{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T18:07:06Z","timestamp":1791914826150,"version":"4.3.4"},"reference-count":51,"publisher":"Elsevier BV","issue":"23","license":[{"start":{"date-parts":[[2013,6,1]],"date-time":"2013-06-01T00:00:00Z","timestamp":1370044800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,11]],"date-time":"2020-09-11T00:00:00Z","timestamp":1599782400000},"content-version":"vor","delay-in-days":2659,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,6]]},"DOI":"10.1074\/jbc.m113.464750","type":"journal-article","created":{"date-parts":[[2013,4,24]],"date-time":"2013-04-24T03:55:41Z","timestamp":1366775741000},"page":"16862-16871","source":"Crossref","is-referenced-by-count":56,"title":["Batroxobin Binds Fibrin with Higher Affinity and Promotes Clot Expansion to a Greater Extent than Thrombin"],"prefix":"10.1016","volume":"288","author":[{"given":"Trang T.","family":"Vu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan R.","family":"Stafford","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beverly A.","family":"Leslie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul Y.","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James C.","family":"Fredenburgh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey I.","family":"Weitz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.464750_bib1","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1097\/MOH.0b013e32835673c2","article-title":"Determinants of fibrin formation, structure, and function","volume":"19","author":"Wolberg","year":"2012","journal-title":"Curr. Opin. Hematol"},{"key":"10.1074\/jbc.M113.464750_bib2","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1111\/j.1538-7836.2005.01365.x","article-title":"Fibrinogen and fibrin structure and functions","volume":"3","author":"Mosesson","year":"2005","journal-title":"J. Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib3","doi-asserted-by":"crossref","first-page":"5069","DOI":"10.1073\/pnas.77.9.5069","article-title":"Human plasma fibrinogen heterogeneity: evidence for an extended carboxyl-terminal sequence in a normal \u03b3 chain variant (\u03b3\u2032)","volume":"77","author":"Wolfenstein-Todel","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.464750_bib4","doi-asserted-by":"crossref","first-page":"4232","DOI":"10.1021\/bi00313a033","article-title":"\u03b3 and \u03b3\u2032 chains of human fibrinogen are produced by alternative mRNA processing","volume":"23","author":"Chung","year":"1984","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.464750_bib5","doi-asserted-by":"crossref","first-page":"12826","DOI":"10.1016\/S0021-9258(18)90821-5","article-title":"Structure of the human \u03b3-fibrinogen gene. Alternate mRNA splicing near the 3\u2032 end of the gene produces \u03b3A and \u03b3B forms of \u03b3-fibrinogen","volume":"259","author":"Fornace","year":"1984","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib6","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1373\/clinchem.2009.138347","article-title":"\u03b3\u2032 fibrinogen: evaluation of a new assay for study of associations with cardiovascular disease","volume":"56","author":"Lovely","year":"2010","journal-title":"Clin. Chem"},{"key":"10.1074\/jbc.M113.464750_bib7","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1160\/TH10-09-0569","article-title":"\u03b3\u2032\/total fibrinogen ratio is associated with short-term outcome in ischaemic stroke","volume":"105","author":"van den Herik","year":"2011","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib8","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/275501a0","article-title":"A two-step fibrinogen-fibrin transition in blood coagulation","volume":"275","author":"Blomb\u00e4ck","year":"1978","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.464750_bib9","doi-asserted-by":"crossref","first-page":"25239","DOI":"10.1074\/jbc.M004142200","article-title":"Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release","volume":"275","author":"Mullin","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib10","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1172\/JCI114723","article-title":"Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors","volume":"86","author":"Weitz","year":"1990","journal-title":"J. Clin. Invest"},{"key":"10.1074\/jbc.M113.464750_bib11","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1111\/j.1538-7836.2005.01363.x","article-title":"Molecular recognition mechanisms of thrombin","volume":"3","author":"Huntington","year":"2005","journal-title":"J. Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib12","doi-asserted-by":"crossref","first-page":"1738","DOI":"10.1161\/01.ATV.0000228844.65168.d1","article-title":"Thrombin-cofactor interactions: structural insights into regulatory mechanisms","volume":"26","author":"Adams","year":"2006","journal-title":"Arterioscler. Thromb. Vasc. Biol"},{"key":"10.1074\/jbc.M113.464750_bib13","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.bpc.2004.07.031","article-title":"Modes and consequences of thrombin's interaction with fibrin","volume":"112","author":"Fredenburgh","year":"2004","journal-title":"Biophys. Chem"},{"key":"10.1074\/jbc.M113.464750_bib14","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1160\/TH07-04-0274","article-title":"Update on antithrombin I (fibrin)","volume":"98","author":"Mosesson","year":"2007","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib15","doi-asserted-by":"crossref","first-page":"23121","DOI":"10.1074\/jbc.271.38.23121","article-title":"Identification and characterization of the thrombin-binding sites on fibrin","volume":"271","author":"Meh","year":"1996","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib16","doi-asserted-by":"crossref","first-page":"21584","DOI":"10.1074\/jbc.M300545200","article-title":"Evidence that both exosites on thrombin participate in its high affinity interaction with fibrin","volume":"278","author":"Pospisil","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib17","doi-asserted-by":"crossref","first-page":"6226","DOI":"10.1074\/jbc.274.10.6226","article-title":"Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II","volume":"274","author":"Becker","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib18","doi-asserted-by":"crossref","first-page":"2470","DOI":"10.1074\/jbc.M707710200","article-title":"Bivalent binding to \u03b3A\/\u03b3\u2032-fibrin engages both exosites of thrombin and protects it from inhibition by the antithrombin-heparin complex","volume":"283","author":"Fredenburgh","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib19","first-page":"89","article-title":"DNA evolution of South American pitvipers of the genus Bothrops (Reptilia:Serpentes:Viperidae)","volume":"70","author":"Da Graca Salomao","year":"1997","journal-title":"Symp. Zool. Soc. Lond"},{"key":"10.1074\/jbc.M113.464750_bib20","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1055\/s-0038-1648004","article-title":"Comparison of the actions of thrombin and the thrombin-like venom enzymes ancrod and batroxobin","volume":"36","author":"Aronson","year":"1976","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib21","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":"10.1074\/jbc.M113.464750_bib22","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1055\/s-0038-1665266","article-title":"Retrospective study on complications and adverse effects of treatment with thrombin-like enzymes\u2013a multicentre trial","volume":"50","author":"Latallo","year":"1983","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib23","series-title":"Hemostasis and Animal Venoms","first-page":"525","author":"Stocker","year":"1998"},{"key":"10.1074\/jbc.M113.464750_bib24","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1097\/MBC.0b013e328040c0f2","article-title":"Feasibility of treating hyperfibrinogenemia with intermittently administered batroxobin in patients with ischemic stroke\/transient ischemic attack for secondary prevention","volume":"18","author":"Xu","year":"2007","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"10.1074\/jbc.M113.464750_bib25","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1016\/j.avsg.2010.03.030","article-title":"Batroxobin for prevention of restenosis in diabetic patients after infrapopliteal arterial angioplasty: a small randomized pilot trial","volume":"24","author":"Wang","year":"2010","journal-title":"Ann. Vasc. Surg"},{"key":"10.1074\/jbc.M113.464750_bib26","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.toxicon.2005.02.030","article-title":"Snake venoms and coagulopathy","volume":"45","author":"White","year":"2005","journal-title":"Toxicon"},{"key":"10.1074\/jbc.M113.464750_bib27","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1055\/s-0030-1254053","article-title":"Snakebite doesn't cause disseminated intravascular coagulation: coagulopathy and thrombotic microangiopathy in snake envenoming","volume":"36","author":"Isbister","year":"2010","journal-title":"Semin. Thromb. Hemost"},{"key":"10.1074\/jbc.M113.464750_bib28","doi-asserted-by":"crossref","first-page":"4257","DOI":"10.1021\/bi0525730","article-title":"Incorporation of fragment X into fibrin clots renders them more susceptible to lysis by plasmin","volume":"45","author":"Schaefer","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.464750_bib29","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1097\/01.SMJ.0000054567.79881.E9","article-title":"Effect of stress on pregnancy outcome among women undergoing assisted reproduction procedures","volume":"96","author":"Lovely","year":"2003","journal-title":"South. Med. J"},{"key":"10.1074\/jbc.M113.464750_bib30","doi-asserted-by":"crossref","first-page":"30314","DOI":"10.1074\/jbc.M111.253831","article-title":"Histidine-rich glycoprotein binds fibrin(ogen) with high affinity and competes with thrombin for binding to the \u03b3\u2032-chain","volume":"286","author":"Vu","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib31","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1160\/TH09-04-0237","article-title":"HD1, a thrombin- and prothrombin-binding DNA aptamer, inhibits thrombin generation by attenuating prothrombin activation and thrombin feedback reactions","volume":"103","author":"Kretz","year":"2010","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib32","doi-asserted-by":"crossref","first-page":"4925","DOI":"10.1016\/S0021-9258(17)30101-1","article-title":"Binding phenomena of isolated unique plasmic degradation products of human cross-linked fibrin","volume":"254","author":"Olexa","year":"1979","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib33","doi-asserted-by":"crossref","first-page":"25620","DOI":"10.1074\/jbc.M109.000042","article-title":"Long range communication between exosites 1 and 2 modulates thrombin function","volume":"284","author":"Petrera","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib34","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1182\/blood-2002-10-3150","article-title":"Fibrinogen \u03b3-chain splice variant \u03b3\u2032 alters fibrin formation and structure","volume":"102","author":"Cooper","year":"2003","journal-title":"Blood"},{"key":"10.1074\/jbc.M113.464750_bib35","doi-asserted-by":"crossref","first-page":"2466","DOI":"10.1182\/blood-2003-01-0204","article-title":"Recombinant B\u03b2Arg14His fibrinogen implies participation of N terminus of B\u03b2 chain in desA fibrin polymerization","volume":"102","author":"Moen","year":"2003","journal-title":"Blood"},{"key":"10.1074\/jbc.M113.464750_bib36","doi-asserted-by":"crossref","first-page":"4622","DOI":"10.1021\/bi00364a025","article-title":"Kinetics of the inhibition of thrombin by hirudin","volume":"25","author":"Stone","year":"1986","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.464750_bib37","doi-asserted-by":"crossref","first-page":"24790","DOI":"10.1074\/jbc.270.42.24790","article-title":"Binding of fibrinogen A\u03b11\u201350-\u03b2-galactosidase fusion protein to thrombin stabilizes the slow form","volume":"270","author":"Lord","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib38","doi-asserted-by":"crossref","first-page":"3467","DOI":"10.1002\/j.1460-2075.1989.tb08511.x","article-title":"The refined 1.9 \u00c5 crystal structure of human \u03b1-thrombin: interaction with d-Phe-Pro-Arg chloromethyl ketone and significance of the Tyr-Pro-Pro-Trp insertion segment","volume":"8","author":"Bode","year":"1989","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M113.464750_bib39","doi-asserted-by":"crossref","first-page":"11320","DOI":"10.1074\/jbc.M211820200","article-title":"Three-dimensional models of proteases involved in patterning of the Drosophila embryo. Crucial role of predicted cation-binding sites","volume":"278","author":"Rose","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464750_bib40","doi-asserted-by":"crossref","first-page":"2718","DOI":"10.1073\/pnas.0303440101","article-title":"Crystal structure of the complex between thrombin and the central \u201cE\u201d-region of fibrin","volume":"101","author":"Pechik","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.464750_bib41","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1749-6632.2001.tb03502.x","article-title":"Determinants of thrombin specificity","volume":"936","author":"Di Cera","year":"2001","journal-title":"Ann. N.Y. Acad. Sci"},{"key":"10.1074\/jbc.M113.464750_bib42","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":"10.1074\/jbc.M113.464750_bib43","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":"10.1074\/jbc.M113.464750_bib44","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":"Henschen-Edman","year":"1999","journal-title":"Thromb. Haemost"},{"key":"10.1074\/jbc.M113.464750_bib45","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":"10.1074\/jbc.M113.464750_bib46","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1002\/jmr.644","article-title":"Identification of the substrate-binding exosites of two snake venom serine proteinases: molecular basis for the partition of two essential functions of thrombin","volume":"17","author":"Maroun","year":"2004","journal-title":"J. Mol. Recognit"},{"key":"10.1074\/jbc.M113.464750_bib47","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":"10.1074\/jbc.M113.464750_bib48","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1172\/JCI115841","article-title":"Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B\u03b268Ala\u2013Thr","volume":"90","author":"Koopman","year":"1992","journal-title":"J. Clin. Invest"},{"key":"10.1074\/jbc.M113.464750_bib49","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1006\/jmbi.1993.1382","article-title":"The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots","volume":"232","author":"Weisel","year":"1993","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M113.464750_bib50","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1182\/blood-2010-08-300301","article-title":"Fibrinopeptides A and B release in the process of surface fibrin formation","volume":"117","author":"Riedel","year":"2011","journal-title":"Blood"},{"key":"10.1074\/jbc.M113.464750_bib51","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1161\/STROKEAHA.111.622753","article-title":"Ancrod and fibrin formation: perspectives on mechanisms of action","volume":"42","author":"Liu","year":"2011","journal-title":"Stroke"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820536922?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820536922?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.464750","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,5]],"date-time":"2022-01-05T00:32:56Z","timestamp":1641342776000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820536922"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,6]]},"references-count":51,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2013,6]]}},"alternative-id":["S0021925820536922"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.464750","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,6]]}}}