{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T03:28:51Z","timestamp":1767929331455,"version":"3.49.0"},"reference-count":26,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2013,9,1]],"date-time":"2013-09-01T00:00:00Z","timestamp":1377993600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Academia Sinica and the National Science Council"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2013,9]]},"DOI":"10.1016\/j.toxicon.2013.05.009","type":"journal-article","created":{"date-parts":[[2013,5,31]],"date-time":"2013-05-31T18:47:15Z","timestamp":1370026035000},"page":"140-146","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"special_numbering":"C","title":["Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors"],"prefix":"10.1016","volume":"71","author":[{"given":"Tsung-Lin","family":"Chou","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cheng-Heng","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kai-Fa","family":"Huang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew H.-J.","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2013.05.009_bib1","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.toxicon.2013.05.009_bib2","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/S0014-5793(97)01401-4","article-title":"2\u00a0\u00c5 X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode","volume":"418","author":"Cirilli","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/j.toxicon.2013.05.009_bib3","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1006\/jmbi.1998.2110","article-title":"Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus","volume":"283","author":"Gong","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.toxicon.2013.05.009_bib4","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0300-9084(00)01163-9","article-title":"Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage","volume":"82","author":"Gutierrez","year":"2000","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2013.05.009_bib5","first-page":"1041","article-title":"Characterization of three fibrinogenolytic proteases isolated from the venom of Taiwan habu (Trimeresurus mucrosquamatus)","volume":"31","author":"Huang","year":"1993","journal-title":"Biochem. Mol. Biol. Int."},{"key":"10.1016\/j.toxicon.2013.05.009_bib6","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1006\/bbrc.1995.2614","article-title":"Characterization of multiple metalloproteinases with fibrinogenolytic activity from the venom of Taiwan habu (Trimeresurus mucrosquamatus): protein microsequencing coupled with cDNA sequence analysis","volume":"216","author":"Huang","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2013.05.009_bib7","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1006\/bbrc.1998.9017","article-title":"Characterization of three endogenous peptide inhibitors for multiple metalloproteinases with fibrinogenolytic activity from the venom of Taiwan habu (Trimeresurus mucrosquamatus)","volume":"248","author":"Huang","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2013.05.009_bib8","doi-asserted-by":"crossref","first-page":"3047","DOI":"10.1046\/j.1432-1033.2002.02982.x","article-title":"Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray crystallography and synthetic inhibitor analogues","volume":"269","author":"Huang","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2013.05.009_bib9","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1107\/S090744490200656X","article-title":"The 1.35 \u00c5 crystal structure of cadmium-substituted TM-3, a snake venom metalloproteinase from Taiwan habu: elucidation of a TNF\u03b1 converting enzyme-like active site structure with a distorted octahedral geometry of cadmium","volume":"58","author":"Huang","year":"2002","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.toxicon.2013.05.009_bib10","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for building protein models in electron density maps and the location of errors in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1016\/j.toxicon.2013.05.009_bib11","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/BF01897766","article-title":"The isolation and amino acid sequences of new pyroglutamylpeptides from snake venoms","volume":"22","author":"Kato","year":"1966","journal-title":"Experientia"},{"key":"10.1016\/j.toxicon.2013.05.009_bib12","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1093\/oxfordjournals.jbchem.a021215","article-title":"Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis","volume":"119","author":"Kumasaka","year":"1996","journal-title":"J. Biochem."},{"key":"10.1016\/j.toxicon.2013.05.009_bib13","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. Crystallogr."},{"key":"10.1016\/j.toxicon.2013.05.009_bib14","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.toxicon.2006.12.003","article-title":"Ammodytase, a metalloprotease from Vipera ammodytes ammodytes venom, possesses strong fibrinolytic activity","volume":"49","author":"Leonardi","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2013.05.009_bib15","doi-asserted-by":"crossref","first-page":"6166","DOI":"10.1021\/bi9002315","article-title":"High-resolution crystal structure of the snake venom metalloproteinase BaP1 complexed with a peptidomimetic: insight into inhibitor binding","volume":"48","author":"Lingott","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2013.05.009_bib16","doi-asserted-by":"crossref","first-page":"2375","DOI":"10.1021\/cr950042j","article-title":"Recent advances in zinc enzymology","volume":"96","author":"Lipscomb","year":"1996","journal-title":"Chem. Rev."},{"key":"10.1016\/j.toxicon.2013.05.009_bib17","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.jsb.2005.09.006","article-title":"Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus","volume":"152","author":"Lou","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.toxicon.2013.05.009_bib18","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","article-title":"Snake venom metalloproteinases","volume":"62","author":"Markland","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2013.05.009_bib19","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1006\/jsbi.1999.4094","article-title":"XtalView\/Xfit \u2013 a versatile program for manipulating atomic coordinates and electron density","volume":"125","author":"McRee","year":"1999","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.toxicon.2013.05.009_bib20","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.toxicon.2004.10.009","article-title":"Presence of peptide inhibitors in rattlesnake venoms and their effects on endogenous metalloproteases","volume":"45","author":"Munekiyo","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2013.05.009_bib21","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1016\/S0041-0101(98)00084-1","article-title":"Citrate inhibition of snake venom proteases","volume":"36","author":"Odell","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2013.05.009_bib22","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2013.05.009_bib23","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1002\/pro.5560040502","article-title":"The metzincins-Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases","volume":"4","author":"St\u00f6cker","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.toxicon.2013.05.009_bib24","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.toxicon.2005.03.008","article-title":"A novel metalloprotease from Vipera lebetina venom induces human endothelial cell apoptosis","volume":"46","author":"Trummal","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2013.05.009_bib25","doi-asserted-by":"crossref","first-page":"8447","DOI":"10.1073\/pnas.91.18.8447","article-title":"Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)","volume":"91","author":"Zhang","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.toxicon.2013.05.009_bib26","doi-asserted-by":"crossref","first-page":"1834","DOI":"10.1107\/S0907444999010306","article-title":"Structure of acutolysin-C, a haemorrhagic toxin from the venom of Agkistrodon acutus, providing further evidence for the mechanism of the pH-dependent proteolytic reaction of zinc metalloproteinases","volume":"55","author":"Zhu","year":"1999","journal-title":"Acta Crystallogr. D"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010113001906?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010113001906?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,10,15]],"date-time":"2018-10-15T15:59:40Z","timestamp":1539619180000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010113001906"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,9]]},"references-count":26,"alternative-id":["S0041010113001906"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2013.05.009","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2013,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2013.05.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}