{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:27:19Z","timestamp":1767929239912,"version":"3.49.0"},"reference-count":33,"publisher":"Elsevier BV","issue":"2-3","license":[{"start":{"date-parts":[[2010,2,1]],"date-time":"2010-02-01T00:00:00Z","timestamp":1264982400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2010,2]]},"DOI":"10.1016\/j.toxicon.2009.08.016","type":"journal-article","created":{"date-parts":[[2009,9,3]],"date-time":"2009-09-03T12:08:34Z","timestamp":1251979714000},"page":"375-380","source":"Crossref","is-referenced-by-count":22,"title":["Expression, purification and characterization of recombinant Jerdonitin, a P-II class snake venom metalloproteinase comprising metalloproteinase and disintegrin domains"],"prefix":"10.1016","volume":"55","author":[{"given":"Lili","family":"Zhu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cai","family":"Yuan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhuo","family":"Chen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wanyu","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mingdong","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2009.08.016_bib1","first-page":"207","article-title":"Integrins: structure and functions","volume":"13","author":"Berman","year":"2000","journal-title":"Membr. Cell Biol."},{"key":"10.1016\/j.toxicon.2009.08.016_bib2","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/0076-6879(95)48023-4","article-title":"Snake venom metalloendopeptidases: reprolysins","volume":"248","author":"Bjarnason","year":"1995","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2009.08.016_bib3","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1111\/j.1574-6976.2000.tb00532.x","article-title":"Heterologous protein expression in the methylotrophic yeast Pichia pastoris","volume":"24","author":"Cereghino","year":"2000","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.toxicon.2009.08.016_bib4","first-page":"616","article-title":"Purification and characterization of Jerdonitin, a non-hemorrhagic metalloproteinase from Trimeresurus jerdonii venom","volume":"26","author":"Chen","year":"2005","journal-title":"Zool. Res."},{"key":"10.1016\/j.toxicon.2009.08.016_bib5","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.bbrc.2003.09.009","article-title":"A new protein structure of P-II class snake venom metalloproteinases: it comprises metalloproteinase and disintegrin domains","volume":"310","author":"Chen","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2009.08.016_bib6","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.2009.08.016_bib7","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1093\/jnci\/93.4.261","article-title":"Snake venom protein paralyzes cancer cells","volume":"93","author":"Finn","year":"2001","journal-title":"J. Natl. Cancer Inst."},{"key":"10.1016\/j.toxicon.2009.08.016_bib8","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.toxicon.2005.02.012","article-title":"Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases","volume":"45","author":"Fox","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2009.08.016_bib9","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0041-0101(97)00150-5","article-title":"Characterization of three fibrinolytic enzymes from Chinese green tree viper (Trimeresurus stejnegeri) venom","volume":"36","author":"Gao","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2009.08.016_bib10","doi-asserted-by":"crossref","first-page":"168","DOI":"10.3181\/00379727-195-43129B","article-title":"Disintegrins: a family of integrin inhibitory proteins from viper venoms","volume":"195","author":"Gould","year":"1990","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"10.1016\/j.toxicon.2009.08.016_bib11","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/j.toxicon.2006.11.030","article-title":"Isolation and characterization of a novel P-II class snake venom metalloproteinase from Trimeresurus stejnegeri","volume":"49","author":"Han","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2009.08.016_bib12","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s000180050181","article-title":"What have snakes taught us about integrins?","volume":"54","author":"Huang","year":"1998","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.toxicon.2009.08.016_bib13","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1016\/S0041-0101(96)00108-0","article-title":"Snake venom metalloproteinases: structure, function and relationship to the ADAMs family of proteins","volume":"34","author":"Jia","year":"1996","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2009.08.016_bib14","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.2009.08.016_bib15","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/0300-9084(96)82187-0","article-title":"Biochemical characterization of a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom","volume":"78","author":"Kawasaki","year":"1996","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2009.08.016_bib16","doi-asserted-by":"crossref","first-page":"290","DOI":"10.5483\/BMBRep.2007.40.2.290","article-title":"Saxatilin, a snake venom disintegrin, suppresses TNF-alpha-induced ovarian cancer cell invasion","volume":"40","author":"Kim","year":"2007","journal-title":"J. Biochem. Mol. Biol."},{"key":"10.1016\/j.toxicon.2009.08.016_bib17","first-page":"6458","article-title":"Inhibitory effect of the salmosin gene transferred by cationic liposomes on the progression of B16BL6 tumors","volume":"63","author":"Kim","year":"2003","journal-title":"Cancer Res."},{"key":"10.1016\/j.toxicon.2009.08.016_bib18","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2009.08.016_bib19","doi-asserted-by":"crossref","first-page":"514","DOI":"10.3748\/wjg.v10.i4.514","article-title":"Inhibition of DNA primase and induction of apoptosis by 3,3\u2032-diethyl-9-methylthia\u2013carbocyanine iodide in hepatocellular carcinoma BEL-7402 cells","volume":"10","author":"Li","year":"2004","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.toxicon.2009.08.016_bib20","first-page":"183","article-title":"A novel snake venom disintegrin that inhibits human ovarian cancer dissemination and angiogenesis in an orthotopic nude mouse model","volume":"31","author":"Markland","year":"2001","journal-title":"Haemostasis"},{"key":"10.1016\/j.toxicon.2009.08.016_bib21","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1093\/oxfordjournals.jbchem.a122756","article-title":"Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis","volume":"105","author":"Miyata","year":"1989","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/j.toxicon.2009.08.016_bib22","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.toxicon.2009.08.016_bib23","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1006\/abbi.2000.1795","article-title":"Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom","volume":"378","author":"Nikai","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2009.08.016_bib24","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/S0041-0101(00)00126-4","article-title":"Differential regulation of tyrosine phosphorylation in tumor cells by contortrostatin, a homodimeric disintegrin, and monomeric disintegrins echistatin and flavoridin","volume":"39","author":"Ritter","year":"2001","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2009.08.016_bib25","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1227\/01.NEU.0000163426.25227.56","article-title":"Potent mimicry of fibronectin-induced intracellular signaling in glioma cells by the homodimeric snake venom disintegrin contortrostatin","volume":"57","author":"Schmitmeier","year":"2005","journal-title":"Neurosurgery"},{"key":"10.1016\/j.toxicon.2009.08.016_bib26","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1006\/abbi.1996.0509","article-title":"Expression, activation, and processing of the recombinant snake venom metalloproteinase, pro-atrolysin E","volume":"335","author":"Shimokawa","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2009.08.016_bib27","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0304-4165(91)90156-B","article-title":"Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom","volume":"1074","author":"Siigur","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2009.08.016_bib28","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/S0006-291X(02)03001-2","article-title":"cDNA cloning and characterization of agkistin, a new metalloproteinase from Agkistrodon halys","volume":"301","author":"Wang","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2009.08.016_bib29","doi-asserted-by":"crossref","first-page":"3268","DOI":"10.1182\/blood.V92.9.3268","article-title":"Accutin, a new disintegrin, inhibits angiogenesis in vitro and in vivo by acting as integrin alphavbeta3 antagonist and inducing apoptosis","volume":"92","author":"Yeh","year":"1998","journal-title":"Blood"},{"key":"10.1016\/j.toxicon.2009.08.016_bib30","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0304-4165(98)00104-4","article-title":"A new short chain RGD-containing disintegrin, accutin, inhibits the common pathway of human platelet aggregation","volume":"1425","author":"Yeh","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2009.08.016_bib31","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.toxicon.2009.08.016_bib32","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.toxicon.2009.08.016_bib33","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.cbpc.2004.06.012","article-title":"A novel disintegrin, jerdonatin, inhibits platelet aggregation and sperm-egg binding","volume":"139","author":"Zhou","year":"2004","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010109004395?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010109004395?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,5,22]],"date-time":"2020-05-22T00:21:45Z","timestamp":1590106905000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010109004395"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,2]]},"references-count":33,"journal-issue":{"issue":"2-3","published-print":{"date-parts":[[2010,2]]}},"alternative-id":["S0041010109004395"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2009.08.016","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2010,2]]}}}