메뉴 건너뛰기




Volumn 55, Issue 24, 2012, Pages 10909-10917

Structure-activity relationships and blood distribution of antiplasmodial aminopeptidase-1 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

2 BENZYL N (2 FLUOROBENZYL) N' HYDROXYMALONAMIDE; 2 BENZYL N (3 FLUOROBENZYL) N' HYDROXYMALONAMIDE; 2 BENZYL N (4 FLUOROBENZYL) N' HYDROXY 2 METHYLMALONAMIDE; 2 BENZYL N (4 FLUOROBENZYL) N' HYDROXYMALONAMIDE; 2 BENZYL N HYDROXY N' PYRIDIN 4 YLMETHYLMALONAMIDE; 2 BENZYLIDENE N HYDROXY N' PYRIDIN 4 YLMETHYLMALONAMIDE; 2,N BIS(4 FLUOROBENZYL) N' HYDROXYMALONAMIDE; 2,N DIBENZYL N' HYDROXYMALONAMIDE; AMINOPEPTIDASE 1 INHIBITOR; ANTIMALARIAL AGENT; ENZYME INHIBITOR; GLUTATHIONE; HALOGEN; HYDROXAMIC ACID; N (4 FLUOROBENZYL) 2 [1 (4 FLUOROPHENYL)METHYLIDENE] N' HYDROXYMALONAMIDE; N (4 FLUOROBENZYL) N' HYDROXY 2 (1 PHENYLMETHYLIDENE)MALONAMIDE; N BENZYL 2 [1 (4 FLUOROPHENYL)METHYLIDENE] N' HYDROXYMALONAMIDE; UNCLASSIFIED DRUG;

EID: 84871655128     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm301506h     Document Type: Article
Times cited : (36)

References (42)
  • 5
    • 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, 59-83
    • (2000) Curr. Drug Targets , vol.1 , pp. 59-83
    • Blackman, M.J.1
  • 6
    • 4544238896 scopus 로고    scopus 로고
    • Proteases in host cell invasion by the malaria parasite
    • DOI 10.1111/j.1462-5822.2004.00437.x
    • Blackman, M. J. Proteases in host cell invasion by the malaria parasite Cell. Microbiol. 2004, 6, 893-903 (Pubitemid 39255603)
    • (2004) Cellular Microbiology , vol.6 , Issue.10 , pp. 893-903
    • Blackman, M.J.1
  • 7
    • 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, 140-145 (Pubitemid 34171491)
    • (2002) Current Opinion in Hematology , vol.9 , Issue.2 , pp. 140-145
    • Rosenthal, P.J.1
  • 8
    • 0242669367 scopus 로고    scopus 로고
    • Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite
    • DOI 10.1101/gr.913403
    • Wu, Y.; Wang, X.; Liu, X.; Wang, Y. Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite Genome Res. 2003, 13, 601-616 (Pubitemid 36511919)
    • (2003) Genome Research , vol.13 , Issue.4 , pp. 601-616
    • Wu, Y.1    Wang, X.2    Liu, X.3    Wang, Y.4
  • 9
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • Drag, M.; Salvesen, G. S. Emerging principles in protease-based drug discovery Nat. Rev. Drug Discovery 2010, 9, 690-701
    • (2010) Nat. Rev. Drug Discovery , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2
  • 10
    • 77949482144 scopus 로고    scopus 로고
    • Proteases of Plasmodium falciparum as potential drug targets and inhibitors thereof
    • Wegscheid-Gerlach, C.; Gerber, H.-D.; Diederich, W. E. Proteases of Plasmodium falciparum as potential drug targets and inhibitors thereof Curr. Top. Med. Chem. 2010, 10, 346-367
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 346-367
    • Wegscheid-Gerlach, C.1    Gerber, H.-D.2    Diederich, W.E.3
  • 11
    • 0141733057 scopus 로고    scopus 로고
    • Plasmodium falciparum falcilysin: A metalloprotease with dual specificity
    • DOI 10.1074/jbc.M306842200
    • Murata, C. E.; Goldberg, D. E. Plasmodium falciparum falcilysin: A metalloprotease with dual specificity J. Biol. Chem. 2003, 278, 38022-38028 (Pubitemid 37175333)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 38022-38028
    • Murata, C.E.1    Goldberg, D.E.2
  • 14
    • 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, 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
  • 15
    • 33644978572 scopus 로고    scopus 로고
    • Overexpression of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin
    • Gardiner, D. L.; Trenholme, K. R.; Skinner-Adams, T. S.; Stack, C. M.; Dalton, J. P. Overexpression of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin J. Biol. Chem. 2006, 281, 1741-1745
    • (2006) J. Biol. Chem. , vol.281 , pp. 1741-1745
    • Gardiner, D.L.1    Trenholme, K.R.2    Skinner-Adams, T.S.3    Stack, C.M.4    Dalton, J.P.5
  • 17
    • 0036062411 scopus 로고    scopus 로고
    • Properties, stage-dependent expression and localization of Plasmodium falciparum M1 family zinc-aminopeptidase
    • DOI 10.1017/S0031182002001828
    • Allary, M.; Schrevel, J.; Florent, I. Properties, stage-dependent expression and localization of Plasmodium falciparum M1 family zinc-aminopeptidase Parasitology 2002, 125, 1-10 (Pubitemid 34785744)
    • (2002) Parasitology , vol.125 , Issue.1 , pp. 1-10
    • Allary, M.1    Schrevel, J.2    Florent, I.3
  • 18
    • 0032583101 scopus 로고    scopus 로고
    • A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages
    • DOI 10.1016/S0166-6851(98)00143-1, PII S0166685198001431
    • Florent, I.; Derhy, Z.; Allary, M.; Monsigny, M.; Mayer, R.; Schrevel, J. A Plasmodium falciparum aminopeptidase gene belonging to the M1 family of zinc-metallopeptidases is expressed in erythrocytic stages Mol. Biochem. Parasitol. 1998, 97, 149-160 (Pubitemid 28558709)
    • (1998) Molecular and Biochemical Parasitology , vol.97 , Issue.1-2 , pp. 149-160
    • Florent, I.1    Derhy, Z.2    Allary, M.3    Monsigny, M.4    Mayer, R.5    Schrevel, J.6
  • 19
    • 79960991925 scopus 로고    scopus 로고
    • Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism
    • Ragheb, D.; Dalal, S.; Bompiani, K. M.; Ray, W. K.; Klemba, M. Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism J. Biol. Chem. 2011, 286, 27255-27265
    • (2011) J. Biol. Chem. , vol.286 , pp. 27255-27265
    • Ragheb, D.1    Dalal, S.2    Bompiani, K.M.3    Ray, W.K.4    Klemba, M.5
  • 20
    • 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, 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
  • 22
    • 28744448728 scopus 로고    scopus 로고
    • Effect of metalloprotease inhibitors on invasion of red blood cell by Plasmodium falciparum
    • DOI 10.1016/j.actatropica.2005.05.015, PII S0001706X05002512
    • Kitjaroentham, A.; Suthiphongchai, T.; Wilairat, P. Effect of metalloprotease inhibitors on invasion of red blood cell by Plasmodium falciparum Acta Trop. 2006, 97, 5-9 (Pubitemid 41758510)
    • (2006) Acta Tropica , vol.97 , Issue.1 , pp. 5-9
    • Kitjaroentham, A.1    Suthiphongchai, T.2    Wilairat, P.3
  • 23
    • 77954037366 scopus 로고    scopus 로고
    • Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole
    • Azimzadeh, O.; Sow, C.; Geze, M.; Nyalwidhe, J.; Florent, I. Plasmodium falciparum PfA-M1 aminopeptidase is trafficked via the parasitophorous vacuole and marginally delivered to the food vacuole Malaria J. 2010, 9, 189
    • (2010) Malaria J. , vol.9 , pp. 189
    • Azimzadeh, O.1    Sow, C.2    Geze, M.3    Nyalwidhe, J.4    Florent, I.5
  • 24
    • 0038825686 scopus 로고    scopus 로고
    • Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors
    • DOI 10.1016/S0960-894X(03)00550-X
    • Flipo, M.; Florent, I.; Grellier, P.; Sergheraert, C.; Deprez-Poulain, R. Design, synthesis and antimalarial activity of novel, quinoline-based, zinc metallo-aminopeptidase inhibitors Bioorg. Med. Chem. Lett. 2003, 13, 2659-2662 (Pubitemid 36851544)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.16 , pp. 2659-2662
    • Flipo, M.1    Florent, I.2    Grellier, P.3    Sergheraert, C.4    Deprez-Poulain, R.5
  • 25
    • 33751120689 scopus 로고    scopus 로고
    • A library of novel hydroxamic acids targeting the metallo-protease family: Design, parallel synthesis and screening
    • DOI 10.1016/j.bmc.2006.10.010, PII S0968089606008303
    • Flipo, M.; Beghyn, T.; Charton, J.; Leroux, V. A.; Deprez, B. P.; Deprez-Poulain, R. F. A library of novel hydroxamic acids targeting the metallo-protease family: Design, parallel synthesis and screening Bioorg. Med. Chem. 2007, 15, 63-76 (Pubitemid 44767995)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.1 , pp. 63-76
    • Flipo, M.1    Beghyn, T.2    Charton, J.3    Leroux, V.A.4    Deprez, B.P.5    Deprez-Poulain, R.F.6
  • 26
    • 33947632299 scopus 로고    scopus 로고
    • Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents
    • DOI 10.1021/jm061169b
    • Flipo, M.; Beghyn, T.; Leroux, V.; Florent, I.; Deprez, B. P.; Deprez-Poulain, R. F. Novel selective inhibitors of the zinc plasmodial aminopeptidase PfA-M1 as potential antimalarial agents J. Med. Chem. 2007, 50, 1322-1334 (Pubitemid 46496331)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.6 , pp. 1322-1334
    • Flipo, M.1    Beghyn, T.2    Leroux, V.3    Florent, I.4    Deprez, B.P.5    Deprez-Poulain, R.F.6
  • 27
    • 50949112789 scopus 로고    scopus 로고
    • Chemical target validation studies of aminopeptidase in malaria parasites using {alpha}-aminoalkylphosphonate and phosphonopeptide inhibitors
    • Cunningham, E.; Drag, M.; Kafarski, P.; Bell, A. Chemical target validation studies of aminopeptidase in malaria parasites using {alpha}-aminoalkylphosphonate and phosphonopeptide inhibitors Antimicrob. Agents Chemother. 2008, 52, 3221-3228
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3221-3228
    • Cunningham, E.1    Drag, M.2    Kafarski, P.3    Bell, A.4
  • 28
    • 79952788440 scopus 로고    scopus 로고
    • Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase
    • Velmourougane, G.; Harbut, M. B.; Dalal, S.; McGowan, S.; Oellig, C. A.; Meinhardt, N.; Whisstock, J. C.; Klemba, M.; Greenbaum, D. C. Synthesis of new (-)-bestatin-based inhibitor libraries reveals a novel binding mode in the S1 pocket of the essential malaria M1 metalloaminopeptidase J. Med. Chem. 2011, 54, 1655-1666
    • (2011) J. Med. Chem. , vol.54 , pp. 1655-1666
    • Velmourougane, G.1    Harbut, M.B.2    Dalal, S.3    McGowan, S.4    Oellig, C.A.5    Meinhardt, N.6    Whisstock, J.C.7    Klemba, M.8    Greenbaum, D.C.9
  • 30
    • 50549086578 scopus 로고    scopus 로고
    • A fluorine scan of non-peptidic inhibitors of neprilysin: Fluorophobic and fluorophilic regions in an enzyme active site
    • Morgenthaler, M.; Aebi, J. D.; Grüninger, F.; Mona, D.; Wagner, B.; Kansy, M.; Diederich, F. A fluorine scan of non-peptidic inhibitors of neprilysin: Fluorophobic and fluorophilic regions in an enzyme active site J. Fluor. Chem. 2008, 129, 852-865
    • (2008) J. Fluor. Chem. , vol.129 , pp. 852-865
    • Morgenthaler, M.1    Aebi, J.D.2    Grüninger, F.3    Mona, D.4    Wagner, B.5    Kansy, M.6    Diederich, F.7
  • 33
    • 77958039726 scopus 로고    scopus 로고
    • Fluorine in health care: Organofluorine containing blockbuster drugs
    • O'Hagan, D. Fluorine in health care: Organofluorine containing blockbuster drugs J. Fluor. Chem. 2010, 131, 1071-1081
    • (2010) J. Fluor. Chem. , vol.131 , pp. 1071-1081
    • O'Hagan, D.1
  • 34
    • 79551562195 scopus 로고    scopus 로고
    • Extreme modulation properties of aromatic fluorine
    • Gakh, A. A.; Burnett, M. N. Extreme modulation properties of aromatic fluorine J. Fluor. Chem. 2011, 132, 88-93
    • (2011) J. Fluor. Chem. , vol.132 , pp. 88-93
    • Gakh, A.A.1    Burnett, M.N.2
  • 35
    • 0034926661 scopus 로고    scopus 로고
    • Fluorine substituent effects (on bioactivity)
    • DOI 10.1016/S0022-1139(01)00375-X, PII S002211390100375X
    • Smart, B. E. Fluorine substituent effects (on bioactivity) J. Fluor. Chem. 2001, 109, 3-11 (Pubitemid 33618184)
    • (2001) Journal of Fluorine Chemistry , vol.109 , Issue.1 , pp. 3-11
    • Smart, B.E.1
  • 36
    • 74349100375 scopus 로고    scopus 로고
    • Synthesis and antimicrobial activity of 2-fluorophenyl-4,6-disubstituted [1,3,5]triazines
    • Saleh, M.; Abbott, S.; Perron, V.; Lauzon, C.; Penney, C.; Zacharie, B. Synthesis and antimicrobial activity of 2-fluorophenyl-4,6-disubstituted [1,3,5]triazines Bioorg. Med. Chem. Lett. 2010, 20, 945-949
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 945-949
    • Saleh, M.1    Abbott, S.2    Perron, V.3    Lauzon, C.4    Penney, C.5    Zacharie, B.6
  • 39
    • 0025971003 scopus 로고
    • Identification and characterization of the glutathione and N -acetylcysteine conjugates of (E)-2-propyl-2,4-pentadienoic acid, a toxic metabolite of valproic acid, in rats and humans
    • Kassahun, K.; Farrell, K.; Abbott, F. Identification and characterization of the glutathione and N -acetylcysteine conjugates of (E)-2-propyl-2,4- pentadienoic acid, a toxic metabolite of valproic acid, in rats and humans Drug Metab. Dispos. 1991, 19, 525-535
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 525-535
    • Kassahun, K.1    Farrell, K.2    Abbott, F.3
  • 40
    • 0028246986 scopus 로고
    • Binding of dorzolamide and its metabolite, N-deethylated dorzolamide, to human erythrocytes in vitro
    • Hasegawa, T.; Hara, K.; Hata, S. Binding of dorzolamide and its metabolite, N-deethylated dorzolamide, to human erythrocytes in vitro Drug Metab. Dispos. 1994, 22, 377-382 (Pubitemid 24158535)
    • (1994) Drug Metabolism and Disposition , vol.22 , Issue.3 , pp. 377-382
    • Hasegawa, T.1    Hara, K.2    Hata, S.3
  • 41
    • 33749817443 scopus 로고    scopus 로고
    • Inhibition profiling of human carbonic anhydrase II by high-throughput screening of structurally diverse, biologically active compounds
    • DOI 10.1177/1087057106289403
    • Iyer, R.; Barrese, A. A.; Parakh, S.; Parker, C. N.; Tripp, B. C. Inhibition profiling of human carbonic anhydrase II by high-throughput screening of structurally diverse, biologically active compounds J. Biomol. Screen. 2006, 11, 782-791 (Pubitemid 44562319)
    • (2006) Journal of Biomolecular Screening , vol.11 , Issue.7 , pp. 782-791
    • Iyer, R.1    Barrese III, A.A.2    Parakh, S.3    Parker, C.N.4    Tripp, B.C.5
  • 42
    • 0035950834 scopus 로고    scopus 로고
    • Separation and identification methods for metalloproteinase inhibitors
    • DOI 10.1016/S0378-4347(01)00316-4, PII S0378434701003164
    • Peng, S. X. Separation and identification methods for metalloproteinase inhibitors J. Chromatogr., B 2001, 764, 59-80 (Pubitemid 33044660)
    • (2001) Journal of Chromatography B: Biomedical Sciences and Applications , vol.764 , Issue.1-2 , pp. 59-80
    • Peng, S.X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.