메뉴 건너뛰기




Volumn 26, Issue 5, 2006, Pages 626-666

Plasmepsins as potential targets for new antimalarial therapy

Author keywords

Aspartic protease; Malaria; Plasmepsin; Plasmodium falciparum; Protease inhibitor

Indexed keywords

4 AMINOQUINOLINE; 8 AMINOQUINOLINE DERIVATIVE; ANTIMALARIAL AGENT; ARTEMETHER; ARTESUNATE; ASPARTIC PROTEINASE; ATOVAQUONE; CHLOROQUINE; DOXYCYCLINE; FANSIDAR; HALOFANTRINE; HEMOGLOBIN; HISTO ASPARTIC PROTEASE; MEFLOQUINE; PEPSTATIN; PHENANTHRENE DERIVATIVE; PLASMEPSIN I; PLASMEPSIN II; PLASMEPSIN IV; PRIMAQUINE; PROGUANIL; PROTEINASE INHIBITOR; PYRIMETHAMINE; QUININE; QUINOLINE DERIVATIVE; RO 40 4388; STATINE; SULFADOXINE; TETRACYCLINE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33747177314     PISSN: 01986325     EISSN: None     Source Type: Journal    
DOI: 10.1002/med.20082     Document Type: Review
Times cited : (151)

References (168)
  • 1
    • 0034972445 scopus 로고    scopus 로고
    • The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden
    • Breman JG. The ears of the hippopotamus: Manifestations, determinants, and estimates of the malaria burden. Am J Trop Med Hyg 2001;64:1-11.
    • (2001) Am J Trop Med Hyg , vol.64 , pp. 1-11
    • Breman, J.G.1
  • 5
    • 0037033984 scopus 로고    scopus 로고
    • The economic and social burden of malaria
    • Sachs J, Malaney P. The economic and social burden of malaria. Nature 2002;415:680-685.
    • (2002) Nature , vol.415 , pp. 680-685
    • Sachs, J.1    Malaney, P.2
  • 6
    • 0027468375 scopus 로고
    • Malaria parasites go ape
    • White NJ. Malaria parasites go ape. Lancet 1993;341:793.
    • (1993) Lancet , vol.341 , pp. 793
    • White, N.J.1
  • 7
    • 7444266246 scopus 로고    scopus 로고
    • Clinical features and pathogenesis of severe malaria
    • Mackintosh CL, Beeson JG, Marsh K. Clinical features and pathogenesis of severe malaria. Trends Parasitol 2004;20:597-603.
    • (2004) Trends Parasitol , vol.20 , pp. 597-603
    • Mackintosh, C.L.1    Beeson, J.G.2    Marsh, K.3
  • 8
    • 4344659893 scopus 로고    scopus 로고
    • Are multilateral malaria research and control programs the most successful? Lessons from the past 100 years in Africa
    • Alilio Martin S, Bygbjerg Ib C, Breman Joel G. Are multilateral malaria research and control programs the most successful? Lessons from the past 100 years in Africa. Am J Trop Medicine Hyg 2004;71:268-278.
    • (2004) Am J Trop Medicine Hyg , vol.71 , pp. 268-278
    • Alilio Martin, S.1    Bygbjerg Ib, C.2    Breman Joel, G.3
  • 9
    • 0037033980 scopus 로고    scopus 로고
    • Progress and challenges for malaria vaccines
    • Richie TL, Saul A. Progress and challenges for malaria vaccines. Nature 2002;415:694-701.
    • (2002) Nature , vol.415 , pp. 694-701
    • Richie, T.L.1    Saul, A.2
  • 14
    • 13544252782 scopus 로고    scopus 로고
    • Using expression information to discover new drug and vaccine targets in the malaria parasite Plasmodium falciparum
    • Young JA, Winzeler EA. Using expression information to discover new drug and vaccine targets in the malaria parasite Plasmodium falciparum. Pharmacogenomics 2005;6:17-26.
    • (2005) Pharmacogenomics , vol.6 , pp. 17-26
    • Young, J.A.1    Winzeler, E.A.2
  • 17
    • 14644411893 scopus 로고    scopus 로고
    • Haemozoin (malaria pigment): A unique crystalline drug target
    • Egan TJ. Haemozoin (malaria pigment): A unique crystalline drug target. Targets 2003;2:115-124.
    • (2003) Targets , vol.2 , pp. 115-124
    • Egan, T.J.1
  • 18
    • 1142297431 scopus 로고    scopus 로고
    • Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs
    • Fitch CD. Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs. Life Sci 2004;74:1957-1972.
    • (2004) Life Sci , vol.74 , pp. 1957-1972
    • Fitch, C.D.1
  • 20
    • 20844440050 scopus 로고    scopus 로고
    • Dispiro-1,2,4-trioxane analogues of a prototype dispiro-1,2,4-trioxolane: Mechanistic comparators for artemisinin in the context of reaction pathways with Iron(II)
    • Tang Y, Dong Y, Wang X, Sriraghavan K, Wood JK, Vennerstrom JL. Dispiro-1,2,4-trioxane analogues of a prototype dispiro-1,2,4-trioxolane: Mechanistic comparators for artemisinin in the context of reaction pathways with Iron(II). J Org Chem 2005;70:5103-5110.
    • (2005) J Org Chem , vol.70 , pp. 5103-5110
    • Tang, Y.1    Dong, Y.2    Wang, X.3    Sriraghavan, K.4    Wood, J.K.5    Vennerstrom, J.L.6
  • 21
    • 14144253009 scopus 로고    scopus 로고
    • Mechanisms of resistance of malaria parasites to antifolates
    • Gregson A, Plowe CV. Mechanisms of resistance of malaria parasites to antifolates. Pharmacol Rev 2005;57:117-145.
    • (2005) Pharmacol Rev , vol.57 , pp. 117-145
    • Gregson, A.1    Plowe, C.V.2
  • 22
    • 3242781734 scopus 로고    scopus 로고
    • Therapy of falciparum malaria in sub-saharan Africa: From molecule to policy
    • Winstanley P, Ward S, Snow R, Breckenridge A. Therapy of falciparum malaria in sub-saharan Africa: From molecule to policy. Clin Microbiol Rev 2004;17:612-637.
    • (2004) Clin Microbiol Rev , vol.17 , pp. 612-637
    • Winstanley, P.1    Ward, S.2    Snow, R.3    Breckenridge, A.4
  • 23
    • 3242692444 scopus 로고    scopus 로고
    • Antimalarial combinations
    • Kremsner PG, Krishna S. Antimalarial combinations. Lancet 2004;364:285-294.
    • (2004) Lancet , vol.364 , pp. 285-294
    • Kremsner, P.G.1    Krishna, S.2
  • 25
    • 2142659388 scopus 로고    scopus 로고
    • Antimalarial drug resistance
    • White Nicholas J. Antimalarial drug resistance. J Clin Invest 2004;113:1084-1092.
    • (2004) J Clin Invest , vol.113 , pp. 1084-1092
    • White Nicholas, J.1
  • 27
    • 13844319811 scopus 로고    scopus 로고
    • Molecular mechanisms of resistance in antimalarial chemotherapy: The unmet challenge
    • 1 plate
    • Arav-Boger R, Shapiro TA. Molecular mechanisms of resistance in antimalarial chemotherapy: The unmet challenge. Annu Rev Pharmacol Toxicol 2005;45:565-585, 1 plate.
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 565-585
    • Arav-Boger, R.1    Shapiro, T.A.2
  • 28
    • 3142618432 scopus 로고    scopus 로고
    • The antimalarial drug resistance protein Plasmodium falciparum chloroquine resistance transporter binds chloroquine
    • Zhang H, Paguio M, Roepe PD. The antimalarial drug resistance protein Plasmodium falciparum chloroquine resistance transporter binds chloroquine. Biochemistry 2004;43:8290-8296.
    • (2004) Biochemistry , vol.43 , pp. 8290-8296
    • Zhang, H.1    Paguio, M.2    Roepe, P.D.3
  • 29
    • 0033004991 scopus 로고    scopus 로고
    • An overview of chemotherapeutic targets for antimalarial drug discovery
    • Olliaro PL, Yuthavong Y. An overview of chemotherapeutic targets for antimalarial drug discovery. Pharmacol Ther 1999;81:91-110.
    • (1999) Pharmacol Ther , vol.81 , pp. 91-110
    • Olliaro, P.L.1    Yuthavong, Y.2
  • 30
    • 0036833617 scopus 로고    scopus 로고
    • Chemotherapeutic agents against malaria: What next after chloroquine?
    • Dominguez JN. Chemotherapeutic agents against malaria: What next after chloroquine? Curr Top Med Chem 2002;2:1173-1185.
    • (2002) Curr Top Med Chem , vol.2 , pp. 1173-1185
    • Dominguez, J.N.1
  • 31
    • 4344696178 scopus 로고    scopus 로고
    • Antimalarial compound identification and design: Advances in the patent literature, 2000-2003
    • Waters NC, Dow GS, Kozar MP. Antimalarial compound identification and design: Advances in the patent literature, 2000-2003. Expert Opin Ther Patents 2004;14:1125-1138.
    • (2004) Expert Opin Ther Patents , vol.14 , pp. 1125-1138
    • Waters, N.C.1    Dow, G.S.2    Kozar, M.P.3
  • 32
    • 5044235372 scopus 로고    scopus 로고
    • New therapies for malaria
    • Woster PM. New therapies for malaria. Ann Rep Med Chem 2003;38:203-211.
    • (2003) Ann Rep Med Chem , vol.38 , pp. 203-211
    • Woster, P.M.1
  • 35
    • 12844269343 scopus 로고    scopus 로고
    • Structure-based drug discovery for Plasmodium falciparum
    • Mehlin C. Structure-based drug discovery for Plasmodium falciparum. Comb Chem High Throughput Screen 2005;8:5-14.
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 5-14
    • Mehlin, C.1
  • 36
    • 0033927095 scopus 로고    scopus 로고
    • Target-based drug discovery for malaria, leishmaniasis, and trypanosomiasis
    • Werbovetz KA. Target-based drug discovery for malaria, leishmaniasis, and trypanosomiasis. Curr Med Chem 2000;7:835-860.
    • (2000) Curr Med Chem , vol.7 , pp. 835-860
    • Werbovetz, K.A.1
  • 37
    • 20444363391 scopus 로고    scopus 로고
    • Malaria parasite transporters as a drug-delivery strategy
    • Biagini GA, Ward SA, Bray PG. Malaria parasite transporters as a drug-delivery strategy. Trends Parasitol 2005;21:299-301.
    • (2005) Trends Parasitol , vol.21 , pp. 299-301
    • Biagini, G.A.1    Ward, S.A.2    Bray, P.G.3
  • 38
    • 1542298986 scopus 로고    scopus 로고
    • Protein kinases as targets for anti-parasitic chemotherapy
    • Doerig C. Protein kinases as targets for anti-parasitic chemotherapy. Biochim Biophys Acta 2004;1697:155-168.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 155-168
    • Doerig, C.1
  • 39
    • 0036833567 scopus 로고    scopus 로고
    • Natural products as trypanocidal, antileishmanial, and antimalarial drugs
    • Fournet A, Munoz V. Natural products as trypanocidal, antileishmanial, and antimalarial drugs. CurrTop Med Chem 2002;2:1215-1237.
    • (2002) CurrTop Med Chem , vol.2 , pp. 1215-1237
    • Fournet, A.1    Munoz, V.2
  • 40
    • 0031894225 scopus 로고    scopus 로고
    • Screening aspartyl proteases with combinatorial libraries
    • Aspartic Proteinases
    • Carroll CD, Orlowski M. Screening aspartyl proteases with combinatorial libraries. Adv Exp Med Biol 1998;436 (Aspartic Proteinases):375-380.
    • (1998) Adv Exp Med Biol , vol.436 , pp. 375-380
    • Carroll, C.D.1    Orlowski, M.2
  • 42
    • 7444266700 scopus 로고    scopus 로고
    • Malaria parasite transmission stages: An update
    • Khan SM, Waters AP. Malaria parasite transmission stages: An update. Trends Parasitol 2004;20:575-580.
    • (2004) Trends Parasitol , vol.20 , pp. 575-580
    • Khan, S.M.1    Waters, A.P.2
  • 43
    • 0027673463 scopus 로고
    • Hemoglobin degradation in Plasmodium-infected red blood cells
    • Goldberg DE. Hemoglobin degradation in Plasmodium-infected red blood cells. Sem Cell Biol 1993;4:355-361.
    • (1993) Sem Cell Biol , vol.4 , pp. 355-361
    • Goldberg, D.E.1
  • 44
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparum
    • Francis SE, Sullivan DJ Jr, Goldberg DE. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu Rev Microbiol 1997;51:97-123.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 45
    • 0345652158 scopus 로고
    • Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine
    • Yayon A, Cabantchik ZI, Ginsburg H. Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine. EMBO J 1984;3:2695-2700.
    • (1984) EMBO J , vol.3 , pp. 2695-2700
    • Yayon, A.1    Cabantchik, Z.I.2    Ginsburg, H.3
  • 46
    • 0001306565 scopus 로고
    • 14C-labeled amino acids by the malaria [parasite] Plasmodium lophurea. IV. In vivo utilization of host-cell hemoglobin
    • 14C-labeled amino acids by the malaria [parasite] Plasmodium lophurea. IV. In vivo utilization of host-cell hemoglobin. Int J Biochem 1970;1:635-637.
    • (1970) Int J Biochem , vol.1 , pp. 635-637
    • Sherman, I.W.1    Tanigoshi, L.2
  • 47
    • 0017693186 scopus 로고
    • Amino acid metabolism and protein synthesis in malarial parasites
    • Sherman IW. Amino acid metabolism and protein synthesis in malarial parasites. Bull WHO 1977;55:265-276.
    • (1977) Bull WHO , vol.55 , pp. 265-276
    • Sherman, I.W.1
  • 48
    • 0037589002 scopus 로고    scopus 로고
    • Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum-infected red blood cells
    • Lew VL, Tiffert T, Ginsburg H. Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum-infected red blood cells. Blood 2003;101:4189-4194.
    • (2003) Blood , vol.101 , pp. 4189-4194
    • Lew, V.L.1    Tiffert, T.2    Ginsburg, H.3
  • 49
    • 0026915311 scopus 로고
    • Plasmodium falciparum: Differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor)
    • Bailly E, Jambou R, Savel J, Jaureguiberry G. Plasmodium falciparum: Differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor). J Protozool 1992;39:593-599.
    • (1992) J Protozool , vol.39 , pp. 593-599
    • Bailly, E.1    Jambou, R.2    Savel, J.3    Jaureguiberry, G.4
  • 51
    • 0028948564 scopus 로고
    • Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites
    • Rosenthal PJ. Plasmodium falciparum: Effects of proteinase inhibitors on globin hydrolysis by cultured malaria parasites. Exp Parasitol 1995;80:272-281.
    • (1995) Exp Parasitol , vol.80 , pp. 272-281
    • Rosenthal, P.J.1
  • 52
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • Olson JE, Lee GK, Semenov A, Rosenthal PJ. Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorg Med Chem 1999;7:633-638.
    • (1999) Bioorg Med Chem , vol.7 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 53
    • 0025754304 scopus 로고
    • Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease
    • Goldberg DE, Slater AFG, Beavis R, Chait B, Cerami A, Henderson GB. Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease. J Exp Med 1991;173:961-969.
    • (1991) J Exp Med , vol.173 , pp. 961-969
    • Goldberg, D.E.1    Slater, A.F.G.2    Beavis, R.3    Chait, B.4    Cerami, A.5    Henderson, G.B.6
  • 55
    • 0028287766 scopus 로고
    • Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum
    • Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C. Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 1994;64:177-190.
    • (1994) Mol Biochem Parasitol , vol.64 , pp. 177-190
    • Dame, J.B.1    Reddy, G.R.2    Yowell, C.A.3    Dunn, B.M.4    Kay, J.5    Berry, C.6
  • 56
    • 0033430156 scopus 로고    scopus 로고
    • The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum
    • Humphreys MJ, Moon RP, Klinder A, Fowler SD, Rupp K, Bur D, Ridley RG, Berry C. The aspartic proteinase from the rodent parasite Plasmodium berghei as a potential model for plasmepsins from the human malaria parasite, Plasmodium falciparum. FEBS Lett 1999;463:43-48.
    • (1999) FEBS Lett , vol.463 , pp. 43-48
    • Humphreys, M.J.1    Moon, R.P.2    Klinder, A.3    Fowler, S.D.4    Rupp, K.5    Bur, D.6    Ridley, R.G.7    Berry, C.8
  • 58
    • 0037154180 scopus 로고    scopus 로고
    • Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine
    • Banerjee R, Liu J, Beatty W, Pelosof L, Klemba M, Goldberg DE. Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc Natl Acad Sci USA 2002;99:990-995.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 59
    • 0029057887 scopus 로고
    • Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase
    • Salas F, Fichmann J, Lee GK, Scott MD, Rosenthal PJ. Functional expression of falcipain, a Plasmodium falciparum cysteine proteinase, supports its role as a malarial hemoglobinase. Infect Immun 1995;63:2120-2125.
    • (1995) Infect Immun , vol.63 , pp. 2120-2125
    • Salas, F.1    Fichmann, J.2    Lee, G.K.3    Scott, M.D.4    Rosenthal, P.J.5
  • 61
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai BR, Sijwali PS, Singh A, Rosenthal PJ. Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J Biol Chem 2000;275:29000-29010.
    • (2000) J Biol Chem , vol.275 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 62
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • Sijwali PS, Rosenthal PJ. Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum. Proc Natl Acad Sci USA 2004;101:4384-4389.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4384-4389
    • Sijwali, P.S.1    Rosenthal, P.J.2
  • 63
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum hemoglobinase falcipain-3
    • Sijwali PS, Shenai BR, Gut J, Singh A, Rosenthal PJ. Expression and characterization of the Plasmodium falciparum hemoglobinase falcipain-3. Biochem J 2001;360:481-489.
    • (2001) Biochem J , vol.360 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.4    Rosenthal, P.J.5
  • 64
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson KK, Duffin KL, Goldberg DE. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J Biol Chem 1999;274:32411-32417.
    • (1999) J Biol Chem , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 65
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • Klemba M, Gluzman I, Goldberg DE. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J Biol Chem 2004;279:43000-43007.
    • (2004) J Biol Chem , vol.279 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 66
  • 67
    • 0034844897 scopus 로고    scopus 로고
    • The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes
    • Gavigan CS, Dalton JP, Bell A. The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes. Mol Biochem Parasitol 2001;117:37-48.
    • (2001) Mol Biochem Parasitol , vol.117 , pp. 37-48
    • Gavigan, C.S.1    Dalton, J.P.2    Bell, A.3
  • 69
    • 0038691865 scopus 로고    scopus 로고
    • Food vacuole plasmepsins are processed at a conserved site by an acidic convertase activity in Plasmodium falciparum
    • Banerjee R, Francis SE, Goldberg DE. Food vacuole plasmepsins are processed at a conserved site by an acidic convertase activity in Plasmodium falciparum. Mol Biochem Parasitol 2003;129:157-165.
    • (2003) Mol Biochem Parasitol , vol.129 , pp. 157-165
    • Banerjee, R.1    Francis, S.E.2    Goldberg, D.E.3
  • 70
    • 0347122968 scopus 로고    scopus 로고
    • Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
    • Klemba M, Beatty W, Gluzman I, Goldberg DE. Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum. J Cell Biol 2004;164:47-56.
    • (2004) J Cell Biol , vol.164 , pp. 47-56
    • Klemba, M.1    Beatty, W.2    Gluzman, I.3    Goldberg, D.E.4
  • 71
    • 0031004534 scopus 로고    scopus 로고
    • Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II
    • Francis SE, Banerjee R, Goldberg DE. Biosynthesis and maturation of the malaria aspartic hemoglobinases plasmepsins I and II. J Biol Chem 1997;272:14961-14968.
    • (1997) J Biol Chem , vol.272 , pp. 14961-14968
    • Francis, S.E.1    Banerjee, R.2    Goldberg, D.E.3
  • 72
    • 0033553410 scopus 로고    scopus 로고
    • Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton
    • Le Bonniec S, Deregnaucourt C, Redeker V, Banerjee R, Grellier P, Goldberg DE, Schrevel J. Plasmepsin II, an acidic hemoglobinase from the Plasmodium falciparum food vacuole, is active at neutral pH on the host erythrocyte membrane skeleton. J Biol Chem 1999;274:14218-14223.
    • (1999) J Biol Chem , vol.274 , pp. 14218-14223
    • Le Bonniec, S.1    Deregnaucourt, C.2    Redeker, V.3    Banerjee, R.4    Grellier, P.5    Goldberg, D.E.6    Schrevel, J.7
  • 73
    • 0037181136 scopus 로고    scopus 로고
    • Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum
    • Wyatt DM, Berry C. Activity and inhibition of plasmepsin IV, a new aspartic proteinase from the malaria parasite, Plasmodium falciparum. FEBS Lett 2002;513:159-162.
    • (2002) FEBS Lett , vol.513 , pp. 159-162
    • Wyatt, D.M.1    Berry, C.2
  • 75
    • 8744303696 scopus 로고    scopus 로고
    • Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site
    • Bjelic S, Aaqvist J. Computational prediction of structure, substrate binding mode, mechanism, and rate for a malaria protease with a novel type of active site. Biochemistry 2004;43:14521-14528.
    • (2004) Biochemistry , vol.43 , pp. 14521-14528
    • Bjelic, S.1    Aaqvist, J.2
  • 76
    • 0037021403 scopus 로고    scopus 로고
    • The integration of genomic and structural information in the development of high affinity plasmepsin inhibitors
    • Nezami A, Freire E. The integration of genomic and structural information in the development of high affinity plasmepsin inhibitors. Int J Parasitol 2002;32:1669-1676.
    • (2002) Int J Parasitol , vol.32 , pp. 1669-1676
    • Nezami, A.1    Freire, E.2
  • 77
    • 33747153201 scopus 로고    scopus 로고
    • note
    • A search in the PDB for plasmepsins found 12 structures, and an additional 5 structures were processed or "on hold", as of August 2005.
  • 79
    • 0031894719 scopus 로고    scopus 로고
    • Structural analysis of plasmepsin II: A comparison with human aspartic proteases
    • Aspartic Proteinases
    • Silva AM, Lee AY, Erickson JW, Goldberg DE. Structural analysis of plasmepsin II: A comparison with human aspartic proteases. Adv Exp Med Biol 1998;436 (Aspartic Proteinases):363-373.
    • (1998) Adv Exp Med Biol , vol.436 , pp. 363-373
    • Silva, A.M.1    Lee, A.Y.2    Erickson, J.W.3    Goldberg, D.E.4
  • 83
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings ND, Barrett AJ. Evolutionary families of peptidases. Biochem J 1993;290:205-218.
    • (1993) Biochem J , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 84
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies DR. The structure and function of the aspartic proteinases. Annu Rev Biophys Biophys Chem 1990;19:189-215.
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 86
    • 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;27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 87
    • 0034778987 scopus 로고    scopus 로고
    • Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases
    • Northrop DB. Follow the protons: A low-barrier hydrogen bond unifies the mechanisms of the aspartic proteases. Acc Chem Res 2001;34:790-797.
    • (2001) Acc Chem Res , vol.34 , pp. 790-797
    • Northrop, D.B.1
  • 88
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn BM. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem Rev 2002;102:4431-4458.
    • (2002) Chem Rev , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 89
    • 0038184354 scopus 로고    scopus 로고
    • HIV-1 protease: Mechanism and drug discovery
    • Brik A, Wong C-H. HIV-1 protease: Mechanism and drug discovery. Org Biomol Chem 2003;1:5-14.
    • (2003) Org Biomol Chem , vol.1 , pp. 5-14
    • Brik, A.1    Wong, C.-H.2
  • 90
    • 0036008530 scopus 로고    scopus 로고
    • Role of water molecules in the structure and function of aspartic proteinases
    • Prasad BVLS, Suguna K. Role of water molecules in the structure and function of aspartic proteinases. Acta Crystallogr D Biol Crystallogr 2002;D58:250-259.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.D58 , pp. 250-259
    • Prasad, B.V.L.S.1    Suguna, K.2
  • 91
    • 0002903441 scopus 로고
    • Analog approaches to the structure of the transition state in enzyme reactions
    • Wolfenden R. Analog approaches to the structure of the transition state in enzyme reactions. Acc Chem Res 1972;5:10-18.
    • (1972) Acc Chem Res , vol.5 , pp. 10-18
    • Wolfenden, R.1
  • 92
    • 0015924871 scopus 로고
    • Enzymic catalysis and transition-state theory
    • Lienhard GE. Enzymic catalysis and transition-state theory. Science 1973;180:149-154.
    • (1973) Science , vol.180 , pp. 149-154
    • Lienhard, G.E.1
  • 93
    • 0037727675 scopus 로고    scopus 로고
    • Aspartic peptidase inhibitors: Implications in drug development
    • Dash C, Kulkarni A, Dunn B, Rao M. Aspartic peptidase inhibitors: Implications in drug development. Crit Rev Biochem Mol Biol 2003;38:89-119.
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 89-119
    • Dash, C.1    Kulkarni, A.2    Dunn, B.3    Rao, M.4
  • 94
    • 0031189711 scopus 로고    scopus 로고
    • Molecular recognition of protein-ligand complexes: Applications to drug design
    • Babine RE, Bender SL. Molecular recognition of protein-ligand complexes: Applications to drug design. Chem Rev 1997;97:1359-1472.
    • (1997) Chem Rev , vol.97 , pp. 1359-1472
    • Babine, R.E.1    Bender, S.L.2
  • 95
    • 0036218648 scopus 로고    scopus 로고
    • Aspartic proteinases in disease: A structural perspective
    • Cooper JB. Aspartic proteinases in disease: A structural perspective. Curr Drug Targets 2002;3:155-173.
    • (2002) Curr Drug Targets , vol.3 , pp. 155-173
    • Cooper, J.B.1
  • 97
    • 0038324472 scopus 로고    scopus 로고
    • Inhibitors of the Plasmodium falciparum parasite aspartic protease plasmepsin II as potential antimalarial agents
    • 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;10:883-907.
    • (2003) Curr Med Chem , vol.10 , pp. 883-907
    • Boss, C.1    Richard-Bildstein, S.2    Weller, T.3    Fischli, W.4    Meyer, S.5    Binkert, C.6
  • 98
    • 0031282557 scopus 로고    scopus 로고
    • 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 malariae parasite
    • Westling J, Yowell CA, Majer P, Erickson JW, Dame JB, Dunn BM. 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 malariae parasite. Exp Parasitol 1997;87:185-193.
    • (1997) Exp Parasitol , vol.87 , pp. 185-193
    • Westling, J.1    Yowell, C.A.2    Majer, P.3    Erickson, J.W.4    Dame, J.B.5    Dunn, B.M.6
  • 101
    • 0034615552 scopus 로고    scopus 로고
    • The two sides of enzyme-substrate specificity: Lessons from the aspartic proteinases
    • Dunn BM, Hung SH. The two sides of enzyme-substrate specificity: Lessons from the aspartic proteinases. Biochim Biophys Acta 2000;1477:231-240.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 231-240
    • Dunn, B.M.1    Hung, S.H.2
  • 102
    • 1842662675 scopus 로고    scopus 로고
    • Recombinant expression and enzymatic subsite characterization of plasmepsin 4 from the four Plasmodium species infecting man
    • Li T, Yowell CA, Beyer BB, Hung S-H, Westling J, Lam MT, Dunn BM, Dame JB. Recombinant expression and enzymatic subsite characterization of plasmepsin 4 from the four Plasmodium species infecting man. Mol Biochem Parasitol 2004;135:101-109.
    • (2004) Mol Biochem Parasitol , vol.135 , pp. 101-109
    • Li, T.1    Yowell, C.A.2    Beyer, B.B.3    Hung, S.-H.4    Westling, J.5    Lam, M.T.6    Dunn, B.M.7    Dame, J.B.8
  • 103
    • 13644263256 scopus 로고    scopus 로고
    • Active-site specificity of digestive aspartic peptidases from the four species of Plasmodium that infect humans using chromogenic combinatorial peptide libraries
    • Beyer BB, Johnson JV, Chung AY, Li T, Madabushi A, Agbandje-McKenna M, McKenna R, Dame JB, Dunn BM. Active-site specificity of digestive aspartic peptidases from the four species of Plasmodium that infect humans using chromogenic combinatorial peptide libraries. Biochemistry 2005;44:1768-1779.
    • (2005) Biochemistry , vol.44 , pp. 1768-1779
    • Beyer, B.B.1    Johnson, J.V.2    Chung, A.Y.3    Li, T.4    Madabushi, A.5    Agbandje-McKenna, M.6    McKenna, R.7    Dame, J.B.8    Dunn, B.M.9
  • 104
    • 0037175033 scopus 로고    scopus 로고
    • Active site contribution to specificity of the aspartic proteases plasmepsins I and II
    • Siripurkpong P, Yuvaniyama J, Wilairat P, Goldberg DE. Active site contribution to specificity of the aspartic proteases plasmepsins I and II. J Biol Chem 2002;277:41009-41013.
    • (2002) J Biol Chem , vol.277 , pp. 41009-41013
    • Siripurkpong, P.1    Yuvaniyama, J.2    Wilairat, P.3    Goldberg, D.E.4
  • 105
    • 0032977210 scopus 로고    scopus 로고
    • Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum
    • Tyas L, Gluzman I, Moon RP, Rupp K, Westling J, Ridley RG, Kay J, Goldberg DE, Berry C. Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum. FEBS Lett 1999;454:210-214.
    • (1999) FEBS Lett , vol.454 , pp. 210-214
    • Tyas, L.1    Gluzman, I.2    Moon, R.P.3    Rupp, K.4    Westling, J.5    Ridley, R.G.6    Kay, J.7    Goldberg, D.E.8    Berry, C.9
  • 106
    • 14844302643 scopus 로고    scopus 로고
    • Distal substrate interactions enhance plasmepsin activity
    • Istvan ES, Goldberg DE. Distal substrate interactions enhance plasmepsin activity. J Biol Chem 2005;280:6890-6896.
    • (2005) J Biol Chem , vol.280 , pp. 6890-6896
    • Istvan, E.S.1    Goldberg, D.E.2
  • 108
    • 0000406130 scopus 로고    scopus 로고
    • Development of anti-malarial inhibitors of hemoglobinases
    • Radding JA. Development of anti-malarial inhibitors of hemoglobinases. Annu Rep Med Chem 1999;34:159-168.
    • (1999) Annu Rep Med Chem , vol.34 , pp. 159-168
    • Radding, J.A.1
  • 109
    • 0033781741 scopus 로고    scopus 로고
    • Plasmepsins as antimalarial targets
    • Berry C. Plasmepsins as antimalarial targets. Curr Opin Drug Di De 2000;3:624-629.
    • (2000) Curr Opin Drug Di De , vol.3 , pp. 624-629
    • Berry, C.1
  • 110
    • 1642513580 scopus 로고    scopus 로고
    • Malarial proteinases: A review of the recent patent literature
    • Eckstein Jens W. Malarial proteinases: A review of the recent patent literature. I Drugs 2002;5:342-348.
    • (2002) I Drugs , vol.5 , pp. 342-348
    • Eckstein Jens, W.1
  • 112
    • 0031472092 scopus 로고    scopus 로고
    • New targets for antimalarial therapy: The plasmepsins, malaria parasite proteases
    • Berry C. New targets for antimalarial therapy: The plasmepsins, malaria parasite proteases. Biochem Educ 1997;25:191-194.
    • (1997) Biochem Educ , vol.25 , pp. 191-194
    • Berry, C.1
  • 113
    • 0002876387 scopus 로고    scopus 로고
    • Proteases as drug targets for the treatment of malaria
    • Berry C. Proteases as drug targets for the treatment of malaria. Prot Infect Agents 1999;165-188.
    • (1999) Prot Infect Agents , pp. 165-188
    • Berry, C.1
  • 114
    • 0030200511 scopus 로고    scopus 로고
    • Kinetic analysis of plasmepsins I and II, aspartic proteases of the Plasmodium falciparum digestive vacuole
    • Luker KE, Francis SE, Gluzman IY, Goldberg DE. Kinetic analysis of plasmepsins I and II, aspartic proteases of the Plasmodium falciparum digestive vacuole. Mol Biochem Parasitol 1996;79:71-78.
    • (1996) Mol Biochem Parasitol , vol.79 , pp. 71-78
    • Luker, K.E.1    Francis, S.E.2    Gluzman, I.Y.3    Goldberg, D.E.4
  • 115
    • 0037780064 scopus 로고    scopus 로고
    • High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor
    • Nezami A, Kimura T, Hidaka K, Kiso A, Liu J, Kiso Y, Goldberg DE, Freire E. High-affinity inhibition of a family of Plasmodium falciparum proteases by a designed adaptive inhibitor. Biochemistry 2003;42:8459-8464.
    • (2003) Biochemistry , vol.42 , pp. 8459-8464
    • Nezami, A.1    Kimura, T.2    Hidaka, K.3    Kiso, A.4    Liu, J.5    Kiso, Y.6    Goldberg, D.E.7    Freire, E.8
  • 117
    • 12544251879 scopus 로고    scopus 로고
    • The role of Plasmodium falciparum food vacuole plasmepsins
    • Liu J, Gluzman IY, Drew ME, Goldberg DE. The role of Plasmodium falciparum food vacuole plasmepsins. J BiolChem 2005;280:1432-1437.
    • (2005) J BiolChem , vol.280 , pp. 1432-1437
    • Liu, J.1    Gluzman, I.Y.2    Drew, M.E.3    Goldberg, D.E.4
  • 119
    • 0037133223 scopus 로고    scopus 로고
    • Identification and characterization of allophenylnorstatine-based inhibitors of plasmepsin II, an antimalarial target
    • Nezami A, Luque I, Kimura T, Kiso Y, Freire E. Identification and characterization of allophenylnorstatine-based inhibitors of plasmepsin II, an antimalarial target. Biochemistry 2002;41:2273-2280.
    • (2002) Biochemistry , vol.41 , pp. 2273-2280
    • Nezami, A.1    Luque, I.2    Kimura, T.3    Kiso, Y.4    Freire, E.5
  • 120
    • 0036900890 scopus 로고    scopus 로고
    • Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370
    • Asojo OA, Afonina E, Gulnik SV, Yu B, Erickson JW, Randad R, Medjahed D, Silva AM. Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 Å in complex with the inhibitors rs367 and rs370. Acta Crystallogr D 2002;D58:2001-2008.
    • (2002) Acta Crystallogr D , vol.D58 , pp. 2001-2008
    • Asojo, O.A.1    Afonina, E.2    Gulnik, S.V.3    Yu, B.4    Erickson, J.W.5    Randad, R.6    Medjahed, D.7    Silva, A.M.8
  • 122
    • 33747169481 scopus 로고    scopus 로고
    • (F. Hoffmann-La Roche A.-G., Switz.). assignee. Pharmaceutical preparations containing piperidine derivatives as antimalarials. Wo patent 9912532.1999
    • Bur D, Fischli W, Matile H, Ridley RG, Wostl W, (F. Hoffmann-La Roche A.-G., Switz.). assignee. Pharmaceutical preparations containing piperidine derivatives as antimalarials. Wo patent 9912532.1999.
    • Bur, D.1    Fischli, W.2    Matile, H.3    Ridley, R.G.4    Wostl, W.5
  • 127
    • 17044432545 scopus 로고    scopus 로고
    • Aspartic proteases of Plasmodium falciparum as the target of HIV-1 protease inhibitors
    • Savarino A, Cauda R, Cassone A. Aspartic proteases of Plasmodium falciparum as the target of HIV-1 protease inhibitors. Comments J Infect Dis 2005;191:1381-1382.
    • (2005) Comments J Infect Dis , vol.191 , pp. 1381-1382
    • Savarino, A.1    Cauda, R.2    Cassone, A.3
  • 129
    • 9944242396 scopus 로고    scopus 로고
    • Fluorinated peptidomimetics: Synthesis, conformational and biological features
    • Molteni M, Pesenti C, Sani M, Volonterio A, Zanda M. Fluorinated peptidomimetics: Synthesis, conformational and biological features. J Fluorine Chem 2004;125:1735-1743.
    • (2004) J Fluorine Chem , vol.125 , pp. 1735-1743
    • Molteni, M.1    Pesenti, C.2    Sani, M.3    Volonterio, A.4    Zanda, M.5
  • 130
    • 11244267140 scopus 로고    scopus 로고
    • Trifluoromethyl group: An effective xenobiotic function for peptide backbone modification
    • Zanda M. Trifluoromethyl group: An effective xenobiotic function for peptide backbone modification. New J Chem 2004;28:1401-1411.
    • (2004) New J Chem , vol.28 , pp. 1401-1411
    • Zanda, M.1
  • 136
    • 0037333352 scopus 로고    scopus 로고
    • Solid-phase library synthesis of reversed-statine type inhibitors of the malarial aspartyl proteases plasmepsin I and II
    • Dahlgren A, Kvarnstrom I, Vrang L, Hamelink E, Hallberg A, Rosenquist A, Samuelsson B. Solid-phase library synthesis of reversed-statine type inhibitors of the malarial aspartyl proteases plasmepsin I and II. Bioorg med Chem 2003;111:827-841.
    • (2003) Bioorg Med Chem , vol.111 , pp. 827-841
    • Dahlgren, A.1    Kvarnstrom, I.2    Vrang, L.3    Hamelink, E.4    Hallberg, A.5    Rosenquist, A.6    Samuelsson, B.7
  • 138
    • 0037436389 scopus 로고    scopus 로고
    • Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum
    • Asojo OA, Gulnik SV, Afonina E, Yu B, Ellman JA, Haque TS, Silva AM. Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum. J Mol Biol 2003;327:173-181.
    • (2003) J Mol Biol , vol.327 , pp. 173-181
    • Asojo, O.A.1    Gulnik, S.V.2    Afonina, E.3    Yu, B.4    Ellman, J.A.5    Haque, T.S.6    Silva, A.M.7
  • 139
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 1997;23:3-25.
    • (1997) Adv Drug Deliv Rev , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 140
    • 0037468420 scopus 로고    scopus 로고
    • Design and synthesis of plasmepsin I and plasmepsin II inhibitors with activity in Plasmodium falciparum-infected cultured human erythrocytes
    • Nöteberg D, Hamelink E, Hulten J, Wahlgren M, Vrang L, Samuelsson B, Hallberg A. Design and synthesis of plasmepsin I and plasmepsin II inhibitors with activity in Plasmodium falciparum-infected cultured human erythrocytes. J Med Chem 2003;46:734-746.
    • (2003) J Med Chem , vol.46 , pp. 734-746
    • Nöteberg, D.1    Hamelink, E.2    Hulten, J.3    Wahlgren, M.4    Vrang, L.5    Samuelsson, B.6    Hallberg, A.7
  • 141
    • 0141787013 scopus 로고    scopus 로고
    • High-speed optimization of inhibitors of the malarial proteases plasmepsin I and II
    • Nöteberg D, Schaal W, Hamelink E, Vrang L, Larhed M. High-speed optimization of inhibitors of the malarial proteases plasmepsin I and II. J Comb Chem 2003;5:456-464.
    • (2003) J Comb Chem , vol.5 , pp. 456-464
    • Nöteberg, D.1    Schaal, W.2    Hamelink, E.3    Vrang, L.4    Larhed, M.5
  • 143
    • 8644243887 scopus 로고    scopus 로고
    • Search for substrate-based inhibitors fitting the S2′ space of malarial aspartic protease plasmepsin II
    • Kiso A, Hidaka K, Kimura T, Hayashi Y, Nezami A, Freire E, Kiso Y Search for substrate-based inhibitors fitting the S2′ space of malarial aspartic protease plasmepsin II. J Pept Sci 2004;10:641-647.
    • (2004) J Pept Sci , vol.10 , pp. 641-647
    • Kiso, A.1    Hidaka, K.2    Kimura, T.3    Hayashi, Y.4    Nezami, A.5    Freire, E.6    Kiso, Y.7
  • 148
    • 0032924352 scopus 로고    scopus 로고
    • Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum
    • Bernstein NK, Cherney MM, Loetscher H, Ridley RG, James MNG. Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum. Nat Struct Biol 1999;6:32-37.
    • (1999) Nat Struct Biol , vol.6 , pp. 32-37
    • Bernstein, N.K.1    Cherney, M.M.2    Loetscher, H.3    Ridley, R.G.4    James, M.N.G.5
  • 149
    • 0043027664 scopus 로고    scopus 로고
    • Development of a new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 7-azabicyclo[2.2.1]heptane scaffold
    • Carcache DA, Hoertner SR, Seiler P, Diederich F, Dorn A, Maerki HP, Binkert C, Bur D. Development of a new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 7-azabicyclo[2.2.1]heptane scaffold. Helv Chim Acta 2003;86:2173-2191.
    • (2003) Helv Chim Acta , vol.86 , pp. 2173-2191
    • Carcache, D.A.1    Hoertner, S.R.2    Seiler, P.3    Diederich, F.4    Dorn, A.5    Maerki, H.P.6    Binkert, C.7    Bur, D.8
  • 150
    • 0041524759 scopus 로고    scopus 로고
    • A new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 11-azatricyclo[6.2.1.02,7]undeca-2,4,6-triene scaffold
    • Carcache DA, Hoertner SR, Bertogg A, Diederich F, Dorn A, Maerki HP, Binkert C, Bur D. A new class of inhibitors for the malarial aspartic protease plasmepsin II based on a central 11-azatricyclo[6.2.1.02,7]undeca-2,4,6-triene scaffold. Helv Chim Acta 2003;86:2192-2209.
    • (2003) Helv Chim Acta , vol.86 , pp. 2192-2209
    • Carcache, D.A.1    Hoertner, S.R.2    Bertogg, A.3    Diederich, F.4    Dorn, A.5    Maerki, H.P.6    Binkert, C.7    Bur, D.8
  • 151
    • 0037021351 scopus 로고    scopus 로고
    • De novo design, synthesis, and in vitro evaluation of a new class of nonpeptidic inhibitors of the malarial enzyme plasmepsin II
    • Carcache DA, Hortner SR, Bertogg A, Binkert C, Bur D, Marki HP, Dorn A, Diederich F. De novo design, synthesis, and in vitro evaluation of a new class of nonpeptidic inhibitors of the malarial enzyme plasmepsin II. Chem Bio Chem 2002;3:1137-1141.
    • (2002) Chem Bio Chem , vol.3 , pp. 1137-1141
    • Carcache, D.A.1    Hortner, S.R.2    Bertogg, A.3    Binkert, C.4    Bur, D.5    Marki, H.P.6    Dorn, A.7    Diederich, F.8
  • 152
    • 3242748959 scopus 로고    scopus 로고
    • Synthesis of plasmepsin II inhibitors-Potential antimalarial agents
    • Mueller R, Huerzeler M, Boss C. Synthesis of plasmepsin II inhibitors-Potential antimalarial agents. Molecules 2003;8:556-564.
    • (2003) Molecules , vol.8 , pp. 556-564
    • Mueller, R.1    Huerzeler, M.2    Boss, C.3
  • 157
    • 0037188608 scopus 로고    scopus 로고
    • Spermine alkaloids from Albizia adinocephala with activity against Plasmodium falciparum plasmepsin II
    • Ovenden SPB, Cao S, Leong C, Flotow H, Gupta MP, Buss AD, Butler MS. Spermine alkaloids from Albizia adinocephala with activity against Plasmodium falciparum plasmepsin II. Phytochemistry 2002;60:175-177.
    • (2002) Phytochemistry , vol.60 , pp. 175-177
    • Ovenden, S.P.B.1    Cao, S.2    Leong, C.3    Flotow, H.4    Gupta, M.P.5    Buss, A.D.6    Butler, M.S.7
  • 158
    • 0344643059 scopus 로고    scopus 로고
    • In vitro studies on the mechanism of action of two compounds with antiplasmodial activity: Ellagic acid and 3,4,5-trimethoxyphenyl (6′-O-galloyl)-b-D-glucopyranoside
    • Dell'Agli M, Parapini S, Basilico N, Verotta L, Taramelli D, Berry C, Bosisio E. In vitro studies on the mechanism of action of two compounds with antiplasmodial activity: Ellagic acid and 3,4,5-trimethoxyphenyl (6′-O-galloyl)-b-D-glucopyranoside. Planta Med 2003;69:162-164.
    • (2003) Planta Med , vol.69 , pp. 162-164
    • Dell'Agli, M.1    Parapini, S.2    Basilico, N.3    Verotta, L.4    Taramelli, D.5    Berry, C.6    Bosisio, E.7
  • 159
    • 0008331792 scopus 로고
    • Homology among acid proteases: Comparison of crystal structures at 3. ANG. resolution of acid proteases from Rhizopus chinensis and Endothia parasitica
    • Subramanian E, Swan IDA, Liu M, Davies DR, Jenkins JA, Tickle IJ, Blundell TL. Homology among acid proteases: Comparison of crystal structures at 3. ANG. resolution of acid proteases from Rhizopus chinensis and Endothia parasitica. Proc Natl Acad Sci USA 1977;74:556-559.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 556-559
    • Subramanian, E.1    Swan, I.D.A.2    Liu, M.3    Davies, D.R.4    Jenkins, J.A.5    Tickle, I.J.6    Blundell, T.L.7
  • 161
    • 33747186018 scopus 로고    scopus 로고
    • Preparation of peptidomimetic inhibitors of cathepsin D and plasmepsins I and II. Wo patent 9730072. 1997
    • Majer P, Collins J, Gulnik S, Erickson J, Pan W, Eissenstat MA, (United States Department of Health and Human Services, USA), assignee. Preparation of peptidomimetic inhibitors of cathepsin D and plasmepsins I and II. Wo patent 9730072. 1997.
    • Majer, P.1    Collins, J.2    Gulnik, S.3    Erickson, J.4    Pan, W.5    Eissenstat, M.A.6
  • 164
    • 33747197345 scopus 로고    scopus 로고
    • (Enanta Pharmaceuticals, Inc., USA), assignee. Preparation of linked plasmepsin and falcipain inhibitors for treatment of malaria. Wo patent 2001083433. 2001
    • Eckstein JW, (Enanta Pharmaceuticals, Inc., USA), assignee. Preparation of linked plasmepsin and falcipain inhibitors for treatment of malaria. Wo patent 2001083433. 2001.
    • Eckstein, J.W.1
  • 168


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.