{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T02:06:26Z","timestamp":1793066786696,"version":"4.5.0"},"reference-count":72,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,7,1]],"date-time":"2016-07-01T00:00:00Z","timestamp":1467331200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Cassandra M"},{"name":"Colorado Office of Economic Development and International Trade","award":["11BGF-10"],"award-info":[{"award-number":["11BGF-10"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2016,7]]},"DOI":"10.1016\/j.ijbiomac.2016.04.008","type":"journal-article","created":{"date-parts":[[2016,4,5]],"date-time":"2016-04-05T15:08:59Z","timestamp":1459868939000},"page":"457-464","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":51,"special_numbering":"C","title":["The disintegrin tzabcanin inhibits adhesion and migration in melanoma and lung cancer cells"],"prefix":"10.1016","volume":"88","author":[{"given":"Anthony J.","family":"Saviola","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick D.","family":"Burns","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashis K.","family":"Mukherjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen P.","family":"Mackessy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0005","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/0092-8674(87)90233-9","article-title":"Integrins: a family of cell surface receptors","volume":"48","author":"Hynes","year":"1987","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0010","doi-asserted-by":"crossref","first-page":"2868","DOI":"10.1096\/fasebj.4.11.2199285","article-title":"Integrins and other cell adhesion molecules","volume":"4","author":"Albelda","year":"1990","journal-title":"FASEB. J."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0015","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1016\/S0092-8674(02)00971-6","article-title":"Integrins: bidirectional allosteric signaling machines","volume":"110","author":"Hynes","year":"2002","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0020","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1016\/S0955-0674(99)00045-9","article-title":"Cell adhesion molecules: signal transduction and cell growth","volume":"11","author":"Aplin","year":"1999","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0025","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/s00441-009-0834-6","article-title":"Integrins","volume":"339","author":"Barczyk","year":"2010","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0030","doi-asserted-by":"crossref","first-page":"21785","DOI":"10.1074\/jbc.R000003200","article-title":"Ligand binding to integrins","volume":"275","author":"Plow","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0035","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s004410100417","article-title":"Function and interactions of integrins","volume":"305","author":"van der Flier","year":"2001","journal-title":"Cell Tissue Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0040","doi-asserted-by":"crossref","first-page":"3901","DOI":"10.1242\/jcs.03098","article-title":"Integrin ligands at a glance","volume":"119","author":"Humphries","year":"2006","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0045","doi-asserted-by":"crossref","first-page":"8049","DOI":"10.1016\/S0021-9258(18)34295-9","article-title":"Identification of the fibrinogen receptor on human platelets by photoaffinity labeling","volume":"257","author":"Bennett","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0050","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.2970671","article-title":"The human laminin receptor is a member of the integrin family of cell adhesion receptors","volume":"241","author":"Gehlsen","year":"1988","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0055","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1002\/path.1399","article-title":"Integrin\u2010dependent pathologies","volume":"200","author":"Wehrle\u2010Halle","year":"2003","journal-title":"J. Pathol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0060","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nrc2748","article-title":"Integrins in cancer: biological implication and therapeutic opportunities","volume":"10","author":"Desgrosellier","year":"2010","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0065","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s10555-010-9211-x","article-title":"Important role of integrins in the cancer biology","volume":"29","author":"Rathinam","year":"2010","journal-title":"Cancer Metastasis Rev."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0070","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1097\/CAD.0000000000000145","article-title":"Integrins: players in cancer progression and targets in cancer therapy","volume":"25","author":"Sun","year":"2014","journal-title":"Anti-cancer Drug"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0075","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1126\/science.7716514","article-title":"Integrins and signal transduction pathways: the road taken","volume":"268","author":"Clark","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0080","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.yexcr.2005.10.020","article-title":"Integrins and angiogenesis: a sticky business","volume":"5","author":"Serini","year":"2006","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0085","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.ijbiomac.2016.04.008_bib0090","doi-asserted-by":"crossref","first-page":"123","DOI":"10.2174\/1389450033346830","article-title":"Integrin \u03b1v\u03b23 as a therapeutic target for blocking tumor-induced angiogenesis","volume":"4","author":"Kumar","year":"2003","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0095","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/BF00114587","article-title":"Integrin expression in human melanoma cells with differing invasive and metastatic properties","volume":"10","author":"Gehlsen","year":"1992","journal-title":"Clin. Exp. Metastasis"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0100","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1158\/0008-5472.CAN-09-2319","article-title":"Breast cancer cells in three-dimensional culture display an enhanced radioresponse after coordinate targeting of integrin \u03b15\u03b21 and fibronectin","volume":"70","author":"Nam","year":"2010","journal-title":"Cancer Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.med.57.121304.131306","article-title":"Angiogenesis","volume":"57","author":"Folkman","year":"2006","journal-title":"Annu. Rev. Med."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0110","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1038\/nrd2115","article-title":"Angiogenesis: an organizing principle for drug discovery?","volume":"6","author":"Folkman","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0115","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.ijbiomac.2016.04.008_bib0120","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1126\/science.7512751","article-title":"Requirement of vascular integrin alpha v beta 3 for angiogenesis","volume":"264","author":"Brooks","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0125","first-page":"69","article-title":"Tumor angiogenesis and the role of vascular cell integrin alphavbeta3","author":"Varner","year":"1995","journal-title":"Important Adv. Oncol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0130","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/ncb2953","article-title":"An integrin \u03b23-KRAS-RalB complex drives tumour stemness and resistance to EGFR inhibition","volume":"16","author":"Seguin","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0135","doi-asserted-by":"crossref","first-page":"2927","DOI":"10.2174\/138161207782023739","article-title":"Approaching the golden age of natural product pharmaceuticals from venom libraries: an overview of toxins and toxin-derivatives currently involved in therapeutic or diagnostic applications","volume":"13","author":"Fox","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0140","series-title":"Encyclopedia of Toxicology","first-page":"252","article-title":"Animal venom in medicine","author":"Takacs","year":"2014"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0145","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1517\/14712598.2011.621940","article-title":"Venoms as a platform for human drugs: translating toxins into therapeutics","volume":"11","author":"King","year":"2011","journal-title":"Expert Opin. Biol. Ther."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0150","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1002\/bies.201000117","article-title":"Snake venom: from fieldwork to the clinic","volume":"33","author":"Vonk","year":"2011","journal-title":"Bioessays"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0155","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/nature11494","article-title":"Black mamba venom peptides target acid-sensing ion channels to abolish pain","volume":"490","author":"Diochot","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0160","doi-asserted-by":"crossref","first-page":"185","DOI":"10.3109\/15569543.2014.942040","article-title":"Rear-fanged snake venoms: an untapped source of novel compounds and potential drug leads","volume":"33","author":"Saviola","year":"2014","journal-title":"Toxin Rev."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0165","series-title":"Venoms to Drugs: Venom as a Source for the Development of Human Therapeutics","first-page":"129","article-title":"Reptile venoms as a platform for drug development","author":"McCleary","year":"2015"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0170","series-title":"Handbook of Venoms and Toxins of Reptiles","first-page":"3","article-title":"The field of reptile toxinology: snakes, lizards, and their venoms","author":"Mackessy","year":"2010"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0175","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1002\/pros.21173","article-title":"The disintegrin contortrostatin in combination with docetaxel is a potent inhibitor of prostate cancer in vitro and in vivo","volume":"70","author":"Lin","year":"2010","journal-title":"Prostate"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0180","doi-asserted-by":"crossref","first-page":"1358","DOI":"10.1007\/s10495-015-1157-6","article-title":"Apoptosis induction in human breast cancer (MCF-7) cells by a novel venom l-amino acid oxidase (Rusvinoxidase) is independent of its enzymatic activity and is accompanied by caspase-7 activation and reactive oxygen species production","volume":"20","author":"Mukherjee","year":"2015","journal-title":"Apoptosis"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0185","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0041-0101(92)90869-7","article-title":"Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor","volume":"30","author":"Kini","year":"1992","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0190","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.ijbiomac.2016.04.008_bib0195","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.ijbiomac.2016.04.008_bib0200","series-title":"Handbook of Venoms and Toxins of Reptiles","first-page":"337","article-title":"Snake venomics and disintegrins: portrait and evolution of a family of snake venom integrin antagonists","author":"Calvete","year":"2010"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0205","first-page":"4993","article-title":"Contortrostatin a snake venom disintegrin, inhibits \u03b21 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis","volume":"54","author":"Trikha","year":"1994","journal-title":"Cancer Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0210","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1023\/A:1009059210733","article-title":"Contortrostatin a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits angiogenesis","volume":"3","author":"Zhou","year":"1999","journal-title":"Angiogenesis"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0215","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1023\/A:1006457903545","article-title":"Contortrostatin a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits breast cancer progression","volume":"61","author":"Zhou","year":"2000","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0220","first-page":"2020","article-title":"Obtustatin, a potent selective inhibitor of \u03b11\u03b21 integrin in vitro and angiogenesis in vivo","volume":"63","author":"Marcinkiewicz","year":"2003","journal-title":"Cancer Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0225","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1016\/j.toxicon.2008.02.004","article-title":"Inhibition of lung tumor colonization and cell migration with the disintegrin crotatroxin 2 isolated from the venom of Crotalus atrox","volume":"51","author":"Gal\u00e1n","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0230","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1007\/s00204-008-0358-y","article-title":"Colombistatin: a disintegrin isolated from the venom of the South American snake (Bothrops colombiensis) that effectively inhibits platelet aggregation and SK-mel-28 cell adhesion","volume":"83","author":"S\u00e1nchez","year":"2009","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0235","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.biochi.2015.07.005","article-title":"Disintegrins of Crotalus simus tzabcan venom: isolation, characterization and evaluation of the cytotoxic and anti-adhesion activities of tzabcanin, a new RGD disintegrin","volume":"116","author":"Saviola","year":"2015","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0240","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1038\/bjc.1996.158","article-title":"Multiplicity of fibronectin-binding alpha V integrin receptors in colorectal cancer","volume":"73","author":"Agrez","year":"1996","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0245","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1186\/1471-2407-11-293","article-title":"Differences in integrin expression and signaling within human breast cancer cells","volume":"11","author":"Taherian","year":"2011","journal-title":"BMC Cancer"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0250","doi-asserted-by":"crossref","first-page":"92","DOI":"10.2307\/1445927","article-title":"Venom ontogeny in the Pacific rattlesnakes Crotalus viridis helleri and C. v. oreganus","author":"Mackessy","year":"1988","journal-title":"Copeia"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0255","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0022-1759(83)90303-4","article-title":"Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays","volume":"65","author":"Mosmann","year":"1983","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0260","first-page":"1","article-title":"Evaluation of cytotoxic activities of snake venoms toward breast (MCF-7) and skin cancer (A-375) cell lines","author":"Bradshaw","year":"2014","journal-title":"Cytotechnology"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0265","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/nprot.2007.30","article-title":"In vitro scratch assay: a convenient and inexpensive method for analysis of cell migration in vitro","volume":"2","author":"Liang","year":"2007","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0270","doi-asserted-by":"crossref","first-page":"26270","DOI":"10.1074\/jbc.270.44.26270","article-title":"Regulation of integrin \u03b15\u03b21-fibronectin interactions by divalent cations: evidence for distinct classes of binding sites for Mn2+ Mg2+, and Ca2+","volume":"270","author":"Mould","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0275","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/S1357-2725(96)00155-0","article-title":"The \u03b1v\u03b23 integrin vitronectin receptor","volume":"29","author":"Horton","year":"1997","journal-title":"Int. J. Biochem. Cell Biol"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0280","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1002\/ijc.25134","article-title":"MMP-2 alters VEGF expression via \u03b1V\u03b23 integrin-mediated PI3K\/AKT signaling in A549 lung cancer cells","volume":"127","author":"Chetty","year":"2010","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0285","doi-asserted-by":"crossref","first-page":"5","DOI":"10.3322\/caac.21254","article-title":"Cancer statistics","volume":"65","author":"Siegel","year":"2015","journal-title":"CA Cancer J. Clin."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0290","doi-asserted-by":"crossref","first-page":"277","DOI":"10.3322\/caac.20073","article-title":"Cancer statistics","volume":"60","author":"Jemal","year":"2010","journal-title":"CA Cancer J. Clin."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0295","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/0092-8674(91)90642-C","article-title":"Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation","volume":"64","author":"Liotta","year":"1991","journal-title":"Cell"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0300","doi-asserted-by":"crossref","first-page":"175","DOI":"10.3109\/10409239709082573","article-title":"The biochemistry of cancer dissemination","volume":"32","author":"Price","year":"1997","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0305","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/S0046-8177(97)90033-2","article-title":"Expression of \u03b1v\u03b23 integrin is less frequent in ovarian epithelial tumors of low malignant potential in contrast to ovarian carcinomas","volume":"28","author":"Liapis","year":"1997","journal-title":"Hum. Pathol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0310","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.ijbiomac.2016.04.008_bib0315","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1992.250","article-title":"The Walter Herbert Lecture. Control of cell motility and tumour invasion by extracellular matrix interactions","volume":"662","author":"Ruoslahti","year":"1992","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0320","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1146\/annurev.cellbio.12.1.697","article-title":"RGD and other recognition sequences for integrins","volume":"12","author":"Ruoslahti","year":"1996","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0325","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1002\/pmic.200900758","article-title":"Matrigel: a complex protein mixture required for optimal growth of cell culture","volume":"10","author":"Hughes","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0330","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.jprot.2013.05.024","article-title":"Intraspecies variation in the venom of the rattlesnake Crotalus simus from Mexico: different expression of crotoxin results in highly variable toxicity in the venoms of three subspecies","volume":"87","author":"Castro","year":"2013","journal-title":"J. Proteomics"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0335","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.toxicon.2014.11.228","article-title":"Inhibition of pancreatic tumoral cells by snake venom disintegrins","volume":"93","author":"Lucena","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0340","doi-asserted-by":"crossref","first-page":"9482","DOI":"10.1073\/pnas.1633689100","article-title":"Activated integrin \u03b1v\u03b23 cooperates with metalloproteinase MMP-9 in regulating migration of metastatic breast cancer cells","volume":"100","author":"Rolli","year":"2003","journal-title":"Proc. Nat. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0345","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1016\/j.yexcr.2005.11.011","article-title":"\u03b1v\u03b23 integrin and cofilin modulate K1735 melanoma cell invasion","volume":"312","author":"Dang","year":"2006","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0350","doi-asserted-by":"crossref","first-page":"R20","DOI":"10.1186\/bcr1398","article-title":"Tumor-specific expression of \u03b1v\u03b23 integrin promotes spontaneous metastasis of breast cancer to bone","volume":"8","author":"Sloan","year":"2006","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0355","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1083\/jcb.137.2.481","article-title":"Regulation of cell motility by mitogen-activated protein kinase","volume":"137","author":"Klemke","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2016.04.008_bib0360","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0022-4804(03)00004-0","article-title":"Adhesion and migration of extracellular matrix-stimulated breast cancer","volume":"110","author":"Bartsch","year":"2003","journal-title":"J. Surg. Res."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813016303166?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813016303166?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,15]],"date-time":"2024-06-15T14:22:46Z","timestamp":1718461366000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813016303166"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,7]]},"references-count":72,"alternative-id":["S0141813016303166"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2016.04.008","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2016,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The disintegrin tzabcanin inhibits adhesion and migration in melanoma and lung cancer cells","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2016.04.008","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}