{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T06:49:19Z","timestamp":1789195759295,"version":"build-2803163510"},"reference-count":46,"publisher":"Elsevier BV","issue":"12","license":[{"start":{"date-parts":[[2014,12,1]],"date-time":"2014-12-01T00:00:00Z","timestamp":1417392000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,12,1]],"date-time":"2014-12-01T00:00:00Z","timestamp":1417392000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001823","name":"Ministerstvo \u0160kolstv\u00ed, Ml\u00e1de\u017ee a T\u011blov\u00fdchovy","doi-asserted-by":"publisher","award":["RVO 61388963"],"award-info":[{"award-number":["RVO 61388963"]}],"id":[{"id":"10.13039\/501100001823","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001824","name":"Grantov\u00e1 Agentura \u010cesk\u00e9 Republiky","doi-asserted-by":"publisher","award":["LH12023"],"award-info":[{"award-number":["LH12023"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001824","name":"Grantov\u00e1 Agentura \u010cesk\u00e9 Republiky","doi-asserted-by":"publisher","award":["LO1302"],"award-info":[{"award-number":["LO1302"]}],"id":[{"id":"10.13039\/501100001824","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006224","name":"Argonne National Laboratory","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006224","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004813","name":"Helmholtz-Zentrum f\u00fcr Umweltforschung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004813","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000062","name":"Bibliographical Society of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000062","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Structure"],"published-print":{"date-parts":[[2014,12]]},"DOI":"10.1016\/j.str.2014.09.015","type":"journal-article","created":{"date-parts":[[2014,11,16]],"date-time":"2014-11-16T20:12:56Z","timestamp":1416168776000},"page":"1786-1798","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":34,"title":["Activation Route of the Schistosoma mansoni Cathepsin B1 Drug Target: Structural Map with a Glycosaminoglycan Switch"],"prefix":"10.1016","volume":"22","author":[{"given":"Ad\u00e9la","family":"J\u00edlkov\u00e1","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Horn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavl\u00edna","family":"\u0158ez\u00e1\u010dov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucie","family":"Mare\u0161ov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pavla","family":"Fajtov\u00e1","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ji\u0159\u00ed","family":"Brynda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ji\u0159\u00ed","family":"Vondr\u00e1\u0161ek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James\u00a0H.","family":"McKerrow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Conor\u00a0R.","family":"Caffrey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Mare\u0161","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.str.2014.09.015_bib1","doi-asserted-by":"crossref","first-page":"e14","DOI":"10.1371\/journal.pmed.0040014","article-title":"Schistosomiasis mansoni: novel chemotherapy using a cysteine protease inhibitor","volume":"4","author":"Abdulla","year":"2007","journal-title":"PLoS Med."},{"key":"10.1016\/j.str.2014.09.015_bib2","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1074\/jbc.M003820200","article-title":"Cathepsin B activity regulation. Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation","volume":"276","author":"Almeida","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib3","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1515\/BC.2006.130","article-title":"Production and processing of a recombinant Fasciola hepatica cathepsin B-like enzyme (FhcatB1) reveals potential processing mechanisms in the parasite","volume":"387","author":"Beckham","year":"2006","journal-title":"Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib4","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1006\/bbrc.2000.3553","article-title":"The slow-binding inhibition of cathepsin K by its propeptide","volume":"276","author":"Billington","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.str.2014.09.015_bib5","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1006\/abio.1997.2494","article-title":"Quantitation of proteoglycans as glycosaminoglycans in biological fluids using an alcian blue dot blot analysis","volume":"256","author":"Bj\u00f6rnsson","year":"1998","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.str.2014.09.015_bib6","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0166-6851(97)00098-4","article-title":"Proteolytic degradation of host hemoglobin by schistosomes","volume":"89","author":"Brindley","year":"1997","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.str.2014.09.015_bib7","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.cbpa.2007.05.031","article-title":"Chemotherapy of schistosomiasis: present and future","volume":"11","author":"Caffrey","year":"2007","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib8","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1007\/s004360050310","article-title":"Cathepsin B-like activity predominates over cathepsin L-like activity in adult Schistosoma mansoni and S. japonicum","volume":"83","author":"Caffrey","year":"1997","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.str.2014.09.015_bib9","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1097\/QCO.0b013e328349156f","article-title":"Schistosomiasis: from drug deployment to drug development","volume":"24","author":"Caffrey","year":"2011","journal-title":"Curr. Opin. Infect. Dis."},{"key":"10.1016\/j.str.2014.09.015_bib10","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/S0014-5793(99)01798-6","article-title":"Identification of a cDNA encoding an active asparaginyl endopeptidase of Schistosoma mansoni and its expression in Pichia pastoris","volume":"466","author":"Caffrey","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.str.2014.09.015_bib11","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.pt.2004.03.004","article-title":"Blood \u2018n\u2019 guts: an update on schistosome digestive peptidases","volume":"20","author":"Caffrey","year":"2004","journal-title":"Trends Parasitol."},{"key":"10.1016\/j.str.2014.09.015_bib12","doi-asserted-by":"crossref","first-page":"33076","DOI":"10.1074\/jbc.M705761200","article-title":"Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions","volume":"282","author":"Caglic","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib13","doi-asserted-by":"crossref","first-page":"8988","DOI":"10.1074\/jbc.M110.126706","article-title":"Structure-activity analysis of cathepsin K\/chondroitin 4-sulfate interactions","volume":"286","author":"Cherney","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib14","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1016\/S0140-6736(13)61949-2","article-title":"Human schistosomiasis","volume":"383","author":"Colley","year":"2014","journal-title":"Lancet"},{"key":"10.1016\/j.str.2014.09.015_bib15","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0969-2126(96)00046-9","article-title":"Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion","volume":"4","author":"Cygler","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.str.2014.09.015_bib16","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0169-4758(96)80676-4","article-title":"Schistosome asparaginyl endopeptidase SM32 in hemoglobin digestion","volume":"12","author":"Dalton","year":"1996","journal-title":"Parasitol. Today (Regul. Ed.)"},{"key":"10.1016\/j.str.2014.09.015_bib17","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1017\/S0031182000077052","article-title":"Asparaginyl endopeptidase activity in adult Schistosoma mansoni","volume":"111","author":"Dalton","year":"1995","journal-title":"Parasitology"},{"key":"10.1016\/j.str.2014.09.015_bib18","doi-asserted-by":"crossref","first-page":"39316","DOI":"10.1074\/jbc.M607128200","article-title":"A multienzyme network functions in intestinal protein digestion by a platyhelminth parasite","volume":"281","author":"Delcroix","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib19","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1016\/j.chembiol.2005.10.005","article-title":"De novo design of alpha-amylase inhibitor: a small linear mimetic of macromolecular proteinaceous ligands","volume":"12","author":"Doleckov\u00e1-Maresov\u00e1","year":"2005","journal-title":"Chem. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib20","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1016\/j.bbrc.2007.12.062","article-title":"A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation","volume":"366","author":"Fairhead","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.str.2014.09.015_bib21","doi-asserted-by":"crossref","first-page":"12571","DOI":"10.1021\/bi00165a005","article-title":"Potent slow-binding inhibition of cathepsin B by its propeptide","volume":"31","author":"Fox","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2014.09.015_bib22","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1111\/j.1747-0285.2008.00741.x","article-title":"The structure of glycosaminoglycans and their interactions with proteins","volume":"72","author":"Gandhi","year":"2008","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.str.2014.09.015_bib23","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1074\/mcp.T100003-MCP200","article-title":"Chemical approaches for functionally probing the proteome","volume":"1","author":"Greenbaum","year":"2002","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.str.2014.09.015_bib24","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.chembiol.2009.09.009","article-title":"Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics","volume":"16","author":"Horn","year":"2009","journal-title":"Chem. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib25","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1021\/cb100411v","article-title":"Mapping the pro-peptide of the Schistosoma mansoni cathepsin B1 drug target: modulation of inhibition by heparin and design of mimetic inhibitors","volume":"6","author":"Horn","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib26","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1006\/bbrc.1995.2820","article-title":"Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in\u00a0vitro","volume":"217","author":"Ishidoh","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.str.2014.09.015_bib27","doi-asserted-by":"crossref","first-page":"35770","DOI":"10.1074\/jbc.M111.271304","article-title":"Structural basis for inhibition of cathepsin B drug target from the human blood fluke, Schistosoma mansoni","volume":"286","author":"J\u00edlkov\u00e1","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib28","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.molbiopara.2007.12.011","article-title":"Schistosome asparaginyl endopeptidase (legumain) is not essential for cathepsin B1 activation in\u00a0vivo","volume":"159","author":"Krautz-Peterson","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.str.2014.09.015_bib29","doi-asserted-by":"crossref","first-page":"28669","DOI":"10.1074\/jbc.M204004200","article-title":"Collagenase activity of cathepsin K depends on complex formation with chondroitin sulfate","volume":"277","author":"Li","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib30","doi-asserted-by":"crossref","first-page":"13030","DOI":"10.1016\/S0021-9258(18)99979-5","article-title":"Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in\u00a0vitro, are primarily unimolecular processes","volume":"269","author":"Mach","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib31","doi-asserted-by":"crossref","first-page":"13955","DOI":"10.1074\/jbc.272.21.13955","article-title":"Autocatalytic activation of human cathepsin K","volume":"272","author":"McQueney","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib32","doi-asserted-by":"crossref","first-page":"4478","DOI":"10.1074\/jbc.273.8.4478","article-title":"Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in\u00a0vitro","volume":"273","author":"M\u00e9nard","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib33","doi-asserted-by":"crossref","first-page":"262","DOI":"10.3389\/fgene.2014.00262","article-title":"Deciphering the glycogenome of schistosomes","volume":"5","author":"Mickum","year":"2014","journal-title":"Front. Genet."},{"key":"10.1016\/j.str.2014.09.015_bib34","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1097\/JTO.0b013e3182286d41","article-title":"Serum heparan sulfate concentration is correlated with the failure of epidermal growth factor receptor tyrosine kinase inhibitor treatment in patients with lung adenocarcinoma","volume":"6","author":"Nishio","year":"2011","journal-title":"J.\u00a0Thorac. Oncol."},{"key":"10.1016\/j.str.2014.09.015_bib35","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1006\/jmbi.1997.1218","article-title":"Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen","volume":"271","author":"Podobnik","year":"1997","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib36","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1111\/j.1742-4658.2008.06815.x","article-title":"Autocatalytic processing of procathepsin B is triggered by proenzyme activity","volume":"276","author":"Pungercar","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.str.2014.09.015_bib37","doi-asserted-by":"crossref","first-page":"5017","DOI":"10.1021\/bi981950o","article-title":"The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide","volume":"38","author":"Quraishi","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.str.2014.09.015_bib38","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.chembiol.2004.11.020","article-title":"Structural insights into biological roles of protein-glycosaminoglycan interactions","volume":"12","author":"Raman","year":"2005","journal-title":"Chem. Biol."},{"key":"10.1016\/j.str.2014.09.015_bib39","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.molbiopara.2008.04.008","article-title":"A family of cathepsin B cysteine proteases expressed in the gut of the human hookworm, Necator americanus","volume":"160","author":"Ranjit","year":"2008","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.str.2014.09.015_bib40","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1126\/science.1229663","article-title":"Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an X-ray laser","volume":"339","author":"Redecke","year":"2013","journal-title":"Science"},{"key":"10.1016\/j.str.2014.09.015_bib41","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/S0014-5793(99)01302-2","article-title":"Autocatalytic processing of recombinant human procathepsin B is a bimolecular process","volume":"459","author":"Rozman","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.str.2014.09.015_bib42","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0166-6851(03)00194-4","article-title":"Functional expression and characterization of Schistosoma mansoni cathepsin B and its trans-activation by an endogenous asparaginyl endopeptidase","volume":"131","author":"Sajid","year":"2003","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.str.2014.09.015_bib43","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1515\/BC.2003.103","article-title":"Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases","volume":"384","author":"Serveau","year":"2003","journal-title":"Biol. Chem."},{"key":"10.1016\/j.str.2014.09.015_bib44","doi-asserted-by":"crossref","first-page":"7936","DOI":"10.1002\/anie.201208390","article-title":"Schistosomiasis chemotherapy","volume":"52","author":"Th\u00e9tiot-Laurent","year":"2013","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.str.2014.09.015_bib45","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.bbapap.2011.10.002","article-title":"Cysteine cathepsins: from structure, function and regulation to new frontiers","volume":"1824","author":"Turk","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.str.2014.09.015_bib46","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/j.febslet.2004.12.093","article-title":"Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans","volume":"579","author":"Vasiljeva","year":"2005","journal-title":"FEBS Lett."}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212614003220?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212614003220?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T02:29:50Z","timestamp":1760840990000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212614003220"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,12]]},"references-count":46,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2014,12]]}},"alternative-id":["S0969212614003220"],"URL":"https:\/\/doi.org\/10.1016\/j.str.2014.09.015","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2014,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Activation Route of the Schistosoma mansoni Cathepsin B1 Drug Target: Structural Map with a Glycosaminoglycan Switch","name":"articletitle","label":"Article Title"},{"value":"Structure","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.str.2014.09.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}