{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T14:57:56Z","timestamp":1791644276854,"version":"4.3.4"},"reference-count":75,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,8,1]],"date-time":"2023-08-01T00:00:00Z","timestamp":1690848000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,9,6]],"date-time":"2023-09-06T00:00:00Z","timestamp":1693958400000},"content-version":"vor","delay-in-days":36,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100008908","name":"University of Messina","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100008908","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["390713860"],"award-info":[{"award-number":["390713860"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2023,8]]},"DOI":"10.1016\/j.bioorg.2023.106587","type":"journal-article","created":{"date-parts":[[2023,5,3]],"date-time":"2023-05-03T20:51:12Z","timestamp":1683147072000},"page":"106587","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Influence of amino acid size at the P3 position of N-Cbz-tripeptide Michael acceptors targeting falcipain-2 and rhodesain for the treatment of malaria and human african trypanosomiasis"],"prefix":"10.1016","volume":"137","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8473-3321","authenticated-orcid":false,"given":"Santo","family":"Previti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta","family":"Ettari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carla","family":"Di Chio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jenny","family":"Legac","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Bogacz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Collin","family":"Zimmer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanja","family":"Schirmeister","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip J.","family":"Rosenthal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Zappal\u00e0","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2023.106587_b0005","doi-asserted-by":"crossref","first-page":"179","DOI":"10.3390\/microorganisms7060179","article-title":"Malaria: The Past and the Present","volume":"7","author":"Talapko","year":"2019","journal-title":"Microorganisms"},{"key":"10.1016\/j.bioorg.2023.106587_b0010","unstructured":"World Health Organization. Malaria. Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/malaria (accessed on Accessed November 18, 2022)."},{"key":"10.1016\/j.bioorg.2023.106587_b0015","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/S0140-6736(19)31097-9","article-title":"Mapping the global prevalence, incidence, and mortality of Plasmodium falciparum, 2000\u201317: a spatial and temporal modelling study","volume":"394","author":"Weiss","year":"2019","journal-title":"Lancet"},{"key":"10.1016\/j.bioorg.2023.106587_b0020","doi-asserted-by":"crossref","first-page":"e100","DOI":"10.1016\/S2542-5196(21)00296-5","article-title":"Optimising the deployment of vector control tools against malaria: a data-informed modelling study","volume":"6","author":"Sherrard-Smith","year":"2022","journal-title":"Lancet Planet. Health"},{"key":"10.1016\/j.bioorg.2023.106587_b0025","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1186\/s12936-019-2724-z","article-title":"The past, present and future of anti-malarial medicines","volume":"18","author":"Tse","year":"2019","journal-title":"Malar. J."},{"key":"10.1016\/j.bioorg.2023.106587_b0030","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a025619","article-title":"Antimalarial Drug Resistance: A Threat to Malaria Elimination","volume":"7","author":"Menard","year":"2017","journal-title":"Cold Spring Harb Perspect. Med."},{"key":"10.1016\/j.bioorg.2023.106587_b0035","doi-asserted-by":"crossref","first-page":"e209","DOI":"10.1016\/S2666-5247(20)30094-X","article-title":"Molecular surveillance of antimalarial partner drug resistance in sub-Saharan Africa: a spatial-temporal evidence mapping study","volume":"1","author":"Ehrlich","year":"2020","journal-title":"Lancet Microbe"},{"key":"10.1016\/j.bioorg.2023.106587_b0040","doi-asserted-by":"crossref","first-page":"e338","DOI":"10.1016\/S1473-3099(19)30261-0","article-title":"Antimalarial drug resistance in Africa: the calm before the storm?","volume":"19","author":"Conrad","year":"2019","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.bioorg.2023.106587_b0045","doi-asserted-by":"crossref","DOI":"10.3389\/fgene.2021.668574","article-title":"Chloroquine and Sulfadoxine-Pyrimethamine Resistance in Sub-Saharan Africa-A Review","volume":"12","author":"Roux","year":"2021","journal-title":"Front. Genet."},{"key":"10.1016\/j.bioorg.2023.106587_b0050","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1097\/QCO.0000000000000766","article-title":"Artemisinin and multidrug-resistant Plasmodium falciparum - a threat for malaria control and elimination","volume":"34","author":"Dhorda","year":"2021","journal-title":"Curr Opin Infect Dis"},{"key":"10.1016\/j.bioorg.2023.106587_b0055","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/S1473-3099(15)00487-9","article-title":"Dihydroartemisinin-piperaquine resistance in Plasmodium falciparum malaria in Cambodia: a multisite prospective cohort study","volume":"16","author":"Amaratunga","year":"2016","journal-title":"The Lancet. Infectious diseases"},{"key":"10.1016\/j.bioorg.2023.106587_b0060","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1016\/S1473-3099(21)00142-0","article-title":"Association of Plasmodium falciparum kelch13 R561H genotypes with delayed parasite clearance in Rwanda: an open-label, single-arm, multicentre, therapeutic efficacy study","volume":"21","author":"Uwimana","year":"2021","journal-title":"The Lancet. Infectious diseases"},{"key":"10.1016\/j.bioorg.2023.106587_b0065","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1056\/NEJMoa2101746","article-title":"Evidence of Artemisinin-Resistant Malaria in Africa","volume":"385","author":"Balikagala","year":"2021","journal-title":"The New England journal of medicine"},{"key":"10.1016\/j.bioorg.2023.106587_b0070","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/S0140-6736(09)60829-1","article-title":"Human African trypanosomiasis","volume":"375","author":"Brun","year":"2010","journal-title":"Lancet"},{"key":"10.1016\/j.bioorg.2023.106587_b0075","doi-asserted-by":"crossref","DOI":"10.3389\/fvets.2021.621699","article-title":"Epidemiology of trypanosomiasis in wildlife-implications for humans at the wildlife interface in Africa","volume":"8","author":"Kasozi","year":"2021","journal-title":"Front. Vet. Sci."},{"key":"10.1016\/j.bioorg.2023.106587_b0080","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1017\/S0031182020000645","article-title":"Human African trypanosomiasis: the current situation in endemic regions and the risks for non-endemic regions from imported cases","volume":"147","author":"Gao","year":"2020","journal-title":"Parasitology"},{"key":"10.1016\/j.bioorg.2023.106587_b0085","doi-asserted-by":"crossref","DOI":"10.3389\/fvets.2022.828111","article-title":"An Update on African Trypanocide Pharmaceutics and Resistance","volume":"9","author":"Kasozi","year":"2022","journal-title":"Front. Vet. Sci."},{"key":"10.1016\/j.bioorg.2023.106587_b0090","doi-asserted-by":"crossref","first-page":"e720","DOI":"10.1371\/journal.pntd.0000720","article-title":"NECT is next: implementing the new drug combination therapy for Trypanosoma brucei gambiense sleeping sickness","volume":"4","author":"Yun","year":"2010","journal-title":"PLoS neglected tropical diseases"},{"key":"10.1016\/j.bioorg.2023.106587_b0095","first-page":"658","article-title":"FDA approves first all-oral sleeping sickness drug","volume":"20","author":"Mullard","year":"2021","journal-title":"Nature reviews. Drug discovery"},{"key":"10.1016\/j.bioorg.2023.106587_b0100","first-page":"14","article-title":"The Drugs of Sleeping Sickness: Their Mechanisms of Action and Resistance, and a Brief History","volume":"5","author":"De Koning","year":"2020","journal-title":"Trop. Med. Infect. Dis."},{"key":"10.1016\/j.bioorg.2023.106587_b0105","doi-asserted-by":"crossref","first-page":"e0006512","DOI":"10.1371\/journal.pntd.0006512","article-title":"Cysteine proteases in protozoan parasites","volume":"12","author":"Siqueira-Neto","year":"2018","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bioorg.2023.106587_b0110","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1002\/med.20163","article-title":"Falcipain-2 inhibitors","volume":"30","author":"Ettari","year":"2010","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.bioorg.2023.106587_b0115","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2020.140362","article-title":"Falcipain cysteine proteases of malaria parasites: An update","volume":"1868","author":"Rosenthal","year":"2020","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"10.1016\/j.bioorg.2023.106587_b0120","doi-asserted-by":"crossref","first-page":"3010","DOI":"10.2174\/0929867327666200730215316","article-title":"Falcipain-2 and falcipain-3 inhibitors as promising antimalarial agents","volume":"28","author":"Ettari","year":"2020","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0125","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":"Kerr","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0130","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1186\/s12936-019-3043-0","article-title":"The complex of Plasmodium falciparum falcipain-2 protease with an (E)-chalcone-based inhibitor highlights a novel, small, molecule-binding site","volume":"18","author":"Machin","year":"2019","journal-title":"Malar. J."},{"key":"10.1016\/j.bioorg.2023.106587_b0135","doi-asserted-by":"crossref","first-page":"11503","DOI":"10.1073\/pnas.0600489103","article-title":"Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease","volume":"103","author":"Wang","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bioorg.2023.106587_b0140","doi-asserted-by":"crossref","first-page":"5637","DOI":"10.1021\/jm301424d","article-title":"Inhibition of rhodesain as a novel therapeutic modality for human African trypanosomiasis","volume":"56","author":"Ettari","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0145","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":"Nikolskaia","year":"2006","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bioorg.2023.106587_b0150","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1038\/s41467-017-00959-w","article-title":"Variant surface glycoprotein density defines an immune evasion threshold for African trypanosomes undergoing antigenic variation","volume":"8","author":"Pinger","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bioorg.2023.106587_b0155","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.2174\/1389557515666160509125243","article-title":"The inhibition of cysteine proteases rhodesain and TbCatB: a valuable approach to treat Human African Trypanosomiasis","volume":"16","author":"Ettari","year":"2016","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0160","doi-asserted-by":"crossref","first-page":"e701","DOI":"10.1371\/journal.pntd.0000701","article-title":"Crystal Structures of TbCatB and rhodesain, potential chemotherapeutic targets and major cysteine proteases of Trypanosoma brucei","volume":"4","author":"Kerr","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.bioorg.2023.106587_b0165","doi-asserted-by":"crossref","first-page":"25697","DOI":"10.1074\/jbc.M109.014340","article-title":"Vinyl sulfones as antiparasitic agents and a structural basis for drug design","volume":"284","author":"Kerr","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0170","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2021.100565","article-title":"Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes","volume":"296","author":"Johe","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0175","doi-asserted-by":"crossref","first-page":"3370","DOI":"10.1021\/acs.jmedchem.7b01870","article-title":"2 H-1,2,3-Triazole-based dipeptidyl nitriles: potent, selective, and trypanocidal rhodesain inhibitors by structure-based design","volume":"61","author":"Giroud","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0180","doi-asserted-by":"crossref","first-page":"7053","DOI":"10.1016\/j.bmc.2015.09.029","article-title":"Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation","volume":"23","author":"Ettari","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0185","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1016\/j.bmc.2015.02.062","article-title":"Identification of novel class of falcipain-2 inhibitors as potential antimalarial agents","volume":"23","author":"Chakka","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0190","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.3109\/14756366.2015.1108972","article-title":"Synthesis and biological evaluation of novel peptidomimetics as rhodesain inhibitors","volume":"31","author":"Ettari","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0195","doi-asserted-by":"crossref","first-page":"4624","DOI":"10.1016\/j.bmc.2018.07.015","article-title":"Antiprotozoal and cysteine proteases inhibitory activity of dipeptidyl enoates","volume":"26","author":"Royo","year":"2018","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0200","doi-asserted-by":"crossref","first-page":"4928","DOI":"10.1016\/j.bmc.2010.06.010","article-title":"Constrained peptidomimetics as antiplasmodial falcipain-2 inhibitors","volume":"18","author":"Bova","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0205","doi-asserted-by":"crossref","first-page":"299","DOI":"10.3109\/14756366.2014.920839","article-title":"Synthetic compounds from an in house library as inhibitors of falcipain-2 from Plasmodium falciparum","volume":"30","author":"Bertoldo","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0210","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1002\/cmdc.201402079","article-title":"Synthesis and biological evaluation of papain-family cathepsin L-like cysteine protease inhibitors containing a 1,4-benzodiazepine scaffold as antiprotozoal agents","volume":"9","author":"Ettari","year":"2014","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bioorg.2023.106587_b0215","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1002\/cmdc.202000158","article-title":"Development of novel benzodiazepine-based peptidomimetics as inhibitors of rhodesain from Trypanosoma brucei rhodesiense","volume":"15","author":"Di Chio","year":"2020","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bioorg.2023.106587_b0220","doi-asserted-by":"crossref","first-page":"3453","DOI":"10.1016\/j.bmcl.2016.06.047","article-title":"Development of novel 1,4-benzodiazepine-based Michael acceptors as antitrypanosomal agents","volume":"26","author":"Ettari","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2023.106587_b0225","doi-asserted-by":"crossref","first-page":"6911","DOI":"10.1021\/acs.jmedchem.7b00405","article-title":"Development of novel peptide-based Michael acceptors targeting rhodesain and falcipain-2 for the treatment of Neglected Tropical Diseases (NTDs)","volume":"60","author":"Previti","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0230","doi-asserted-by":"crossref","first-page":"10617","DOI":"10.1021\/acs.jmedchem.9b00908","article-title":"Optimization strategy of novel peptide-based Michael acceptors for the treatment of Human African Trypanosomiasis","volume":"62","author":"Ettari","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0235","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1021\/jm701141u","article-title":"Development of peptidomimetics with a vinyl sulfone warhead as irreversible falcipain-2 inhibitors","volume":"51","author":"Ettari","year":"2008","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0240","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1021\/jm900047j","article-title":"Novel peptidomimetics containing a vinyl ester moiety as highly potent and selective falcipain-2 inhibitors","volume":"52","author":"Ettari","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0245","doi-asserted-by":"crossref","first-page":"12322","DOI":"10.1021\/acs.jmedchem.1c01002","article-title":"Fluorovinylsulfones and -sulfonates as potent covalent reversible inhibitors of the trypanosomal cysteine protease rhodesain: structure-activity relationship, inhibition mechanism, metabolism, and in vivo studies","volume":"64","author":"Jung","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0250","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1172\/JCI115456","article-title":"Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase","volume":"88","author":"Rosenthal","year":"1991","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bioorg.2023.106587_b0255","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1006\/expr.1998.4386","article-title":"Cysteine proteinase inhibitors kill cultured bloodstream forms of Trypanosoma brucei brucei","volume":"91","author":"Troeberg","year":"1999","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.bioorg.2023.106587_b0260","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114328","article-title":"Development of novel dipeptide nitriles as inhibitors of rhodesain of Trypanosoma brucei rhodesiense","volume":"236","author":"Di Chio","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0265","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1039\/c1md00115a","article-title":"Peptidomimetic nitriles as selective inhibitors for the malarial cysteine protease falcipain-2","volume":"2","author":"Ehmke","year":"2011","journal-title":"Medchemcomm"},{"key":"10.1016\/j.bioorg.2023.106587_b0270","doi-asserted-by":"crossref","unstructured":"J.M. Coteron; D. Catterick; J. Castro; M.J. Chaparro; B. Diaz; E. Fernandez; S. Ferrer; F.J. Gamo; M. Gordo; J. Gut; L. de las Heras; J. Legac; M. Marco; J. Miguel; V. Munoz; E. Porras; J.C. de la Rosa; J.R. Ruiz; E. Sandoval; P. Ventosa; P.J. Rosenthal; J.M. Fiandor. Falcipain inhibitors: optimization studies of the 2-pyrimidinecarbonitrile lead series. J. Med. Chem. 53 (2010) 6129\u20136152.","DOI":"10.1021\/jm100556b"},{"key":"10.1016\/j.bioorg.2023.106587_b0275","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0924-8579(03)00096-7","article-title":"Improved trypanocidal activities of cathepsin L inhibitors","volume":"22","author":"Nkemgu","year":"2003","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.bioorg.2023.106587_b0280","doi-asserted-by":"crossref","first-page":"3810","DOI":"10.1128\/AAC.47.12.3810-3814.2003","article-title":"Antimalarial activities of novel synthetic cysteine protease inhibitors","volume":"47","author":"Lee","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bioorg.2023.106587_b0285","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1021\/acschembio.0c00911","article-title":"Warhead Reactivity Limits the Speed of Inhibition of the Cysteine Protease Rhodesain","volume":"16","author":"Johe","year":"2021","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.bioorg.2023.106587_b0290","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":"Dahl","year":"2005","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.bioorg.2023.106587_b0295","doi-asserted-by":"crossref","first-page":"10497","DOI":"10.1021\/acs.jmedchem.9b00683","article-title":"Can Cysteine Protease Cross-Class Inhibitors Achieve Selectivity?","volume":"62","author":"Cianni","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0300","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1002\/cmdc.202000360","article-title":"Peptidyl vinyl ketone irreversible inhibitors of rhodesain: modifications of the P2 fragment","volume":"15","author":"Maiorana","year":"2020","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bioorg.2023.106587_b0305","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114460","article-title":"New peptidomimetic rhodesain inhibitors with improved selectivity towards human cathepsins","volume":"238","author":"Jung","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0310","doi-asserted-by":"crossref","first-page":"1540","DOI":"10.1016\/j.bmcl.2018.03.069","article-title":"Peptidomimetic nitrile inhibitors of malarial protease falcipain-2 with high selectivity against human cathepsins","volume":"28","author":"Nizi","year":"2018","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2023.106587_b0315","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":"Stolze","year":"2012","journal-title":"Chem. Biol."},{"key":"10.1016\/j.bioorg.2023.106587_b0320","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":"Conroy","year":"2014","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0325","doi-asserted-by":"crossref","first-page":"e202201636","DOI":"10.1002\/chem.202201636","article-title":"Two Tags in One Probe: Combining Fluorescence- and Biotin-based Detection of the Trypanosomal Cysteine Protease Rhodesain","volume":"28","author":"Lemke","year":"2022","journal-title":"Chem. - Eur. J."},{"key":"10.1016\/j.bioorg.2023.106587_b0330","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1021\/acsmedchemlett.2c00084","article-title":"Development of urea bond-containing Michael acceptors as antitrypanosomal agents targeting rhodesain","volume":"13","author":"Previti","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2023.106587_b0335","doi-asserted-by":"crossref","first-page":"2952","DOI":"10.2174\/0929867328666210810125309","article-title":"Dual inhibition of parasitic targets: a valuable strategy to treat malaria and neglected tropical diseases","volume":"29","author":"Previti","year":"2022","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bioorg.2023.106587_b0340","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1006\/prep.2001.1416","article-title":"Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2","volume":"22","author":"Sijwali","year":"2001","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bioorg.2023.106587_b0345","doi-asserted-by":"crossref","first-page":"8332","DOI":"10.1021\/jacs.6b03052","article-title":"Quantum chemical-based protocol for the rational design of covalent inhibitors","volume":"138","author":"Schirmeister","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bioorg.2023.106587_b0350","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1021\/bi00534a031","article-title":"Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier","volume":"21","author":"Tian","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.bioorg.2023.106587_b0355","unstructured":"GraFit, Version 5.0.1.3; Erithacus Software Ltd.: London 2006."},{"key":"10.1016\/j.bioorg.2023.106587_b0360","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1016\/j.bmcl.2006.02.026","article-title":"Aziridine-2,3-dicarboxylate inhibitors targeting the major cysteine protease of Trypanosoma brucei as lead trypanocidal agents","volume":"16","author":"Vicik","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2023.106587_b0365","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/S0166-6851(96)02815-0","article-title":"Vectors for inducible expression of toxic gene products in bloodstream and procyclic Trypanosoma brucei","volume":"85","author":"Biebinger","year":"1997","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.bioorg.2023.106587_b0370","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/0035-9203(62)90088-3","article-title":"Antigenic analysis in the Trypanosoma brucei group, using the agglutination reaction","volume":"56","author":"Cunningham","year":"1962","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.bioorg.2023.106587_b0375","doi-asserted-by":"crossref","first-page":"3765","DOI":"10.3390\/molecules27123765","article-title":"Development of reduced peptide bond pseudopeptide Michael acceptors for the treatment of Human African Trypanosomiasis","volume":"27","author":"Previti","year":"2022","journal-title":"Molecules"}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206823002481?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206823002481?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T11:56:24Z","timestamp":1777463784000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206823002481"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,8]]},"references-count":75,"alternative-id":["S0045206823002481"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2023.106587","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2023,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Influence of amino acid size at the P3 position of N-Cbz-tripeptide Michael acceptors targeting falcipain-2 and rhodesain for the treatment of malaria and human african trypanosomiasis","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2023.106587","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"106587"}}