{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:31:17Z","timestamp":1791307877544,"version":"4.3.1"},"reference-count":43,"publisher":"Public Library of Science (PLoS)","issue":"1","license":[{"start":{"date-parts":[[2013,1,15]],"date-time":"2013-01-15T00:00:00Z","timestamp":1358208000000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0054104","type":"journal-article","created":{"date-parts":[[2013,1,15]],"date-time":"2013-01-15T22:23:13Z","timestamp":1358288593000},"page":"e54104","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":25,"title":["The structure of Human Microplasmin in Complex with Textilinin-1, an Aprotinin-like Inhibitor from the Australian Brown Snake"],"prefix":"10.1371","volume":"8","author":[{"given":"Emma-Karin I.","family":"Millers","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lambro A.","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geoff W.","family":"Birrell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul P.","family":"Masci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin F.","family":"Lavin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"de Jersey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luke W.","family":"Guddat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2013,1,15]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.1056\/NEJMoa0802395","article-title":"A comparison of aprotinin and lysine analogues in high-risk cardiac surgery","volume":"358","author":"DA Fergusson","year":"2008","journal-title":"N Engl J Med"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1056\/NEJMoa051379","article-title":"The risk associated with aprotinin in cardiac surgery","volume":"354","author":"DT Mangano","year":"2006","journal-title":"N Engl J Med"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1053\/j.jvca.2010.11.018","article-title":"The post-BART anti-fibrinolytic dilemma?","volume":"25","author":"WS Beattie","year":"2011","journal-title":"J Cardiothorac Vasc Anesth"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1038\/nrd1197","article-title":"Therapeutic potential of venom peptides","volume":"2","author":"RJ Lewis","year":"2003","journal-title":"Nat Rev Drug Discov"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M700094-MCP200","article-title":"Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia)","volume":"7","author":"BG Fry","year":"2008","journal-title":"Mol Cell Proteomics"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1074\/mcp.M600419-MCP200","article-title":"The diversity of bioactive proteins in Australian snake venoms","volume":"6","author":"GW Birrell","year":"2007","journal-title":"Mol Cell Proteomics"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1056\/NEJMoa0707768","article-title":"The effect of aprotinin on outcome after coronary-artery bypass grafting","volume":"358","author":"AD Shaw","year":"2008","journal-title":"N Engl J Med"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1056\/NEJMoa0707571","article-title":"Aprotinin during coronary-artery bypass grafting and risk of death","volume":"358","author":"S Schneeweiss","year":"2008","journal-title":"N Engl J Med"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1111\/j.1365-2141.2009.07605.x","article-title":"Textilinin-1, an alternative anti-bleeding agent to aprotinin: Importance of plasmin inhibition in controlling blood loss","volume":"145","author":"SM Flight","year":"2009","journal-title":"Br J Haematol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1159\/000092421","article-title":"Comparison of textilinin-1 with aprotinin as serine protease inhibitors and as antifibrinolytic agents","volume":"34","author":"S Flight","year":"2005","journal-title":"Pathophysiol Haemost Thromb"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.celrep.2012.02.012","article-title":"The X-ray crystal structure of full-length human plasminogen","volume":"1","author":"HP Law","year":"2012","journal-title":"Cell Rep"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1126\/science.281.5383.1662","article-title":"Crystal structure of the catalytic domain of human plasmin complexed with streptokinase","volume":"281","author":"X Wang","year":"1998","journal-title":"Science"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"41077","DOI":"10.1074\/jbc.M506766200","article-title":"Expression, crystallization, and three-dimensional structure of the catalytic domain of human plasma kallikrein","volume":"280","author":"J Tang","year":"2005","journal-title":"J Biol Chem"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of the active site in proteases. I. Papain","volume":"27","author":"I Schechter","year":"1967","journal-title":"Biochem Biophys Res Commun"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"3163","DOI":"10.1111\/j.1742-4658.2009.07034.x","article-title":"Crystal structure of textilinin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake <italic>Pseudonaja textilis<\/italic>","volume":"276","author":"EK Millers","year":"2009","journal-title":"FEBS J"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.jmb.2006.11.003","article-title":"Rigidification of a flexible protease inhibitor variant upon binding to trypsin","volume":"366","author":"WM Hanson","year":"2007","journal-title":"J Mol Biol"},{"key":"ref17","first-page":"479","article-title":"Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs","volume":"33","author":"H Fritz","year":"1983","journal-title":"Arzneimittelforschung"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0022-2836(73)90448-8","article-title":"Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region","volume":"77","author":"A R\u00fchlmann","year":"1973","journal-title":"J Mol Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1093\/protein\/12.3.243","article-title":"Structural and mutagenesis studies of Leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power","volume":"12","author":"JC Williams","year":"1999","journal-title":"Protein Eng"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1006\/jmbi.1999.3397","article-title":"Human plasminogen catalytic domain undergoes an unusual conformational change upon activation","volume":"295","author":"X Wang","year":"2000","journal-title":"J Mol Biol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"32989","DOI":"10.1074\/jbc.R109.027946","article-title":"Functional roles of human kallikrein-related peptidases","volume":"284","author":"G Sotiropoulou","year":"2009","journal-title":"J Biol Chem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1210\/er.2009-0034","article-title":"Kallikreins on steroids: structure, function, and hormonal regulation of prostate-specific antigen and the extended kallikrein locus","volume":"31","author":"MG Lawrence","year":"2010","journal-title":"Endocr Rev"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1213\/00000539-200002000-00005","article-title":"The significance of preformed aprotinin-specific antibodies in cardiosurgical patients","volume":"90","author":"AM Scheule","year":"2000","journal-title":"Anesth Analg"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1016\/j.athoracsur.2007.05.015","article-title":"Aprotinin and anaphylaxis: analysis of 12,403 exposures to aprotinin in cardiac surgery","volume":"84","author":"W Dietrich","year":"2007","journal-title":"Ann Thorac Surg"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1515\/bchm3.1989.370.2.677","article-title":"Immunological characterization of natural and semisynthetic aprotinin variants","volume":"370","author":"J Siekmann","year":"1989","journal-title":"Biol Chem Hoppe-Seyler"},{"key":"ref26","first-page":"368","article-title":"Evaluation and management of bleeding during cardiac surgery","volume":"4","author":"JH Levy","year":"2005","journal-title":"Curr Hematol Rep"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1111\/j.1749-6632.2001.tb03547.x","article-title":"Fibrin degradation products. A review of structures found <italic>in vitro<\/italic> and <italic>in vivo<\/italic>","volume":"936","author":"PJ Gaffney","year":"2001","journal-title":"Ann N Y Acad Sci"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1006\/jmbi.1998.2089","article-title":"Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity","volume":"282","author":"H Jing","year":"1998","journal-title":"J Mol Biol"},{"key":"ref29","first-page":"20","article-title":"Titration of trypsin, plasmin and thrombin with p-nitrophenyl-p&apos;-guanidinobenzoate HCl: A new active site titrant for trypsin Methods Enzymol","volume":"19","author":"TA Chase","year":"1970"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/0076-6879(70)19003-3","article-title":"Principles of active site titration of proteolytic enzymes","volume":"19","author":"FJ Kedzy","year":"1970","journal-title":"Methods Enzymol"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0003-2697(89)90602-7","article-title":"Calculation of protein extinction coefficients from amino acid sequence data","volume":"182","author":"SC Gill","year":"1989","journal-title":"Anal Biochem"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1046\/j.1365-2141.2002.03878.x","article-title":"A family of textilinin genes, two of which encode proteins with antihaemorrhagic properties","volume":"119","author":"I Filippovich","year":"2002","journal-title":"Br J Haematol"},{"key":"ref33","first-page":"201","article-title":"The behavior and significance of slow-binding enzyme inhibitors","volume":"61","author":"JF Morrison","year":"1988","journal-title":"Adv Enzymol Relat Areas Mol Biol"},{"key":"ref34","unstructured":"Burnham K, Anderson D (2002) Model selection and multimodal inference. ISBN 0\u2013387\u201395364\u20137."},{"key":"ref35","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"JW Pflugrath","year":"1999","journal-title":"Acta Crystallogr D"},{"key":"ref36","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":"Z Otwinowski","year":"1997","journal-title":"Methods in Enzymology: Macromolecular Crystallography, part A"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1107\/S0907444998012517","article-title":"Rapid automated molecular replacement by evolutionary search","volume":"55","author":"CR Kissinger","year":"1999","journal-title":"Acta Crystallogr D"},{"key":"ref38","first-page":"240","article-title":"Refinement of macromolecular structures by maximum likelihood method","volume":"D53","author":"GN Murshudov","year":"1997","journal-title":"Acta Cryst"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"PD Adams","year":"2010","journal-title":"Acta Crystallogr D"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"P Emsley","year":"2010","journal-title":"Acta Crystallogr D"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"VB Chen","year":"2010","journal-title":"Acta Crystallogr D"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0022-2836(71)90324-X","article-title":"The interpretation of protein structures: estimation of static accessibility","volume":"55","author":"B Lee","year":"1971","journal-title":"J Mol Biol"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1515\/BC.2006.082","article-title":"A comprehensive nomenclature for serine proteases with homology to tissue kallikreins","volume":"387","author":"A Lundwall","year":"2006","journal-title":"Biol Chem"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0054104","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,6,28]],"date-time":"2023-06-28T18:23:58Z","timestamp":1687976638000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0054104"}},"subtitle":[],"editor":[{"given":"Michael","family":"Massiah","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,1,15]]},"references-count":43,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2013,1,15]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0054104","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,1,15]]}}}