{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T14:26:58Z","timestamp":1787840818109,"version":"build-2784847793"},"reference-count":78,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,3,1]],"date-time":"2019-03-01T00:00:00Z","timestamp":1551398400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,3,1]],"date-time":"2019-03-01T00:00:00Z","timestamp":1551398400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001655","name":"DAAD","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001655","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"CAPES","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"CNPq","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"FAPESP","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2019,3]]},"DOI":"10.1016\/j.toxicon.2018.12.005","type":"journal-article","created":{"date-parts":[[2019,1,3]],"date-time":"2019-01-03T13:36:12Z","timestamp":1546522572000},"page":"22-31","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"special_numbering":"C","title":["Leucurogin and melanoma therapy"],"prefix":"10.1016","volume":"159","author":[{"given":"Meire C.","family":"Almeida","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivan C.","family":"Santos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thaysa","family":"Paschoalin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luiz R.","family":"Travassos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cornelia","family":"Mauch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paola","family":"Zigrino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00e3o B.","family":"Pesquero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge L.","family":"Pesquero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Debora A.","family":"Higuchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2018.12.005_bib1","doi-asserted-by":"crossref","first-page":"2451","DOI":"10.1038\/jid.2012.153","article-title":"Stromal fibroblast-specific expression of ADAM-9 modulates proliferation and apoptosis in melanoma cells in vitro and in vivo","volume":"132","author":"Abety","year":"2012","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib2","series-title":"Cancer Facts & Figures 2013","year":"2013"},{"key":"10.1016\/j.toxicon.2018.12.005_bib3","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/s10555-006-7889-6","article-title":"ADAMs, cell migration and cancer","volume":"25","author":"Arribas","year":"2006","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.toxicon.2018.12.005_bib4","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1007\/s00432-011-1073-2","article-title":"VEGF gene alternative splicing: pro-and anti-angiogenic isoforms in cancer","volume":"138","author":"Biselli-Chicote","year":"2012","journal-title":"J. Cancer Res. Clin. Oncol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib5","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1038\/35020115","article-title":"Molecular classification of cutaneous malignant melanoma by gene expression profiling","volume":"406","author":"Bittner","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2018.12.005_bib6","series-title":"World Cancer Report","author":"Boyle","year":"2008"},{"key":"10.1016\/j.toxicon.2018.12.005_bib7","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib8","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":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib9","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/j.toxicon.2005.02.024","article-title":"Snake venom disintegrins: evolution of structure and function","volume":"45","author":"Calvete","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib10","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1126\/science.2011740","article-title":"In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells","volume":"251","author":"Chan","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.toxicon.2018.12.005_bib11","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.ab.2013.12.018","article-title":"Glycosylation of A Disintegrin and Metalloprotease 17 (ADAM17) affects its activity and inhibition","volume":"449","author":"Chavaroche","year":"2014","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib12","doi-asserted-by":"crossref","first-page":"18247","DOI":"10.1074\/jbc.M311771200","article-title":"Alternagin-C, a disintegrin-like protein, induces vascular endothelial cell growth factor (VEGF) expression and endothelial cell proliferation in vitro","volume":"279","author":"Cominetti","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib13","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1002\/cncr.11181","article-title":"Stromal factors involved in prostate carcinoma metastasis to bone","volume":"97","author":"Cooper","year":"2003","journal-title":"Cancer"},{"key":"10.1016\/j.toxicon.2018.12.005_bib14","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0165-6147(00)01676-X","article-title":"FGF and VEGF function in angiogenesis: signalling pathways, biological responses and therapeutic inhibition","volume":"22","author":"Cross","year":"2001","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.toxicon.2018.12.005_bib15","doi-asserted-by":"crossref","first-page":"1582","DOI":"10.1126\/science.7521539","article-title":"Control of angiogenesis in fibroblasts by p53 regulation of thrombospondin-1","volume":"9","author":"Dameron","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.toxicon.2018.12.005_bib16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2013\/135164","article-title":"Integrin signaling as a cancer drug target","author":"Danen","year":"2013","journal-title":"ISRN Cell Biol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib17","doi-asserted-by":"crossref","first-page":"321","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.2018.12.005_bib18","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.canlet.2015.11.030","article-title":"Blocking FGF2 with a new specific monoclonal antibody impairs angiogenesis and experimental metastatic melanoma, suggesting a potential role in adjuvant settings","volume":"371","author":"De Aguiar","year":"2016","journal-title":"Cancer Lett."},{"key":"10.1016\/j.toxicon.2018.12.005_bib19","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1007\/s10555-006-7886-9","article-title":"Matrix metalloproteinases and tumor metastasis","volume":"25","author":"Deryugina","year":"2006","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.toxicon.2018.12.005_bib20","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.ajpath.2012.04.012","article-title":"Highly invasive melanoma cells activate the vascular endothelium via an MMP-2\/Integrin \u03b1v\u03b25\u2013induced secretion of VEGF-A","volume":"181","author":"Desch","year":"2012","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib21","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrc2748","article-title":"Integrins in cancer: biological implications and therapeutic opportunities","volume":"10","author":"Desgrosellier","year":"2010","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.toxicon.2018.12.005_bib22","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1111\/j.1582-4934.2007.00001.x","article-title":"Human mesenchymal stem cells in contact with their environment: surface characteristics and the integrin system","volume":"11","author":"Docheva","year":"2007","journal-title":"J. Cell Mol. Med."},{"key":"10.1016\/j.toxicon.2018.12.005_bib23","doi-asserted-by":"crossref","first-page":"12274","DOI":"10.1074\/jbc.M009338200","article-title":"\u03b12\u03b21 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen","volume":"276","author":"Eble","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib24","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1172\/JCI6869","article-title":"The role of \u03b1v integrins during angiogenesis: insights into potential mechanisms of action and clinical development","volume":"103","author":"Eliceiri","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.toxicon.2018.12.005_bib25","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.130.2.441","article-title":"Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo","volume":"130","author":"Filardo","year":"1995","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib26","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1111\/j.1742-4658.2008.06466.x","article-title":"Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity","volume":"275","author":"Fox","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.toxicon.2018.12.005_bib27","first-page":"2061","article-title":"Migration of highly aggressive MV3 melanoma cells in 3-dimensional collagen lattices results in local matrix reorganization and shedding of \u03b12 and \u03b21 integrins and CD44","volume":"57","author":"Friedl","year":"1997","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib28","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1590\/S1678-91992012000100004","article-title":"Tumor cytotoxicity of leucurolysin-B, a P-III snake venom metalloproteinase from Bothrops leucurus","volume":"18","author":"Gabriel","year":"2012","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.toxicon.2018.12.005_bib29","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1126\/science.285.5430.1028","article-title":"Integrin signaling","volume":"285","author":"Giancotti","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.toxicon.2018.12.005_bib30","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3390\/toxins8040122","article-title":"A Disintegrin and Metalloprotease (ADAM): historical overview of their functions","volume":"8","author":"Giebeler","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2018.12.005_bib31","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.2018.12.005_bib32","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1007\/s00280-017-3322-9","article-title":"A phase I study of cilengitide and paclitaxel in patients with advanced solid tumors","volume":"79","author":"Haddad","year":"2017","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib33","doi-asserted-by":"crossref","first-page":"6089","DOI":"10.1158\/0008-5472.CAN-12-2773","article-title":"Engineering approaches for investigating tumor angiogenesis: exploiting the role of the extracellular matrix","volume":"72","author":"Hielscher","year":"2012","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib34","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.toxicon.2011.05.013","article-title":"Leucurogin, a new recombinant disintegrin cloned from Bothrops leucurus (white-tailed-jararaca) with potent activity upon platelet aggregation and tumor growth","volume":"58","author":"Higuchi","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib35","doi-asserted-by":"crossref","first-page":"7471","DOI":"10.1021\/acs.jmedchem.8b01123","article-title":"isoDGR-peptides for integrin targeting: is the time up for RGD?","volume":"61","author":"H\u00f6ltke","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib36","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1016\/S0002-9440(10)65730-6","article-title":"Adenoviral gene transfer of \u03b23 integrin subunit induces conversion from radial to vertical growth phase in primary human melanoma","volume":"153","author":"Hsu","year":"1998","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib37","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.dci.2015.05.005","article-title":"A novel integrin function in innate immunity from Chinese mitten crab (Eriocheir sinensis)","volume":"52","author":"Huang","year":"2015","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib38","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.2018.12.005_bib39","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nrn2175","article-title":"Angiogenesis in brain tumours","volume":"8","author":"Jain","year":"2007","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.toxicon.2018.12.005_bib40","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1158\/0008-5472.CAN-13-1742","article-title":"\u03b21 integrin: critical path to antiangiogenic therapy resistance and beyond","volume":"74","author":"Jahangiri","year":"2014","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib41","first-page":"3754","article-title":"A novel disintegrin salmosin inhibits tumor angiogenesis","volume":"59","author":"Kang","year":"1999","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib42","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1006\/bbrc.2000.3130","article-title":"Suppressive mechanism of salmosin, a novel disintegrin in B16 melanoma cell metastasis","volume":"275","author":"Kang","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2018.12.005_bib43","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1083\/jcb.115.5.1427","article-title":"Integrin alpha 2 beta 1 is upregulated in fibroblasts and highly aggressive melanoma cells in three-dimensional collagen lattices and mediates the reorganization of collagen I fibrils","volume":"115","author":"Klein","year":"1991","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib44","doi-asserted-by":"crossref","first-page":"639","DOI":"10.2174\/156800909789057006","article-title":"The role of fibroblast growth factors in tumor growth","volume":"9","author":"Korc","year":"2009","journal-title":"Curr. Cancer Drug Targets"},{"key":"10.1016\/j.toxicon.2018.12.005_bib45","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/s10555-005-1572-1","article-title":"Integrin signaling in malignant melanoma","volume":"24","author":"Kuphal","year":"2005","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.toxicon.2018.12.005_bib46","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/labinvest.3780007","article-title":"Platelet-derived growth factors stimulate proliferation and extracellular matrix synthesis of pancreatic stellate cells: implications in pathogenesis of pancreas fibrosis","volume":"80","author":"Luttenberger","year":"2000","journal-title":"Lab. Invest."},{"key":"10.1016\/j.toxicon.2018.12.005_bib47","doi-asserted-by":"crossref","first-page":"3067","DOI":"10.1091\/mbc.10.10.3067","article-title":"Functional hierarchy of simultaneously expressed adhesion receptors: integrin \u03b12\u03b21 but not CD44 mediates MV3 melanoma cell migration and matrix reorganization within three-dimensional hyaluronan containing collagen matrices","volume":"10","author":"Maaser","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.toxicon.2018.12.005_bib48","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1186\/1472-6882-14-446","article-title":"Antiproliferative effect of the jararhagin toxin on B16F10 murine melanoma","volume":"14","author":"Maria","year":"2014","journal-title":"BMC Complement Altern. Med."},{"key":"10.1016\/j.toxicon.2018.12.005_bib49","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1182\/blood.V90.4.1565","article-title":"Significance of RGD loop and C-terminal domain of echistatin for recognition of \u03b1IIb\u03b23 and av\u03b23 integrins and expression of ligand-induced binding site","volume":"90","author":"Marcinkiewicz","year":"1997","journal-title":"Blood"},{"key":"10.1016\/j.toxicon.2018.12.005_bib50","doi-asserted-by":"crossref","first-page":"9859","DOI":"10.1021\/bi000428a","article-title":"Isolation and characterization of EMS16, a C-lectin type protein from Echis multisquamatus venom, a potent and selective inhibitor of the \u03b12\u03b21 integrin","volume":"39","author":"Marcinkiewicz","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2018.12.005_bib51","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.toxicon.2011.02.020","article-title":"Development of a chimeric recombinant disintegrin as a cost-effective anti-cancer agent with promising translational potential","volume":"59","author":"Minea","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib52","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1002\/1097-0215(20000901)87:5<716::AID-IJC14>3.0.CO;2-R","article-title":"In vivo therapy of malignant melanoma by means of antagonists of \u03b1v integrins","volume":"87","author":"Mitjans","year":"2000","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.toxicon.2018.12.005_bib53","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1046\/j.1525-1373.1999.d01-122.x","article-title":"Role of integrins in cancer: survey of expression patterns","volume":"222","author":"Mizejewski","year":"1999","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.toxicon.2018.12.005_bib54","doi-asserted-by":"crossref","first-page":"862","DOI":"10.3390\/toxins4100862","article-title":"Vixapatin (VP12), a c-type lectin-protein from Vipera xantina palestinae venom: characterization as a novel antiangiogenic compound","volume":"4","author":"Momic","year":"2012","journal-title":"Toxins"},{"key":"10.1016\/j.toxicon.2018.12.005_bib55","first-page":"289","article-title":"Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors","volume":"vol. 31","author":"Niewiarowski","year":"1994"},{"key":"10.1016\/j.toxicon.2018.12.005_bib56","doi-asserted-by":"crossref","first-page":"22869","DOI":"10.1016\/S0021-9258(18)50027-2","article-title":"Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family","volume":"267","author":"Paine","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2018.12.005_bib57","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/1476-4598-6-44","article-title":"Characterization of thimet oligopeptidase and neurolysin activities in B16F10-Nex2 tumor cells and their involvement in angiogenesis and tumor growth","volume":"6","author":"Paschoalin","year":"2007","journal-title":"Mol. Cancer"},{"issue":"110","key":"10.1016\/j.toxicon.2018.12.005_bib58","first-page":"2","article-title":"Integrins as therapeutic targets: successes and cancers","volume":"9","author":"Raab-Westphal","year":"2017","journal-title":"Cancers"},{"key":"10.1016\/j.toxicon.2018.12.005_bib59","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1097\/00001813-199502000-00001","article-title":"Consequences of angiogenesis for tumor progression, metastasis and cancer therapy","volume":"6","author":"Rak","year":"1995","journal-title":"Anti Canccer Drugs"},{"key":"10.1016\/j.toxicon.2018.12.005_bib60","doi-asserted-by":"crossref","first-page":"1704","DOI":"10.1126\/science.1092053","article-title":"Cell migration: integrating signals from front to back","volume":"302","author":"Ridley","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.toxicon.2018.12.005_bib61","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1111\/j.1349-7006.2009.01403.x","article-title":"Angiostatic activity of human plasminogen fragments is highly dependent on glycosylation","volume":"101","author":"Santos","year":"2010","journal-title":"Cancer Sci."},{"key":"10.1016\/j.toxicon.2018.12.005_bib62","first-page":"1503","article-title":"Signaling by integrins: implications for tumorigenesis","volume":"53","author":"Schwartz","year":"1993","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib63","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1007\/s00109-013-1019-z","article-title":"Mechanisms of neovascularization and resistance to antiangiogenic therapies in glioblastoma multiforme","volume":"91","author":"Soda","year":"2013","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.toxicon.2018.12.005_bib64","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1006\/abbi.2000.2120","article-title":"The disintegrin-like domain of the snake venom metalloprotease alternagin inhibits \u03b12\u03b21 integrin-mediated cell adhesion","volume":"384","author":"Souza","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2018.12.005_bib65","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1093\/carcin\/bgu018","article-title":"The interplay between hypoxia, endothelial and melanoma cells regulates vascularization and cell motility through endothelin-1 and vascular endothelial growth factor","volume":"35","author":"Spinella","year":"2014","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.toxicon.2018.12.005_bib90","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.toxicon.2016.09.007","article-title":"Expression, purification, and analysis of three recombinant ECD disintegrins (r-colombistatins) from P-III class snake venom metalloproteinases affecting platelet aggregation and SK-MEL-28 cell adhesion","volume":"122","author":"Suntravat","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib66","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1159\/000092418","article-title":"Contortrostatin, a snake venom disintegrin with anti-angiogenic and anti-tumor activity","volume":"34","author":"Swenson","year":"2006","journal-title":"Pathophysiol. Haemostasis Thrombosis"},{"key":"10.1016\/j.toxicon.2018.12.005_bib67","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s11523-010-0156-3","article-title":"Targeting integrins in malignant glioma","volume":"5","author":"Tabatabai","year":"2010","journal-title":"Targeted Oncol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib68","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1016\/j.toxicon.2003.10.011","article-title":"Phylogenetic conservation of a snake venom metalloproteinase epitope recognized by a monoclonal antibody that neutralizes hemorrhagic activity","volume":"42","author":"Tanjoni","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib69","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/j.toxicon.2009.12.010","article-title":"Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to \u03b12\u03b21 integrin and collagen","volume":"55","author":"Tanjoni","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib70","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1590\/S0074-02762005000900031","article-title":"Inflammatory effects of snake venom metalloproteinases","volume":"100","author":"Teixeira","year":"2005","journal-title":"Mem. Inst. Oswaldo Cruz"},{"key":"10.1016\/j.toxicon.2018.12.005_bib71","doi-asserted-by":"crossref","first-page":"2062","DOI":"10.1158\/0008-5472.CAN-03-3272","article-title":"Evidence of antiangiogenic and antimetastatic activities of the recombinant disintegrin domain of metargidin","volume":"64","author":"Trochon-Joseph","year":"2004","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib72","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1006\/bbrc.1994.1706","article-title":"A 28-kDa protein with disintegrin-like structure (jararhagin-C) purified from Bothrops jararaca venom inhibits collagen and ADP-induced platelet aggregation","volume":"201","author":"Usami","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2018.12.005_bib73","first-page":"6237","article-title":"Identification of melanoma inhibitory activity and other differentially expressed messenger RNAs in human melanoma cell lines with different metastatic capacity by messenger RNA differential display","volume":"55","author":"Van Groningen","year":"1995","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2018.12.005_bib74","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1093\/neuonc\/nos119","article-title":"Importance of interaction of NGF with \u03b19\u03b21 integrin in progression of glioma angiogenesis","volume":"14","author":"Walsh","year":"2012","journal-title":"Neuro Oncol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib75","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/j.toxicon.2005.01.013","article-title":"Inhibition of tumor formation by snake venom disintegrin","volume":"45","author":"Yang","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2018.12.005_bib76","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1078\/0171-9335-00134","article-title":"Collagen-induced proMMP-2 activation by MT1-MMP in human dermal fibroblasts and the possible role of \u03b12\u03b21 integrins","volume":"80","author":"Zigrino","year":"2001","journal-title":"Eur. J. Cell Biol."},{"key":"10.1016\/j.toxicon.2018.12.005_bib77","doi-asserted-by":"crossref","first-page":"30785","DOI":"10.1074\/jbc.M701658200","article-title":"Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration","volume":"282","author":"Zigrino","year":"2007","journal-title":"J. Biol. Chem."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010119300029?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010119300029?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:10:48Z","timestamp":1758575448000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010119300029"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,3]]},"references-count":78,"alternative-id":["S0041010119300029"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2018.12.005","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2019,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Leucurogin and melanoma therapy","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2018.12.005","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}