{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T00:39:44Z","timestamp":1791938384495,"version":"4.3.4"},"reference-count":163,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2018,8,23]],"date-time":"2018-08-23T00:00:00Z","timestamp":1534982400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"DOI":"10.1371\/journal.pntd.0006512","type":"journal-article","created":{"date-parts":[[2018,8,23]],"date-time":"2018-08-23T13:30:51Z","timestamp":1535031051000},"page":"e0006512","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":149,"title":["Cysteine proteases in protozoan parasites"],"prefix":"10.1371","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9574-8174","authenticated-orcid":true,"given":"Jair L.","family":"Siqueira-Neto","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anjan","family":"Debnath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura-Isobel","family":"McCall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean A.","family":"Bernatchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Momar","family":"Ndao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sharon L.","family":"Reed","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip J.","family":"Rosenthal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2018,8,23]]},"reference":[{"issue":"1","key":"ref1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0166-6851(01)00438-8","article-title":"Cysteine proteases of parasitic organisms","volume":"120","author":"M Sajid","year":"2002","journal-title":"Mol Biochem Parasitol"},{"issue":"12","key":"ref2","doi-asserted-by":"crossref","first-page":"5160","DOI":"10.1128\/AAC.49.12.5160-5161.2005","article-title":"A cysteine protease inhibitor protects dogs from cardiac damage during infection by Trypanosoma cruzi","volume":"49","author":"SC Barr","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"issue":"4","key":"ref3","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1084\/jem.188.4.725","article-title":"Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection","volume":"188","author":"JC Engel","year":"1998","journal-title":"J Exp Med"},{"issue":"9859","key":"ref4","doi-asserted-by":"crossref","first-page":"2095","DOI":"10.1016\/S0140-6736(12)61728-0","article-title":"Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010","volume":"380","author":"R Lozano","year":"2012","journal-title":"Lancet"},{"key":"ref5","author":"H Nakajima","year":"1998"},{"issue":"12","key":"ref6","doi-asserted-by":"crossref","first-page":"2772","DOI":"10.1128\/JCM.27.12.2772-2777.1989","article-title":"Thiol proteinase expression and pathogenicity of Entamoeba histolytica","volume":"27","author":"SL Reed","year":"1989","journal-title":"J Clin Microbiol"},{"issue":"2","key":"ref7","doi-asserted-by":"crossref","first-page":"838","DOI":"10.1128\/IAI.71.2.838-844.2003","article-title":"Entamoeba histolytica cysteine proteinases disrupt the polymeric structure of colonic mucin and alter its protective function","volume":"71","author":"D Moncada","year":"2003","journal-title":"Infect Immun"},{"issue":"25","key":"ref8","doi-asserted-by":"crossref","first-page":"22650","DOI":"10.1074\/jbc.M300142200","article-title":"Proteolysis of enteric cell villin by Entamoeba histolytica cysteine proteinases","volume":"278","author":"T Lauwaet","year":"2003","journal-title":"J Biol Chem"},{"issue":"2","key":"ref9","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1128\/CMR.13.2.318-331.2000","article-title":"Pathogenesis of intestinal amebiasis: from molecules to disease","volume":"13","author":"M Espinosa-Cantellano","year":"2000","journal-title":"Clin Microbiol Rev"},{"issue":"8\u20139","key":"ref10","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1016\/j.ijpara.2007.01.016","article-title":"Transcriptional and secretory responses of Entamoeba histolytica to mucins, epithelial cells and bacteria","volume":"37","author":"A Debnath","year":"2007","journal-title":"Int J Parasitol"},{"issue":"4","key":"ref11","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.parint.2008.04.013","article-title":"Degradation of human secretory IgA1 and IgA2 by Entamoeba histolytica surface-associated proteolytic activity","volume":"57","author":"RM Garcia-Nieto","year":"2008","journal-title":"Parasitol Int"},{"issue":"2","key":"ref12","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1086\/517388","article-title":"The neutral cysteine proteinase of Entamoeba histolytica degrades IgG and prevents its binding","volume":"177","author":"VQ Tran","year":"1998","journal-title":"J Infect Dis"},{"issue":"1","key":"ref13","doi-asserted-by":"crossref","first-page":"266","DOI":"10.4049\/jimmunol.155.1.266","article-title":"The extracellular neutral cysteine proteinase of Entamoeba histolytica degrades anaphylatoxins C3a and C5a","volume":"155","author":"SL Reed","year":"1995","journal-title":"J Immunol"},{"issue":"3","key":"ref14","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1046\/j.1365-2958.2000.02037.x","article-title":"Entamoeba histolytica cysteine proteinases with interleukin-1 beta converting enzyme (ICE) activity cause intestinal inflammation and tissue damage in amoebiasis","volume":"37","author":"Z Zhang","year":"2000","journal-title":"Mol Microbiol"},{"issue":"3","key":"ref15","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1128\/IAI.71.3.1274-1280.2003","article-title":"A surface amebic cysteine proteinase inactivates interleukin-18","volume":"71","author":"X Que","year":"2003","journal-title":"Infect Immun"},{"issue":"8","key":"ref16","doi-asserted-by":"crossref","first-page":"e1006592","DOI":"10.1371\/journal.ppat.1006592","article-title":"The macrophage cytoskeleton acts as a contact sensor upon interaction with Entamoeba histolytica to trigger IL-1beta secretion","volume":"13","author":"J St-Pierre","year":"2017","journal-title":"PLoS Pathog"},{"issue":"4","key":"ref17","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.parint.2008.07.002","article-title":"An Entamoeba cysteine peptidase specifically expressed during encystation","volume":"57","author":"F Ebert","year":"2008","journal-title":"Parasitol Int"},{"issue":"3","key":"ref18","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1111\/j.1365-2958.2009.06672.x","article-title":"Major cysteine peptidases of Entamoeba histolytica are required for aggregation and digestion of erythrocytes but are dispensable for phagocytosis and cytopathogenicity","volume":"72","author":"H Irmer","year":"2009","journal-title":"Mol Microbiol"},{"issue":"7","key":"ref19","doi-asserted-by":"crossref","first-page":"1130","DOI":"10.1128\/EC.00094-07","article-title":"Use of recombinant Entamoeba histolytica cysteine proteinase 1 to identify a potent inhibitor of amebic invasion in a human colonic model","volume":"6","author":"SG Melendez-Lopez","year":"2007","journal-title":"Eukaryot Cell"},{"issue":"9963","key":"ref20","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0140-6736(14)61682-2","article-title":"Global, regional, and national age-sex specific all-cause and cause-specific mortality for 240 causes of death, 1990\u20132013: a systematic analysis for the Global Burden of Disease Study 2013","volume":"385","author":"GBD Mortality","year":"2015","journal-title":"Lancet"},{"issue":"1","key":"ref21","doi-asserted-by":"crossref","first-page":"e1003053","DOI":"10.1371\/journal.ppat.1003053","article-title":"Determinants for the development of visceral leishmaniasis disease","volume":"9","author":"LI McCall","year":"2013","journal-title":"PLoS Pathog"},{"issue":"12","key":"ref22","doi-asserted-by":"crossref","first-page":"6794","DOI":"10.4049\/jimmunol.161.12.6794","article-title":"Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a Th1 response","volume":"161","author":"J Alexander","year":"1998","journal-title":"J Immunol"},{"issue":"3","key":"ref23","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1515\/bmc-2012-0054","article-title":"Papain-like peptidases: structure, function, and evolution","volume":"4","author":"M Novinec","year":"2013","journal-title":"Biomol Concepts"},{"issue":"1","key":"ref24","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":"V Turk","year":"2012","journal-title":"Biochim Biophys Acta"},{"issue":"2","key":"ref25","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/0014-5793(92)81382-V","article-title":"Characterization of a multi-copy gene for a major stage-specific cysteine proteinase of Leishmania mexicana","volume":"311","author":"AE Souza","year":"1992","journal-title":"FEBS Lett"},{"issue":"4","key":"ref26","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.mib.2004.06.010","article-title":"Cysteine peptidases as virulence factors of Leishmania","volume":"7","author":"JC Mottram","year":"2004","journal-title":"Curr Opin Microbiol"},{"issue":"1\u20132","key":"ref27","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0378-1119(01)00851-4","article-title":"Genomic organization and functional expression of differentially regulated cysteine protease genes of Leishmania donovani complex","volume":"282","author":"V Mundodi","year":"2002","journal-title":"Gene"},{"issue":"1\u20132","key":"ref28","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0166-6851(95)00113-F","article-title":"Isolation of lmcpc, a gene encoding a Leishmania mexicana cathepsin-B-like cysteine proteinase","volume":"73","author":"G Bart","year":"1995","journal-title":"Mol Biochem Parasitol"},{"issue":"14","key":"ref29","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1111\/j.1365-2958.1992.tb01365.x","article-title":"A developmentally regulated cysteine proteinase gene of Leishmania mexicana","volume":"6","author":"JC Mottram","year":"1992","journal-title":"Mol Microbiol"},{"issue":"22","key":"ref30","doi-asserted-by":"crossref","first-page":"14285","DOI":"10.1074\/jbc.272.22.14285","article-title":"The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences","volume":"272","author":"JC Mottram","year":"1997","journal-title":"J Biol Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1471-2199-6-3","article-title":"Role of Leishmania (Leishmania) chagasi amastigote cysteine protease in intracellular parasite survival: studies by gene disruption and antisense mRNA inhibition","volume":"6","author":"V Mundodi","year":"2005","journal-title":"BMC Mol Biol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1471-2199-7-42","article-title":"Studies on the CPA cysteine peptidase in the Leishmania infantum genome strain JPCM5","volume":"7","author":"H Denise","year":"2006","journal-title":"BMC Mol Biol"},{"issue":"12","key":"ref33","doi-asserted-by":"crossref","first-page":"6008","DOI":"10.1073\/pnas.93.12.6008","article-title":"Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors","volume":"93","author":"JC Mottram","year":"1996","journal-title":"P Natl Acad Sci USA"},{"issue":"6","key":"ref34","doi-asserted-by":"crossref","first-page":"3190","DOI":"10.1128\/IAI.71.6.3190-3195.2003","article-title":"Expression of multiple CPB genes encoding cysteine proteases is required for Leishmania mexicana virulence in vivo","volume":"71","author":"H Denise","year":"2003","journal-title":"Infect Immun"},{"issue":"5","key":"ref35","doi-asserted-by":"crossref","first-page":"3297","DOI":"10.4049\/jimmunol.173.5.3297","article-title":"Inhibition of lipopolysaccharide-induced macrophage IL-12 production by Leishmania mexicana amastigotes: the role of cysteine peptidases and the NF-kappaB signaling pathway","volume":"173","author":"P Cameron","year":"2004","journal-title":"J Immunol"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1242\/jcs.108.10.3219","article-title":"Intracellular Leishmania-Amazonensis Amastigotes Internalize and Degrade Mhc Class-Ii Molecules of Their Host-Cells","volume":"108","author":"SD Leao","year":"1995","journal-title":"J Cell Sci"},{"issue":"5","key":"ref37","doi-asserted-by":"crossref","first-page":"e1005658","DOI":"10.1371\/journal.ppat.1005658","article-title":"Cysteine Peptidase B Regulates Leishmania mexicana Virulence through the Modulation of GP63 Expression","volume":"12","author":"PA Casgrain","year":"2016","journal-title":"PLoS Pathog"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"e71","DOI":"10.1038\/cddis.2010.51","article-title":"Cathepsin B-like and cell death in the unicellular human pathogen Leishmania","volume":"1","author":"AK El-Fadili","year":"2010","journal-title":"Cell Death Dis"},{"issue":"11","key":"ref39","doi-asserted-by":"crossref","first-page":"e79951","DOI":"10.1371\/journal.pone.0079951","article-title":"Cathepsin B gene disruption induced Leishmania donovani proteome remodeling implies cathepsin B role in secretome regulation","volume":"8","author":"TK Gerbaba","year":"2013","journal-title":"PLoS ONE"},{"issue":"1\u20132","key":"ref40","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0166-6851(97)00072-8","article-title":"Cathepsin B-like cysteine proteinase-deficient mutants of Leishmania mexicana","volume":"88","author":"G Bart","year":"1997","journal-title":"Mol Biochem Parasitol"},{"issue":"5","key":"ref41","doi-asserted-by":"crossref","first-page":"3678","DOI":"10.1074\/jbc.M112.415372","article-title":"Distinct roles in autophagy and importance in infectivity of the two ATG4 cysteine peptidases of Leishmania major","volume":"288","author":"RA Williams","year":"2013","journal-title":"J Biol Chem"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3389\/fchem.2017.00013","article-title":"Revealing a Novel Otubain-Like Enzyme from Leishmania infantum with Deubiquitinating Activity toward K48-Linked Substrate","volume":"5","author":"CS Azevedo","year":"2017","journal-title":"Front Chem"},{"issue":"20","key":"ref43","doi-asserted-by":"crossref","first-page":"11015","DOI":"10.1073\/pnas.96.20.11015","article-title":"Cysteine protease inhibitors as chemotherapy: lessons from a parasite target","volume":"96","author":"PM Selzer","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"ref44","doi-asserted-by":"crossref","first-page":"e1626","DOI":"10.1371\/journal.pntd.0001626","article-title":"In vitro and in vivo activity of a palladacycle complex on Leishmania (Leishmania) amazonensis","volume":"6","author":"S Paladi Cde","year":"2012","journal-title":"PLoS Negl Trop Dis"},{"issue":"3","key":"ref45","doi-asserted-by":"crossref","first-page":"213","DOI":"10.3347\/kjp.2009.47.3.213","article-title":"A novel organotellurium compound (RT-01) as a new antileishmanial agent","volume":"47","author":"CB Lima","year":"2009","journal-title":"Korean J Parasitol"},{"issue":"11","key":"ref46","doi-asserted-by":"crossref","first-page":"e48780","DOI":"10.1371\/journal.pone.0048780","article-title":"In vitro and in vivo activity of an organic tellurium compound on Leishmania (Leishmania) chagasi","volume":"7","author":"IA Salerno Pimentel","year":"2012","journal-title":"PLoS ONE"},{"issue":"10","key":"ref47","doi-asserted-by":"crossref","first-page":"e77460","DOI":"10.1371\/journal.pone.0077460","article-title":"Identification of semicarbazones, thiosemicarbazones and triazine nitriles as inhibitors of Leishmania mexicana cysteine protease CPB","volume":"8","author":"J Schroder","year":"2013","journal-title":"PLoS ONE"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.biopha.2015.08.030","article-title":"Benzophenone derivatives as cysteine protease inhibitors and biological activity against Leishmania(L.) amazonensis amastigotes","volume":"75","author":"L de Almeida","year":"2015","journal-title":"Biomed Pharmacother"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1007\/978-1-4419-8414-2_6","article-title":"Cysteine peptidases of kinetoplastid parasites","volume":"712","author":"CR Caffrey","year":"2011","journal-title":"Adv Exp Med Biol"},{"issue":"7","key":"ref50","doi-asserted-by":"crossref","first-page":"e479","DOI":"10.1371\/journal.pntd.0000479","article-title":"Protease Activated Receptor Signaling Is Required for African Trypanosome Traversal of Human Brain Microvascular Endothelial Cells","volume":"3","author":"DJ Grab","year":"2009","journal-title":"PloS Negl Trop Dis"},{"issue":"10","key":"ref51","doi-asserted-by":"crossref","first-page":"2739","DOI":"10.1172\/JCI27798.","article-title":"Blood-brain barrier traversal by African trypanosomes requires calcium signaling induced by parasite cysteine protease","volume":"116","author":"OV Nikolskaia","year":"2006","journal-title":"J Clin Invest"},{"issue":"5","key":"ref52","doi-asserted-by":"crossref","first-page":"e1004130","DOI":"10.1371\/journal.ppat.1004130","article-title":"Cathepsin-L Can Resist Lysis by Human Serum in Trypanosoma brucei brucei","volume":"10","author":"S Alsford","year":"2014","journal-title":"PLoS Pathog"},{"issue":"7467","key":"ref53","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/nature12516","article-title":"Mechanism of Trypanosoma brucei gambiense resistance to human serum","volume":"501","author":"P Uzureau","year":"2013","journal-title":"Nature"},{"issue":"4","key":"ref54","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1111\/j.1365-2958.2007.05970.x","article-title":"Role of the Trypanosoma brucei natural cysteine peptidase inhibitor ICP in differentiation and virulence","volume":"66","author":"CC Santos","year":"2007","journal-title":"Mol Microbiol"},{"issue":"1","key":"ref55","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0166-6851(01)00368-1","article-title":"Active site mapping, biochemical properties and subcellular localization of rhodesain, the major cysteine protease of Trypanosoma brucei rhodesiense","volume":"118","author":"CR Caffrey","year":"2001","journal-title":"Mol Biochem Parasitol"},{"issue":"46","key":"ref56","doi-asserted-by":"crossref","first-page":"48426","DOI":"10.1074\/jbc.M402470200","article-title":"A cathepsin B-like protease is required for host protein degradation in Trypanosoma brucei","volume":"279","author":"ZB Mackey","year":"2004","journal-title":"J Biol Chem"},{"issue":"43","key":"ref57","doi-asserted-by":"crossref","first-page":"28934","DOI":"10.1074\/jbc.M805824200","article-title":"A Parasite Cysteine Protease Is Key to Host Protein Degradation and Iron Acquisition","volume":"283","author":"TC O'Brien","year":"2008","journal-title":"J Biol Chem"},{"issue":"43","key":"ref58","doi-asserted-by":"crossref","first-page":"28934","DOI":"10.1074\/jbc.M805824200","article-title":"A parasite cysteine protease is key to host protein degradation and iron acquisition","volume":"283","author":"TC O'Brien","year":"2008","journal-title":"J Biol Chem"},{"issue":"5","key":"ref59","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.ijpara.2012.03.009","article-title":"Trypanosoma brucei: chemical evidence that cathepsin L is essential for survival and a relevant drug target","volume":"42","author":"D Steverding","year":"2012","journal-title":"Int J Parasitol"},{"issue":"2","key":"ref60","doi-asserted-by":"crossref","first-page":"155","DOI":"10.2174\/1389450003349290","article-title":"Cysteine proteinases of trypanosome parasites: novel targets for chemotherapy","volume":"1","author":"CR Caffrey","year":"2000","journal-title":"Curr Drug Targets"},{"issue":"4","key":"ref61","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1006\/expr.1998.4381","article-title":"Trypanosoma brucei: killing of bloodstream forms in vitro and in vivo by the cysteine proteinase inhibitor Z-phe-ala-CHN2","volume":"91","author":"S Scory","year":"1999","journal-title":"Exp Parasitol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.exppara.2015.01.016","article-title":"Evaluation of trypanocidal activity of combinations of anti-sleeping sickness drugs with cysteine protease inhibitors","volume":"151\u2013152","author":"D Steverding","year":"2015","journal-title":"Exp Parasitol"},{"issue":"1","key":"ref63","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.bmcl.2016.11.036","article-title":"Evaluation of dipeptide nitriles as inhibitors of rhodesain, a major cysteine protease of Trypanosoma brucei","volume":"27","author":"T Schirmeister","year":"2017","journal-title":"Bioorg Med Chem Lett"},{"issue":"6","key":"ref64","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1002\/cmdc.201300112","article-title":"Optimization of triazine nitriles as rhodesain inhibitors: structure-activity relationships, bioisosteric imidazopyridine nitriles, and X-ray crystal structure analysis with human cathepsin L","volume":"8","author":"V Ehmke","year":"2013","journal-title":"ChemMedChem"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.pharmthera.2017.06.004","article-title":"Targeting cysteine proteases in trypanosomatid disease drug discovery","volume":"180","author":"LG Ferreira","year":"2017","journal-title":"Pharmacol Ther"},{"issue":"10115","key":"ref66","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0140-6736(17)31612-4","article-title":"Chagas disease","volume":"391","author":"JA Perez-Molina","year":"2017","journal-title":"Lancet"},{"issue":"4","key":"ref67","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.4049\/jimmunol.137.4.1336","article-title":"Trypanosoma cruzi: characterization and isolation of a 57\/51,000 m.w. surface glycoprotein (GP57\/51) expressed by epimastigotes and bloodstream trypomastigotes","volume":"137","author":"J Scharfstein","year":"1986","journal-title":"J Immunol"},{"issue":"24","key":"ref68","doi-asserted-by":"crossref","first-page":"3174","DOI":"10.2174\/092986709788802971","article-title":"Cruzipain, the major cysteine protease of Trypanosoma cruzi: a sulfated glycoprotein antigen as relevant candidate for vaccine development and drug target. A review","volume":"16","author":"VG Duschak","year":"2009","journal-title":"Curr Med Chem"},{"issue":"1","key":"ref69","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/j.1574-6968.1994.tb07265.x","article-title":"Effects of proteinase inhibitors on the growth and differentiation of Trypanosoma cruzi","volume":"124","author":"BM Franke de Cazzulo","year":"1994","journal-title":"FEMS Microbiol Lett"},{"issue":"1","key":"ref70","first-page":"1","article-title":"Cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi","volume":"378","author":"JJ Cazzulo","year":"1997","journal-title":"Biol Chem"},{"issue":"2","key":"ref71","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/0166-6851(92)90050-T","article-title":"Inhibitors of the major cysteinyl proteinase (GP57\/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi in vitro","volume":"52","author":"MN Meirelles","year":"1992","journal-title":"Mol Biochem Parasitol"},{"issue":"11","key":"ref72","doi-asserted-by":"crossref","first-page":"7411","DOI":"10.1016\/S0021-9258(18)42533-1","article-title":"The sequence, organization, and expression of the major cysteine protease (cruzain) from Trypanosoma cruzi","volume":"267","author":"AE Eakin","year":"1992","journal-title":"J Biol Chem"},{"issue":"2","key":"ref73","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1006\/jmbi.1994.0137","article-title":"The crystal structure of cruzain: a therapeutic target for Chagas' disease","volume":"247","author":"ME McGrath","year":"1995","journal-title":"J Mol Biol"},{"issue":"1","key":"ref74","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0166-6851(00)00237-1","article-title":"Altered expression of cruzipain and a cathepsin B-like target in a Trypanosoma cruzi cell line displaying resistance to synthetic inhibitors of cysteine-proteinases","volume":"109","author":"V Yong","year":"2000","journal-title":"Mol Biochem Parasitol"},{"issue":"3","key":"ref75","doi-asserted-by":"crossref","first-page":"479","DOI":"10.32604\/biocell.2006.30.479","article-title":"Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators","volume":"30","author":"G Kosec","year":"2006","journal-title":"Biocell"},{"issue":"11","key":"ref76","doi-asserted-by":"crossref","first-page":"e0006049","DOI":"10.1371\/journal.pntd.0006049","article-title":"The regulation of autophagy differentially affects Trypanosoma cruzi metacyclogenesis","volume":"11","author":"MC Vanrell","year":"2017","journal-title":"PLoS Negl Trop Dis"},{"issue":"16","key":"ref77","doi-asserted-by":"crossref","first-page":"5005","DOI":"10.1021\/jm9009229","article-title":"Divergent modes of enzyme inhibition in a homologous structure-activity series","volume":"52","author":"RS Ferreira","year":"2009","journal-title":"J Med Chem"},{"issue":"5","key":"ref78","doi-asserted-by":"crossref","first-page":"2666","DOI":"10.1128\/AAC.04601-14","article-title":"Synthesis of a sugar-based thiosemicarbazone series and structure-activity relationship versus the parasite cysteine proteases rhodesain, cruzain, and Schistosoma mansoni cathepsin B1","volume":"59","author":"NC Fonseca","year":"2015","journal-title":"Antimicrob Agents Chemother"},{"issue":"20","key":"ref79","doi-asserted-by":"crossref","first-page":"3527","DOI":"10.1016\/S0960-894X(03)00756-X","article-title":"Synthesis and evaluation of isatins and thiosemicarbazone derivatives against cruzain, falcipain-2 and rhodesain","volume":"13","author":"I Chiyanzu","year":"2003","journal-title":"Bioorg Med Chem Lett"},{"issue":"5","key":"ref80","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1111\/j.1365-2125.2012.04471.x","article-title":"Odanacatib, a selective cathepsin K inhibitor to treat osteoporosis: safety, tolerability, pharmacokinetics and pharmacodynamics\u2014results from single oral dose studies in healthy volunteers","volume":"75","author":"SA Stoch","year":"2013","journal-title":"Br J Clin Pharmacol"},{"issue":"2","key":"ref81","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1128\/AAC.01855-13","article-title":"Reversible cysteine protease inhibitors show promise for a Chagas disease cure","volume":"58","author":"M Ndao","year":"2014","journal-title":"Antimicrob Agents Chemother"},{"issue":"1","key":"ref82","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1021\/acsmedchemlett.5b00336","article-title":"Synthesis and Evaluation of Oxyguanidine Analogues of the Cysteine Protease Inhibitor WRR-483 against Cruzain","volume":"7","author":"BD Jones","year":"2016","journal-title":"ACS Med Chem Lett"},{"issue":"7","key":"ref83","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.drudis.2015.02.004","article-title":"Cruzain inhibitors: efforts made, current leads and a structural outlook of new hits","volume":"20","author":"K Martinez-Mayorga","year":"2015","journal-title":"Drug Discov Today"},{"issue":"5","key":"ref84","doi-asserted-by":"crossref","first-page":"e0004729","DOI":"10.1371\/journal.pntd.0004729","article-title":"Burden of Cryptosporidium Diarrheal Disease among Children < 24 Months of Age in Moderate\/High Mortality Regions of Sub-Saharan Africa and South Asia, Utilizing Data from the Global Enteric Multicenter Study (GEMS)","volume":"10","author":"SO Sow","year":"2016","journal-title":"PLoS Negl Trop Dis"},{"issue":"2","key":"ref85","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1586\/14787210.1.2.297","article-title":"A review of chemotherapeutic approaches to the treatment of cryptosporidiosi","volume":"1","author":"A Armson","year":"2003","journal-title":"Expert Rev Anti Infect Ther"},{"issue":"2","key":"ref86","article-title":"A Retrospective Cohort Study of an Outbreak of Cryptosporidiosis among Veterinary Students","volume":"4","author":"J Benschop","year":"2017","journal-title":"Vet Sci"},{"issue":"3","key":"ref87","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1056\/NEJM199407213310304","article-title":"A massive outbreak in Milwaukee of cryptosporidium infection transmitted through the public water supply","volume":"331","author":"WR Mac Kenzie","year":"1994","journal-title":"N Engl J Med"},{"issue":"4","key":"ref88","doi-asserted-by":"crossref","first-page":"426","DOI":"10.3201\/eid0904.020417","article-title":"Cost of illness in the 1993 waterborne Cryptosporidium outbreak, Milwaukee, Wisconsin","volume":"9","author":"PS Corso","year":"2003","journal-title":"Emerg Infect Dis"},{"issue":"5669","key":"ref89","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1126\/science.1094786","article-title":"Complete genome sequence of the apicomplexan, Cryptosporidium parvum","volume":"304","author":"MS Abrahamsen","year":"2004","journal-title":"Science"},{"issue":"2","key":"ref90","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1017\/S0031182008005350","article-title":"Cryptopain-1, a cysteine protease of Cryptosporidium parvum, does not require the pro-domain for folding","volume":"136","author":"BK Na","year":"2009","journal-title":"Parasitology"},{"issue":"12","key":"ref91","doi-asserted-by":"crossref","first-page":"6063","DOI":"10.1128\/AAC.00734-13","article-title":"A cysteine protease inhibitor rescues mice from a lethal Cryptosporidium parvum infection","volume":"57","author":"M Ndao","year":"2013","journal-title":"Antimicrob Agents Chemother"},{"issue":"5","key":"ref92","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/j.cell.2005.11.007","article-title":"A genomic and functional inventory of deubiquitinating enzymes","volume":"123","author":"SM Nijman","year":"2005","journal-title":"Cell"},{"issue":"4","key":"ref93","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1016\/j.parint.2014.03.005","article-title":"Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum","volume":"63","author":"HL Ju","year":"2014","journal-title":"Parasitol Int"},{"issue":"25","key":"ref94","doi-asserted-by":"crossref","first-page":"2435","DOI":"10.1056\/NEJMoa1606701","article-title":"Mapping Plasmodium falciparum Mortality in Africa between 1990 and 2015","volume":"375","author":"PW Gething","year":"2016","journal-title":"N Engl J Med"},{"key":"ref95","author":"TA Ghebreyesus","year":"2017"},{"key":"ref96","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1007\/978-1-4419-8414-2_3","article-title":"Falcipains and other cysteine proteases of malaria parasites","volume":"712","author":"PJ Rosenthal","year":"2011","journal-title":"Adv Exp Med Biol"},{"key":"ref97","first-page":"1907","article-title":"Handbook of Proteolytic Enzymes","author":"PJ Rosenthal","year":"2013"},{"issue":"16","key":"ref98","doi-asserted-by":"crossref","first-page":"2604","DOI":"10.1111\/febs.14130","article-title":"Proteases as antimalarial targets: strategies for genetic, chemical, and therapeutic validation","volume":"284","author":"E Deu","year":"2017","journal-title":"FEBS J"},{"key":"ref99","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1146\/annurev.micro.51.1.97","article-title":"Hemoglobin metabolism in the malaria parasite Plasmodium falciparum","volume":"51","author":"SE Francis","year":"1997","journal-title":"Annu Rev Microbiol"},{"issue":"19","key":"ref100","doi-asserted-by":"crossref","first-page":"12870","DOI":"10.1074\/jbc.M708949200","article-title":"Plasmodium food vacuole plasmepsins are activated by falcipains","volume":"283","author":"ME Drew","year":"2008","journal-title":"J Biol Chem"},{"issue":"13","key":"ref101","doi-asserted-by":"crossref","first-page":"4384","DOI":"10.1073\/pnas.0307720101","article-title":"Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum","volume":"101","author":"PS Sijwali","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"ref102","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.molbiopara.2006.06.013","article-title":"Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum","volume":"150","author":"PS Sijwali","year":"2006","journal-title":"Mol Biochem Parasitol"},{"issue":"10","key":"ref103","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1111\/j.1462-5822.2008.01176.x","article-title":"Malarial proteases and host cell egress: an 'emerging' cascade","volume":"10","author":"MJ Blackman","year":"2008","journal-title":"Cell Microbiol"},{"issue":"7","key":"ref104","doi-asserted-by":"crossref","first-page":"e1006453","DOI":"10.1371\/journal.ppat.1006453","article-title":"The Plasmodium falciparum pseudoprotease SERA5 regulates the kinetics and efficiency of malaria parasite egress from host erythrocytes","volume":"13","author":"CR Collins","year":"2017","journal-title":"PLoS Pathog"},{"issue":"45","key":"ref105","doi-asserted-by":"crossref","first-page":"37949","DOI":"10.1074\/jbc.M112.400820","article-title":"Proteolytic activation of the essential parasitophorous vacuole cysteine protease SERA6 accompanies malaria parasite egress from its host erythrocyte","volume":"287","author":"A Ruecker","year":"2012","journal-title":"J Biol Chem"},{"issue":"3","key":"ref106","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1038\/nchembio.70","article-title":"Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum","volume":"4","author":"S Arastu-Kapur","year":"2008","journal-title":"Nat Chem Biol"},{"issue":"3","key":"ref107","doi-asserted-by":"crossref","first-page":"e0193538","DOI":"10.1371\/journal.pone.0193538","article-title":"The cysteine protease dipeptidyl aminopeptidase 3 does not contribute to egress of Plasmodium falciparum from host red blood cells","volume":"13","author":"S Ghosh","year":"2018","journal-title":"PLoS ONE"},{"issue":"4","key":"ref108","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1038\/s41564-018-0111-0","article-title":"A protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells","volume":"3","author":"JA Thomas","year":"2018","journal-title":"Nat Microbiol"},{"issue":"5600","key":"ref109","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1126\/science.1077426","article-title":"A role for the protease falcipain 1 in host cell invasion by the human malaria parasite","volume":"298","author":"DC Greenbaum","year":"2002","journal-title":"Science"},{"issue":"1","key":"ref110","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1111\/j.1365-2958.2004.04108.x","article-title":"Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth","volume":"53","author":"S Eksi","year":"2004","journal-title":"Mol Microbiol"},{"issue":"23","key":"ref111","doi-asserted-by":"crossref","first-page":"8721","DOI":"10.1073\/pnas.0402738101","article-title":"Plasmodium falciparum cysteine protease falcipain-1 is not essential in erythrocytic stage malaria parasites","volume":"101","author":"PS Sijwali","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"11","key":"ref112","doi-asserted-by":"crossref","first-page":"e117","DOI":"10.1371\/journal.ppat.0020117","article-title":"Falstatin, a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion","volume":"2","author":"KC Pandey","year":"2006","journal-title":"PLoS Pathog"},{"issue":"1","key":"ref113","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1111\/j.1365-2958.2009.06639.x","article-title":"Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus","volume":"72","author":"I Russo","year":"2009","journal-title":"Mol Microbiol"},{"issue":"5","key":"ref114","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1073\/pnas.0806926106","article-title":"A calpain unique to alveolates is essential in Plasmodium falciparum and its knockdown reveals an involvement in pre-S-phase development","volume":"106","author":"I Russo","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"9","key":"ref115","doi-asserted-by":"crossref","first-page":"e12748","DOI":"10.1111\/cmi.12748","article-title":"Plasmodium falciparum OTU-like cysteine protease (PfOTU) is essential for apicoplast homeostasis and associates with noncanonical role of Atg8","volume":"19","author":"G Datta","year":"2017","journal-title":"Cell Microbiol"},{"issue":"1","key":"ref116","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1084\/jem.20040989","article-title":"The Plasmodium circumsporozoite protein is proteolytically processed during cell invasion","volume":"201","author":"A Coppi","year":"2005","journal-title":"J Exp Med"},{"issue":"9","key":"ref117","doi-asserted-by":"crossref","first-page":"e1006586","DOI":"10.1371\/journal.ppat.1006586","article-title":"Deletion of the rodent malaria ortholog for falcipain-1 highlights differences between hepatic and blood stage merozoites","volume":"13","author":"CS Hopp","year":"2017","journal-title":"PLoS Pathog"},{"issue":"3","key":"ref118","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1128\/AAC.01012-06","article-title":"Inhibition of Plasmodium falciparum oocyst production by membrane-permeant cysteine protease inhibitor E64d","volume":"51","author":"S Eksi","year":"2007","journal-title":"Antimicrob Agents Chemother"},{"issue":"10","key":"ref119","doi-asserted-by":"crossref","first-page":"3243","DOI":"10.1074\/mcp.M116.060681","article-title":"Comparative Proteomics and Functional Analysis Reveal a Role of Plasmodium falciparum Osmiophilic Bodies in Malaria Parasite Transmission","volume":"15","author":"P Suarez-Cortes","year":"2016","journal-title":"Mol Cell Proteomics"},{"issue":"2","key":"ref120","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.molbiopara.2004.11.009","article-title":"Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum","volume":"139","author":"EL Dahl","year":"2005","journal-title":"Mol Biochem Parasitol"},{"issue":"37","key":"ref121","doi-asserted-by":"crossref","first-page":"29000","DOI":"10.1074\/jbc.M004459200","article-title":"Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum","volume":"275","author":"BR Shenai","year":"2000","journal-title":"J Biol Chem"},{"issue":"3","key":"ref122","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.exppara.2005.10.007","article-title":"Plasmodium falciparum: biochemical characterization of the cysteine protease falcipain-2'","volume":"112","author":"N Singh","year":"2006","journal-title":"Exp Parasitol"},{"issue":"17","key":"ref123","doi-asserted-by":"crossref","first-page":"14910","DOI":"10.1074\/jbc.M109680200","article-title":"Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain","volume":"277","author":"PS Sijwali","year":"2002","journal-title":"J Biol Chem"},{"issue":"5","key":"ref124","doi-asserted-by":"crossref","first-page":"408","DOI":"10.2174\/156802612799362913","article-title":"Falcipain inhibition as a promising antimalarial target","volume":"12","author":"M Marco","year":"2012","journal-title":"Curr Top Med Chem"},{"issue":"3","key":"ref125","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1021\/jm8013663","article-title":"Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity","volume":"52","author":"ID Kerr","year":"2009","journal-title":"J Med Chem"},{"issue":"4","key":"ref126","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/S0968-0896(99)00004-8","article-title":"Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors","volume":"7","author":"JE Olson","year":"1999","journal-title":"Bioorg Med Chem"},{"issue":"16","key":"ref127","doi-asserted-by":"crossref","first-page":"6129","DOI":"10.1021\/jm100556b","article-title":"Falcipain inhibitors: optimization studies of the 2-pyrimidinecarbonitrile lead series","volume":"53","author":"JM Coteron","year":"2010","journal-title":"J Med Chem"},{"issue":"24","key":"ref128","doi-asserted-by":"crossref","first-page":"10557","DOI":"10.1021\/jm501439w","article-title":"Synthesis of gallinamide A analogues as potent falcipain inhibitors and antimalarials","volume":"57","author":"T Conroy","year":"2014","journal-title":"J Med Chem"},{"issue":"2","key":"ref129","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.parint.2017.12.005","article-title":"Inhibition of Plasmodium falciparum cysteine proteases by the sugarcane cystatin CaneCPI-4","volume":"67","author":"PMS Melo","year":"2018","journal-title":"Parasitol Int"},{"issue":"34","key":"ref130","doi-asserted-by":"crossref","first-page":"35236","DOI":"10.1074\/jbc.M404235200","article-title":"Selection of cysteine protease inhibitor-resistant malaria parasites is accompanied by amplification of falcipain genes and alteration in inhibitor transport","volume":"279","author":"A Singh","year":"2004","journal-title":"J Biol Chem"},{"issue":"28","key":"ref131","doi-asserted-by":"crossref","first-page":"11405","DOI":"10.1073\/pnas.1104063108","article-title":"Artemisinin activity against Plasmodium falciparum requires hemoglobin uptake and digestion","volume":"108","author":"N Klonis","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"9","key":"ref132","doi-asserted-by":"crossref","first-page":"2254","DOI":"10.1128\/AAC.42.9.2254","article-title":"Antimalarial synergy of cysteine and aspartic protease inhibitors","volume":"42","author":"A Semenov","year":"1998","journal-title":"Antimicrob Agents Chemother"},{"issue":"2","key":"ref133","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1128\/CMR.05013-11","article-title":"Epidemiology of and diagnostic strategies for toxoplasmosis","volume":"25","author":"F Robert-Gangneux","year":"2012","journal-title":"Clin Microbiol Rev"},{"issue":"4","key":"ref134","first-page":"e01188","article-title":"Toxoplasma gondii ingests and digests host cytosolic proteins","volume":"5","author":"Z Dou","year":"2014","journal-title":"MBio"},{"issue":"39","key":"ref135","doi-asserted-by":"crossref","first-page":"26839","DOI":"10.1074\/jbc.M109.003780","article-title":"Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl","volume":"284","author":"ET Larson","year":"2009","journal-title":"J Biol Chem"},{"issue":"2","key":"ref136","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1128\/AAC.01059-06","article-title":"Cysteine protease inhibitors block Toxoplasma gondii microneme secretion and cell invasion","volume":"51","author":"CF Teo","year":"2007","journal-title":"Antimicrob Agents Chemother"},{"issue":"7","key":"ref137","doi-asserted-by":"crossref","first-page":"4994","DOI":"10.1074\/jbc.M606764200","article-title":"Cathepsin Cs are key for the intracellular survival of the protozoan parasite, Toxoplasma gondii","volume":"282","author":"X Que","year":"2007","journal-title":"J Biol Chem"},{"key":"ref138","doi-asserted-by":"crossref","first-page":"17096","DOI":"10.1038\/nmicrobiol.2017.96","article-title":"Toxoplasma depends on lysosomal consumption of autophagosomes for persistent infection","volume":"2","author":"M Di Cristina","year":"2017","journal-title":"Nat Microbiol"},{"key":"ref139","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/1471-2164-8-170","article-title":"The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes","volume":"8","author":"M Tillack","year":"2007","journal-title":"BMC Genomics"},{"issue":"28","key":"ref140","doi-asserted-by":"crossref","first-page":"25791","DOI":"10.1074\/jbc.M202659200","article-title":"The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing","volume":"277","author":"X Que","year":"2002","journal-title":"J Biol Chem"},{"issue":"1","key":"ref141","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.molbiopara.2008.11.012","article-title":"The cathepsin L of Toxoplasma gondii (TgCPL) and its endogenous macromolecular inhibitor, toxostatin","volume":"164","author":"R Huang","year":"2009","journal-title":"Mol Biochem Parasitol"},{"issue":"5","key":"ref142","doi-asserted-by":"crossref","first-page":"2915","DOI":"10.1128\/IAI.72.5.2915-2921.2004","article-title":"Toxopain-1 is critical for infection in a novel chicken embryo model of congenital toxoplasmosis","volume":"72","author":"X Que","year":"2004","journal-title":"Infect Immun"},{"issue":"5","key":"ref143","doi-asserted-by":"crossref","first-page":"3523","DOI":"10.1074\/jbc.M112.443697","article-title":"Non-canonical maturation of two papain-family proteases in Toxoplasma gondii","volume":"288","author":"Z Dou","year":"2013","journal-title":"J Biol Chem"},{"issue":"3","key":"ref144","doi-asserted-by":"crossref","first-page":"e0193982","DOI":"10.1371\/journal.pone.0193982","article-title":"Two key cathepsins, TgCPB and TgCPL, are targeted by the vinyl sulfone inhibitor K11777 in in vitro and in vivo models of toxoplasmosis","volume":"13","author":"JD Chaparro","year":"2018","journal-title":"PLoS ONE"},{"issue":"6","key":"ref145","doi-asserted-by":"crossref","first-page":"e12712","DOI":"10.1111\/cmi.12712","article-title":"Toxoplasma gondii autophagy-related protein ATG9 is crucial for the survival of parasites in their host","volume":"19","author":"HM Nguyen","year":"2017","journal-title":"Cell Microbiol"},{"key":"ref146","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1186\/1471-2334-13-207","article-title":"Toxoplasma gondii cathepsin proteases are undeveloped prominent vaccine antigens against toxoplasmosis","volume":"13","author":"G Zhao","year":"2013","journal-title":"BMC Infect Dis"},{"issue":"5","key":"ref147","doi-asserted-by":"crossref","first-page":"505","DOI":"10.3347\/kjp.2017.55.5.505","article-title":"DNA Vaccines Encoding Toxoplasma gondii Cathepsin C 1 Induce Protection against Toxoplasmosis in Mice","volume":"55","author":"Y Han","year":"2017","journal-title":"Korean J Parasitol"},{"issue":"7","key":"ref148","doi-asserted-by":"crossref","first-page":"e479","DOI":"10.1371\/journal.pntd.0000479","article-title":"Protease activated receptor signaling is required for African trypanosome traversal of human brain microvascular endothelial cells","volume":"3","author":"DJ Grab","year":"2009","journal-title":"PLoS Negl Trop Dis"},{"issue":"3\u20134","key":"ref149","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.exppara.2004.03.005","article-title":"Leishmania tropica: cysteine proteases are essential for growth and pathogenicity","volume":"106","author":"H Mahmoudzadeh-Niknam","year":"2004","journal-title":"Exp Parasitol"},{"issue":"16","key":"ref150","doi-asserted-by":"crossref","first-page":"11384","DOI":"10.1074\/jbc.M512307200","article-title":"Endosome sorting and autophagy are essential for differentiation and virulence of Leishmania major","volume":"281","author":"S Besteiro","year":"2006","journal-title":"J Biol Chem"},{"issue":"Pt 10","key":"ref151","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1242\/jcs.108.10.3219","article-title":"Intracellular Leishmania amazonensis amastigotes internalize and degrade MHC class II molecules of their host cells","volume":"108","author":"S De Souza Leao","year":"1995","journal-title":"J Cell Sci"},{"issue":"9","key":"ref152","doi-asserted-by":"crossref","first-page":"e298","DOI":"10.1371\/journal.pntd.0000298","article-title":"RNA interference of Trypanosoma brucei cathepsin B and L affects disease progression in a mouse model","volume":"2","author":"MH Abdulla","year":"2008","journal-title":"PLoS Negl Trop Dis"},{"issue":"2","key":"ref153","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0166-6851(97)00205-3","article-title":"Characterisation of a Trypanosoma cruzi acidic 30 kDa cysteine protease","volume":"91","author":"MP Garcia","year":"1998","journal-title":"Mol Biochem Parasitol"},{"issue":"8","key":"ref154","doi-asserted-by":"crossref","first-page":"890","DOI":"10.2460\/ajvr.77.8.890","article-title":"In vitro effects of cysteine protease inhibitors on Trichomonas foetus-induced cytopathic changes in porcine intestinal epithelial cells","volume":"77","author":"MK Tolbert","year":"2016","journal-title":"Am J Vet Res"},{"issue":"3","key":"ref155","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.ijantimicag.2011.09.026","article-title":"Effect of vinyl sulfone inhibitors of cysteine proteinases on Tritrichomonas foetus infection","volume":"39","author":"ER Cobo","year":"2012","journal-title":"Int J Antimicrob Agents"},{"issue":"9","key":"ref156","doi-asserted-by":"crossref","first-page":"e825","DOI":"10.1371\/journal.pntd.0000825","article-title":"In vitro and in vivo studies of the trypanocidal properties of WRR-483 against Trypanosoma cruzi","volume":"4","author":"YT Chen","year":"2010","journal-title":"PLoS Negl Trop Dis"},{"issue":"12","key":"ref157","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.chembiol.2012.09.020","article-title":"The antimalarial natural product symplostatin 4 is a nanomolar inhibitor of the food vacuole falcipains","volume":"19","author":"SC Stolze","year":"2012","journal-title":"Chem Biol"},{"issue":"4","key":"ref158","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1021\/jm901633v","article-title":"Nonpeptidic tetrafluorophenoxymethyl ketone cruzain inhibitors as promising new leads for Chagas disease chemotherapy","volume":"53","author":"K Brak","year":"2010","journal-title":"J Med Chem"},{"issue":"3","key":"ref159","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1016\/j.bmcl.2007.12.047","article-title":"The discovery of odanacatib (MK-0822), a selective inhibitor of cathepsin K","volume":"18","author":"JY Gauthier","year":"2008","journal-title":"Bioorg Med Chem Lett"},{"issue":"4","key":"ref160","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1007\/s00223-015-0051-0","article-title":"Cathepsin K Inhibition: A New Mechanism for the Treatment of Osteoporosis","volume":"98","author":"T Duong le","year":"2016","journal-title":"Calcif Tissue Int"},{"issue":"339","key":"ref161","doi-asserted-by":"crossref","first-page":"339ra69","DOI":"10.1126\/scitranslmed.aad3099","article-title":"The caspase-8 inhibitor emricasan combines with the SMAC mimetic birinapant to induce necroptosis and treat acute myeloid leukemia","volume":"8","author":"G Brumatti","year":"2016","journal-title":"Sci Transl Med"},{"issue":"6","key":"ref162","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/S0020-7519(99)00044-2","article-title":"Development of cysteine protease inhibitors as chemotherapy for parasitic diseases: insights on safety, target validation, and mechanism of action","volume":"29","author":"JH McKerrow","year":"1999","journal-title":"Int J Parasitol"},{"key":"ref163","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1146\/annurev.pathol.1.110304.100151","article-title":"Proteases in parasitic diseases","volume":"1","author":"JH McKerrow","year":"2006","journal-title":"Annu Rev Pathol"}],"container-title":["PLOS Neglected Tropical Diseases"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pntd.0006512","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,4]],"date-time":"2023-09-04T10:47:34Z","timestamp":1693824454000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0006512"}},"subtitle":[],"editor":[{"given":"Photini","family":"Sinnis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2018,8,23]]},"references-count":163,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2018,8,23]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pntd.0006512","relation":{},"ISSN":["1935-2735"],"issn-type":[{"value":"1935-2735","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,8,23]]}}}