메뉴 건너뛰기




Volumn 18, Issue 10, 2011, Pages 1555-1572

Falcipains, plasmodium falciparum cysteine proteases as key drug targets against malaria

Author keywords

Cysteine proteases; Drug design; Falcipain inhibitors; Falcipains; Malaria; Plasmodium Falciparum

Indexed keywords

ANTIMALARIAL AGENT; ASPARTIC PROTEINASE; ATOVAQUONE; CHLOROQUINE; CYSTEINE PROTEINASE; FALCIPAIN; FOSMIDOMYCIN; GLYPHOSATE; HEMOGLOBIN; IMMUCILIN H; LEUPEPTIN; METHOTREXATE; NAS 21; NAS 91; PEPSTATIN; PROBENECID; THIOLACTOMYCIN; TRICLOSAN; UNCLASSIFIED DRUG;

EID: 79955015664     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711795328328     Document Type: Article
Times cited : (80)

References (142)
  • 1
    • 77249141616 scopus 로고    scopus 로고
    • History of the discovery of the malaria parasites and their vectors
    • Cox, F.E. History of the discovery of the malaria parasites and their vectors. Parasit. Vectors. 2010, 3 (1), 5.
    • (2010) Parasit. Vectors. , vol.3 , Issue.1 , pp. 5
    • Cox, F.E.1
  • 2
    • 2442619444 scopus 로고    scopus 로고
    • Malaria: From prehistory to present
    • DOI 10.1016/j.idc.2004.01.002, PII S0891552004000170
    • Schlagenhauf, P. Malaria: from prehistory to present. Infect. Dis. Clin. North Am., 2004, 18 (2), 189-205. (Pubitemid 38622399)
    • (2004) Infectious Disease Clinics of North America , vol.18 , Issue.2 , pp. 189-205
    • Schlagenhauf, P.1
  • 3
    • 0000576760 scopus 로고
    • Note sur un nouveau parasite trouvé dans le sang de plusieurs malades atteints de fièvre palustre
    • Laveran, A. Note sur un nouveau parasite trouvé dans le sang de plusieurs malades atteints de fièvre palustre. Bull. Acad. Med., 1888, 2nd Series (9), 1235-1236.
    • (1888) Bull. Acad. Med. , vol.IIND SERIES , Issue.9 , pp. 1235-1236
    • Laveran, A.1
  • 4
    • 84965228039 scopus 로고
    • On Some Peculiar Pigmented Cells Round in Two Mosquitoes Red on Malarial Blood
    • Ross, R. On Some Peculiar Pigmented Cells Round in Two Mosquitoes Red on Malarial Blood. Br. Med. J., 1897, 2, 1786-1788.
    • (1897) Br. Med. J. , vol.2 , pp. 1786-1788
    • Ross, R.1
  • 5
    • 0004812168 scopus 로고
    • A Cielo evolutivo delle semilune ell'Anopheles claviger ed altri studie sulla malaria dall'Ottobre 1898 al Maggio 1899
    • Grassi, B.; Bigmami, A. A Cielo evolutivo delle semilune ell'Anopheles claviger ed altri studie sulla malaria dall'Ottobre 1898 al Maggio 1899. Ann. d'Igien. Sper., 1899, 9, 258-271.
    • (1899) Ann. d'Igien. Sper. , vol.9 , pp. 258-271
    • Grassi, B.1    Bigmami, A.2
  • 6
    • 0031878060 scopus 로고    scopus 로고
    • Tropical medicine: 100 years of progress
    • Gilles, H.M.; Lucas, A.O. Tropical medicine: 100 years of progress. Br. Med. Bull., 1998, 54 (2), 269-80. (Pubitemid 28342654)
    • (1998) British Medical Bulletin , vol.54 , Issue.2 , pp. 269-280
    • Gilles, H.M.1    Lucas, A.O.2
  • 7
    • 0037033984 scopus 로고    scopus 로고
    • The economic and social burden of malaria
    • DOI 10.1038/415680a
    • Sachs, J.; Malaney, P. The economic and social burden of malaria. Nature. 2002, 415 (6872), 680-5. (Pubitemid 34136401)
    • (2002) Nature , vol.415 , Issue.6872 , pp. 680-685
    • Sachs, J.1    Malaney, P.2
  • 8
    • 79955035793 scopus 로고    scopus 로고
    • accessed 21/05/2010
    • http://www.who.int/mediacentre/factsheets/fs094/en/index.html. (accessed 21/05/2010).
  • 9
    • 77955716299 scopus 로고    scopus 로고
    • First case of detection of Plasmodium knowlesi in Spain by Real Time PCR in a traveller from Southeast Asia
    • Tang, T.-H. T.; Salas, A.; Ali-Tammam, M.; Martinez, M.-C.; Lanza, M.; Arroyo, E.; Rubio. J. M. First case of detection of Plasmodium knowlesi in Spain by Real Time PCR in a traveller from Southeast Asia. Malaria J. 2010, 9, 219.
    • (2010) Malaria J. , vol.9 , pp. 219
    • Tang, T.-H.T.1    Salas, A.2    Ali-Tammam, M.3    Martinez, M.-C.4    Lanza, M.5    Arroyo, E.6    Rubio, J.M.7
  • 10
    • 4344659893 scopus 로고    scopus 로고
    • Are multilateral malaria research and control programs the most successful? Lessons from the past 100 years in Africa
    • Alílio, M.S.; Bygbjerg, I.C.; Breman, J.G. Are multilateral Malarial Research and Control Programs the Most Successful? Lessons from the Past 100 Years in Africa. Am. J. Trop. Medicine Hyg., 2004, 71, 268-278. (Pubitemid 39121332)
    • (2004) American Journal of Tropical Medicine and Hygiene , vol.71 , Issue.2 SUPPL. , pp. 268-278
    • Alilio, M.S.1    Bygbjerg, I.C.2    Breman, J.G.3
  • 11
    • 0037033980 scopus 로고    scopus 로고
    • Progress and challenges for malaria vaccines
    • DOI 10.1038/415694a
    • Richie, T.L.; Saul, A. Progress and challenges for malaria vaccines. Nature. 2002, 415 (6872), 694-701. (Pubitemid 34136403)
    • (2002) Nature , vol.415 , Issue.6872 , pp. 694-701
    • Richie, T.L.1    Saul, A.2
  • 12
    • 0034972445 scopus 로고    scopus 로고
    • The ears of the hippopotamus: Manifestations, determinants and estimates of the malaria burden
    • Breman, J.G. The Ears of the Hippopotamus: Manifestations, Determinants and Estimates of the Malaria Burden. Am. J. Trop. Medicine Hyg., 2001, 64 ((1,2)S), 1-11.
    • (2001) Am. J. Trop. Medicine Hyg. , vol.64 , Issue.1-2
    • Breman, J.G.1
  • 13
    • 0035700572 scopus 로고    scopus 로고
    • The past, present and future of childhood malaria mortality in Africa
    • DOI 10.1016/S1471-4922(01)02031-1, PII S1471492201020311
    • Snow, R.W.; Trape, J.R.; Marsh, K. The past, present and future of childhood malaria mortality in Africa. Trends. Parasitol., 2001, 17 (12), 593-7. (Pubitemid 34088120)
    • (2001) Trends in Parasitology , vol.17 , Issue.12 , pp. 593-597
    • Snow, R.W.1    Trape, J.-F.2    Marsh, K.3
  • 14
    • 33645870423 scopus 로고    scopus 로고
    • Malaria breakthrough raises spectre of drug resistance
    • Towie, N. Malaria breakthrough raises spectre of drug resistance. Nature. 2006, 440 (7086), 852-3.
    • (2006) Nature , vol.440 , Issue.7086 , pp. 852-853
    • Towie, N.1
  • 15
    • 0031752556 scopus 로고    scopus 로고
    • Drug resistance in malaria
    • White, N.J. Drug resistance in malaria. Br. Med. Bull., 1998, 54 (3), 703-15. (Pubitemid 28477205)
    • (1998) British Medical Bulletin , vol.54 , Issue.3 , pp. 703-715
    • White, N.J.1
  • 16
    • 2142659388 scopus 로고    scopus 로고
    • Antimalarial drug resistance
    • DOI 10.1172/JCI200421682
    • White, N.J. Antimalarial drug resistance. J. Clin. Invest., 2004, 113 (8), 1084-92. (Pubitemid 38544090)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.8 , pp. 1084-1092
    • White, N.J.1
  • 17
    • 77953519649 scopus 로고    scopus 로고
    • High chloroquine treatment failure rates and predominance of mutant genotypes associated with chloroquine and antifolate resistance among falciparum malaria patients from the island of Car Nicobar, India
    • Das, M.K.; Lumb, V.; Mittra, P.; Singh, S.S.; Dash, A.P.; Sharma, Y.D. High chloroquine treatment failure rates and predominance of mutant genotypes associated with chloroquine and antifolate resistance among falciparum malaria patients from the island of Car Nicobar, India. J. Antimicrob. Chemother., 2010, 65 (6), 1258-61.
    • (2010) J. Antimicrob. Chemother. , vol.65 , Issue.6 , pp. 1258-1261
    • Das, M.K.1    Lumb, V.2    Mittra, P.3    Singh, S.S.4    Dash, A.P.5    Sharma, Y.D.6
  • 18
    • 4944253804 scopus 로고    scopus 로고
    • The malaria parasite's chloroquine resistance transporter is a member of the drug/metabolite transporter superfamily
    • DOI 10.1093/molbev/msh205
    • Martin, R.E.; Kirk, K. The malaria parasite's chloroquine resistance transporter is a member of the drug/metabolite transporter superfamily. Mol. Biol. Evol., 2004, 21 (10), 1938-49. (Pubitemid 39331640)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.10 , pp. 1938-1949
    • Martin, R.E.1    Kirk, K.2
  • 23
    • 0033516474 scopus 로고    scopus 로고
    • Artemisinin an endoperoxide antimalarial, disrupts the hemoglobin catabolism and heme detoxification systems in malarial parasite
    • Pandey, A.V.; Tekwani, B.L.; Singh, R.L.; Chauhan, V.S. Artemisinin, an endoperoxide antimalarial, disrupts the hemoglobin catabolism and heme detoxification systems in malarial parasite. J. Biol. Chem., 1999, 274 (27), 19383-8.
    • (1999) J. Biol. Chem. , vol.274 , Issue.27 , pp. 19383-19388
    • Pandey, A.V.1    Tekwani, B.L.2    Singh, R.L.3    Chauhan, V.S.4
  • 26
    • 0037370645 scopus 로고    scopus 로고
    • Probing the structure of falcipain-3, a cysteine protease from Plasmodium falciparum: Comparative protein modeling and docking studies
    • DOI 10.1110/ps.0228103
    • Sabnis, Y.A.; Desai, P. V.; Rosenthal, P.J.; Avery, M.A. Probing the structure of falcipain-3, a cysteine protease from Plasmodium falciparum: comparative protein modeling and docking studies. Protein Sci., 2003, 12 (3), 501-9. (Pubitemid 36241108)
    • (2003) Protein Science , vol.12 , Issue.3 , pp. 501-509
    • Sabnis, Y.A.1    Desai, P.V.2    Rosenthal, P.J.3    Avery, M.A.4
  • 27
    • 0034895595 scopus 로고    scopus 로고
    • Recombinant falcipain-2 cleaves erythrocyte membrane ankyrin and protein 4.1
    • DOI 10.1016/S0166-6851(01)00306-1, PII S0166685101003061
    • Dua, M.; Raphael, P.; Sijwali, P.S.; Rosenthal, P.J.; Hanspal, M. Recombinant falcipain-2 cleaves erythrocyte membrane ankyrin and protein 4.1. Mol. Biochem. Parasitol., 2001, 116 (1), 95-9. (Pubitemid 32706432)
    • (2001) Molecular and Biochemical Parasitology , vol.116 , Issue.1 , pp. 95-99
    • Dua, M.1    Raphael, P.2    Sijwali, P.S.3    Rosenthal, P.J.4    Hanspal, M.5
  • 28
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • Rosenthal, P.J. Cysteine proteases of malaria parasites. Int. J. Parasitol., 2004, 34 (13-14), 1489-99.
    • (2004) Int. J. Parasitol. , vol.34 , Issue.13-14 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 29
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai, B.R.; Sijwali, P.S.; Singh, A.; Rosenthal, P.J. Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J. Biol. Chem., 2000, 275 (37), 29000-10.
    • (2000) J. Biol. Chem. , vol.275 , Issue.37 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 30
    • 7444266700 scopus 로고    scopus 로고
    • Malaria parasite transmission stages: An update
    • DOI 10.1016/j.pt.2004.10.001, PII S1471492204002582
    • Khan, S.M.; Waters, A.P. Malaria parasite transmission stages: an update. Trends. Parasitol., 2004, 20 (12), 575-80. (Pubitemid 39446748)
    • (2004) Trends in Parasitology , vol.20 , Issue.12 , pp. 575-580
    • Khan, S.M.1    Waters, A.P.2
  • 35
    • 16844376016 scopus 로고    scopus 로고
    • Effectiveness of antimalarial drugs
    • Baird, J.K. Effectiveness of antimalarial drugs. N. Engl. J. Med., 2005, 352 (15), 1565-77.
    • (2005) N. Engl. J. Med. , vol.352 , Issue.15 , pp. 1565-1577
    • Baird, J.K.1
  • 37
    • 1642565140 scopus 로고    scopus 로고
    • Genetic and biochemical aspects of drug resistance in malaria parasites
    • Hayton, K.; Su, X.Z. Genetic and biochemical aspects of drug resistance in malaria parasites. Curr. Drug Targets Infect. Disord., 2004, 4 (1), 1-10. (Pubitemid 38404692)
    • (2004) Current Drug Targets - Infectious Disorders , vol.4 , Issue.1 , pp. 1-10
    • Hayton, K.1    Su, X.-Z.2
  • 39
    • 68049146050 scopus 로고    scopus 로고
    • Artemisinin-resistant malaria in Asia
    • Noedl, H.; Socheat, D.; Satimai, W. Artemisinin-resistant malaria in Asia. N. Engl. J. Med., 2009, 361 (5), 540-1.
    • (2009) N. Engl. J. Med. , vol.361 , Issue.5 , pp. 540-541
    • Noedl, H.1    Socheat, D.2    Satimai, W.3
  • 43
    • 0036833617 scopus 로고    scopus 로고
    • Chemotherapeutic agents against malaria: What next after chloroquine?
    • Dominguez, J.N. Chemotherapeutic agents against malaria: what next after chloroquine? Curr. Top. Med. Chem., 2002, 2 (11), 1173-85.
    • (2002) Curr. Top. Med. Chem. , vol.2 , Issue.11 , pp. 1173-1185
    • Dominguez, J.N.1
  • 44
    • 34249981805 scopus 로고    scopus 로고
    • Novel molecular targets for antimalarial chemotherapy
    • DOI 10.1016/j.ijantimicag.2007.01.002, PII S0924857907000556
    • Jana, S.; Paliwal, J. Novel molecular targets for antimalarial chemotherapy. Int. J. Antimicrob. Agents. 2007, 30 (1), 4-10. (Pubitemid 46887588)
    • (2007) International Journal of Antimicrobial Agents , vol.30 , Issue.1 , pp. 4-10
    • Jana, S.1    Paliwal, J.2
  • 45
    • 0036183460 scopus 로고    scopus 로고
    • Hydrolysis of erythrocyte proteins by proteases of malaria parasites
    • DOI 10.1097/00062752-200203000-00010
    • Rosenthal, P.J. Hydrolysis of erythrocyte proteins by proteases of malaria parasites. Curr. Opin. Hematol., 2002, 9 (2), 140-5. (Pubitemid 34171491)
    • (2002) Current Opinion in Hematology , vol.9 , Issue.2 , pp. 140-145
    • Rosenthal, P.J.1
  • 46
    • 3342910277 scopus 로고    scopus 로고
    • Unraveling the mode of action of the antimalarial choline analog G25 in Plasmodium falciparum and Saccharomyces cerevisiae
    • DOI 10.1128/AAC.48.8.2816-2824.2004
    • Roggero, R.; Zufferey, R.; Minca, M.; Richier, E.; Calas, M.; Vial, H.; Ben Mamoun, C. Unraveling the mode of action of the antimalarial choline analog G25 in Plasmodium falciparum and Saccharomyces cerevisiae. Antimicrob. Agents Chemother., 2004, 48 (8), 2816-24. (Pubitemid 38989141)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.8 , pp. 2816-2824
    • Roggero, R.1    Zufferey, R.2    Minca, M.3    Richier, E.4    Calas, M.5    Vial, H.6    Mamoun, C.B.7
  • 49
    • 0242580787 scopus 로고    scopus 로고
    • Identification, Characterization, and Inhibition of Plasmodium falciparum β-Hydroxyacyl-Acyl Carrier Protein Dehydratase (FabZ)
    • DOI 10.1074/jbc.M304283200
    • Sharma, S.K.; Kapoor, M.; Ramya, T.N.; Kumar, S.; Kumar, G.; Modak, R.; Sharma, S.; Surolia, N.; Surolia, A. Identification, characterization, and inhibition of Plasmodium falciparum beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ). J. Biol. Chem., 2003, 278 (46), 45661-71. (Pubitemid 37432708)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45661-45671
    • Sharma, S.K.1    Kapoor, M.2    Ramya, T.N.C.3    Kumar, S.4    Kumar, G.5    Modak, R.6    Sharma, S.7    Surolia, N.8    Surolia, A.9
  • 50
    • 3342944977 scopus 로고    scopus 로고
    • 1,2-Dithiole-3-ones as potent inhibitors of the bacterial 3-ketoacyl acyl carrier protein synthase III (FabH)
    • DOI 10.1128/AAC.48.8.3093-3102.2004
    • He, X.; Reeve, A.M.; Desai, U.R.; Kellogg, G.E.; Reynolds, K.A. 1,2-dithiole-3-ones as potent inhibitors of the bacterial 3-ketoacyl acyl carrier protein synthase III (FabH). Antimicrob. Agents Chemother., 2004, 48 (8), 3093-102. (Pubitemid 38989179)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.8 , pp. 3093-3102
    • He, X.1    Reeve, A.M.2    Desai, U.R.3    Kellogg, G.E.4    Reynolds, K.A.5
  • 53
    • 0031052025 scopus 로고    scopus 로고
    • Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite
    • DOI 10.1074/jbc.272.7.3961
    • Srivastava, I.K.; Rottenberg, H.; Vaidya, A.B. Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite. J. Biol. Chem., 1997, 272 (7), 3961-6. (Pubitemid 27078454)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 3961-3966
    • Srivastava, I.K.1    Rottenberg, H.2    Vaidya, A.B.3
  • 55
    • 40649128497 scopus 로고    scopus 로고
    • New antimalarial targets: The example of glucose transport
    • Patel, A. P.; Staines, H.M.; Krishna, S. New antimalarial targets: the example of glucose transport. Travel. Med. Infect. Dis., 2008, 6 (1-2), 58-66.
    • (2008) Travel. Med. Infect. Dis. , vol.6 , Issue.1-2 , pp. 58-66
    • Patel, A.P.1    Staines, H.M.2    Krishna, S.3
  • 56
    • 0038324472 scopus 로고    scopus 로고
    • Inhibitors of the Plasmodium palciparum parasite aspartic protease plasmepsin II as potential antimalarial agents
    • DOI 10.2174/0929867033457674
    • Boss, C.; Richard-Bildstein, S.; Weller, T.; Fischli, W.; Meyer, S.; Binkert, C. Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents. Curr. Med. Chem., 2003, 10 (11), 883-907. (Pubitemid 36582237)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.11 , pp. 883-907
    • Boss, C.1    Richard-Bildstein, S.2    Weller, T.3    Fischli, W.4    Meyer, S.5    Binkert, C.6
  • 58
    • 33846455091 scopus 로고    scopus 로고
    • Antimalarial drugs inhibiting hemozoin (β-hematin) formation: A mechanistic update
    • DOI 10.1016/j.lfs.2006.11.008, PII S0024320506008630
    • Kumar, S.; Guha, M.; Choubey, V.; Maity, P.; Bandyopadhyay, U. Antimalarial drugs inhibiting hemozoin (beta-hematin) formation: a mechanistic update. Life Sci., 2007, 80 (9), 813-28. (Pubitemid 46149853)
    • (2007) Life Sciences , vol.80 , Issue.9 , pp. 813-828
    • Kumar, S.1    Guha, M.2    Choubey, V.3    Maity, P.4    Bandyopadhyay, U.5
  • 59
    • 0027673463 scopus 로고
    • Hemoglobin degradation in Plasmodium-infected red blood cells
    • Goldberg, D.E. Hemoglobin degradation in Plasmodium-infected red blood cells. Semin. Cell Biol., 1993, 4 (5), 355-61.
    • (1993) Semin. Cell Biol. , vol.4 , Issue.5 , pp. 355-361
    • Goldberg, D.E.1
  • 61
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • DOI 10.1016/S0968-0896(99)00004-8, PII S0968089699000048
    • Olson, J.E.; Lee, G.K.; Semenov, A.; Rosenthal, P.J. Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorg. Med. Chem., 1999, 7 (4), 633-8. (Pubitemid 29150306)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.4 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 62
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites
    • Rosenthal, P.J. Plasmodium falciparum: effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites. Exp. Parasitol., 1995, 80 (2), 272-81.
    • (1995) Exp. Parasitol. , vol.80 , Issue.2 , pp. 272-281
    • Rosenthal, P.J.1
  • 63
    • 33747177314 scopus 로고    scopus 로고
    • Plasmepsins as potential targets for new antimalarial therapy
    • DOI 10.1002/med.20082
    • Ersmark, K.; Samuelsson, B.; Hallberg, A. Plasmepsins as potential targets for new antimalarial therapy. Med. Res. Rev., 2006, 26 (5), 626-66. (Pubitemid 44230415)
    • (2006) Medicinal Research Reviews , vol.26 , Issue.5 , pp. 626-666
    • Ersmark, K.1    Samuelsson, B.2    Hallberg, A.3
  • 64
    • 0034232515 scopus 로고    scopus 로고
    • Proteases involved in erythrocyte invasion by the malaria parasite: Function and potential as chemotherapeutic targets
    • Blackman, M.J. Proteases involved in erythrocyte invasion by the malaria parasite: function and potential as chemotherapeutic targets. Curr. Drug Targets. 2000, 1 (1), 59-83.
    • (2000) Curr. Drug Targets. , vol.1 , Issue.1 , pp. 59-83
    • Blackman, M.J.1
  • 65
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson, K.K.; Duffin, K.L.; Goldberg, D.E. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J. Biol. Chem., 1999, 274 (45), 32411-7.
    • (1999) J. Biol. Chem. , vol.274 , Issue.45 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 68
    • 0025754304 scopus 로고
    • Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease
    • Goldberg, D.E.; Slater, A.F.; Beavis, R.; Chait, B.; Cerami, A.; Henderson, G.B. Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease. J. Exp. Med., 1991, 173 (4), 961-9.
    • (1991) J. Exp. Med. , vol.173 , Issue.4 , pp. 961-969
    • Goldberg, D.E.1    Slater, A.F.2    Beavis, R.3    Chait, B.4    Cerami, A.5    Henderson, G.B.6
  • 69
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparium
    • DOI 10.1146/annurev.micro.51.1.97
    • Francis, S.E.; Sullivan, D.J., Jr.; Goldberg, D.E. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu. Rev. Microbiol., 1997, 51 , 97-123. (Pubitemid 27433044)
    • (1997) Annual Review of Microbiology , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 70
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • DOI 10.1074/jbc.M408123200
    • Klemba, M.; Gluzman, I.; Goldberg, D.E. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J. Biol. Chem., 2004, 279 (41), 43000-7. (Pubitemid 39372193)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 71
    • 0034844897 scopus 로고    scopus 로고
    • The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes
    • PII S0166685101003279
    • Gavigan, C.S.; Dalton, J.P.; Bell, A. The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes. Mol. Biochem. Parasitol., 2001, 117 (1), 37-48. (Pubitemid 32823481)
    • (2001) Molecular and Biochemical Parasitology , vol.117 , Issue.1 , pp. 37-48
    • Gavigan, C.S.1    Dalton, J.P.2    Bell, A.3
  • 72
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • DOI 10.1016/0166-6851(93)90069-A
    • Atamna, H.; Ginsburg, H. Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. Mol. Biochem. Parasitol., 1993, 61 (2), 231-41. (Pubitemid 223039723)
    • (1993) Molecular and Biochemical Parasitology , vol.61 , Issue.2 , pp. 231-241
    • Atamna, H.1    Ginsburg, H.2
  • 73
  • 74
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine protease of malaria parasites: Targets for chemotherapy
    • DOI 10.2174/1381612023394197
    • Rosenthal, P.J.; Sijwali, P.S.; Singh, A.; Shenai, B.R. Cysteine proteases of malaria parasites: targets for chemotherapy. Curr. Pharm. Des., 2002, 8 (18), 1659-72. (Pubitemid 34752832)
    • (2002) Current Pharmaceutical Design , vol.8 , Issue.18 , pp. 1659-1672
    • Rosenthal, P.J.1    Sijwali, P.S.2    Singh, A.3    Shenai, B.R.4
  • 75
    • 0025719869 scopus 로고
    • Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase
    • Rosenthal, P.J.; Wollish, W.S.; Palmer, J.T.; Rasnick, D. Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase. J. Clin. Invest., 1991, 88 (5), 1467-72.
    • (1991) J. Clin. Invest. , vol.88 , Issue.5 , pp. 1467-1472
    • Rosenthal, P.J.1    Wollish, W.S.2    Palmer, J.T.3    Rasnick, D.4
  • 78
    • 0035112253 scopus 로고    scopus 로고
    • Comparison of efficacies of cysteine protease inhibitors against five strains of Plasmodium falciparum
    • DOI 10.1128/AAC.45.3.949-951.2001
    • Singh, A.; Rosenthal, P.J. Comparison of efficacies of cysteine protease inhibitors against five strains of Plasmodium falciparum. Antimicrob. Agents Chemother., 2001, 45 (3), 949-51. (Pubitemid 32182053)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.3 , pp. 949-951
    • Singh, A.1    Rosenthal, P.J.2
  • 80
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
    • DOI 10.1042/0264-6021:3600481
    • Sijwali, P.S.; Shenai, B.R.; Gut, J.; Singh, A.; Rosenthal, P.J. Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3. Biochem. J., 2001, 360 (Pt 2), 481-9. (Pubitemid 33151343)
    • (2001) Biochemical Journal , vol.360 , Issue.2 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.4    Rosenthal, P.J.5
  • 81
    • 32644476297 scopus 로고    scopus 로고
    • Plasmodium falciparum: Biochemical characterization of the cysteine protease falcipain-2'
    • DOI 10.1016/j.exppara.2005.10.007, PII S0014489405002808
    • Singh, N.; Sijwali, P.S.; Pandey, K.C.; Rosenthal, P.J. Plasmodium falciparum: biochemical characterization of the cysteine protease falcipain-2'. Exp. Parasitol, 2006, 112 (3), 187-92. (Pubitemid 43247780)
    • (2006) Experimental Parasitology , vol.112 , Issue.3 , pp. 187-192
    • Singh, N.1    Sijwali, P.S.2    Pandey, K.C.3    Rosenthal, P.J.4
  • 82
    • 23944479731 scopus 로고    scopus 로고
    • Characterization of amino acid variation at strategic positions in parasite and human proteases for selective inhibition of falcipains in Plasmodium falciparum
    • DOI 10.1016/j.bbrc.2005.07.147, PII S0006291X05016153
    • Goh, L.L.; Sim, T.S. Characterization of amino acid variation at strategic positions in parasite and human proteases for selective inhibition of falcipains in Plasmodium falciparum. Biochem. Biophys. Res. Commun., 2005, 335 (3), 762-70. (Pubitemid 41188264)
    • (2005) Biochemical and Biophysical Research Communications , vol.335 , Issue.3 , pp. 762-770
    • Liuh, L.G.1    Sim, T.S.2
  • 83
    • 3142626622 scopus 로고    scopus 로고
    • Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth
    • DOI 10.1111/j.1365-2958.2004.04108.x
    • Eksi, S.; Czesny, B.; Greenbaum, D.C.; Bogyo, M.; Williamson, K.C. Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth. Mol. Microbiol., 2004, 53 (1), 243-50. (Pubitemid 38901394)
    • (2004) Molecular Microbiology , vol.53 , Issue.1 , pp. 243-250
    • Eksi, S.1    Czesny, B.2    Greenbaum, D.C.3    Bogyo, M.4    Williamson, K.C.5
  • 84
  • 85
    • 34147117996 scopus 로고    scopus 로고
    • Falcipain-1, a Plasmodium falciparum cysteine protease with vaccine potential
    • DOI 10.1128/IAI.01533-06
    • Kumar, A.; Kumar, K.; Korde, R.; Puri, S.K.; Malhotra, P.; Singh Chauhan, V. Falcipain-1, a Plasmodium falciparum cysteine protease with vaccine potential. Infect. Immun., 2007, 75 (4), 2026-34. (Pubitemid 46559472)
    • (2007) Infection and Immunity , vol.75 , Issue.4 , pp. 2026-2034
    • Kumar, A.1    Kumar, K.2    Korde, R.3    Puri, S.K.4    Malhotra, P.5    Chauhan, V.S.6
  • 88
    • 33751432934 scopus 로고    scopus 로고
    • Falstatin a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion
    • Pandey, K.C.; Singh, N.; Arastu-Kapur, S.; Bogyo, M.; Rosenthal, P.J. Falstatin, a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion. PLoS Pathog., 2006, 2 (11), e117.
    • (2006) PLoS Pathog. , vol.2 , Issue.11
    • Pandey, K.C.1    Singh, N.2    Arastu-Kapur, S.3    Bogyo, M.4    Rosenthal, P.J.5
  • 89
    • 4544367028 scopus 로고    scopus 로고
    • Homology modeling and mutagenesis analyses of Plasmodium falciparum falcipain 2A: Implications for rational drug design
    • DOI 10.1016/j.bbrc.2004.08.130, PII S0006291X0401887X
    • Goh, L.L.; Sim, T.S. Homology modeling and mutagenesis analyses of Plasmodium falciparum falcipain 2A: implications for rational drug design. Biochem. Biophys. Res. Commun., 2004, 323 (2), 565-72. (Pubitemid 39221134)
    • (2004) Biochemical and Biophysical Research Communications , vol.323 , Issue.2 , pp. 565-572
    • Goh, L.L.1    Sim, T.S.2
  • 90
    • 44949174908 scopus 로고    scopus 로고
    • A prodomain peptide of Plasmodium falciparum cysteine protease (falcipain-2) inhibits malaria parasite development
    • DOI 10.1021/jm070735f
    • Korde, R.; Bhardwaj, A.; Singh, R.; Srivastava, A.; Chauhan, V.S.; Bhatnagar, R.K.; Malhotra, P. A prodomain peptide of Plasmodium falciparum cysteine protease (falcipain-2) inhibits malaria parasite development. J. Med. Chem., 2008, 51 (11), 3116-23. (Pubitemid 351821872)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.11 , pp. 3116-3123
    • Korde, R.1    Bhardwaj, A.2    Singh, R.3    Srivastava, A.4    Chauhan, V.S.5    Bhatnagar, R.K.6    Malhotra, P.7
  • 91
    • 0037177832 scopus 로고    scopus 로고
    • Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain
    • DOI 10.1074/jbc.M109680200
    • Sijwali, P.S.; Shenai, B.R.; Rosenthal, P.J. Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. J. Biol. Chem., 2002, 277(17), 14910-5. (Pubitemid 34952565)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14910-14915
    • Sijwali, P.S.1    Shenai, B.R.2    Rosenthal, P.J.3
  • 93
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • DOI 10.1021/jm990412m
    • Leung, D.; Abbenante, G.; Fairlie, D.P. Protease inhibitors: current status and future prospects. J. Med. Chem., 2000, 43 (3), 305-41. (Pubitemid 30102072)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.3 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 94
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I.; Berger, A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun., 1967, 27 (2), 157-62.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , Issue.2 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 95
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • PII S0166685101004388
    • Sajid, M.; McKerrow, J.H. Cysteine proteases of parasitic organisms. Mol. Biochem. Parasitol., 2002, 120 (1), 1-21. (Pubitemid 34159288)
    • (2002) Molecular and Biochemical Parasitology , vol.120 , Issue.1 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 96
    • 0037447948 scopus 로고    scopus 로고
    • Structure-based approach to falcipain-2 inhibitors: Synthesis and biological evaluation of 1,6,7-Trisubstituted dihydroisoquinolines and isoquinolines
    • DOI 10.1016/S0968-0896(03)00117-2
    • Batra, S.; Sabnis, Y.A.; Rosenthal, P.J.; Avery, M.A. Structure-based approach to falcipain-2 inhibitors: synthesis and biological evaluation of 1,6,7-trisubstituted dihydroisoquinolines and isoquinolines. Bioorg. Med. Chem., 2003, 11 (10), 2293-9. (Pubitemid 36457857)
    • (2003) Bioorganic and Medicinal Chemistry , vol.11 , Issue.10 , pp. 2293-2299
    • Batra, S.1    Sabnis, Y.A.2    Rosenthal, P.J.3    Avery, M.A.4
  • 97
    • 0027512171 scopus 로고
    • Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria
    • Rosenthal, P.J.; Lee, G.K.; Smith, R.E. Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria. J. Clin. Invest., 1993, 91 (3), 1052-6. (Pubitemid 23095281)
    • (1993) Journal of Clinical Investigation , vol.91 , Issue.3 , pp. 1052-1056
    • Rosenthal, P.J.1    Lee, G.K.2    Smith, R.E.3
  • 99
    • 0037226491 scopus 로고    scopus 로고
    • Structure-activity relationships for inhibition of cysteine protease activity and development of Plasmodium falciparum by peptidyl vinyl sulfones
    • DOI 10.1128/AAC.47.1.154-160.2003
    • Shenai, B.R.; Lee, B.J.; Alvarez-Hernandez, A.; Chong, P.Y.; Emal, C.D.; Neitz, R.J.; Roush, W.R.; Rosenthal, P.J. Structure-activity relationships for inhibition of cysteine protease activity and development of Plasmodium falciparum by peptidyl vinyl sulfones. Antimicrob. Agents Chemother., 2003, 47 (1), 154-60. (Pubitemid 36070357)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.1 , pp. 154-160
    • Shenai, B.R.1    Lee, B.J.2    Alvarez-Hernandez, A.3    Chong, P.Y.4    Emal, C.D.5    Neitz, R.J.6    Roush, W.R.7    Rosenthal, P.J.8
  • 100
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers, J.C.; Asgian, J.L.; Ekici, O.D.; James, K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev., 2002, 102 (12), 4639-750.
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 101
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer, J.T.; Rasnick, D.; Klaus, J.L.; Bromme, D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J. Med. Chem., 1995, 38 (17), 3193-6.
    • (1995) J. Med. Chem. , vol.38 , Issue.17 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.L.3    Bromme, D.4
  • 105
    • 0029130176 scopus 로고
    • Aziridine analogs of [[trans-(epoxysuccinyl)-L-leucyl]amino]-4- guanidinobutane (E-64) as inhibitors of cysteine proteases
    • Martichonok, V.; Plouffe, C.; Storer, A.C.; Menard, R.; Jones, J.B. Aziridine analogs of [[trans-(epoxysuccinyl)-L-leucyl]amino]-4-guanidinobutane (E-64) as inhibitors of cysteine proteases. J. Med. Chem., 1995, 38 (16), 3078-85.
    • (1995) J. Med. Chem. , vol.38 , Issue.16 , pp. 3078-3085
    • Martichonok, V.1    Plouffe, C.2    Storer, A.C.3    Menard, R.4    Jones, J.B.5
  • 108
    • 0037528821 scopus 로고    scopus 로고
    • Non-peptidic inhibitors of cysteine proteases
    • Schirmeister, T.; Kaeppler, U. Non-peptidic inhibitors of cysteine proteases. Mini Rev. Med. Chem., 2003, 3 (4), 361-73.
    • (2003) Mini Rev. Med. Chem. , vol.3 , Issue.4 , pp. 361-373
    • Schirmeister, T.1    Kaeppler, U.2
  • 109
    • 0141627969 scopus 로고    scopus 로고
    • Synthesis and evaluation of isatins and thiosemicarbazone derivatives against cruzain, falcipain-2 and rhodesain
    • DOI 10.1016/S0960-894X(03)00756-X
    • Chiyanzu, I.; Hansell, E.; Gut, J.; Rosenthal, P.J.; McKerrow, J.H.; Chibale, K. Synthesis and evaluation of isatins and thiosemicarbazone derivatives against cruzain, falcipain-2 and rhodesain. Bioorg. Med. Chem. Lett., 2003, 13 (20), 3527-30. (Pubitemid 37141422)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.20 , pp. 3527-3530
    • Chiyanzu, I.1    Hansell, E.2    Gut, J.3    Rosenthal, P.J.4    McKerrow, J.H.5    Chibale, K.6
  • 113
    • 0036244780 scopus 로고    scopus 로고
    • Homology modeling of falcipain-2: Validation, De Novo ligand design and synthesis of novel inhibitors
    • Sabnis, Y.; Rosenthal, P.J.; Desai, P.; Avery, M.A. Homology modeling of falcipain-2: validation, de novo ligand design and synthesis of novel inhibitors. J. Biomol. Struct. Dyn., 2002, 19 (5), 765-74. (Pubitemid 34475607)
    • (2002) Journal of Biomolecular Structure and Dynamics , vol.19 , Issue.5 , pp. 765-774
    • Sabnis, Y.1    Rosenthal, P.J.2    Desai, P.3    Avery, M.A.4
  • 116
    • 61449267734 scopus 로고    scopus 로고
    • Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: Implications for substrate specificity
    • Kerr, I.D.; Lee, J.H.; Pandey, K.C.; Harrison, A.; Sajid, M.; Rosenthal, P.J.; Brinen, L.S. Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity. J. Med. Chem., 2009, 52 (3), 852-7.
    • (2009) J. Med. Chem. , vol.52 , Issue.3 , pp. 852-857
    • Kerr, I.D.1    Lee, J.H.2    Pandey, K.C.3    Harrison, A.4    Sajid, M.5    Rosenthal, P.J.6    Brinen, L.S.7
  • 118
    • 1642422393 scopus 로고    scopus 로고
    • Exploring the role of putative active site amino acids and pro-region motif of recombinant falcipain-2: A principal hemoglobinase of Plasmodium falciparum
    • DOI 10.1016/j.bbrc.2004.02.177, PII S0006291X04004565
    • Kumar, A.; Dasaradhi, P.V.; Chauhan, V.S.; Malhotra, P. Exploring the role of putative active site amino acids and pro-region motif of recombinant falcipain-2: a principal hemoglobinase of Plasmodium falciparum. Biochem. Biophys. Res. Commun., 2004, 317 (1), 38-45. (Pubitemid 38401962)
    • (2004) Biochemical and Biophysical Research Communications , vol.317 , Issue.1 , pp. 38-45
    • Kumar, A.1    Dasaradhi, P.V.N.2    Chauhan, V.S.3    Malhotra, P.4
  • 119
    • 66349120908 scopus 로고    scopus 로고
    • Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum
    • Pandey, K.C.; Barkan, D.T.; Sali, A.; Rosenthal, P.J. Regulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparum. PLoS One. 2009, 4 (5), e5694.
    • (2009) PLoS One , vol.4 , Issue.5
    • Pandey, K.C.1    Barkan, D.T.2    Sali, A.3    Rosenthal, P.J.4
  • 121
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G.; Willett, P.; Glen, R.C. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol., 1995, 245 (1), 43-53.
    • (1995) J. Mol. Biol. , vol.245 , Issue.1 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 122
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • DOI 10.1006/jmbi.1996.0897
    • Jones, G.; Willett, P.; Glen, R.C.; Leach, A.R.; Taylor, R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol., 1997, 267 (3), 727-48. (Pubitemid 27170693)
    • (1997) Journal of Molecular Biology , vol.267 , Issue.3 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 124
  • 125
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • DOI 10.1023/A:1011115820450
    • Ewing, T.J.; Makino, S.; Skillman, A.G.; Kuntz, I.D. DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J. Comput. Aided Mol. Des., 2001, 15 (5), 411-28. (Pubitemid 32452109)
    • (2001) Journal of Computer-Aided Molecular Design , vol.15 , Issue.5 , pp. 411-428
    • Ewing, T.J.A.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 127
    • 0034649618 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations
    • DOI 10.1021/jm001044l
    • Bissantz, C.; Folkers, G.; Rognan, D. Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations. J. Med. Chem., 2000, 43 (25), 4759-67. (Pubitemid 32002687)
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.25 , pp. 4759-4767
    • Bissantz, C.1    Folkers, G.2    Rognan, D.3
  • 128
    • 11144323163 scopus 로고    scopus 로고
    • Virtual screening of chemical libraries
    • DOI 10.1038/nature03197
    • Shoichet, B.K. Virtual screening of chemical libraries. Nature. 2004, 432 (7019), 862-5. (Pubitemid 40037142)
    • (2004) Nature , vol.432 , Issue.7019 , pp. 862-865
    • Shoichet, B.K.1
  • 129
    • 10644241872 scopus 로고    scopus 로고
    • Identification of novel parasitic cysteine protease inhibitors using virtual screening. 1. The ChemBridge database
    • DOI 10.1021/jm0493717
    • Desai, P.V.; Patny, A.; Sabnis, Y.; Tekwani, B.; Gut, J.; Rosenthal, P.; Srivastava, A.; Avery, M. Identification of novel parasitic cysteine protease inhibitors using virtual screening. 1. The ChemBridge database. J. Med. Chem., 2004, 47 (26), 6609-15. (Pubitemid 39657322)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.26 , pp. 6609-6615
    • Desai, P.V.1    Patny, A.2    Sabnis, Y.3    Tekwani, B.4    Gut, J.5    Rosenthal, P.6    Srivastava, A.7    Avery, M.8
  • 130
    • 33644854957 scopus 로고    scopus 로고
    • Identification of novel parasitic cysteine protease inhibitors by use of virtual screening. 2. The available chemical directory
    • DOI 10.1021/jm0505765
    • Desai, P.V.; Patny, A.; Gut, J.; Rosenthal, P.J.; Tekwani, B.; Srivastava, A.; Avery, M. Identification of novel parasitic cysteine protease inhibitors by use of virtual screening. 2. The available chemical directory. J. Med. Chem., 2006, 49 (5), 1576-84. (Pubitemid 43376503)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.5 , pp. 1576-1584
    • Desai, P.V.1    Patny, A.2    Gut, J.3    Rosenthal, P.J.4    Tekwani, B.5    Srivastava, A.6    Avery, M.7
  • 131
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(96)00423-1, PII S0169409X96004231
    • Lipinski, C.; Lombardo, F.; Dominy, B.; Feeney, P. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Delivery Rev., 1997, 23, 3-25. (Pubitemid 27046991)
    • (1997) Advanced Drug Delivery Reviews , vol.23 , Issue.1-3 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 132
    • 68549087091 scopus 로고    scopus 로고
    • Identification of novel falcipain-2 inhibitors as potential antimalarial agents through structure-based virtual screening
    • Li, H.; Huang, J.; Chen, L.; Liu, X.; Chen, T.; Zhu, J.; Lu, W.; Shen, X.; Li, J.; Hilgenfeld, R.; Jiang, H. Identification of novel falcipain-2 inhibitors as potential antimalarial agents through structure-based virtual screening. J. Med. Chem., 2009, 52 (15), 4936-40.
    • (2009) J. Med. Chem. , vol.52 , Issue.15 , pp. 4936-4940
    • Li, H.1    Huang, J.2    Chen, L.3    Liu, X.4    Chen, T.5    Zhu, J.6    Lu, W.7    Shen, X.8    Li, J.9    Hilgenfeld, R.10    Jiang, H.11
  • 133
    • 8544230644 scopus 로고    scopus 로고
    • GAsDock: A new approach for rapid flexible docking based on an improved multi-population genetic algorithm
    • DOI 10.1016/j.bmcl.2004.06.091, PII S0960894X04008820
    • Li, H.; Li, C.; Gui, C.; Luo, X.; Chen, K.; Shen, J.; Wang, X.; Jiang, H. GAsDock: a new approach for rapid flexible docking based on an improved multi-population genetic algorithm. Bioorg. Med. Chem. Lett., 2004, 14 (18), 4671-6. (Pubitemid 39490287)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.18 , pp. 4671-4676
    • Li, H.1    Li, C.2    Gui, C.3    Luo, X.4    Chen, K.5    Shen, J.6    Wang, X.7    Jiang, H.8
  • 135
    • 0030110888 scopus 로고    scopus 로고
    • A technique to study molecular recognition in drug design: Preliminary application of free energy derivatives to inhibition of a malarial cysteine protease
    • DOI 10.1002/(SICI)1099-1352(199603)9:2<103::AID-JMR246>3.0.CO;2-A
    • Cieplak, P.; Kollman, P.A. A technique to study molecular recognition in drug design: preliminary application of free energy derivatives to inhibition of a malarial cysteine protease. J. Mol. Recognit., 1996, 9 (2), 103-12. (Pubitemid 26369485)
    • (1996) Journal of Molecular Recognition , vol.9 , Issue.2 , pp. 103-112
    • Cieplak, P.1    Kollman, P.A.2
  • 137
    • 65249168707 scopus 로고    scopus 로고
    • Rational design of improved aziridine-based inhibitors of cysteine proteases
    • Buback, V.; Mladenovic, M.; Engels, B.; Schirmeister, T. Rational design of improved aziridine-based inhibitors of cysteine proteases. J. Phys. Chem. B. 2009, 113 (15), 5282-9.
    • (2009) J. Phys. Chem. B. , vol.113 , Issue.15 , pp. 5282-5289
    • Buback, V.1    Mladenovic, M.2    Engels, B.3    Schirmeister, T.4
  • 138
    • 4944256999 scopus 로고    scopus 로고
    • Model Calculations about the Influence of Protic Environments on the Alkylation Step of Epoxide, Aziridine, and Thiirane Based Cysteine Proteases Inhibitors
    • Helten, H.; Schirmeister, T.; Engels, B. Model Calculations about the Influence of Protic Environments on the Alkylation Step of Epoxide, Aziridine, and Thiirane Based Cysteine Proteases Inhibitors. J. Phys. Chem. A. 2004, 105, 7691-7701.
    • (2004) J. Phys. Chem. A. , vol.105 , pp. 7691-7701
    • Helten, H.1    Schirmeister, T.2    Engels, B.3
  • 139
    • 11844285645 scopus 로고    scopus 로고
    • Theoretical studies about the influence of different ring substituents on the nucleophilic ring opening of three-membered heterocycles and possible implications for the mechanisms of cysteine protease inhibitors
    • DOI 10.1021/jo048373w
    • Helten, H.; Schirmeister, T.; Engels, B. Theoretical studies about the influence of different ring substituents on the nucleophilic ring opening of three-membered heterocycles and possible implications for the mechanisms of cysteine protease inhibitors. J. Org. Chem., 2005, 70 (1), 233-7. (Pubitemid 40093412)
    • (2005) Journal of Organic Chemistry , vol.70 , Issue.1 , pp. 233-237
    • Helten, H.1    Schirmeister, T.2    Engels, B.3
  • 140
    • 34547587912 scopus 로고    scopus 로고
    • The importance of the active site histidine for the activity of epoxide-or aziridine-based inhibitors of cysteine proteases
    • Mladenovic, M.; Schirmeister, T.; Thiel, S.; Thiel, W.; Engels, B. The importance of the active site histidine for the activity of epoxide-or aziridine-based inhibitors of cysteine proteases. ChemMedChem. 2007, 2 (1), 120-8.
    • (2007) ChemMedChem. , vol.2 , Issue.1 , pp. 120-128
    • Mladenovic, M.1    Schirmeister, T.2    Thiel, S.3    Thiel, W.4    Engels, B.5
  • 141
    • 33749002536 scopus 로고    scopus 로고
    • Rational design of aziridine-containing cysteine protease inhibitors with improved potency: Studies on inhibition mechanism
    • DOI 10.1002/cmdc.200600081
    • Vicik, R.; Helten, H.; Schirmeister, T.; Engels, B. Rational design of aziridine-containing cysteine protease inhibitors with improved potency: studies on inhibition mechanism. ChemMedChem. 2006, 1 (9), 1021-8. (Pubitemid 44448802)
    • (2006) ChemMedChem , vol.1 , Issue.9 , pp. 1021-1028
    • Vicik, R.1    Helten, H.2    Schirmeister, T.3    Engels, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.