key":"ref_219","doi-asserted-by":"crossref","unstructured":"Barua, A., and Mikheyev, A.S. (2020). Toxin Expression in Snake Venom Evolves Rapidly with Constant Shifts in Evolutionary Rates. Proc. Biol. Sci., 287.","DOI":"10.1098\/rspb.2020.0613"},{"key":"ref_220","doi-asserted-by":"crossref","unstructured":"Xie, B., Dashevsky, D., Rokyta, D., Ghezellou, P., Fathinia, B., Shi, Q., Richardson, M.K., and Fry, B.G. (2022). Dynamic Genetic Differentiation Drives the Widespread Structural and Functional Convergent Evolution of Snake Venom Proteinaceous Toxins. BMC Biol., 20.","DOI":"10.1186\/s12915-021-01208-9"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"763","DOI":"10.6026\/97320630008563","article-title":"Sequence and Phylogenetic Analysis of Viper Venom Serine Proteases","volume":"8","author":"Vaiyapuri","year":"2012","journal-title":"Bioinformation"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0014-5793(96)01144-1","article-title":"Accelerated Evolution of Crotalinae Snake Venom Gland Serine Proteases","volume":"397","author":"Deshimaru","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_223","doi-asserted-by":"crossref","unstructured":"Doley, R., Mackessy, S.P., and Kini, R.M. (2009). Role of Accelerated Segment Switch in Exons to Alter Targeting (ASSET) in the Molecular Evolution of Snake Venom Proteins. BMC Evol. Biol., 9.","DOI":"10.1186\/1471-2148-9-146"},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"9366","DOI":"10.1016\/S0021-9258(17)39373-0","article-title":"Purification and Properties of a Prothrombin Activator from the Venom of Notechis Scutatus Scutatus","volume":"260","author":"Tans","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1160\/TH04-07-0435","article-title":"Two Parallel Prothrombin Activator Systems in Australian Rough-Scaled Snake, Tropidechis Carinatus. Structural Comparison of Venom Prothrombin Activator with Blood Coagulation Factor X","volume":"93","author":"Reza","year":"2005","journal-title":"Thromb. Haemost."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1538-7836.2006.02266.x","article-title":"Structure of Two Genes Encoding Parallel Prothrombin Activators in Tropidechis Carinatus Snake: Gene Duplication and Recruitment of Factor X Gene to the Venom Gland","volume":"5","author":"Reza","year":"2007","journal-title":"J. Thromb. Haemost."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1160\/TH09-03-0162","article-title":"The Recruitment of Blood Coagulation Factor X into Snake Venom Gland as a Toxin: The Role of Promoter Cis-Elements in Its Expression","volume":"102","author":"Kwong","year":"2009","journal-title":"Thromb. Haemost."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.1111\/j.1538-7836.2006.01969.x","article-title":"Molecular Evolution Caught in Action: Gene Duplication and Evolution of Molecular Isoforms of Prothrombin Activators in Pseudonaja textilis (Brown Snake)","volume":"4","author":"Reza","year":"2006","journal-title":"J. Thromb. Haemost."},{"key":"ref_229","doi-asserted-by":"crossref","unstructured":"Lan, D., Song, S., Liu, Y., Jiao, B., and Meng, R. (2021). Use of Batroxobin in Central and Peripheral Ischemic Vascular Diseases: A Systematic Review. Front. Neurol., 12.","DOI":"10.3389\/fneur.2021.716778"},{"key":"ref_230","doi-asserted-by":"crossref","unstructured":"Song, S., Wu, H., Ji, X., and Meng, R. (2022). The BE COOL Treatments (Batroxobin, oxygEn, Conditioning, and cOOLing): Emerging Adjunct Therapies for Ischemic Cerebrovascular Disease. J. Clin. Med., 11.","DOI":"10.3390\/jcm11206193"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1111\/j.1423-0410.2007.01027.x","article-title":"Platelet-Rich Plasma and Platelet Gel Preparation Using Plateltex","volume":"94","author":"Mazzucco","year":"2008","journal-title":"Vox Sang."},{"key":"ref_232","unstructured":"(2024, July 07). Plateltex\u00ae Device for the Activation (Gelification) of Blood Components Destined to the Topical Non-Transfusional Use. Available online: www.plateltex.com\/data\/pdf\/IFU4.3plateltexACTJUNE2016ENG.pdf."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/S0003-4975(98)00470-6","article-title":"Vivostat System Autologous Fibrin Sealant: Preliminary Study in Elective Coronary Bypass Grafting","volume":"66","author":"Kjaergard","year":"1998","journal-title":"Ann. Thorac. Surg."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s40409-017-0109-8","article-title":"Heterologous Fibrin Sealant Derived from Snake Venom: From Bench to Bedside\u2014An Overview","volume":"23","author":"Ferreira","year":"2017","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1161\/STROKEAHA.109.565119","article-title":"Ancrod in Acute Ischemic Stroke: Results of 500 Subjects Beginning Treatment within 6 Hours of Stroke Onset in the Ancrod Stroke Program","volume":"40","author":"Levy","year":"2009","journal-title":"Stroke"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"589","DOI":"10.3760\/cma.j.issn.0366-6999.2010.05.016","article-title":"A Multicenter, Phase III Trial of Hemocoagulase Agkistrodon: Hemostasis, Coagulation, and Safety in Patients Undergoing Abdominal Surgery","volume":"123","author":"Wei","year":"2010","journal-title":"Chin. Med. J."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1002\/ajh.25852","article-title":"Ecarin Based Coagulation Testing","volume":"95","author":"Gosselin","year":"2020","journal-title":"Am. J. Hematol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0049-3848(99)00090-0","article-title":"The Factor V (Leiden) Test: Evaluation of an Assay Based on Dilute Russell Viper Venom Time for the Detection of the Factor V Leiden Mutation","volume":"96","author":"Quehenberger","year":"1999","journal-title":"Thromb. Res."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/978-1-4939-7196-1_14","article-title":"Lupus Anticoagulant Testing: Diluted Russell Viper Venom Time (dRVVT)","volume":"1646","author":"Pengo","year":"2017","journal-title":"Methods Mol. Biol."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1111\/j.1365-2141.1971.tb03415.x","article-title":"Reptilase-R\u2014A New Reagent in Blood Coagulation","volume":"21","author":"Funk","year":"1971","journal-title":"Br. J. Haematol."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1080\/10937400903442514","article-title":"A New Fibrin Sealant from Crotalus durissus terrificus Venom: Applications in Medicine","volume":"12","author":"Barros","year":"2009","journal-title":"J. Toxicol. Environ. Health B Crit. Rev."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.toxicon.2021.12.005","article-title":"Revisiting the Potential of South American Rattlesnake Crotalus durissus terrificus Toxins as Therapeutic, Theranostic and\/or Biotechnological Agents","volume":"206","author":"Hayashi","year":"2022","journal-title":"Toxicon"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.2147\/DDDT.S159210","article-title":"Effects of Hemocoagulase Agkistrodon on the Coagulation Factors and Its Procoagulant Activities","volume":"12","author":"Li","year":"2018","journal-title":"Drug Des. Devel Ther."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"e18534","DOI":"10.1097\/MD.0000000000018534","article-title":"Hemocoagulase Reduces Postoperative Bleeding and Blood Transfusion in Cardiac Surgical Patients: A PRISMA-Compliant Systematic Review and Meta-Analysis","volume":"98","author":"Yao","year":"2019","journal-title":"Medicine"},{"key":"ref_245","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_246","doi-asserted-by":"crossref","unstructured":"Bordon, K.d.C.F., Cologna, C.T., Fornari-Baldo, E.C., Pinheiro-J\u00fanior, E.L., Cerni, F.A., Amorim, F.G., Anjolette, F.A.P., Cordeiro, F.A., Wiezel, G.A., and Cardoso, I.A. (2020). From Animal Poisons and Venoms to Medicines: Achievements, Challenges and Perspectives in Drug Discovery. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.01132"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1111\/j.1399-3011.1997.tb01207.x","article-title":"Structure and Other Chemical Characterizations of Gila Toxin, a Lethal Toxin from Lizard Venom","volume":"50","author":"Datta","year":"1997","journal-title":"J. Pept. Res."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.taap.2018.08.018","article-title":"BjSP, a Novel Serine Protease from Bothrops jararaca Snake Venom That Degrades Fibrinogen without Forming Fibrin Clots","volume":"357","author":"Carone","year":"2018","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"20531","DOI":"10.1074\/jbc.272.33.20531","article-title":"Trimeresurus Stejnegeri Snake Venom Plasminogen Activator. Site-Directed Mutagenesis and Molecular Modeling","volume":"272","author":"Zhang","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1016\/j.toxicon.2007.01.015","article-title":"Expression and Characterization of a Recombinant Fibrinogenolytic Serine Protease from Green Pit Viper (Trimeresurus albolabris) Venom","volume":"49","author":"Muanpasitporn","year":"2007","journal-title":"Toxicon"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.febslet.2004.06.060","article-title":"Functional Characterization of Recombinant Batroxobin, a Snake Venom Thrombin-like Enzyme, Expressed from Pichia pastoris","volume":"571","author":"You","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.toxicon.2016.03.002","article-title":"Expression and Partial Biochemical Characterization of a Recombinant Serine Protease from Bothrops pauloensis Snake Venom","volume":"115","author":"Isabel","year":"2016","journal-title":"Toxicon"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"9971","DOI":"10.1007\/s00253-015-6836-2","article-title":"Expression of a New Serine Protease from Crotalus durissus collilineatus Venom in Pichia pastoris and Functional Comparison with the Native Enzyme","volume":"99","author":"Gomes","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"e147118","DOI":"10.1590\/1678-9199-jvatitd-1471-18","article-title":"Functional and Biological Insights of rCollinein-1, a Recombinant Serine Protease from Crotalus durissus collilineatus","volume":"25","author":"Arantes","year":"2019","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.pep.2009.03.003","article-title":"Expression, Purification and Characterization of Gloydius shedaoensis Venom Gloshedobin as Hsp70 Fusion Protein in Pichia pastoris","volume":"66","author":"Yang","year":"2009","journal-title":"Protein Expr. Purif."},{"key":"ref_256","doi-asserted-by":"crossref","unstructured":"Alomran, N., Blundell, P., Alsolaiss, J., Crittenden, E., Ainsworth, S., Dawson, C.A., Edge, R.J., Hall, S.R., Harrison, R.A., and Wilkinson, M.C. (2022). Exploring the Utility of Recombinant Snake Venom Serine Protease Toxins as Immunogens for Generating Experimental Snakebite Antivenoms. Toxins, 14.","DOI":"10.1101\/2022.05.07.491032"},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1016\/j.toxicon.2008.08.012","article-title":"A Novel Serine Protease from the Snake Venom of Agkistrodon Blomhoffii ussurensis","volume":"52","author":"Liu","year":"2008","journal-title":"Toxicon"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0003-9861(88)90594-2","article-title":"Isolation and Characterization of Horridum Toxin with Arginine Ester Hydrolase Activity from Heloderma horridum (Beaded Lizard) Venom","volume":"264","author":"Nikai","year":"1988","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0041-0101(87)90253-4","article-title":"Characterization of the Protein C Activator Protac from the Venom of the Southern Copperhead (Agkistrodon contortrix) Snake","volume":"25","author":"Stocker","year":"1987","journal-title":"Toxicon"},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1107\/S1744309109046697","article-title":"Crystallization and Preliminary X-Ray Crystallographic Analysis of Blood Coagulation Factor V-Activating Proteinase (RVV-V) from Russell\u2019s Viper Venom","volume":"65","author":"Nakayama","year":"2009","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.biochi.2010.10.004","article-title":"A New Tyrosine-Specific Chymotrypsin-like and Angiotensin-Degrading Serine Proteinase from Vipera lebetina Snake Venom","volume":"93","author":"Siigur","year":"2011","journal-title":"Biochimie"},{"key":"ref_262","doi-asserted-by":"crossref","unstructured":"Rivera-de-Torre, E., Rimbault, C., Jenkins, T.P., S\u00f8rensen, C.V., Damsbo, A., Saez, N.J., Duhoo, Y., Hackney, C.M., Ellgaard, L., and Laustsen, A.H. (2021). Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins. Front. Bioeng. Biotechnol., 9.","DOI":"10.3389\/fbioe.2021.811905"},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1006\/bbrc.2000.3411","article-title":"Expression of a Kallikrein-like Protease from the Snake Venom: Engineering of Autocatalytic Site in the Fusion Protein to Facilitate Protein Refolding","volume":"275","author":"Hung","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.toxicon.2009.03.022","article-title":"Cloning of Serine Protease cDNAs from Crotalus durissus terrificus Venom Gland and Expression of a Functional Gyroxin Homologue in COS-7 Cells","volume":"54","author":"Yonamine","year":"2009","journal-title":"Toxicon"},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"Sahyoun, C., Rima, M., Mattei, C., Sabatier, J.M., Fajloun, Z., and Legros, C. (2022). Separation and Analytical Techniques Used in Snake Venomics: A Review Article. Processes, 10.","DOI":"10.3390\/pr10071380"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.toxicon.2018.01.005","article-title":"Citrus Bioflavonoid, Hesperetin, as Inhibitor of Two Thrombin-like Snake Venom Serine Proteases Isolated from Crotalus simus","volume":"143","author":"Stanisic","year":"2018","journal-title":"Toxicon"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/10\/428\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:09:38Z","timestamp":1760112578000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/10\/428"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10,3]]},"references-count":266,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2024,10]]}},"alternative-id":["toxins16100428"],"URL":"https:\/\/doi.org\/10.3390\/toxins16100428","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,10,3]]}}}