메뉴 건너뛰기




Volumn 30, Issue 1, 2010, Pages 136-167

Falcipain-2 inhibitors

Author keywords

Cysteine protease; Falcipain 2; Malaria; Plasmodium falciparum; Protease inhibitors

Indexed keywords

ALDEHYDE DERIVATIVE; AMODIAQUINE; ANTIMALARIAL AGENT; ARTEMETHER; ARTEMETHER PLUS BENFLUMETOL; ARTESUNATE; ATOVAQUONE; AZIRIDINE DERIVATIVE; BENFLUMETOL; CHALCONE DERIVATIVE; DIHYDROARTEMISININ PLUS PIPERAQUINE; ENZYME INHIBITOR; FALCIPAIN 2; FALCIPAIN 2 INHIBITOR; FLUOROMETHYL KETONE DERIVATIVE; HALOFANTRINE; HEMOGLOBIN; ISOQUINOLINE; ISOQUINOLINE DERIVATIVE; KETOAMIDE ALPHA DERIVATIVE; MEFLOQUINE; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PRIMAQUINE; PROGUANIL; PYRIMETHAMINE; SULFADOXINE; THIOSEMICARBAZONE DERIVATIVE; UNCLASSIFIED DRUG; VINYL SULFONE DERIVATIVE;

EID: 84976351004     PISSN: 01986325     EISSN: None     Source Type: Journal    
DOI: 10.1002/med.20163     Document Type: Review
Times cited : (130)

References (141)
  • 1
    • 84976362626 scopus 로고    scopus 로고
    • World Malaria Report
    • World Malaria Report 2008 http://malaria.who.int/wmr2008/
    • (2008)
  • 2
    • 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
  • 5
    • 0037130254 scopus 로고    scopus 로고
    • Genetic diversity and chloroquine selective sweeps in Plasmodium falciparum
    • DOI 10.1038/nature00813
    • Wootton JC, Feng X, Ferdig MT, Cooper RA, Mu J, Baruch DI, Magill AJ, Su X-Z. Genetic diversity and chloroquine selective sweeps in Plasmodium falciparum. Nature 2002;418:320-323. (Pubitemid 34790681)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 320-323
    • Wootton, J.C.1    Feng, X.2    Ferdig, M.T.3    Cooper, R.A.4    Mu, J.5    Baruch, D.I.6    Magill, A.J.7    Su, X.-Z.8
  • 6
    • 0034112744 scopus 로고    scopus 로고
    • Insecticide resistance in insect vectors of human disease
    • Hemingway J, Ranson H. Insecticide resistance in insect vectors of human disease. Annu Rev Entomol 2000;45:369-389.
    • (2000) Annu Rev Entomol , vol.45 , pp. 369-389
    • Hemingway, J.1    Ranson, H.2
  • 7
    • 0037020190 scopus 로고    scopus 로고
    • An overview of insecticide resistance
    • Hemingway J, Field L, Vontas J. An overview of insecticide resistance. Science 2002;298:96-97.
    • (2002) Science , vol.298 , pp. 96-97
    • Hemingway, J.1    Field, L.2    Vontas, J.3
  • 9
    • 1842486672 scopus 로고    scopus 로고
    • The origin of malaria: Mixed messages from genetic diversity
    • Hartl DL. The origin of malaria: Mixed messages from genetic diversity. Nat Rev Microbiol 2004;2:15-22.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 15-22
    • Hartl, D.L.1
  • 10
    • 33947594387 scopus 로고    scopus 로고
    • Recent advances in antimalarial compounds and their patents
    • DOI 10.2174/092986707780090927
    • Mital A. Recent advances in antimalarial compounds and their patents. Curr Med Chem 2007;14:759-773. (Pubitemid 46477710)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.7 , pp. 759-773
    • Mital, A.1
  • 11
    • 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;30:4-10. (Pubitemid 46887588)
    • (2007) International Journal of Antimicrobial Agents , vol.30 , Issue.1 , pp. 4-10
    • Jana, S.1    Paliwal, J.2
  • 12
    • 34347221494 scopus 로고    scopus 로고
    • Understanding resistance to antimalarial 4-aminoquinolines, cinchona alkaloids and the highly hydrophobic arylaminoalcohols
    • Warhurst DC. Understanding resistance to antimalarial 4-aminoquinolines, cinchona alkaloids and the highly hydrophobic arylaminoalcohols. Curr Sci 2007;92:1556-1560.
    • (2007) Curr Sci , vol.92 , pp. 1556-1560
    • Warhurst, D.C.1
  • 14
    • 7244251635 scopus 로고    scopus 로고
    • Chloroquine resistance in Plasmodium vivax
    • Barid JK. Chloroquine resistance in Plasmodium vivax. Antimicrob Agents Chemother 2004;48:4075-4083.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4075-4083
    • Barid, J.K.1
  • 16
    • 14144253009 scopus 로고    scopus 로고
    • Mechanisms of resistance of malaria parasites to antifolates
    • DOI 10.1124/pr.57.1.4
    • Gregson A, Plowe CV. Mechanisms of resistance of malaria parasites to antifolates. Pharmacol Rev 2005;57:117-145. (Pubitemid 40283971)
    • (2005) Pharmacological Reviews , vol.57 , Issue.1 , pp. 117-145
    • Gregson, A.1    Plowe, C.V.2
  • 17
    • 36749000794 scopus 로고    scopus 로고
    • Malaria chemotherapeutics Part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development
    • Schlitzer M. Malaria chemotherapeutics Part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development. ChemMedChem 2007;2:944-986.
    • (2007) ChemMedChem , vol.2 , pp. 944-986
    • Schlitzer, M.1
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0002439574 scopus 로고    scopus 로고
    • Antimalaria agents
    • Wolff ME, editor. Burger's medicinal chemistry and drug discovery. New York: Wiley
    • Casteel DA. Antimalaria agents. In: Wolff ME, editor. Burger's medicinal chemistry and drug discovery. Volume 5: Therapeutic agents. New York: Wiley; 1997. pp 3-91.
    • (1997) Therapeutic Agents. , vol.5 , pp. 3-91
    • Casteel, D.A.1
  • 23
    • 2142659388 scopus 로고    scopus 로고
    • Antimalarial drug resistance
    • White NJ. Antimalarial drug resistance. J Clin Invest 2004;113:1084-1092.
    • (2004) J Clin Invest , vol.113 , pp. 1084-1092
    • White, N.J.1
  • 30
    • 38449087076 scopus 로고    scopus 로고
    • Randomized comparison of amodiaquine plus sulfadoxine-pyrimethamine, artemether-lumefantrine, and dihydroartemisinin-piperaquine for the treatment of uncomplicated Plasmodium falciparum malaria in Burkina Faso
    • Zongo I, Dorsey G, Rouamba N, Dokomajilar C, Sere Y, Rosenthal PJ, Ouedraogo JB. Randomized comparison of amodiaquine plus sulfadoxine- pyrimethamine, artemether-lumefantrine, and dihydroartemisinin-piperaquine for the treatment of uncomplicated Plasmodium falciparum malaria in Burkina Faso. Clin Infect Dis 2007;45:1453-1461.
    • (2007) Clin Infect Dis , vol.45 , pp. 1453-1461
    • Zongo, I.1    Dorsey, G.2    Rouamba, N.3    Dokomajilar, C.4    Sere, Y.5    Rosenthal, P.J.6    Ouedraogo, J.B.7
  • 34
    • 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
  • 35
    • 33847190634 scopus 로고    scopus 로고
    • Current status and progresses made in malaria hemotherapy
    • García Liñares GE, Rodriguez JB. Current status and progresses made in malaria hemotherapy. Curr Med Chem 2007;14:289-314.
    • (2007) Curr Med Chem , vol.14 , pp. 289-314
    • García Liñares, G.E.1    Rodriguez, J.B.2
  • 36
    • 0027673463 scopus 로고
    • Hemoglobin degradation in Plasmodium-infected red blood cells
    • Goldberg DE. Hemoglobin degradation in Plasmodium-infected red blood cells. Semin Cell Biol 1993;4:355-361.
    • (1993) Semin Cell Biol , vol.4 , pp. 355-361
    • Goldberg, D.E.1
  • 38
    • 0001306565 scopus 로고
    • Incorporation of 14C-amino acids by malaria (Plasmodium lophurae)
    • Sherman IW, Tanigoshi L. Incorporation of 14C-amino acids by malaria (Plasmodium lophurae). Int J Biochem 1970;1:635-637.
    • (1970) Int J Biochem , vol.1 , pp. 635-637
    • Sherman, I.W.1    Tanigoshi, L.2
  • 39
    • 0017693186 scopus 로고
    • Amino acid metabolism and protein synthesis in malarial parasites
    • WHO
    • Sherman IW. Amino acid metabolism and protein synthesis in malarial parasites. Bull WHO 1977;55:265-276.
    • (1977) Bull , vol.55 , pp. 265-276
    • Sherman, I.W.1
  • 40
    • 0037589002 scopus 로고    scopus 로고
    • Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum - Infected red blood cells
    • DOI 10.1182/blood-2002-08-2654
    • 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. (Pubitemid 36857903)
    • (2003) Blood , vol.101 , Issue.10 , pp. 4189-4194
    • Lew, V.L.1    Tiffert, T.2    Ginsburg, H.3
  • 41
    • 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;61:231-241. (Pubitemid 223039723)
    • (1993) Molecular and Biochemical Parasitology , vol.61 , Issue.2 , pp. 231-241
    • Atamna, H.1    Ginsburg, H.2
  • 43
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparium
    • DOI 10.1146/annurev.micro.51.1.97
    • Francis SE, Sullivan Jr DJ, Goldberg DE. 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
  • 46
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • Sijwalai 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
    • Sijwalai, P.S.1    Rosenthal, P.J.2
  • 50
    • 0025754304 scopus 로고
    • Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: A catabolic pathway initiated by a specific aspartic protease
    • Goldberg DE, Slater AF, 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
    • De Goldberg1    Slater, A.F.2    Beavis, R.3    Chait, B.4    Cerami, A.5    Henderson, G.B.6
  • 52
    • 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. (Pubitemid 30704241)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.37 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 53
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
    • DOI 10.1042/0264-6021:3600481
    • 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. (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
  • 54
    • 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
  • 55
    • 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 DE. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J Biol Chem 2004;279:43000-43007. (Pubitemid 39372193)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 57
    • 58149313651 scopus 로고    scopus 로고
    • Irreversible effect of cysteine protease inhibitors on the release of malaria parasites from infected erythrocytes
    • Glushakova S, Mazar J, Hohmann-Marriott MF, Hama E, Zimmerberg J. Irreversible effect of cysteine protease inhibitors on the release of malaria parasites from infected erythrocytes. Cell Microbiol 2009;11:95-105.
    • (2009) Cell Microbiol , vol.11 , pp. 95-105
    • Glushakova, S.1    Mazar, J.2    Hohmann-Marriott, M.F.3    Hama, E.4    Zimmerberg, J.5
  • 58
    • 0034844897 scopus 로고    scopus 로고
    • The role of aminopeptidases in haemoglobin degradation in Plasmodium falciparum-infected erythrocytes
    • PII S0166685101003279
    • 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. (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
  • 59
    • 37249008065 scopus 로고    scopus 로고
    • Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum
    • DOI 10.1074/jbc.M703643200
    • Dalal S, Klemba M. Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum. J Biol Chem 2007;282:35978-35987. (Pubitemid 350277126)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35978-35987
    • Dalal, S.1    Klemba, M.2
  • 60
    • 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 PS, Pandey KC, Rosenthal PJ. Plasmodium falciparum: Biochemical characterization of the cysteine protease falcipain-2'. Exp Parasitol 2006;112:187-192. (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
  • 61
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • Rosenthal PJ. Cysteine proteases of malaria parasites. Int J Parasitol 2004;34:1489-1499.
    • (2004) Int J Parasitol , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 63
    • 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 DC, Bogyo M, Williamson KC. Targeted disruption of Plasmodium falciparum cysteine protease, falcipain 1, reduces oocyst production, not erythrocytic stage growth. Mol Microbiol 2004;53:243-250. (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
  • 64
    • 33749420126 scopus 로고    scopus 로고
    • Substrate mapping and inhibitor profiling of falcipain-2, falcipain-3 and berghepain-2: Implications for peptidase anti-malarial drug discovery
    • DOI 10.1042/BJ20060422
    • Ramjee MK, Flinn NS, Pemberton TP, Quibell M, Wang Y, Watts JP. Substrate mapping and inhibitor profiling of falcipain-2, falcipain-3 and berghepain-2: implications for peptidase anti-malarial drug discovery. Biochem J 2006;399:47-57. (Pubitemid 44505406)
    • (2006) Biochemical Journal , vol.399 , Issue.1 , pp. 47-57
    • Ramjee, M.K.1    Flinn, N.S.2    Pemberton, T.P.3    Quibell, M.4    Wang, Y.5    Watts, J.P.6
  • 65
    • 12344273618 scopus 로고    scopus 로고
    • Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum
    • DOI 10.1016/j.molbiopara.2004.11.009, PII S0166685104003135
    • Dahl EL, Rosenthal PJ. Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum. Mol Biochem Parasitol 2005;139:205-212. (Pubitemid 40128216)
    • (2005) Molecular and Biochemical Parasitology , vol.139 , Issue.2 , pp. 205-212
    • Dahl, E.L.1    Rosenthal, P.J.2
  • 66
    • 0034154995 scopus 로고    scopus 로고
    • Ultrastructure and function of mitochondria in gametocytic stage of Plasmodium falciparum
    • Krungkrai J, Prapunwattana P, Krungkrai SR. Ultrastructure and function of mitochondria in gametocytic stage of Plasmodium falciparum. Parasite 2000;33:19-26.
    • (2000) Parasite , vol.33 , pp. 19-26
    • Krungkrai, J.1    Prapunwattana, P.2    Krungkrai, S.R.3
  • 67
    • 0036682503 scopus 로고    scopus 로고
    • Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development
    • DOI 10.1182/blood-2002-01-0101
    • Hanspal M, Dua M, Takakuwa Y, Chishti AH, Mizuno A. Plasmodium falciparum cysteine protease falcipain-2 cleaves erythrocyte membrane skeletal proteins at late stages of parasite development. Blood 2002;100:1048-1054. (Pubitemid 34832636)
    • (2002) Blood , vol.100 , Issue.3 , pp. 1048-1054
    • Hanspal, M.1    Dua, M.2    Takakuwa, Y.3    Chishti, A.H.4    Mizuno, A.5
  • 68
    • 33748328016 scopus 로고    scopus 로고
    • Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum
    • Sijwali PS, Koo J, Singh N, Rosenthal PJ. Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum.Mol Biochem Parasitol 2006;150:96-106.
    • (2006) Mol Biochem Parasitol , vol.150 , pp. 96-106
    • Sijwali, P.S.1    Koo, J.2    Singh, N.3    Rosenthal, P.J.4
  • 70
    • 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
    • Goh LL, Sim TS. 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;335:762-770.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 762-770
    • Goh, L.L.1    Sim, T.S.2
  • 75
    • 61449267734 scopus 로고    scopus 로고
    • Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: Implications for substrate specificity
    • Kerr ID, Lee JH, Pandey KC, Harrison A, Sajid M, Rosenthal PJ, Brinen LS. Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: implications for substrate specificity. J Med Chem 2009;52:852-857.
    • (2009) J Med Chem , vol.52 , 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
  • 77
    • 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
    • Sijwali PS, Shenai BR, Rosenthal PJ. Folding of the Plasmodium falciparum cysteine protease falcipain-2 is mediated by a chaperone-like peptide and not the prodomain. J Biol Chem 2002;277:14910-14915.
    • (2002) J Biol Chem , vol.277 , pp. 14910-14915
    • Sijwali, P.S.1    Shenai, B.R.2    Rosenthal, P.J.3
  • 78
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers JC, Asgian JL, Ekiei OD, James KE. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem Rev 2002;102:4639-4750.
    • (2002) Chem Rev , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekiei, O.D.3    James, K.E.4
  • 80
    • 0025719869 scopus 로고
    • Antimalarial effects of peptide inhbitors of a Plasmodium falciparum cysteine proteinase
    • Rosenthal PJ, Wollish WS, Palmer JT, Rasnick D. Antimalarial effects of peptide inhbitors of a Plasmodium falciparum cysteine proteinase. J Clin Invest 1991;88:1467-1472.
    • (1991) J Clin Invest , vol.88 , pp. 1467-1472
    • Rosenthal, P.J.1    Wollish, W.S.2    Palmer, J.T.3    Rasnick, D.4
  • 81
    • 0027512171 scopus 로고
    • Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria
    • Rosenthal PJ, Lee GK, Smith RE. Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria. J Clin Invest 1993;91:1052-1056.
    • (1993) J Clin Invest , vol.91 , pp. 1052-1056
    • Rosenthal, P.J.1    Lee, G.K.2    Smith, R.E.3
  • 82
    • 0029099619 scopus 로고
    • Vinyl sulfones as mechanism-based cysteine protease inhibitors
    • Palmer JT, Rasnick D, Klaus JK, Bromme D. Vinyl sulfones as mechanism-based cysteine protease inhibitors. J Med Chem 1995;38:3193-3196.
    • (1995) J Med Chem , vol.38 , pp. 3193-3196
    • Palmer, J.T.1    Rasnick, D.2    Klaus, J.K.3    Bromme, D.4
  • 85
    • 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 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. (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
  • 86
  • 89
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine protease of malaria parasites: Targets for chemotherapy
    • DOI 10.2174/1381612023394197
    • Rosenthal PJ, Sijwali PS, Singh A, Shenai BR. Cysteine proteases of malaria parasites: Targets for chemotherapy. Curr Pharm Des 2002;8:1659-1672. (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
  • 90
    • 0037113235 scopus 로고    scopus 로고
    • Critical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites
    • DOI 10.1042/BJ20020753
    • Singh A, Shenai BR, Choe Y, Gut J, Sijwali PS, Craik CS, Rosenthal PJ. Critical role of amino acid 23 in mediating activity and specificity of vinckepain-2, a papain-family cysteine protease of rodent malaria parasites. Biochem J 2002;368:273-281. (Pubitemid 35463430)
    • (2002) Biochemical Journal , vol.368 , Issue.1 , pp. 273-281
    • Singh, A.1    Shenai, B.R.2    Choe, Y.3    Gut, J.4    Sijwali, P.S.5    Craik, C.S.6    Rosenthal, P.J.7
  • 91
    • 0017841848 scopus 로고
    • Isolation and characterization of e 64, a new thiol protease inhibitor
    • Hanada K, Tamai M, Yamagishi S, Ohmura S, Sawada J, Tanaka I. Isolation and characterization of E-64, a new thiol protease inhibitor. Agric Biol Chem 1978;42:523-528. (Pubitemid 8343851)
    • (1978) Agricultural and Biological Chemistry , vol.42 , Issue.3 , pp. 523-528
    • Hanada, K.1    Tamai, M.2    Yamagishi, M.3
  • 92
    • 0017803444 scopus 로고
    • Studies on thiol protease inhibitors. Part II. Structure and synthesis of E-64, a new thiol protease inhibitor
    • Hanada K, Tamai M, Yamagishi S, Ohmura S, Sawada J, Tanaka I. Studies on thiol protease inhibitors. Part II. Structure and synthesis of E-64, a new thiol protease inhibitor. Agric Biol Chem 1978;42:529-536.
    • (1978) Agric Biol Chem , vol.42 , pp. 529-536
    • Hanada, K.1    Tamai, M.2    Yamagishi, S.3    Ohmura, S.4    Sawada, J.5    Tanaka, I.6
  • 93
    • 0001543361 scopus 로고
    • Inhibition of cathepsin B1 by E-64, a thiol proteinase inhibitor, and its derivatives
    • Inaba T, Hirayama Y, Fujinaga N. Inhibition of cathepsin B1 by E-64, a thiol proteinase inhibitor, and its derivatives. Agric Biol Chem 1979;43:655-656.
    • (1979) Agric Biol Chem , vol.43 , pp. 655-656
    • Inaba, T.1    Hirayama, Y.2    Fujinaga, N.3
  • 95
    • 0018895711 scopus 로고
    • Inhibition of epoxide derivatives on chicken calcium-activated neutral protease (CANP) in vitro and in vivo
    • Sugita H, Ishiura S, Suzuki K, Imahori K. Inhibition of epoxide derivatives on chicken calcium-activated neutral protease (CANP) in vitro and in vivo. J Biochem 1980;87:339-341. (Pubitemid 10138348)
    • (1980) Journal of Biochemistry , vol.87 , Issue.1 , pp. 339-341
    • Sugita, H.1    Ishiura, S.2    Suzuki, K.3    Imahori, K.4
  • 96
    • 0020755321 scopus 로고
    • Reaction of calcium-activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid
    • Suzuki K. Reaction of calcium-activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid. J Biochem 1983;93:1305-1312.
    • (1983) J Biochem , vol.93 , pp. 1305-1312
    • Suzuki, K.1
  • 97
    • 0034624239 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of D-homophenylalanyl epoxysuccinate inhibitors of the trypanosomal cysteine protease cruzain
    • Roush WR, Hernandez AA, McKerrow JH, Selzer PM, Hansell E, Engel JC. Design, synthesis and evaluation of D-homophenylalanyl epoxysuccinate inhibitors of the trypanosomal cysteine protease cruzain. Tetrahedron 2000;56:9747-9762.
    • (2000) Tetrahedron , vol.56 , pp. 9747-9762
    • Roush, W.R.1    Hernandez, A.A.2    McKerrow, J.H.3    Selzer, P.M.4    Hansell, E.5    Engel, J.C.6
  • 98
    • 0026604849 scopus 로고
    • Inhibition of interleukin 1-stimulated cartilage proteoglycan degradation by a lipophilic inactivator of cysteine endopeptidases
    • Buttle DJ, Saklatvala J, Tamai M, Barrett AJ. Inhibition of interleukin 1-stimulated cartilage proteoglycan degradation by a lipophilic inactivator of cysteine endopeptidases. Biochem J 1992;281:175-177.
    • (1992) Biochem J , vol.281 , pp. 175-177
    • Buttle, D.J.1    Saklatvala, J.2    Tamai, M.3    Barrett, A.J.4
  • 99
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays
    • Kembhavi AA, Buttle DJ, Knight CG, Barrett AJ. The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays. Arch Biochem Biophys 1993;303:208-213.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 100
    • 0026644069 scopus 로고
    • Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis
    • Chen Z, Potempa J, Polanowski A, Wikstrom M, Travis J. Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis. J Biol Chem 1992;267:18896-18901.
    • (1992) J Biol Chem , vol.267 , pp. 18896-18901
    • Chen, Z.1    Potempa, J.2    Polanowski, A.3    Wikstrom, M.4    Travis, J.5
  • 101
    • 0026567878 scopus 로고
    • Purification and characterization of cathepsin J from rat liver
    • Nikawa T, Towatari T, Katunuma N. Purification and characterization of cathepsin J from rat liver. Eur J Biochem 1992;204:381-393.
    • (1992) Eur J Biochem , vol.204 , pp. 381-393
    • Nikawa, T.1    Towatari, T.2    Katunuma, N.3
  • 103
    • 0032491264 scopus 로고    scopus 로고
    • Design and synthesis of dipeptidyl α',β'- Epoxy ketones, potent irreversible inhibitors of the cysteine protease cruzain
    • Roush WR, González FV, McKerrow JH, Hansell E. Design and synthesis of dipeptidyl α',β'- epoxy ketones, potent irreversible inhibitors of the cysteine protease cruzain. Bioorg Med Chem Lett 1998;8:2809-2812.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 2809-2812
    • Roush, W.R.1    González, F.V.2    McKerrow, J.H.3    Hansell, E.4
  • 104
    • 1542328053 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8
    • James HK, Asgian JL, Li ZZ, Ekici OD, Rubin JR, Mikolajczyk J, Salvesen GS, Powers JC. Design, synthesis, and evaluation of aza-peptide epoxides as selective and potent inhibitors of caspases-1, -3, -6, and -8. J Med Chem 2004;47:1553-1574.
    • (2004) J Med Chem , vol.47 , pp. 1553-1574
    • James, H.K.1    Asgian, J.L.2    Li, Z.Z.3    Ekici, O.D.4    Rubin, J.R.5    Mikolajczyk, J.6    Salvesen, G.S.7    Powers, J.C.8
  • 105
    • 0023950936 scopus 로고
    • Irreversible inhibition of papain by epoxysuccinyl peptides. Carbon-13 NMR characterization of the site of alkylation
    • Yabe Y, Guillaume D, Rich DH. Irreversible inhibition of papain by epoxysuccinyl peptides. Carbon-13 NMR characterization of the site of alkylation. J Am Chem Soc 1988;110:4043-4044.
    • (1988) J Am Chem Soc , vol.110 , pp. 4043-4044
    • Yabe, Y.1    Guillaume, D.2    Rich, D.H.3
  • 106
    • 0024577165 scopus 로고
    • Mode of binding of E-64-c, a potent thiol protease inhibitor, to papain as determined by X-ray crystal analysis of the complex
    • Matsumoto K, Yamamoto D, Ohishi H, Tomoo K, Ishida T, Inoue M, Sadatome T, Kitamura K, Mizuno H. Mode of binding of E-64-c, a potent thiol protease inhibitor, to papain as determined by X-ray crystal analysis of the complex. FEBS Lett 1989;245:177-180.
    • (1989) FEBS Lett , vol.245 , pp. 177-180
    • Matsumoto, K.1    Yamamoto, D.2    Ohishi, H.3    Tomoo, K.4    Ishida, T.5    Inoue, M.6    Sadatome, T.7    Kitamura, K.8    Mizuno, H.9
  • 107
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D, Medzihradszky K, Burlingame A, Bogyo M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem Biol 2000;7:569-581.
    • (2000) Chem Biol , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.2    Burlingame, A.3    Bogyo, M.4
  • 110
    • 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. Chem Med Chem 2007;2:120-128.
    • (2007) Chem Med Chem , vol.2 , pp. 120-128
    • Mladenovic, M.1    Schirmeister, T.2    Thiel, S.3    Thiel, W.4    Engels, B.5
  • 111
    • 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;3:361-373.
    • (2003) Mini Rev Med Chem , vol.3 , pp. 361-373
    • Schirmeister, T.1    Kaeppler, U.2
  • 112
    • 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 AC, Menard R, Jones JB. Aziridine analogs of [[trans-(epoxysuccinyl)-L-leucyl]amino]-4-guanidinobutane (E-64) as inhibitors of cysteine proteases. J Med Chem 1995;38:3078-3085.
    • (1995) J Med Chem , vol.38 , pp. 3078-3085
    • Martichonok, V.1    Plouffe, C.2    Storer, A.C.3    Menard, R.4    Jones, J.B.5
  • 113
    • 0027215523 scopus 로고
    • Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates
    • Bucciarelli M, Forni A, Moretti I, Prati F, Torre G. Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates. Tetrahedron Asymm 1993;4:903-906.
    • (1993) Tetrahedron Asymm , vol.4 , pp. 903-906
    • Bucciarelli, M.1    Forni, A.2    Moretti, I.3    Prati, F.4    Torre, G.5
  • 114
    • 37049067996 scopus 로고
    • Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates
    • Bucciarelli M, Forni A, Moretti I, Prati F, Torre G. Candida cylindracea lipase-catalyzed hydrolysis of methyl aziridine-2-carboxylates and -2,3-dicarboxylates. J Chem Soc Perkin Trans 1 1993; 3041-3045.
    • (1993) J Chem Soc Perkin Trans 1 , pp. 3041-3045
    • Bucciarelli, M.1    Forni, A.2    Moretti, I.3    Prati, F.4    Torre, G.5
  • 115
    • 33749002536 scopus 로고    scopus 로고
    • Rational design of aziridine containing cysteine protease inhibitors with improved potency studies on inhibition mechanism
    • 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;1:1021-1028.
    • (2006) ChemMedChem , vol.1 , pp. 1021-1028
    • Vicik, R.1    Helten, H.2    Schirmeister, T.3    Engels, B.4
  • 117
    • 0033003497 scopus 로고    scopus 로고
    • Inhibition of cysteine proteases by peptides containing aziridine-2,3-dicarboxylic acid building blocks
    • Schirmeister T. Inhibition of cysteine proteases by peptides containing aziridine-2,3-dicarboxylic acid building blocks. Biopolymers 1999;51:87-97.
    • (1999) Biopolymers , vol.51 , pp. 87-97
    • Schirmeister, T.1
  • 118
    • 0033602268 scopus 로고    scopus 로고
    • New peptidic cysteine protease inhibitors derived from the electrophilic a-amino acid aziridine-2,3-dicarboxylic acid
    • Schirmeister T. New peptidic cysteine protease inhibitors derived from the electrophilic a-amino acid aziridine-2,3-dicarboxylic acid. J Med Chem 1999;42:560-572.
    • (1999) J Med Chem , vol.42 , pp. 560-572
    • Schirmeister, T.1
  • 119
    • 0026597863 scopus 로고
    • Aziridine-2-carboxylic acid. a reactive amino acid unit for a new class of cysteine proteinase inhibitors
    • Moroder L, Musiol HJ, Scharf R. Aziridine-2-carboxylic acid. A reactive amino acid unit for a new class of cysteine proteinase inhibitors. FEBS Lett 1992;299:51-53.
    • (1992) FEBS Lett , vol.299 , pp. 51-53
    • Moroder, L.1    Musiol, H.J.2    Scharf, R.3
  • 120
    • 0035959447 scopus 로고    scopus 로고
    • β-Turn mimetic library synthesis: Scaffolds and applications
    • Souers AJ, Ellman JA. β-Turn mimetic library synthesis: Scaffolds and applications. Tetrahedron 2001;57:7431-7448.
    • (2001) Tetrahedron , vol.57 , pp. 7431-7448
    • Souers, A.J.1    Ellman, J.A.2
  • 121
    • 0034778418 scopus 로고    scopus 로고
    • Solid-phase syntheses of β-turn analogues to mimic or disrupt protein-protein interactions
    • Burgess K. Solid-phase syntheses of β-turn analogues to mimic or disrupt protein-protein interactions. Acc Chem Res 2001;34:826-835.
    • (2001) Acc Chem Res , vol.34 , pp. 826-835
    • Burgess, K.1
  • 122
    • 17744399693 scopus 로고    scopus 로고
    • Approaches to cyclic peptide β-turn mimics
    • MacDonald M, Aubé J. Approaches to cyclic peptide β-turn mimics. Curr Org Chem 2001;5:417-438.
    • (2001) Curr Org Chem , vol.5 , pp. 417-438
    • MacDonald, M.1    Aubé, J.2
  • 123
    • 0036783393 scopus 로고    scopus 로고
    • Design, synthesis, and application of peptide secondary structure mimetics
    • Eguchi M, Kahn M. Design, synthesis, and application of peptide secondary structure mimetics. Mini Rev Med Chem 2002;2:447-462.
    • (2002) Mini Rev Med Chem , vol.2 , pp. 447-462
    • Eguchi, M.1    Kahn, M.2
  • 124
    • 0033535143 scopus 로고    scopus 로고
    • The design of non-peptide human bradykinin B2 receptor antagonists employing the benzodiazepine peptidomimetic scaffold
    • Dziadulewicz EK, Brown MC, Dunstan AR, Lee W, Said NB, Garratt PJ. The design of non-peptide human bradykinin B2 receptor antagonists employing the benzodiazepine peptidomimetic scaffold. Bioorg Med Chem Lett 1999;9:463-468.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 463-468
    • Dziadulewicz, E.K.1    Brown, M.C.2    Dunstan, A.R.3    Lee, W.4    Said, N.B.5    Garratt, P.J.6
  • 125
    • 0037156352 scopus 로고    scopus 로고
    • A practical synthesis of (S) 3-tert-butoxycarbonylamino-2- Oxo-2,3,4,5-tetrahydro-1,5-benzodiazepine-1-acetic acid methyl ester as a conformationally restricted dipeptido-mimetic for caspase-1 (ICE) inhibitors
    • Lauffer DJ, Mullican MD. A practical synthesis of (S) 3-tert-butoxycarbonylamino-2- oxo-2,3,4,5-tetrahydro-1,5-benzodiazepine-1-acetic acid methyl ester as a conformationally restricted dipeptido-mimetic for caspase-1 (ICE) inhibitors. Bioorg Med Chem Lett 2002;12:1225-1227.
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 1225-1227
    • Lauffer, D.J.1    Mullican, M.D.2
  • 130
    • 0028357495 scopus 로고
    • Licochalcone A, a new antimalarial agent, inhibits in vitro growth of the human malaria parasite Plasmodium falciparum and protects mice from P. yoelii infection
    • Chen M, Theander TG, Christensen BS, Hviid L, Zhai L, Kharazmi A. Licochalcone A, a new antimalarial agent, inhibits in vitro growth of the human malaria parasite Plasmodium falciparum and protects mice from P. yoelii infection. Antimicrob Agents Chemother 1994;38:1470-1475. (Pubitemid 24203554)
    • (1994) Antimicrobial Agents and Chemotherapy , vol.38 , Issue.7 , pp. 1470-1475
    • Chen, M.1    Theander, T.G.2    Christensen, S.B.3    Hviid, L.4    Zhai, L.5    Kharazmi, A.6
  • 131
    • 0030830227 scopus 로고    scopus 로고
    • The novel oxygenated chalcone, 2,4-dimethoxy-4′-butoxychalcone, exhibits potent activity against human malaria parasite Plasmodium falciparum in vitro and rodent parasites Plasmodium berghei and Plasmodium yoelii in vivo
    • Chen M, Christensen SB, Zhai L, Rasmussen MH, Theander TG, Frokjaer S, Steffansen S, Davidsen J, Kharazmi A. The novel oxygenated chalcone, 2,4-dimethoxy-4′-butoxychalcone, exhibits potent activity against human malaria parasite Plasmodium falciparum in vitro and rodent parasites Plasmodium berghei and Plasmodium yoelii in vivo. J Infect Dis 1997;176:1327-1333.
    • (1997) J Infect Dis , vol.176 , pp. 1327-1333
    • Chen, M.1    Christensen, S.B.2    Zhai, L.3    Rasmussen, M.H.4    Theander, T.G.5    Frokjaer, S.6    Steffansen, S.7    Davidsen, J.8    Kharazmi, A.9
  • 133
    • 0035818913 scopus 로고    scopus 로고
    • Antimalarial alkoxylated and hydroxylated chalones: Structure-activity relationship analysis
    • DOI 10.1021/jm0101747
    • Liu M, Wilairat P, Go ML. Antimalarial alkoxylated and hydroxylated chalcones: Structure-activity relationship analysis. J Med Chem 2001;44:4443-4452. (Pubitemid 33131668)
    • (2001) Journal of Medicinal Chemistry , vol.44 , Issue.25 , pp. 4443-4452
    • Liu, M.1    Wilairat, P.2    Go, M.-L.3
  • 135
    • 45849146887 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships of a series of chalcone derivatives (1,3-diphenyl-2-propen-1-one) as anti Plasmodium falciparum agents (anti malaria agents)
    • Motta LF, Gaudio AC, Takahata Y. Quantitative structure-activity relationships of a series of chalcone derivatives (1,3-diphenyl-2-propen-1-one) as anti Plasmodium falciparum agents (anti malaria agents). Internet Electron J Mol Des 2006:5;555-569.
    • (2006) Internet Electron J Mol des , vol.5 , pp. 555-569
    • Motta, L.F.1    Gaudio, A.C.2    Takahata, Y.3
  • 136
  • 137
    • 0037447948 scopus 로고    scopus 로고
    • Structure-based approach to falcipain-2 inhibitors: Synthesis and biological evaluation of 1,6,7-trisubstituted dihydroisoquinolines and isoquinolines
    • Batra S, Sabnis YA, Rosenthal PJ, Avery MA. Structure-based approach to falcipain-2 inhibitors: synthesis and biological evaluation of 1,6,7-trisubstituted dihydroisoquinolines and isoquinolines. Bioorg Med Chem 2003;11:2293-2299.
    • (2003) Bioorg Med Chem , vol.11 , pp. 2293-2299
    • Batra, S.1    Sabnis, Y.A.2    Rosenthal, P.J.3    Ma, A.4
  • 139
    • 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 PJ, McKerrowb JH, Chibale K. Synthesis and evaluation of isatins and thiosemicarbazone derivatives against cruzain, falcipain-2 and rhodesain. Bioorg Med Chem Lett 2003;13:3527-3530. (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
  • 140
    • 2542533103 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of parasiticidal thiosemicarbazone cysteine protease inhibitors against Plasmodium falciparum, Trypanosoma brucei, and Trypanosoma cruzi
    • DOI 10.1021/jm030549j
    • Greenbaum DC, Mackey Z, Hansell E, Doyle P, Gut J, Caffrey CR, Lehrman J, Rosenthal PJ, McKerrow JH, Chibale K. Synthesis and structure-activity relationships of parasiticidal thiosemicarbazone cysteine protease inhibitors against Plasmodium falciparum, Trypanosoma brucei, and Trypanosoma cruzi. J Med Chem 2004;47:3212-3219. (Pubitemid 38702713)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.12 , pp. 3212-3219
    • Greenbaum, D.C.1    Mackey, Z.2    Hansell, E.3    Doyle, P.4    Gut, J.5    Caffrey, C.R.6    Lehrman, J.7    Rosenthal, P.J.8    McKerrow, J.H.9    Chibale, K.10
  • 141
    • 33750947149 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of phenolic Mannich bases of benzaldehyde and (thio)semicarbazone derivatives against the cysteine protease falcipain-2 and a chloroquine resistant strain of Plasmodium falciparum
    • DOI 10.1016/j.bmc.2006.09.055, PII S0968089606007991
    • Chipeleme A, Gut J, Rosenthal PJ, Chibale K. Synthesis and biological evaluation of phenolic Mannich bases of benzaldehyde and (thio)semicarbazone derivatives against the cysteine protease falcipain-2 and a chloroquine resistant strain of Plasmodium falciparum. Bioorg Med Chem 2007;15:273-282. (Pubitemid 44738573)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.1 , pp. 273-282
    • Chipeleme, A.1    Gut, J.2    Rosenthal, P.J.3    Chibale, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.