{"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":1767929239828,"version":"3.49.0"},"reference-count":38,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2011,2,1]],"date-time":"2011-02-01T00:00:00Z","timestamp":1296518400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2011,2,1]],"date-time":"2011-02-01T00:00:00Z","timestamp":1296518400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2011,10,16]],"date-time":"2011-10-16T00:00:00Z","timestamp":1318723200000},"content-version":"vor","delay-in-days":257,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2011,2]]},"DOI":"10.1016\/j.biochi.2010.10.007","type":"journal-article","created":{"date-parts":[[2010,10,17]],"date-time":"2010-10-17T04:14:02Z","timestamp":1287288842000},"page":"345-351","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":25,"title":["Disintegrin-like\/cysteine-rich domains of the reprolysin HF3: Site-directed mutagenesis reveals essential role of specific residues"],"prefix":"10.1016","volume":"93","author":[{"given":"Milene C.","family":"Menezes","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana Karina","family":"de Oliveira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robson L.","family":"Melo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M\u00f4nica","family":"Lopes-Ferreira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vanessa","family":"Rioli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrea","family":"Balan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adriana F.","family":"Paes Leme","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Solange M.T.","family":"Serrano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2010.10.007_bib1","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/S0955-0674(98)80042-2","article-title":"ADAMs: focus on the protease domain","volume":"10","author":"Black","year":"1998","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.biochi.2010.10.007_bib2","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1038\/nrc2459","article-title":"The ADAMs: signalling scissors in the tumour microenvironment","volume":"8","author":"Murphy","year":"2008","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.biochi.2010.10.007_bib3","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0014-5793(99)00119-2","article-title":"ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats","volume":"445","author":"Tang","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2010.10.007_bib4","doi-asserted-by":"crossref","first-page":"31493","DOI":"10.1074\/jbc.R109.052340","article-title":"A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms","volume":"284","author":"Apte","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2010.10.007_bib5","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1042\/BJ20040424","article-title":"The ADAMTS metalloproteinases","volume":"386","author":"Porter","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2010.10.007_bib6","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.biochi.2010.10.007_bib7","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.biochi.2010.10.007_bib8","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1111\/j.1742-4658.2008.06466.x","article-title":"Insights and speculations into 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.biochi.2010.10.007_bib9","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1101\/gad.1039703","article-title":"The ADAMs family of metalloproteases: multidomain proteins with multiple functions","volume":"17","author":"Seals","year":"2003","journal-title":"Genes Dev."},{"key":"10.1016\/j.biochi.2010.10.007_bib10","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1016\/j.jmb.2007.07.047","article-title":"Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains","volume":"373","author":"Gerhardt","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.biochi.2010.10.007_bib11","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1038\/sj.emboj.7601131","article-title":"Crystal structures of VAP1 reveal ADAMs\u2019 MDC domain architecture and its unique C-shaped scaffold","volume":"25","author":"Takeda","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2010.10.007_bib12","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/j.febslet.2007.04.057","article-title":"Crystal structures of catrocollastatin\/VAP2B reveal a dynamic, modular architecture of ADAM\/adamalysin\/reprolysin family proteins","volume":"581","author":"Igarashi","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2010.10.007_bib13","doi-asserted-by":"crossref","first-page":"5859","DOI":"10.1016\/j.febslet.2007.11.062","article-title":"Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases","volume":"581","author":"Takeda","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2010.10.007_bib14","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/0041-0101(86)90094-2","article-title":"Comparison of immunological, biochemical and biophysical properties of three hemorrhagic factors isolated from the venom of Bothrops jararaca (jararaca)","volume":"24","author":"Assakura","year":"1986","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2010.10.007_bib15","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1016\/j.bbrc.2004.08.012","article-title":"Activation of \u03b1M\u03b22-mediated phagocytosis by HF3, a P-III class metalloproteinase isolated from the venom of Bothrops jararaca","volume":"322","author":"Silva","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2010.10.007_bib16","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1042\/BJ20050483","article-title":"Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor","volume":"391","author":"Serrano","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2010.10.007_bib17","doi-asserted-by":"crossref","first-page":"39746","DOI":"10.1074\/jbc.M604855200","article-title":"The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: role in substrate targeting","volume":"281","author":"Serrano","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2010.10.007_bib18","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1111\/j.1742-4658.2007.05895.x","article-title":"Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation","volume":"274","author":"Serrano","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2010.10.007_bib19","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.abb.2006.10.010","article-title":"Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain","volume":"457","author":"Pinto","year":"2006","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2010.10.007_bib20","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1016\/j.febslet.2008.10.034","article-title":"Activation of leukocyte rolling by the cysteine-rich domain and the hyper-variable region of HF3, a snake venom hemorrhagic metalloproteinase","volume":"582","author":"Menezes","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2010.10.007_bib21","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1016\/j.toxicon.2009.02.019","article-title":"Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like\/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom","volume":"53","author":"Oliveira","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2010.10.007_bib22","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.biochi.2010.10.007_bib23","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0003-2697(81)90281-5","article-title":"\u2018\u2018Western blotting\u2019\u2019: electrophoretic transfer of proteins from sodium dodecyl sulfate\u2013polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A","volume":"112","author":"Burnette","year":"1981","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.biochi.2010.10.007_bib24","series-title":"Solid Phase Peptide Synthesis \u2013 A Practical Approach","author":"Atherton","year":"1989"},{"key":"10.1016\/j.biochi.2010.10.007_bib25","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1111\/j.1365-2141.1972.tb08800.x","article-title":"Preparations of suspensions of washed platelet from humans","volume":"22","author":"Mustard","year":"1972","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.biochi.2010.10.007_bib26","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1172\/JCI104970","article-title":"Platelet sequestration in man. I. Methods","volume":"43","author":"Aster","year":"1964","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.biochi.2010.10.007_bib27","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.toxicon.2008.08.021","article-title":"The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups","volume":"52","author":"Muniz","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2010.10.007_bib28","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein modelling by satisfaction of spatial restraints","volume":"234","author":"Sali","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.biochi.2010.10.007_bib29","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J. Appl. Cryst."},{"key":"10.1016\/j.biochi.2010.10.007_bib30","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1126\/science.1853201","article-title":"A method to identify protein sequences that fold into a known tridimensional structure","volume":"253","author":"Bowie","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.biochi.2010.10.007_bib31","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/0263-7855(90)80070-V","article-title":"WhatIF: a molecular modelling and drug design program","volume":"8","author":"Vriend","year":"1990","journal-title":"J. Mol. Graph."},{"key":"10.1016\/j.biochi.2010.10.007_bib32","first-page":"2126","article-title":"Coot: model-building tools for molecular graphics","volume":"D60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr."},{"key":"10.1016\/j.biochi.2010.10.007_bib33","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0014-5793(03)00799-3","article-title":"Identification of sites in the cysteine-rich domain of the class P-III snake venom metalloproteinases responsible for inhibition of platelet function","volume":"549","author":"Kamiguti","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2010.10.007_bib34","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0960-9822(95)00124-2","article-title":"Integrin-ligand binding. Do integrins use a \u2019MIDAS touch\u2019 to grasp an Asp?","volume":"5","author":"Bergelson","year":"1995","journal-title":"Curr. Biol."},{"key":"10.1016\/j.biochi.2010.10.007_bib35","doi-asserted-by":"crossref","first-page":"13094","DOI":"10.1074\/jbc.272.20.13094","article-title":"Function of disintegrin-like\/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists","volume":"272","author":"Jia","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2010.10.007_bib36","doi-asserted-by":"crossref","first-page":"11576","DOI":"10.1074\/jbc.275.16.11576","article-title":"Sequence-specific interaction between the disintegrin domain of mouse ADAM2 (fertilin beta) and murine eggs. Role of the alpha(6) integrin subunit","volume":"275","author":"Bigler","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2010.10.007_bib37","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1091\/mbc.12.4.809","article-title":"Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: role of b1 integrin-associated proteins CD9, CD81, and CD98","volume":"12","author":"Takahashi","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.biochi.2010.10.007_bib38","series-title":"Animal Toxins: State of the Art. Perspectives in Health an Biotechnology","first-page":"525","article-title":"Snake venom metalloproteinases. Structure, function and effects on snake bite pathology","author":"Moura-da-Silva","year":"2009"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908410003676?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908410003676?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:05:46Z","timestamp":1759539946000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908410003676"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,2]]},"references-count":38,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2011,2]]}},"alternative-id":["S0300908410003676"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2010.10.007","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2011,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Disintegrin-like\/cysteine-rich domains of the reprolysin HF3: Site-directed mutagenesis reveals essential role of specific residues","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2010.10.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}]}}