{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T11:02:50Z","timestamp":1782817370306,"version":"3.54.5"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004586","name":"FAPERJ","doi-asserted-by":"publisher","award":["E-26\/010.003016\/2014"],"award-info":[{"award-number":["E-26\/010.003016\/2014"]}],"id":[{"id":"10.13039\/501100004586","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004586","name":"FAPERJ","doi-asserted-by":"publisher","award":["E-26\/200.963\/2021"],"award-info":[{"award-number":["E-26\/200.963\/2021"]}],"id":[{"id":"10.13039\/501100004586","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004586","name":"FAPERJ","doi-asserted-by":"publisher","award":["E-26\/010.101030\/2018"],"award-info":[{"award-number":["E-26\/010.101030\/2018"]}],"id":[{"id":"10.13039\/501100004586","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004586","name":"FAPERJ","doi-asserted-by":"publisher","award":["E-26\/203.059\/2017"],"award-info":[{"award-number":["E-26\/203.059\/2017"]}],"id":[{"id":"10.13039\/501100004586","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"CNPq","doi-asserted-by":"publisher","award":["308376\/2020-0 6"],"award-info":[{"award-number":["308376\/2020-0 6"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"CNPq","doi-asserted-by":"publisher","award":["308179\/2015-3"],"award-info":[{"award-number":["308179\/2015-3"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"CNPq","doi-asserted-by":"publisher","award":["429583\/2016-8"],"award-info":[{"award-number":["429583\/2016-8"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"CNPq","doi-asserted-by":"publisher","award":["426945\/2016-6"],"award-info":[{"award-number":["426945\/2016-6"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","award":["88887.163373\/2018-00"],"award-info":[{"award-number":["88887.163373\/2018-00"]}],"id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2022,10]]},"DOI":"10.1016\/j.toxicon.2022.08.010","type":"journal-article","created":{"date-parts":[[2022,8,15]],"date-time":"2022-08-15T10:19:08Z","timestamp":1660558748000},"page":"87-95","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"special_numbering":"C","title":["The recombinant disintegrin, jarastatin, inhibits platelet adhesion and endothelial cell migration"],"prefix":"10.1016","volume":"217","author":[{"given":"Barbara Barbosa","family":"Succar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta F.G.","family":"Saldanha-Gama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aline Sol","family":"Valle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luciana Serr\u00e3o","family":"Wermelinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina","family":"Barja-Fidalgo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eleonora","family":"Kurtenbach","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3156-6923","authenticated-orcid":false,"given":"Russolina Benedeta","family":"Zingali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2022.08.010_bib1","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbamem.2018.12.020","article-title":"Psd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterol","volume":"1861","author":"Amaral","year":"2019","journal-title":"BBA - Biomembr."},{"key":"10.1016\/j.toxicon.2022.08.010_bib2","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/j.thromres.2004.07.020","article-title":"Platelet physiology and thrombosis","volume":"114","author":"Andrews","year":"2004","journal-title":"Thromb. Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib3","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.toxicon.2013.01.001","article-title":"Identification of \u03b12\u03b21 integrin inhibitor VP-i with anti-platelet properties in the venom of Vipera palaestinae","volume":"64","author":"Arlinghaus","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2022.08.010_bib4","article-title":"Platelet shape and spreading","volume":"vol. 788","author":"Aslan","year":"2012"},{"key":"10.1016\/j.toxicon.2022.08.010_bib5","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ijms18010189","article-title":"Integrins and cell metabolism: an intimate relationship impacting cancer","volume":"18","author":"Ata","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.toxicon.2022.08.010_bib6","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1038\/nrc2353","article-title":"Integrins in angiogenesis and lymphangiogenesis","volume":"8","author":"Avraamides","year":"2008","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.toxicon.2022.08.010_bib7","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1152\/ajpcell.00078.2012","article-title":"Heme modulates intestinal epithelial cell activation: involvement of NADPHox-derived ROS signaling","volume":"304","author":"Barcellos-de-Souza","year":"2013","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib8","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/s00441-009-0834-6","volume":"339","author":"Barczyk","year":"2010","journal-title":"Integrins. Cell Tissue Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib9","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s10295-013-1235-0","article-title":"Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells","volume":"40","author":"Berlec","year":"2013","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib10","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1161\/CIRCRESAHA.112.300570","article-title":"Integrin \u03b1IIb\u03b23: from discovery to efficacious therapeutic target","volume":"112","author":"Bledzka","year":"2013","journal-title":"Circ. Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib11","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S1046-5928(03)00136-0","article-title":"Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease","volume":"31","author":"Cabral","year":"2003","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.toxicon.2022.08.010_bib12","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.toxicon.2012.09.005","article-title":"The continuing saga of snake venom disintegrins","volume":"62","author":"Calvete","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2022.08.010_bib13","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1006\/bbrc.1993.1037","article-title":"Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells","volume":"190","author":"Chang","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2022.08.010_bib14","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/j.toxicon.2006.07.010","article-title":"Molecular diversity of disintegrin-like domains within metalloproteinase precursors of Bothrops jararaca","volume":"48","author":"Cidade","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2022.08.010_bib15","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1006\/excr.1999.4583","article-title":"Effects of jarastatin, a novel snake venom disintegrin, on neutrophil migration and actin cytoskeleton dynamics","volume":"251","author":"Coelho","year":"1999","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib16","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1038\/nrd3266","article-title":"Integrins as therapeutic targets: lessons and opportunities","volume":"9","author":"Cox","year":"2010","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.toxicon.2022.08.010_bib17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/toxins10080321","article-title":"Recombinant and chimeric disintegrins in preclinical Research","volume":"10","author":"David","year":"2018","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2022.08.010_bib18","first-page":"1","article-title":"Snake venoms in drug discovery: valuable therapeutic tools for life saving","volume":"11","author":"El-Aziz","year":"2019","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2022.08.010_bib19","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.bbrc.2005.01.148","article-title":"Molecular cloning, functional expression, and molecular modeling of bothrostatin, a new highly active disintegrin from Bothrops jararaca venom","volume":"329","author":"Fernandez","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2022.08.010_bib20","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.jprot.2015.04.029","article-title":"Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two Bothrops jararaca populations from geographic isolated regions within the Brazilian Atlantic rainforest","volume":"135","author":"Gon\u00e7alves-Machado","year":"2016","journal-title":"J. Proteonomics"},{"key":"10.1016\/j.toxicon.2022.08.010_bib21","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.tips.2012.04.002","article-title":"Integrins as therapeutic targets","volume":"33","author":"Goodman","year":"2012","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.toxicon.2022.08.010_bib22","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1002\/prot.1061","article-title":"Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin","volume":"43","author":"Guo","year":"2001","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/j.toxicon.2022.08.010_bib23","doi-asserted-by":"crossref","first-page":"2464","DOI":"10.1002\/jcp.25358","article-title":"Priming endothelial cells with a melanoma-derived extracellular matrix triggers the activation of \u03b1v\u03b23\/VEGFR2 axis","volume":"231","author":"Helal-Neto","year":"2016","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib24","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0301-4622(88)80007-3","article-title":"Origin of the positive 225-230 nm circular dichroism band in proteins its application to conformational analysis","volume":"31","author":"Hider","year":"1988","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.toxicon.2022.08.010_bib25","article-title":"Processes for preparing eptifbatde","author":"Ho","year":"2010","journal-title":"US 7,674,768 B2"},{"key":"10.1016\/j.toxicon.2022.08.010_bib26","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/S0006-291X(02)00258-9","article-title":"Structural and functional significance of disulfide bonds in saxatilin, a 7.7 kDa disintegrin","volume":"293","author":"Hong","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2022.08.010_bib27","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/S1357-2725(96)00155-0","article-title":"The \u03b1v\u03b23 integrin \u201cvitronectin receptor.\u201d","volume":"29","author":"Horton","year":"1997","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib28","doi-asserted-by":"crossref","first-page":"16157","DOI":"10.1016\/S0021-9258(18)47710-1","article-title":"Trigramin: a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex","volume":"262","author":"Huang","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2022.08.010_bib29","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/0092-8674(92)90115-S","article-title":"Integrins: versatility, modulation and signaling in cell adhesion","volume":"69","author":"Hynes","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.toxicon.2022.08.010_bib30","doi-asserted-by":"crossref","first-page":"295","DOI":"10.4070\/kcj.2012.42.5.295","article-title":"Mechanisms of platelet activation and integrin \u03b1IIb\u03b23","volume":"42","author":"Joo","year":"2012","journal-title":"Korean Circ. J."},{"key":"10.1016\/j.toxicon.2022.08.010_bib31","doi-asserted-by":"crossref","first-page":"6604","DOI":"10.2741\/3176","article-title":"Hemostatic effects of recombinant DisBa-01, a disintegrin from Bothrops alternatus","volume":"13","author":"Kauskot","year":"2008","journal-title":"Front. Biosci."},{"key":"10.1016\/j.toxicon.2022.08.010_bib32","first-page":"1","article-title":"Integrin-based therapeutics: biological basis, clinical use and new drugs","author":"Ley","year":"2016","journal-title":"Nat. Rev. Drug Discov. Perspectiv"},{"key":"10.1016\/j.toxicon.2022.08.010_bib33","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1002\/ddr.20265","article-title":"Integrin \u03b1v\u03b23-targeted cancer therapy","volume":"69","author":"Liu","year":"2008","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib34","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.toxicon.2013.11.005","article-title":"Anti-angiogenic activities of two recombinant disintegrins derived from the Mohave and Prairie rattlesnakes","volume":"78","author":"Lucena","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2022.08.010_bib35","doi-asserted-by":"crossref","first-page":"6617","DOI":"10.2741\/3177","article-title":"Disintegrins in health and disease","volume":"13","author":"McLane","year":"2008","journal-title":"Front. Biosci."},{"key":"10.1016\/j.toxicon.2022.08.010_bib36","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1124\/jpet.114.214643","article-title":"Vimocin and Vidapin, cyclic KTS peptides, are dual antagonists of \u03b11\u03b21\/\u03b12\u03b21 integrins with antiangiogenic activity","volume":"350","author":"Momic","year":"2014","journal-title":"J. Pharmacol. Exp. Therapeut."},{"key":"10.1016\/j.toxicon.2022.08.010_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/cancers9090116","article-title":"Exploring the role of RGD-recognizing integrins in cancer","volume":"9","author":"Nieberler","year":"2017","journal-title":"Cancers"},{"key":"10.1016\/j.toxicon.2022.08.010_bib38","doi-asserted-by":"crossref","first-page":"14248","DOI":"10.1021\/bi025876s","article-title":"A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region","volume":"41","author":"Okuda","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2022.08.010_bib39","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.toxicon.2007.07.016","article-title":"Effect of RGD-disintegrins on melanoma cell growth and metastasis: involvement of the actin cytoskeleton, FAK and c-Fos","volume":"50","author":"Oliva","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2022.08.010_bib40","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.1016\/j.clinthera.2017.11.002","article-title":"Integrins: integrating the biology and therapy of cell\u2013cell interactions","volume":"39","author":"Pandolfi","year":"2017","journal-title":"Clin. Therapeut."},{"key":"10.1016\/j.toxicon.2022.08.010_bib41","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1159\/000437143","article-title":"The EP3 agonist sulprostone enhances platelet adhesion but not thrombus formation under flow conditions","volume":"96","author":"Pasterk","year":"2015","journal-title":"Pharmacology"},{"key":"10.1016\/j.toxicon.2022.08.010_bib42","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1161\/ATVBAHA.110.216374","article-title":"The prostaglandin E2 receptor EP4 is expressed by human platelets and potently inhibits platelet aggregation and thrombus formation","volume":"30","author":"Philipose","year":"2010","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib43","first-page":"11B","article-title":"Clinical pharmacology of eptifibatide","volume":"80","author":"Phillips","year":"1997","journal-title":"Excerpta Med"},{"key":"10.1016\/j.toxicon.2022.08.010_bib44","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1007\/s10585-007-9101-y","article-title":"A novel \u03b1v\u03b23-blocking disintegrin containing the RGD motive, DisBa-01, inhibits bFGF-induced angiogenesis and melanoma metastasis","volume":"25","author":"Ramos","year":"2008","journal-title":"Clin. Exp. Metastasis"},{"key":"10.1016\/j.toxicon.2022.08.010_bib45","doi-asserted-by":"crossref","first-page":"e211","DOI":"10.1016\/j.thromres.2010.06.006","article-title":"Cloning, expression, and hemostatic activities of a disintegrin, r-mojastin 1, from the mohave rattlesnake (Crotalus scutulatus scutulatus)","volume":"126","author":"S\u00e1nchez","year":"2010","journal-title":"Thromb. Res."},{"key":"10.1016\/j.toxicon.2022.08.010_bib46","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1016\/S0021-9258(18)54041-2","article-title":"Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms","volume":"268","author":"Scarborough","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2022.08.010_bib47","doi-asserted-by":"crossref","first-page":"10142","DOI":"10.1073\/pnas.1002257107","article-title":"Ancient origin of the integrin-mediated adhesion and signaling machinery","volume":"107","author":"Seb\u00e9-Pedr\u00f3s","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.toxicon.2022.08.010_bib48","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1006\/abio.2000.4879","article-title":"Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2022.08.010_bib49","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1006\/abio.2000.4880","article-title":"Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2022.08.010_bib50","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.bbapap.2011.04.009","article-title":"Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM\/ADAMTS family proteins","volume":"1824","author":"Takeda","year":"2012","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.toxicon.2022.08.010_bib51","first-page":"1","article-title":"Mutational constraints on local unfolding inhibit the rheological adaptation of von Willebrand factor","author":"Tischer","year":"2015","journal-title":"JBC"},{"key":"10.1016\/j.toxicon.2022.08.010_bib52","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/prot.24464","article-title":"A molten globule intermediate of the von Willebrand factor A1 domain firmly tethers platelets under shear flow","volume":"82","author":"Tischer","year":"2014","journal-title":"Proteins: Struct., Funct., Bioinf."},{"key":"10.1016\/j.toxicon.2022.08.010_bib53","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fmolb.2021.783301","article-title":"Structure-function relationship of the disintegrin family: sequence signature and integrin interaction","volume":"8","author":"Vasconcelos","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.toxicon.2022.08.010_bib54","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.abb.2008.11.023","article-title":"Integrin inhibitors from snake venom: exploring the relationship between the structure and activity of RGD-peptides","volume":"482","author":"Wermelinger","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2022.08.010_bib55","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1111\/1523-1747.ep12382086","article-title":"Characterization of expression and modulation of cell adhesion molecules on an immortalized human dermal microvascular endothelial cell line (HMEC-1)","volume":"102","author":"Xu","year":"1994","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.toxicon.2022.08.010_bib56","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.biotechadv.2017.11.002","article-title":"Engineering strategies for enhanced production of protein and bio-products in Pichia pastoris: a review","volume":"36","author":"Yang","year":"2018","journal-title":"Biotechnol. Adv."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010122002446?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010122002446?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T10:26:00Z","timestamp":1777458360000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010122002446"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10]]},"references-count":56,"alternative-id":["S0041010122002446"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2022.08.010","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2022,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The recombinant disintegrin, jarastatin, inhibits platelet adhesion and endothelial cell migration","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2022.08.010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}