{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,29]],"date-time":"2026-06-29T12:42:36Z","timestamp":1782736956770,"version":"3.54.5"},"reference-count":124,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,4,1]],"date-time":"2023-04-01T00:00:00Z","timestamp":1680307200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2023,4]]},"DOI":"10.1016\/j.ejmech.2023.115299","type":"journal-article","created":{"date-parts":[[2023,3,23]],"date-time":"2023-03-23T03:36:00Z","timestamp":1679542560000},"page":"115299","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"special_numbering":"C","title":["Falcipains: Biochemistry, target validation and structure-activity relationship studies of inhibitors as antimalarials"],"prefix":"10.1016","volume":"252","author":[{"given":"Jeevan","family":"Patra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Devika","family":"Rana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Smriti","family":"Arora","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mintu","family":"Pal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3611-7388","authenticated-orcid":false,"given":"Neeraj","family":"Mahindroo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2023.115299_bib1","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.ejmech.2023.115299_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.coph.2018.05.006","article-title":"The antimalarial pipeline","volume":"42","author":"Hooft van Huijsduijnen","year":"2018","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.ejmech.2023.115299_bib3","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1016\/S1473-3099(19)30391-3","article-title":"Determinants of dihydroartemisinin-piperaquine treatment failure in Plasmodium falciparum malaria in Cambodia, Thailand, and Vietnam: a prospective clinical, pharmacological, and genetic study","volume":"19","author":"van der Pluijm","year":"2019","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.ejmech.2023.115299_bib4","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 Proteomics"},{"key":"10.1016\/j.ejmech.2023.115299_bib5","series-title":"World Malaria Report 2021","year":"2021"},{"key":"10.1016\/j.ejmech.2023.115299_bib6","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nrmicro.2017.161","article-title":"Drug resistance in plasmodium","volume":"16","author":"Haldar","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.ejmech.2023.115299_bib7","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1586\/ecp.09.28","article-title":"Novel antimalarial drug targets: hope for new antimalarial drugs","volume":"2","author":"Alam","year":"2009","journal-title":"Expet Rev. Clin. Pharmacol."},{"key":"10.1016\/j.ejmech.2023.115299_bib8","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.ejmech.2023.115299_bib9","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S0022-3565(24)29564-1","article-title":"Primaquine-induced hemolytic anemia: formation and hemotoxicity of the arylhydroxylamine metabolite 6-methoxy-8-hydroxylaminoquinoline","volume":"297","author":"Bolchoz","year":"2001","journal-title":"J. Pharmacol. Exp. Therapeut."},{"key":"10.1016\/j.ejmech.2023.115299_bib10","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/j.drudis.2018.01.050","article-title":"Drug targeting of one or more aminoacyl-tRNA synthetase in the malaria parasite Plasmodium falciparum","volume":"23","author":"Manickam","year":"2018","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.ejmech.2023.115299_bib11","doi-asserted-by":"crossref","first-page":"4047","DOI":"10.2147\/IDR.S279433","article-title":"Antimalarial drug resistance and novel targets for antimalarial drug discovery","volume":"13","author":"Shibeshi","year":"2020","journal-title":"Infect. Drug Resist."},{"key":"10.1016\/j.ejmech.2023.115299_bib12","article-title":"Malaria","volume":"3","author":"Phillips","year":"2017","journal-title":"Nat. Rev. Dis. Prim."},{"key":"10.1016\/j.ejmech.2023.115299_bib13","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.1016\/j.bbagen.2014.02.009","article-title":"Malarial hemozoin: from target to tool","volume":"1840","author":"Coronado","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2023.115299_bib14","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1146\/annurev.biochem.71.090501.145453","article-title":"Biological roles of proteases in parasitic protozoa","volume":"71","author":"Klemba","year":"2002","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.ejmech.2023.115299_bib15","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1074\/jbc.M409740200","article-title":"The role of Plasmodium falciparum food vacuole plasmepsins","volume":"280","author":"Liu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib16","doi-asserted-by":"crossref","first-page":"32411","DOI":"10.1074\/jbc.274.45.32411","article-title":"Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum","volume":"274","author":"Eggleson","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib17","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.molbiopara.2010.08.004","article-title":"Biochemical characterization of Plasmodium falciparum dipeptidyl aminopeptidase 1","volume":"175","author":"Wang","year":"2011","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.ejmech.2023.115299_bib18","doi-asserted-by":"crossref","first-page":"35978","DOI":"10.1074\/jbc.M703643200","article-title":"Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum","volume":"282","author":"Dalal","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib19","doi-asserted-by":"crossref","first-page":"30817","DOI":"10.1074\/jbc.M704938200","article-title":"The M18 aspartyl aminopeptidase of the human malaria parasite Plasmodium falciparum","volume":"282","author":"Teuscher","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib20","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1084\/jem.173.4.961","article-title":"Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease","volume":"173","author":"Goldberg","year":"1991","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.ejmech.2023.115299_bib21","doi-asserted-by":"crossref","first-page":"4448","DOI":"10.1182\/blood.V87.10.4448.bloodjournal87104448","article-title":"Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites","volume":"87","author":"Gamboa de Dom\u00ednguez","year":"1996","journal-title":"Blood"},{"key":"10.1016\/j.ejmech.2023.115299_bib22","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":"Drew","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib23","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1146\/annurev.pathol.1.110304.100151","article-title":"Proteases in parasitic diseases","volume":"1","author":"McKerrow","year":"2006","journal-title":"Annu. Rev. Pathol."},{"key":"10.1016\/j.ejmech.2023.115299_bib24","doi-asserted-by":"crossref","first-page":"861","DOI":"10.18388\/abp.2004_3519","article-title":"Modes of inhibition of cysteine proteases","volume":"51","author":"Rzychon","year":"2004","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.ejmech.2023.115299_bib25","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1021\/cr950025u","article-title":"Cysteine proteases and their inhibitors","volume":"97","author":"Otto","year":"1997","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2023.115299_bib26","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1101\/gr.913403","article-title":"Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite","volume":"13","author":"Wu","year":"2003","journal-title":"Genome Res."},{"key":"10.1016\/j.ejmech.2023.115299_bib27","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":"Rosenthal","year":"2011","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.ejmech.2023.115299_bib28","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":"Shenai","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib29","doi-asserted-by":"crossref","first-page":"1560","DOI":"10.1172\/JCI113766","article-title":"A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum","volume":"82","author":"Rosenthal","year":"1988","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.ejmech.2023.115299_bib30","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1084\/jem.166.3.816","article-title":"Identification of three stage-specific proteinases of Plasmodium falciparum","volume":"166","author":"Rosenthal","year":"1987","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.ejmech.2023.115299_bib31","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0166-6851(92)90209-3","article-title":"Isolation and characterization of a cysteine proteinase gene of Plasmodium falciparum","volume":"51","author":"Rosenthal","year":"1992","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.ejmech.2023.115299_bib32","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":"Singh","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib33","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1042\/bj3600481","article-title":"Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3","volume":"360","author":"Sijwali","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115299_bib34","doi-asserted-by":"crossref","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":"Hopp","year":"2017","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ejmech.2023.115299_bib35","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0166-6851(01)00306-1","article-title":"Recombinant falcipain-2 cleaves erythrocyte membrane ankyrin and protein 4.1","volume":"116","author":"Dua","year":"2001","journal-title":"Mol. Biochem. Parasitol."},{"key":"10.1016\/j.ejmech.2023.115299_bib36","series-title":"Presented in Part in Abstract Form at the 43rd Annual Meeting of the","first-page":"1048","article-title":"Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development","volume":"vol. 100","author":"Hanspal","year":"2002"},{"key":"10.1016\/j.ejmech.2023.115299_bib37","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":"Sijwali","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2023.115299_bib38","doi-asserted-by":"crossref","first-page":"25425","DOI":"10.1074\/jbc.M603776200","article-title":"Structural and functional characterization of Falcipain-2, a hemoglobinase from the malarial parasite Plasmodium falciparum","volume":"281","author":"Hogg","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib39","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.ejmech.2023.115299_bib40","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1182\/blood-2002-01-0101","article-title":"Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development","volume":"100","author":"Hanspal","year":"2002","journal-title":"Blood"},{"key":"10.1016\/j.ejmech.2023.115299_bib41","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.ejmech.2023.115299_bib42","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.ejmech.2023.115299_bib43","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.ejmech.2023.115299_bib44","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.ejmech.2023.115299_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2019.115155","article-title":"Identification of antimalarial leads with dual falcipain-2 and falcipain-3 inhibitory activity","volume":"28","author":"Rana","year":"2020","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib46","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":"Coteron","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib47","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.ejmech.2023.115299_bib48","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.ejmech.2023.115299_bib49","doi-asserted-by":"crossref","first-page":"8840","DOI":"10.1073\/pnas.0601876103","article-title":"Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems","volume":"103","author":"Liu","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2023.115299_bib50","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2019.00394","article-title":"Structural insights into key plasmodium proteases as therapeutic drug targets","volume":"10","author":"Mishra","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.ejmech.2023.115299_bib51","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":"Greenbaum","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2023.115299_bib52","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1042\/BJ20060422","article-title":"Substrate mapping and inhibitor profiling of falcipain-2, falcipain-3 and berghepain-2: implications for peptidase anti-malarial drug discovery","volume":"399","author":"Ramjee","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2023.115299_bib53","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.ejmech.2023.115299_bib54","doi-asserted-by":"crossref","first-page":"9138","DOI":"10.1073\/pnas.0502368102","article-title":"The Plasmodium falciparum cysteine protease falcipain-2 captures its substrate, hemoglobin, via a unique motif","volume":"102","author":"Pandey","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ejmech.2023.115299_bib55","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.ejmech.2023.115299_bib56","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1093\/infdis\/jiy188","article-title":"Plasmodium falciparum falcipain-2a polymorphisms in southeast Asia and their association with artemisinin resistance","volume":"218","author":"Siddiqui","year":"2018","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.ejmech.2023.115299_bib57","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0014-5793(90)80022-B","article-title":"Inhibition of intraerythrocytic development of Plasmodium falciparum by proteinase inhibitors","volume":"259","author":"Rockett","year":"1990","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ejmech.2023.115299_bib58","doi-asserted-by":"crossref","first-page":"4639","DOI":"10.1021\/cr010182v","article-title":"Irreversible inhibitors of serine, cysteine, and threonine proteases","volume":"102","author":"Powers","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.ejmech.2023.115299_bib59","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.ejmech.2023.115299_bib60","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1128\/AAC.40.7.1600","article-title":"Antimalarial effects of vinyl sulfone cysteine proteinase inhibitors","volume":"40","author":"Rosenthal","year":"1996","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2023.115299_bib61","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":"Olson","year":"1999","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib62","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.ejmech.2023.115299_bib63","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.ejmech.2023.115299_bib64","doi-asserted-by":"crossref","first-page":"5562","DOI":"10.1021\/acs.jmedchem.9b00504","article-title":"Falcipain inhibitors based on the natural product gallinamide A are potent in vitro and in vivo antimalarials","volume":"62","author":"Stoye","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib65","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.ejmech.2023.115299_bib66","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.ejmech.2023.115299_bib67","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/cbic.201500312","article-title":"Peptide backbone composition and protease susceptibility: impact of modification type, position, and tandem substitution","volume":"17","author":"Werner","year":"2016","journal-title":"Chembiochem"},{"key":"10.1016\/j.ejmech.2023.115299_bib68","doi-asserted-by":"crossref","first-page":"963","DOI":"10.2174\/0929867024606731","article-title":"Converting a peptide into a drug: strategies to improve stability and bioavailability","volume":"9","author":"Adessi","year":"2002","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib69","doi-asserted-by":"crossref","first-page":"3064","DOI":"10.1021\/jm060405f","article-title":"Novel peptidomimetic cysteine protease inhibitors as potential antimalarial agents","volume":"49","author":"Micale","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib70","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1128\/AAC.47.1.154-160.2003","article-title":"Structure-activity relationships for inhibition of cysteine protease activity and development of Plasmodium falciparum by peptidyl vinyl sulfones","volume":"47","author":"Shenai","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2023.115299_bib71","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.ejmech.2023.115299_bib72","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.ejmech.2023.115299_bib73","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/S0169-4758(99)01622-1","article-title":"Chemotherapy for falciparum malaria: the armoury, the problems and the prospects","volume":"16","author":"Winstanley","year":"2000","journal-title":"Parasitol. Today"},{"key":"10.1016\/j.ejmech.2023.115299_bib74","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/S0223-5234(01)01245-4","article-title":"Synthesis of quinolinyl chalcones and evaluation of their antimalarial activity","volume":"36","author":"Dom\u00ednguez","year":"2001","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib75","doi-asserted-by":"crossref","first-page":"3249","DOI":"10.1016\/j.bmc.2005.02.037","article-title":"Design, synthesis and anti-plasmodial evaluation in vitro of new 4-aminoquinoline isatin derivatives","volume":"13","author":"Chiyanzu","year":"2005","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib76","doi-asserted-by":"crossref","first-page":"5605","DOI":"10.1016\/j.bmc.2006.04.035","article-title":"Application of multicomponent reactions to antimalarial drug discovery. Part 2: new antiplasmodial and antitrypanosomal 4-aminoquinoline gamma- and delta-lactams via a 'catch and release' protocol","volume":"14","author":"Musonda","year":"2006","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib77","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1080\/07391102.2002.10506783","article-title":"Homology modeling of falcipain-2: validation, de novo ligand design and synthesis of novel inhibitors","volume":"19","author":"Sabnis","year":"2002","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ejmech.2023.115299_bib78","doi-asserted-by":"crossref","first-page":"6505","DOI":"10.1016\/j.bmc.2009.08.013","article-title":"Novel 2H-isoquinolin-3-ones as antiplasmodial falcipain-2 inhibitors","volume":"17","author":"Micale","year":"2009","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib79","doi-asserted-by":"crossref","first-page":"39410","DOI":"10.1039\/C9RA06571G","article-title":"Quinoline-triazole hybrids inhibit falcipain-2 and arrest the development of Plasmodium falciparum at the trophozoite stage","volume":"9","author":"Singh","year":"2019","journal-title":"RSC Adv."},{"key":"10.1016\/j.ejmech.2023.115299_bib80","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104514","article-title":"Quinoline carboxamide core moiety-based compounds inhibit P. falciparumfalcipain-2: design, synthesis and antimalarial efficacy studies","volume":"108","author":"Singh","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib81","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.bbrc.2004.02.177","article-title":"Exploring the role of putative active site amino acids and pro-region motif of recombinant falcipain-2: a principal hemoglobinase of Plasmodium falciparum","volume":"317","author":"Kumar","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ejmech.2023.115299_bib82","doi-asserted-by":"crossref","first-page":"494","DOI":"10.3390\/molecules14010494","article-title":"2-amido-3-(1H-indol-3-yl)-N-substituted-propanamides as a new class of falcipain-2 inhibitors. 1. Design, synthesis, biological evaluation and binding model studies","volume":"14","author":"Zhu","year":"2009","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2023.115299_bib83","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.ejmech.2014.11.061","article-title":"Synthesis and structure activity-relationship studies of thiazolidinediones as antiplasmodial inhibitors of the Plasmodium falciparum cysteine protease falcipain-2","volume":"90","author":"Sharma","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib84","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1007\/s10822-013-9685-z","article-title":"Novel anti-Plasmodial hits identified by virtual screening of the ZINC database","volume":"27","author":"Mugumbate","year":"2013","journal-title":"J. Comput. Aided Mol. Des."},{"key":"10.1016\/j.ejmech.2023.115299_bib85","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":"Semenov","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2023.115299_bib86","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.bmc.2006.09.055","article-title":"Synthesis and biological evaluation of phenolic Mannich bases of benzaldehyde and (thio)semicarbazone derivatives against the cysteine protease falcipain-2 and a chloroquine resistant strain of Plasmodium falciparum","volume":"15","author":"Chipeleme","year":"2007","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib87","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1021\/jm00193a020","article-title":"2-Acetylpyridine thiosemicarbazones. 1. A new class of potential antimalarial agents","volume":"22","author":"Klayman","year":"1979","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib88","doi-asserted-by":"crossref","first-page":"4527","DOI":"10.3390\/molecules16064527","article-title":"Synthesis and antimalarial activity of novel dihydro-artemisinin derivatives","volume":"16","author":"Liu","year":"2011","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2023.115299_bib89","doi-asserted-by":"crossref","first-page":"4916","DOI":"10.1021\/jm5004528","article-title":"Tetraoxane\u2212Pyrimidine nitrile hybrids as dual stage antimalarials","volume":"57","author":"Oliveira","year":"2014","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib90","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1002\/cmdc.201300202","article-title":"An endoperoxide-based hybrid approach to deliver falcipain inhibitors inside malaria parasites","volume":"8","author":"Oliveira","year":"2013","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2023.115299_bib91","doi-asserted-by":"crossref","first-page":"785","DOI":"10.3390\/molecules14020785","article-title":"2-(3,4-dihydro-4-oxothieno[2,3-d]pyrimidin-2-ylthio) acetamides as a new class of falcipain-2 inhibitors. 3. design, synthesis and biological evaluation","volume":"14","author":"Zhu","year":"2009","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2023.115299_bib92","doi-asserted-by":"crossref","first-page":"6296","DOI":"10.1016\/j.bmc.2012.09.008","article-title":"Pyrido [1, 2-a] pyrimidin-4-ones as antiplasmodial falcipain-2 inhibitors","volume":"20","author":"Mane","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib93","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.bioorg.2018.01.007","article-title":"Synthesis of pyrazole acrylic acid based oxadiazole and amide derivatives as antimalarial and anticancer agents","volume":"77","author":"Verma","year":"2018","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib94","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2019.102986","article-title":"Targeting malaria and leishmaniasis: synthesis and pharmacological evaluation of novel pyrazole-1,3,4-oxadiazole hybrids. Part II","volume":"89","author":"Verma","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib95","doi-asserted-by":"crossref","first-page":"3636","DOI":"10.1016\/j.bmc.2016.06.003","article-title":"Bistacrine derivatives as new potent antimalarials","volume":"24","author":"Schmidt","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib96","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1007\/BF00932261","article-title":"Effects of microtubule inhibitors on protein synthesis in Plasmodium falciparum","volume":"79","author":"Bell","year":"1993","journal-title":"Parasitol. Res."},{"key":"10.1016\/j.ejmech.2023.115299_bib97","first-page":"351","article-title":"Synthesis of novel benzimidazole acrylonitriles for inhibition of Plasmodium falciparum growth by dual target inhibition","author":"Sharma","year":"2018","journal-title":"Arch. Pharm. (Weinheim)"},{"key":"10.1016\/j.ejmech.2023.115299_bib98","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/s41467-020-20629-8","article-title":"Multistage and transmission-blocking targeted antimalarials discovered from the open-source MMV Pandemic Response Box","volume":"12","author":"Reader","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2023.115299_bib99","doi-asserted-by":"crossref","first-page":"7318","DOI":"10.1021\/bi400852h","article-title":"Elucidating features that drive the design of selective antifolates using crystal structures of human dihydrofolate reductase","volume":"52","author":"Lamb","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2023.115299_bib100","doi-asserted-by":"crossref","first-page":"6467","DOI":"10.1016\/j.bmc.2017.10.017","article-title":"Discovery of new antimalarial agents: second-generation dual inhibitors against FP-2 and PfDHFR via fragments assembely","volume":"25","author":"Chen","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib101","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1016\/j.bmcl.2011.12.011","article-title":"Design and synthesis of small molecular dual inhibitor of falcipain-2 and dihydrofolate reductase as antimalarial agent","volume":"22","author":"Huang","year":"2012","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2023.115299_bib102","doi-asserted-by":"crossref","first-page":"2603","DOI":"10.1128\/AAC.01526-09","article-title":"Preclinical evaluation of the antifolate QN254, 5-chloro- N'6'-(2,5-dimethoxy-benzyl)-quinazoline-2,4,6-triamine, as an antimalarial drug candidate","volume":"54","author":"Nzila","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.ejmech.2023.115299_bib103","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1007\/s11427-019-1581-2","article-title":"Discovery of a natural fluorescent probe targeting the Plasmodium falciparum cysteine protease falcipain-2","volume":"63","author":"Zhu","year":"2020","journal-title":"Sci. China Life Sci."},{"key":"10.1016\/j.ejmech.2023.115299_bib104","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1021\/acs.jmedchem.7b01430","article-title":"Discovery of peptidomimetic antibody-drug conjugate linkers with enhanced protease specificity","volume":"61","author":"Wei","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib105","doi-asserted-by":"crossref","first-page":"6928","DOI":"10.1021\/acs.jmedchem.5b00746","article-title":"Development of N-(Functionalized benzoyl)-homocycloleucyl-glycinonitriles as potent cathepsin K inhibitors","volume":"58","author":"Bori\u0161ek","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib106","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jsb.2010.09.007","article-title":"Structural basis for reversible and irreversible inhibition of human cathepsin L by their respective dipeptidyl glyoxal and diazomethylketone inhibitors","volume":"173","author":"Shenoy","year":"2011","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.ejmech.2023.115299_bib107","doi-asserted-by":"crossref","first-page":"6890","DOI":"10.1016\/j.bmcl.2010.10.012","article-title":"Trifluoromethylphenyl as P2 for ketoamide-based cathepsin S inhibitors","volume":"20","author":"Cai","year":"2010","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.ejmech.2023.115299_bib108","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bmc.2018.10.017","article-title":"Active site mapping with peptidic substrates and inhibitors","volume":"27","author":"Schmitz","year":"2019","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib109","doi-asserted-by":"crossref","first-page":"2084","DOI":"10.1080\/07391102.2015.1108231","article-title":"Analysis of non-peptidic compounds as potential malarial inhibitors against Plasmodial cysteine proteases via integrated virtual screening workflow","volume":"34","author":"Musyoka","year":"2016","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ejmech.2023.115299_bib110","doi-asserted-by":"crossref","DOI":"10.1038\/srep23690","article-title":"Structure based docking and molecular dynamic studies of plasmodial cysteine proteases against a South African natural compound and its analogs","volume":"6","author":"Musyoka","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2023.115299_bib111","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1186\/s12936-019-2790-2","article-title":"Comparing sequence and structure of falcipains and human homologs at prodomain and catalytic active site for malarial peptide based inhibitor design","volume":"18","author":"Musyoka","year":"2019","journal-title":"Malar. J."},{"key":"10.1016\/j.ejmech.2023.115299_bib112","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":"Med. Chem. Comm."},{"key":"10.1016\/j.ejmech.2023.115299_bib113","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep42717","article-title":"SwissADME: a free web tool to evaluate pharmacokinetics, drug-likeness and medicinal chemistry friendliness of small molecules","volume":"7","author":"Daina","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2023.115299_bib114","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1093\/bioinformatics\/bty707","article-title":"admetSAR 2.0: web-service for prediction and optimization of chemical ADMET properties","volume":"35","author":"Yang","year":"2019","journal-title":"Bioinformatics"},{"key":"10.1016\/j.ejmech.2023.115299_bib115","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkab255","article-title":"ADMETlab 2.0: an integrated online platform for accurate and comprehensive predictions of ADMET properties","volume":"49","author":"Xiong","year":"2021","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ejmech.2023.115299_bib116","doi-asserted-by":"crossref","first-page":"W257","DOI":"10.1093\/nar\/gky318","article-title":"ProTox-II: a webserver for the prediction of toxicity of chemicals","volume":"46","author":"Banerjee","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ejmech.2023.115299_bib117","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0001023","article-title":"Mining a cathepsin inhibitor library for new antiparasitic drug leads","volume":"5","author":"Ang","year":"2011","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.ejmech.2023.115299_bib118","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1007\/978-0-387-77570-8_3","article-title":"Drugs and transporters in kinetoplastid protozoa","volume":"625","author":"Landfear","year":"2008","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.ejmech.2023.115299_bib119","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1016\/j.addr.2009.11.024","article-title":"Nanotechnology applied to the treatment of malaria","volume":"62","author":"Santos-Magalh\u00e3es","year":"2010","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ejmech.2023.115299_bib120","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1016\/j.addr.2006.09.009","article-title":"Multifunctional nanocarriers","volume":"58","author":"Torchilin","year":"2006","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ejmech.2023.115299_bib121","doi-asserted-by":"crossref","first-page":"3116","DOI":"10.1021\/jm070735f","article-title":"A prodomain peptide of plasmodium falciparum cysteine protease (Falcipain-2) inhibits malaria parasite development","volume":"51","author":"Korde","year":"2008","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2023.115299_bib122","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1038\/nchembio.192","article-title":"Inhibition of a viral enzyme by a small-molecule dimer disruptor","volume":"5","author":"Shahian","year":"2009","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ejmech.2023.115299_bib123","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1038\/nrd3680","article-title":"Protein-protein interaction inhibitors get into the groove","volume":"11","author":"Mullard","year":"2012","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2023.115299_bib124","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0047227","article-title":"The Ionic and hydrophobic interactions are required for the auto activation of cysteine proteases of Plasmodium falciparum","volume":"7","author":"Sundararaj","year":"2012","journal-title":"PLoS One"}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423002659?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523423002659?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:52:18Z","timestamp":1759330338000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523423002659"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,4]]},"references-count":124,"alternative-id":["S0223523423002659"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115299","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2023,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Falcipains: Biochemistry, target validation and structure-activity relationship studies of inhibitors as antimalarials","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2023.115299","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Masson SAS. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"115299"}}