{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T01:37:14Z","timestamp":1777599434690,"version":"3.51.4"},"reference-count":153,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2017,9,1]],"date-time":"2017-09-01T00:00:00Z","timestamp":1504224000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["clinicalkey.jp","ijaaonline.com","clinicalkey.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Antimicrobial Agents"],"published-print":{"date-parts":[[2017,9]]},"DOI":"10.1016\/j.ijantimicag.2017.04.006","type":"journal-article","created":{"date-parts":[[2017,6,28]],"date-time":"2017-06-28T20:02:07Z","timestamp":1498680127000},"page":"287-302","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":50,"title":["Targeting the active sites of malarial proteases for antimalarial drug discovery: approaches, progress and challenges"],"prefix":"10.1016","volume":"50","author":[{"given":"Kuldeep K.","family":"Roy","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0010","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/nrd4573","article-title":"Malaria medicines: a glass half full?","volume":"14","author":"Wells","year":"2015","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0015","series-title":"World malaria report 2015","author":"World Health Organization","year":"2015"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0020","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/415680a","article-title":"The economic and social burden of malaria","volume":"415","author":"Sachs","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0025","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1186\/1475-2875-12-307","article-title":"The economic costs of malaria in children in three sub-Saharan countries: Ghana, Tanzania and Kenya","volume":"12","author":"Sicuri","year":"2013","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0030","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1186\/1475-2875-9-149","article-title":"The economic costs of malaria in four Kenyan districts: do household costs differ by disease endemicity?","volume":"9","author":"Chuma","year":"2010","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0035","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1586\/eri.09.93","article-title":"Plasmodium falciparum: new molecular targets with potential for antimalarial drug development","volume":"7","author":"Gardiner","year":"2009","journal-title":"Expert Rev Anti Infect Ther"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0040","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1475-2875-11-36","article-title":"Human Plasmodium knowlesi infection in Ranong Province, southwestern border of Thailand","volume":"11","author":"Sermwittayawong","year":"2012","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0045","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1186\/1475-2875-9-219","article-title":"First case of detection of Plasmodium knowlesi in Spain by real time PCR in a traveller from Southeast Asia","volume":"9","author":"Ta","year":"2010","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0050","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/S0169-4758(00)01758-0","article-title":"Antimalarial drug development and new targets","volume":"16","author":"Macreadie","year":"2000","journal-title":"Parasitol Today"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0055","doi-asserted-by":"crossref","first-page":"e001854","DOI":"10.1136\/bmjopen-2012-001854","article-title":"Geographical concentration of falciparum malaria treated in the UK and delay to treatment with artesunate in severe cases: an observational study","volume":"2","author":"Broderick","year":"2012","journal-title":"BMJ Open"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0060","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1016\/j.trstmh.2012.08.006","article-title":"Severe febrile illness in adult hospital admissions in Tanzania: a prospective study in an area of high malaria transmission","volume":"106","author":"Nadjm","year":"2012","journal-title":"Trans R Soc Trop Med Hyg"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0065","doi-asserted-by":"crossref","first-page":"e2116","DOI":"10.1136\/bmj.e2116","article-title":"Risk factors for mortality from imported falciparum malaria in the United Kingdom over 20 years: an observational study","volume":"344","author":"Checkley","year":"2012","journal-title":"BMJ"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0070","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1006\/expr.1997.4225","article-title":"Plasmodium falciparum, P. vivax, and P. malariae: a comparison of the active site properties of plasmepsins cloned and expressed from three different species of the malaria parasite","volume":"87","author":"Westling","year":"1997","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0075","first-page":"139","article-title":"Variations in structure and function during the life cycle of malarial parasites","volume":"55","author":"Aikawa","year":"1977","journal-title":"Bull World Health Organ"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0080","first-page":"6","article-title":"Mitochondrial changes during the malarial life cycle","volume":"64","author":"Howells","year":"1970","journal-title":"Trans R Soc Trop Med Hyg"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0085","first-page":"280","article-title":"The life cycle of malarial parasites","volume":"5","author":"Lavier","year":"1950","journal-title":"Therapie"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0090","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1146\/annurev.micro.091208.073403","article-title":"Malaria parasite development in the mosquito and infection of the mammalian host","volume":"63","author":"Aly","year":"2009","journal-title":"Annu Rev Microbiol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0095","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1038\/nature01097","article-title":"Genome sequence of the human malaria parasite Plasmodium falciparum","volume":"419","author":"Gardner","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0100","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.molbiopara.2013.02.008","article-title":"Folate metabolism in human malaria parasites\u201475 years on","volume":"188","author":"Muller","year":"2013","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0105","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1111\/j.1753-4887.2010.00362.x","article-title":"Folate metabolism pathway and Plasmodium falciparum malaria infection in pregnancy","volume":"69","author":"Chango","year":"2011","journal-title":"Nutr Rev"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0110","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.pt.2005.05.008","article-title":"Comparative folate metabolism in humans and malaria parasites (part II): activities as yet untargeted or specific to Plasmodium","volume":"21","author":"Nzila","year":"2005","journal-title":"Trends Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0115","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1186\/1475-2875-10-283","article-title":"In vitro susceptibility to pyrimethamine of DHFR I164L single mutant Plasmodium falciparum","volume":"10","author":"Andriantsoanirina","year":"2011","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0120","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1021\/cr0301144","article-title":"DNA and RNA synthesis: antifolates","volume":"105","author":"Kompis","year":"2005","journal-title":"Chem Rev"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0125","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1186\/1475-2875-10-119","article-title":"Selection of drug resistant mutants from random library of Plasmodium falciparum dihydrofolate reductase in Plasmodium berghei model","volume":"10","author":"Tipsuwan","year":"2011","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0130","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.exppara.2006.12.001","article-title":"Selective killing of the human malaria parasite Plasmodium falciparum by a benzylthiazolium dye","volume":"116","author":"Kelly","year":"2007","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0135","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1128\/EC.00212-06","article-title":"Specific inhibition of the plasmodial surface anion channel by dantrolene","volume":"5","author":"Lisk","year":"2006","journal-title":"Eukaryot Cell"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0140","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1186\/1475-2875-9-36","article-title":"Uptake of purines in Plasmodium falciparum-infected human erythrocytes is mostly mediated by the human equilibrative nucleoside transporter and the human facilitative nucleobase transporter","volume":"9","author":"Quashie","year":"2010","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0145","doi-asserted-by":"crossref","first-page":"4585","DOI":"10.1021\/jm0703340","article-title":"Second generation tetrahydroquinoline-based protein farnesyltransferase inhibitors as antimalarials","volume":"50","author":"Bendale","year":"2007","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0150","doi-asserted-by":"crossref","first-page":"5176","DOI":"10.1021\/jm800113p","article-title":"Potent, Plasmodium-selective farnesyltransferase inhibitors that arrest the growth of malaria parasites: structure\u2013activity relationships of ethylenediamine-analogue scaffolds and homology model validation","volume":"51","author":"Fletcher","year":"2008","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0155","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1002\/cmdc.200800043","article-title":"Development of benzophenone-based farnesyltransferase inhibitors as novel antimalarials","volume":"3","author":"Kohring","year":"2008","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0160","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1021\/cb200292c","article-title":"A multifunctional protease inhibitor to regulate endolysosomal function","volume":"6","author":"van Kasteren","year":"2011","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0165","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1051\/parasite\/2014059","article-title":"Challenges of drug-resistant malaria","volume":"21","author":"Sinha","year":"2014","journal-title":"Parasite"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0170","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/0169-4758(95)80042-5","article-title":"The Plasmodium digestive vacuole: metabolic headquarters and choice drug target","volume":"11","author":"Olliaro","year":"1995","journal-title":"Parasitol Today"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0175","doi-asserted-by":"crossref","first-page":"49","DOI":"10.3201\/eid0401.980107","article-title":"Proteases of malaria parasites: new targets for chemotherapy","volume":"4","author":"Rosenthal","year":"1998","journal-title":"Emerg Infect Dis"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0180","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.2174\/1381612023394197","article-title":"Cysteine proteases of malaria parasites: targets for chemotherapy","volume":"8","author":"Rosenthal","year":"2002","journal-title":"Curr Pharm Des"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0185","first-page":"275","article-title":"Hemoglobin degradation","volume":"295","author":"Goldberg","year":"2005","journal-title":"Curr Top Microbiol Immunol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0190","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1186\/s12936-016-1097-9","article-title":"Comparative genome-wide analysis and evolutionary history of haemoglobin-processing and haem detoxification enzymes in malarial parasites","volume":"15","author":"Ponsuwanna","year":"2016","journal-title":"Malar J"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0195","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 USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0200","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1002\/med.20082","article-title":"Plasmepsins as potential targets for new antimalarial therapy","volume":"26","author":"Ersmark","year":"2006","journal-title":"Med Res Rev"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0205","doi-asserted-by":"crossref","first-page":"445","DOI":"10.2174\/156802612799362959","article-title":"Recent advances in plasmepsin medicinal chemistry and implications for future antimalarial drug discovery efforts","volume":"12","author":"Meyers","year":"2012","journal-title":"Curr Top Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0210","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/S0166-6851(03)00098-7","article-title":"Plasmodium falciparum falcilysin: an unprocessed food vacuole enzyme","volume":"129","author":"Murata","year":"2003","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0215","doi-asserted-by":"crossref","first-page":"38022","DOI":"10.1074\/jbc.M306842200","article-title":"Plasmodium falciparum falcilysin: a metalloprotease with dual specificity","volume":"278","author":"Murata","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0220","doi-asserted-by":"crossref","first-page":"43000","DOI":"10.1074\/jbc.M408123200","article-title":"A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation","volume":"279","author":"Klemba","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0225","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.ijantimicag.2017.04.006_bib0230","doi-asserted-by":"crossref","first-page":"5151","DOI":"10.1021\/jm5014133","article-title":"Fighting malaria: structure-guided discovery of nonpeptidomimetic plasmepsin inhibitors","volume":"58","author":"Huizing","year":"2015","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0235","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1073\/pnas.022630099","article-title":"Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine","volume":"99","author":"Banerjee","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0240","doi-asserted-by":"crossref","first-page":"10034","DOI":"10.1073\/pnas.93.19.10034","article-title":"Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum","volume":"93","author":"Silva","year":"1996","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0245","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1110\/ps.8.10.2001","article-title":"Active site specificity of plasmepsin II","volume":"8","author":"Westling","year":"1999","journal-title":"Protein Sci"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0250","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/0166-6851(94)90024-8","article-title":"Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum","volume":"64","author":"Dame","year":"1994","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0255","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1021\/ar000184m","article-title":"Follow the protons: a low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases","volume":"34","author":"Northrop","year":"2001","journal-title":"Acc Chem Res"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0260","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0022-2836(03)00036-6","article-title":"Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum","volume":"327","author":"Asojo","year":"2003","journal-title":"J Mol Biol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0265","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1107\/S0907444902014695","article-title":"Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8\u2009\u00c5 in complex with the inhibitors rs367 and rs370","volume":"58","author":"Asojo","year":"2002","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0270","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1039\/C6MB00077K","article-title":"The binding landscape of plasmepsin V and the implications for flap dynamics","volume":"12","author":"L","year":"2016","journal-title":"Mol Biosyst"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0275","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1039\/C4MB00631C","article-title":"Flap dynamics of plasmepsin proteases: insight into proposed parameters and molecular dynamics","volume":"11","author":"Karubiu","year":"2015","journal-title":"Mol Biosyst"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0280","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.2174\/0929867311320250003","article-title":"Development of Plasmodium falciparum protease inhibitors in the past decade (2002\u20132012)","volume":"20","author":"Perez","year":"2013","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0285","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1021\/jm030933g","article-title":"Potent inhibitors of the Plasmodium falciparum enzymes plasmepsin I and II devoid of cathepsin D inhibitory activity","volume":"47","author":"Ersmark","year":"2004","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0290","doi-asserted-by":"crossref","first-page":"1768","DOI":"10.1021\/bi047886u","article-title":"Active-site specificity of digestive aspartic peptidases from the four species of Plasmodium that infect humans using chromogenic combinatorial peptide libraries","volume":"44","author":"Beyer","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0295","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/S0968-0896(02)00568-0","article-title":"Solid-phase library synthesis of reversed-statine type inhibitors of the malarial aspartyl proteases plasmepsin I and II","volume":"11","author":"Dahlgren","year":"2003","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0300","doi-asserted-by":"crossref","first-page":"3423","DOI":"10.1016\/S0968-0896(03)00312-2","article-title":"New inhibitors of the malaria aspartyl proteases plasmepsin I and II","volume":"11","author":"Dahlgren","year":"2003","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0305","doi-asserted-by":"crossref","first-page":"3723","DOI":"10.1016\/S0968-0896(03)00339-0","article-title":"C2-symmetric inhibitors of Plasmodium falciparum plasmepsin II: synthesis and theoretical predictions","volume":"11","author":"Ersmark","year":"2003","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0310","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1021\/jm031106i","article-title":"Design and synthesis of potent inhibitors of the malaria aspartyl proteases plasmepsin I and II. Use of solid-phase synthesis to explore novel statine motifs","volume":"47","author":"Johansson","year":"2004","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0315","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1021\/jm020951i","article-title":"Design and synthesis of plasmepsin I and plasmepsin II inhibitors with activity in Plasmodium falciparum-infected cultured human erythrocytes","volume":"46","author":"Noteberg","year":"2003","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0320","doi-asserted-by":"crossref","first-page":"4400","DOI":"10.1021\/jm040884n","article-title":"Design and synthesis of potent inhibitors of plasmepsin I and II: X-ray crystal structure of inhibitor in complex with plasmepsin II","volume":"48","author":"Johansson","year":"2005","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0325","doi-asserted-by":"crossref","first-page":"8459","DOI":"10.1021\/bi034131z","article-title":"High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor","volume":"42","author":"Nezami","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0330","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1021\/cc0301014","article-title":"High-speed optimization of inhibitors of the malarial proteases plasmepsin I and II","volume":"5","author":"Noteberg","year":"2003","journal-title":"J Comb Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0335","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.molbiopara.2004.01.010","article-title":"Recombinant expression and enzymatic subsite characterization of plasmepsin 4 from the four Plasmodium species infecting man","volume":"135","author":"Li","year":"2004","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0340","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1002\/psc.609","article-title":"Search for substrate-based inhibitors fitting the S2\u2032 space of malarial aspartic protease plasmepsin II","volume":"10","author":"Kiso","year":"2004","journal-title":"J Pept Sci"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0345","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1016\/S0968-0896(02)00643-0","article-title":"New potent C2-symmetric malaria plasmepsin I and II inhibitors","volume":"11","author":"Oscarsson","year":"2003","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0350","doi-asserted-by":"crossref","first-page":"2931","DOI":"10.1016\/j.bmcl.2004.03.030","article-title":"Plasmepsin II inhibition and antiplasmodial activity of primaquine\u2013statine \u2018double-drugs\u2019","volume":"14","author":"Romeo","year":"2004","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0355","doi-asserted-by":"crossref","first-page":"10049","DOI":"10.1016\/j.bmc.2008.10.011","article-title":"Antimalarial activity enhancement in hydroxymethylcarbonyl (HMC) isostere-based dipeptidomimetics targeting malarial aspartic protease plasmepsin","volume":"16","author":"Hidaka","year":"2008","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0360","doi-asserted-by":"crossref","first-page":"3048","DOI":"10.1016\/j.bmcl.2007.03.052","article-title":"Additional interaction of allophenylnorstatine-containing tripeptidomimetics with malarial aspartic protease plasmepsin II","volume":"17","author":"Hidaka","year":"2007","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0365","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0014-5793(02)02241-X","article-title":"Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum","volume":"513","author":"Wyatt","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0370","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/S0014-5793(99)00805-4","article-title":"Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum","volume":"454","author":"Tyas","year":"1999","journal-title":"FEBS Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0375","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1111\/j.1432-1033.1997.00552.x","article-title":"Expression and characterisation of plasmepsin I from Plasmodium falciparum","volume":"244","author":"Moon","year":"1997","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0380","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1111\/j.1550-7408.1992.tb04856.x","article-title":"Plasmodium falciparum: differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and pepstatin A (aspartyl protease inhibitor)","volume":"39","author":"Bailly","year":"1992","journal-title":"J Protozool"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0385","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1111\/j.1747-0285.2011.01276.x","article-title":"Insight into selectivity of peptidomimetic inhibitors with modified statine core for plasmepsin II of Plasmodium falciparum over human cathepsin D","volume":"79","author":"Dali","year":"2012","journal-title":"Chem Biol Drug Des"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0390","doi-asserted-by":"crossref","first-page":"4234","DOI":"10.1021\/jm100233b","article-title":"Mechanism-based inhibitors of the aspartyl protease plasmepsin II as potential antimalarial agents","volume":"53","author":"Gupta","year":"2010","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0395","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.1016\/S0960-894X(98)00419-3","article-title":"Identification of potent inhibitors of Plasmodium falciparum plasmepsin II from an encoded statine combinatorial library","volume":"8","author":"Carroll","year":"1998","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0400","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1021\/cc000052k","article-title":"A statistical-based approach to assessing the fidelity of combinatorial libraries encoded with electrophoric molecular tags. Development and application of tag decode-assisted single bead LC\/MS analysis","volume":"2","author":"Dolle","year":"2000","journal-title":"J Comb Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0405","doi-asserted-by":"crossref","first-page":"6090","DOI":"10.1021\/jm050463l","article-title":"Synthesis of malarial plasmepsin inhibitors and prediction of binding modes by molecular dynamics simulations","volume":"48","author":"Ersmark","year":"2005","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0410","doi-asserted-by":"crossref","first-page":"1428","DOI":"10.1021\/jm980641t","article-title":"Potent, low-molecular-weight non-peptide inhibitors of malarial aspartyl protease plasmepsin II","volume":"42","author":"Haque","year":"1999","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0415","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1021\/bi0117549","article-title":"Identification and characterization of allophenylnorstatine-based inhibitors of plasmepsin II, an antimalarial target","volume":"41","author":"Nezami","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0420","doi-asserted-by":"crossref","first-page":"4836","DOI":"10.1016\/j.bmcl.2010.06.099","article-title":"Improvement of both plasmepsin inhibitory activity and antimalarial activity by 2-aminoethylamino substitution","volume":"20","author":"Miura","year":"2010","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0425","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1128\/AAC.45.9.2577-2584.2001","article-title":"New class of small nonpeptidyl compounds blocks Plasmodium falciparum development in vitro by inhibiting plasmepsins","volume":"45","author":"Jiang","year":"2001","journal-title":"Antimicrob Agents Chemother"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0430","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1016\/j.ijpara.2004.10.003","article-title":"Cysteine proteases of malaria parasites","volume":"34","author":"Rosenthal","year":"2004","journal-title":"Int J Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0435","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.ijantimicag.2017.04.006_bib0440","doi-asserted-by":"crossref","first-page":"e5156","DOI":"10.1371\/journal.pone.0005156","article-title":"Hemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3","volume":"4","author":"Subramanian","year":"2009","journal-title":"PLoS ONE"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0445","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 USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0450","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\u2032","volume":"112","author":"Singh","year":"2006","journal-title":"Exp Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0455","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.ijantimicag.2017.04.006_bib0460","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.2174\/092986711795328328","article-title":"Falcipains, Plasmodium falciparum cysteine proteases as key drug targets against malaria","volume":"18","author":"Teixeira","year":"2011","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0465","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.ijantimicag.2017.04.006_bib0470","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":"Pandey","year":"2006","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0475","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":"Eksi","year":"2004","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0480","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.bbrc.2004.08.130","article-title":"Homology modeling and mutagenesis analyses of Plasmodium falciparum falcipain 2A: implications for rational drug design","volume":"323","author":"Goh","year":"2004","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0485","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of the active site in proteases. I. Papain","volume":"27","author":"Schechter","year":"1967","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0490","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":"Sajid","year":"2002","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0495","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.ijantimicag.2017.04.006_bib0500","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 USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0505","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1093\/molbev\/msg076","article-title":"Gene conversion as a source of nucleotide diversity in Plasmodium falciparum","volume":"20","author":"Nielsen","year":"2003","journal-title":"Mol Biol Evol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0510","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.ijantimicag.2017.04.006_bib0515","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.ijantimicag.2017.04.006_bib0520","doi-asserted-by":"crossref","first-page":"3193","DOI":"10.1021\/jm00017a002","article-title":"Vinyl sulfones as mechanism-based cysteine protease inhibitors","volume":"38","author":"Palmer","year":"1995","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0525","doi-asserted-by":"crossref","first-page":"331","DOI":"10.2174\/156802606776287081","article-title":"Inhibitors of cysteine proteases","volume":"6","author":"Vicik","year":"2006","journal-title":"Curr Top Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0530","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1002\/cmdc.200700070","article-title":"Screening of protease inhibitors as antiplasmodial agents. Part I: aziridines and epoxides","volume":"2","author":"Schulz","year":"2007","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0535","doi-asserted-by":"crossref","first-page":"3078","DOI":"10.1021\/jm00016a011","article-title":"Aziridine analogs of [[trans-(epoxysuccinyl)-l-leucyl]amino]-4-guanidinobutane (E-64) as inhibitors of cysteine proteases","volume":"38","author":"Martichonok","year":"1995","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0540","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.ijantimicag.2017.04.006_bib0545","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1172\/JCI116262","article-title":"Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria","volume":"91","author":"Rosenthal","year":"1993","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0550","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.ijantimicag.2017.04.006_bib0555","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1128\/AAC.47.1.154-160.2003","article-title":"Structure\u2013activity 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.ijantimicag.2017.04.006_bib0560","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2174\/1568005043480925","article-title":"Genetic and biochemical aspects of drug resistance in malaria parasites","volume":"4","author":"Hayton","year":"2004","journal-title":"Curr Drug Targets Infect Disord"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0565","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1021\/jm990412m","article-title":"Protease inhibitors: current status and future prospects","volume":"43","author":"Leung","year":"2000","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0570","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.ijantimicag.2017.04.006_bib0575","doi-asserted-by":"crossref","first-page":"4210","DOI":"10.1016\/j.bmcl.2008.05.068","article-title":"Design and synthesis of novel 2-pyridone peptidomimetic falcipain 2\/3 inhibitors","volume":"18","author":"Verissimo","year":"2008","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0580","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.ijantimicag.2017.04.006_bib0585","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/j.ejmech.2012.05.022","article-title":"Novel cinnamic acid\/4-aminoquinoline conjugates bearing non-proteinogenic amino acids: towards the development of potential dual action antimalarials","volume":"54","author":"Perez","year":"2012","journal-title":"Eur J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0590","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.ijantimicag.2017.04.006_bib0595","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.ijantimicag.2017.04.006_bib0600","doi-asserted-by":"crossref","first-page":"4115","DOI":"10.1016\/j.bmcl.2006.04.079","article-title":"Dipeptide vinyl sultams: synthesis via the Wittig\u2013Horner reaction and activity against papain, falcipain-2 and Plasmodium falciparum","volume":"16","author":"Valente","year":"2006","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0605","doi-asserted-by":"crossref","first-page":"7635","DOI":"10.1016\/j.bmc.2011.10.018","article-title":"Aza vinyl sulfones: synthesis and evaluation as antiplasmodial agents","volume":"19","author":"Gloria","year":"2011","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0610","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1039\/c2md20011b","article-title":"Squaric acid: a valuable scaffold for developing antimalarials?","volume":"3","author":"Kumar","year":"2012","journal-title":"MedChemComm"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0615","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.ejmech.2011.01.008","article-title":"Design, synthesis and evaluation of 3-methylene-substituted indolinones as antimalarials","volume":"46","author":"Praveen Kumar","year":"2011","journal-title":"Eur J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0620","doi-asserted-by":"crossref","first-page":"8202","DOI":"10.1021\/jm1009567","article-title":"Endoperoxide carbonyl falcipain 2\/3 inhibitor hybrids: toward combination chemotherapy of malaria through a single chemical entity","volume":"53","author":"Gibbons","year":"2010","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0625","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.ijantimicag.2017.04.006_bib0630","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.ijantimicag.2017.04.006_bib0635","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1016\/S0968-0896(03)00117-2","article-title":"Structure-based approach to falcipain-2 inhibitors: synthesis and biological evaluation of 1,6,7-trisubstituted dihydroisoquinolines and isoquinolines","volume":"11","author":"Batra","year":"2003","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0640","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1023\/A:1020155510718","article-title":"A review of protein-small molecule docking methods","volume":"16","author":"Taylor","year":"2002","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0645","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.ijantimicag.2017.04.006_bib0650","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.1021\/jm200149e","article-title":"Enone\u2013 and chalcone\u2013chloroquinoline hybrid analogues: in silico guided design, synthesis, antiplasmodial activity, in vitro metabolism, and mechanistic studies","volume":"54","author":"Guantai","year":"2011","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0655","doi-asserted-by":"crossref","first-page":"8243","DOI":"10.1016\/j.bmc.2010.10.009","article-title":"Design, synthesis and in vitro antimalarial evaluation of triazole-linked chalcone and dienone hybrid compounds","volume":"18","author":"Guantai","year":"2010","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0660","doi-asserted-by":"crossref","first-page":"883","DOI":"10.2174\/0929867033457674","article-title":"Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents","volume":"10","author":"Boss","year":"2003","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0665","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.ijantimicag.2017.04.006_bib0670","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1111\/j.1365-2958.2006.05443.x","article-title":"A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast","volume":"63","author":"Ponpuak","year":"2007","journal-title":"Mol Microbiol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0675","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.ijantimicag.2017.04.006_bib0680","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.1124\/mol.108.045682","article-title":"In vivo inhibition of serine protease processing requires a high fractional inhibition of cathepsin C","volume":"73","author":"Methot","year":"2008","journal-title":"Mol Pharmacol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0685","doi-asserted-by":"crossref","first-page":"20836","DOI":"10.1074\/jbc.M702615200","article-title":"Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing","volume":"282","author":"Methot","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0690","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.chembiol.2010.06.007","article-title":"Functional studies of Plasmodium falciparum dipeptidyl aminopeptidase I using small molecule inhibitors and active site probes","volume":"17","author":"Deu","year":"2010","journal-title":"Chem Biol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0695","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tibs.2009.08.004","article-title":"Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials","volume":"35","author":"Skinner-Adams","year":"2010","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0700","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0968-0004(98)01227-4","article-title":"N-terminal processing: the methionine aminopeptidase and N \u03b1-acetyl transferase families","volume":"23","author":"Bradshaw","year":"1998","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0705","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/j.bcmd.2004.01.006","article-title":"Excess haemoglobin digestion by malaria parasites: a strategy to prevent premature host cell lysis","volume":"32","author":"Lew","year":"2004","journal-title":"Blood Cells Mol Dis"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0710","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/S1074-5521(97)90198-8","article-title":"Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin","volume":"4","author":"Griffith","year":"1997","journal-title":"Chem Biol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0715","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1007\/BF02256576","article-title":"Angiogenesis inhibitors specific for methionine aminopeptidase 2 as drugs for malaria and leishmaniasis","volume":"9","author":"Zhang","year":"2002","journal-title":"J Biomed Sci"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0720","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0166-6851(01)00327-9","article-title":"The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes","volume":"117","author":"Gavigan","year":"2001","journal-title":"Mol Biochem Parasitol"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0725","doi-asserted-by":"crossref","first-page":"1741","DOI":"10.1074\/jbc.M508955200","article-title":"Overexpression of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin","volume":"281","author":"Gardiner","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0730","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0031182002001828","article-title":"Properties, stage-dependent expression and localization of Plasmodium falciparum M1 family zinc-aminopeptidase","volume":"125","author":"Allary","year":"2002","journal-title":"Parasitology"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0735","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1021\/jm061169b","article-title":"Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents","volume":"50","author":"Flipo","year":"2007","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0740","doi-asserted-by":"crossref","first-page":"e28589","DOI":"10.1371\/journal.pone.0028589","article-title":"The Plasmodium falciparum malaria M1 alanyl aminopeptidase (PfA-M1): insights of catalytic mechanism and function from MD simulations","volume":"6","author":"Jones","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0745","doi-asserted-by":"crossref","first-page":"2537","DOI":"10.1073\/pnas.0807398106","article-title":"Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase","volume":"106","author":"McGowan","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0750","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1021\/jm101227t","article-title":"Synthesis of new (\u2013)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase","volume":"54","author":"Velmourougane","year":"2011","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0755","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1016\/S0960-894X(03)00550-X","article-title":"Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors","volume":"13","author":"Flipo","year":"2003","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0760","doi-asserted-by":"crossref","first-page":"6024","DOI":"10.1021\/jm070733v","article-title":"Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds","volume":"50","author":"Skinner-Adams","year":"2007","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0765","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1021\/jm030795v","article-title":"The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity","volume":"46","author":"Grembecka","year":"2003","journal-title":"J Med Chem"},{"key":"10.1016\/j.ijantimicag.2017.04.006_bib0770","doi-asserted-by":"crossref","first-page":"5435","DOI":"10.1021\/bi9003638","article-title":"The M17 leucine aminopeptidase of the malaria parasite Plasmodium falciparum: importance of active site metal ions in the binding of substrates and inhibitors","volume":"48","author":"Maric","year":"2009","journal-title":"Biochemistry"}],"container-title":["International Journal of Antimicrobial Agents"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0924857917301966?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0924857917301966?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,10,11]],"date-time":"2020-10-11T03:47:34Z","timestamp":1602388054000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0924857917301966"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9]]},"references-count":153,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2017,9]]}},"alternative-id":["S0924857917301966"],"URL":"https:\/\/doi.org\/10.1016\/j.ijantimicag.2017.04.006","relation":{},"ISSN":["0924-8579"],"issn-type":[{"value":"0924-8579","type":"print"}],"subject":[],"published":{"date-parts":[[2017,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting the active sites of malarial proteases for antimalarial drug discovery: approaches, progress and challenges","name":"articletitle","label":"Article Title"},{"value":"International Journal of Antimicrobial Agents","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijantimicag.2017.04.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier B.V. and International Society of Chemotherapy. All rights reserved.","name":"copyright","label":"Copyright"}]}}