메뉴 건너뛰기




Volumn 41, Issue 2, 1998, Pages 148-156

Phenothiazine inhibitors of trypanothione reductase as potential antitrypanosomal and antileishmanial drugs

Author keywords

[No Author keywords available]

Indexed keywords

ACYLPROMAZINE; CHLORPROMAZINE DERIVATIVE; GLUTATHIONE; GLUTATHIONE REDUCTASE; OXIDOREDUCTASE; PHENOTHIAZINE DERIVATIVE; PROMAZINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRIFLUOPERAZINE; TRYPANOTHIONE; TRYPANOTHIONE REDUCTASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 15144347577     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm960814j     Document Type: Article
Times cited : (154)

References (42)
  • 1
    • 0028366196 scopus 로고
    • The treatment of human African trypanosomiasis
    • Pepin, J.; Milord, F. The treatment of human African trypanosomiasis. Adv. Parasitol. 1994, 33, 1-47.
    • (1994) Adv. Parasitol. , vol.33 , pp. 1-47
    • Pepin, J.1    Milord, F.2
  • 2
    • 0027156559 scopus 로고
    • Recent advances in the treatment of visceral leishmaniasis
    • Davidson, R. N.; Croft, S. L. Recent advances in the treatment of visceral leishmaniasis. Trans. R. Soc. Trop. Med. Hyg. 1993, 87, 130-131.
    • (1993) Trans. R. Soc. Trop. Med. Hyg. , vol.87 , pp. 130-131
    • Davidson, R.N.1    Croft, S.L.2
  • 3
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb, A. H.; Blackburn, P.; Ulrich, P.; Chait, B. T.; Cerami, A. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 1985, 227, 1485-1487.
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 4
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb, A. H.; Cerami, A. Metabolism and functions of trypanothione in the kinetoplastida. Annu. Rev. Microbiol. 1992, 46, 695-729.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 5
    • 0023150396 scopus 로고
    • Trypanothione reductase from Trypanosoma cruzi: Purification and characterization of the crystalline enzyme
    • Krauth-Siegel, R. L.; Enders, B.; Henderson, G. B.; Fairlamb, A. H.; Schirmer, R. H. Trypanothione reductase from Trypanosoma cruzi: purification and characterization of the crystalline enzyme. Eur. J. Biochem. 1987, 164, 123-128.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 123-128
    • Krauth-Siegel, R.L.1    Enders, B.2    Henderson, G.B.3    Fairlamb, A.H.4    Schirmer, R.H.5
  • 6
    • 0023051830 scopus 로고
    • Purification and characterization of trypanothione reductase from Crithidia fasciculata, a new member of the family of disulfide-containing flavoprotein reductases
    • Shames, S. L.; Fairlamb, A. H.; Cerami, A.; Walsh, C. T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a new member of the family of disulfide-containing flavoprotein reductases. Biochemistry 1986, 25, 3519-3526.
    • (1986) Biochemistry , vol.25 , pp. 3519-3526
    • Shames, S.L.1    Fairlamb, A.H.2    Cerami, A.3    Walsh, C.T.4
  • 7
    • 33748233963 scopus 로고
    • Disulfide-reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer, R. H.; Müller, J. G.; Krauth-Siegel, R. L. Disulfide-reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria. Angew. Chem., Int. Ed. Engl. 1995, 34, 141-154.
    • (1995) Angew. Chem., Int. Ed. Engl. , vol.34 , pp. 141-154
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 9
    • 0028357962 scopus 로고
    • Rational design of peptide-based inhibitors of trypanothione reductase as potential antitrypanosomal drugs
    • Garforth, J.; McKie, J. H.; Jaouhari, R.; Benson, T. J.; Fairlamb, A. H.; Douglas, K. T. Rational design of peptide-based inhibitors of trypanothione reductase as potential antitrypanosomal drugs. Amino Acids 1994, 6, 295-300.
    • (1994) Amino Acids , vol.6 , pp. 295-300
    • Garforth, J.1    McKie, J.H.2    Jaouhari, R.3    Benson, T.J.4    Fairlamb, A.H.5    Douglas, K.T.6
  • 10
    • 0024580811 scopus 로고
    • The activity of tricyclic antidepressant drugs against Trypanosoma cruzi
    • Doyle, P. S.; Weinbach, E. C. The activity of tricyclic antidepressant drugs against Trypanosoma cruzi. Exp. Parasitol. 1989, 68, 230-234.
    • (1989) Exp. Parasitol. , vol.68 , pp. 230-234
    • Doyle, P.S.1    Weinbach, E.C.2
  • 11
    • 0027935555 scopus 로고
    • Antileishmanial actions of tricyclic neuroleptics appear to lack structural specificity
    • Evans, A. T.; Croft, S. L. Antileishmanial actions of tricyclic neuroleptics appear to lack structural specificity. Biochem. Pharmacol. 1994, 48, 613-616.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 613-616
    • Evans, A.T.1    Croft, S.L.2
  • 13
    • 0019966292 scopus 로고
    • Lethal effect of phenothiazine neuroleptics on pathogenic protozoan Leishmania donovani
    • Pearson, R. D.; Manian, A. A.; Harcus, J. L.; Hall, D.; Hewlett, E. K. Lethal effect of phenothiazine neuroleptics on pathogenic protozoan Leishmania donovani. Science 1982, 217, 369-371.
    • (1982) Science , vol.217 , pp. 369-371
    • Pearson, R.D.1    Manian, A.A.2    Harcus, J.L.3    Hall, D.4    Hewlett, E.K.5
  • 15
    • 0021674394 scopus 로고
    • Antidepressants cause lethal disruption of membrane function in the human protozoan parasite Leishmania
    • Zilberstein, D.; Dwyer, D. M. Antidepressants cause lethal disruption of membrane function in the human protozoan parasite Leishmania. Science 1984, 226, 977-979.
    • (1984) Science , vol.226 , pp. 977-979
    • Zilberstein, D.1    Dwyer, D.M.2
  • 16
    • 0021052732 scopus 로고
    • Trypanocidal action of neuroleptic phenothiazines in Trypanosoma brucei
    • Seebeck, T.; Gehr, P. Trypanocidal action of neuroleptic phenothiazines in Trypanosoma brucei. Mol. Biochem. Parasitol. 1983, 9, 197-208.
    • (1983) Mol. Biochem. Parasitol. , vol.9 , pp. 197-208
    • Seebeck, T.1    Gehr, P.2
  • 17
    • 0022922407 scopus 로고
    • Monoclonal antibodies against a 60 kDa phenothiazine-binding protein from Trypanosoma brucei can discriminate between different trypanosome species
    • Stieger, J.; Seebeck, T. Monoclonal antibodies against a 60 kDa phenothiazine-binding protein from Trypanosoma brucei can discriminate between different trypanosome species. Mol. Biochem. Parasitol. 1986, 21, 37-45.
    • (1986) Mol. Biochem. Parasitol. , vol.21 , pp. 37-45
    • Stieger, J.1    Seebeck, T.2
  • 18
    • 0024026095 scopus 로고
    • Screening of drugs for rapid activity against Trypanosoma cruzi trypomastigotes in vitro
    • Croft, S. L.; Walker, J. J.; Gutteridge, W. E. Screening of drugs for rapid activity against Trypanosoma cruzi trypomastigotes in vitro. Trop. Med. Parasitol. 1988, 39, 145-148.
    • (1988) Trop. Med. Parasitol. , vol.39 , pp. 145-148
    • Croft, S.L.1    Walker, J.J.2    Gutteridge, W.E.3
  • 19
    • 0021807169 scopus 로고
    • Trypanosoma cruzi: Possible control of parasite transmission by blood transfusion using amphiphilic cationic drugs
    • Hammond, D. J.; Hogg, J.; Gutteridge, W. E. Trypanosoma cruzi: possible control of parasite transmission by blood transfusion using amphiphilic cationic drugs. Exp. Parasitol. 1985, 60, 32-42.
    • (1985) Exp. Parasitol. , vol.60 , pp. 32-42
    • Hammond, D.J.1    Hogg, J.2    Gutteridge, W.E.3
  • 20
    • 0021326405 scopus 로고
    • A novel series of chemical structures active in vitro against the trypomastigote form of Trypanosoma cruzi
    • Hammond, D. J.; Cover, B.; Gutteridge, W. E. A novel series of chemical structures active in vitro against the trypomastigote form of Trypanosoma cruzi. Trans. R. Soc. Trop. Med. Hyg. 1984, 78, 91-95.
    • (1984) Trans. R. Soc. Trop. Med. Hyg. , vol.78 , pp. 91-95
    • Hammond, D.J.1    Cover, B.2    Gutteridge, W.E.3
  • 24
    • 0028057659 scopus 로고
    • The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state
    • Lantwin, C. B.; Schlichting, I.; Kabsch, W.; Pai, E. F.; Krauth-Siegel, R. L. The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. Proteins 1994, 18, 161-173.
    • (1994) Proteins , vol.18 , pp. 161-173
    • Lantwin, C.B.1    Schlichting, I.2    Kabsch, W.3    Pai, E.F.4    Krauth-Siegel, R.L.5
  • 25
    • 0030045604 scopus 로고    scopus 로고
    • The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution
    • Zhang, Y.; Bond, C. S.; Bailey, S.; Cunningham, M. L.; Fairlamb, A. H.; Hunter, W. N. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. Protein Sci. 1996, 5, 52-61.
    • (1996) Protein Sci. , vol.5 , pp. 52-61
    • Zhang, Y.1    Bond, C.S.2    Bailey, S.3    Cunningham, M.L.4    Fairlamb, A.H.5    Hunter, W.N.6
  • 26
    • 0030057025 scopus 로고    scopus 로고
    • Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex
    • Jacoby, E. M.; Schlichting, I.; Lantwin, C. B.; Kabsch, W.; Krauth-Siegel, R. L. Crystal structure of the Trypanosoma cruzi trypanothione reductase.mepacrine complex. Proteins 1996, 24, 73-80.
    • (1996) Proteins , vol.24 , pp. 73-80
    • Jacoby, E.M.1    Schlichting, I.2    Lantwin, C.B.3    Kabsch, W.4    Krauth-Siegel, R.L.5
  • 27
    • 0026000158 scopus 로고
    • Synthesis of N-benzyloxycarbonyl-L-cysteinylglycine 3-dimethyl-aminopropylamide disulfide: A cheap and convenient new assay for trypanothione reductase
    • El-Waer, A. F.; Douglas, K. T.; Smith, K.; Fairlamb, A. H. Synthesis of N-benzyloxycarbonyl-L-cysteinylglycine 3-dimethyl-aminopropylamide disulfide: A cheap and convenient new assay for trypanothione reductase. Anal. Biochem. 1991, 198, 212-216.
    • (1991) Anal. Biochem. , vol.198 , pp. 212-216
    • El-Waer, A.F.1    Douglas, K.T.2    Smith, K.3    Fairlamb, A.H.4
  • 29
    • 69249097642 scopus 로고
    • Use of competitive inhibitors to study substrate binding order
    • Purich, D. L., Ed.; Academic Press: New York
    • Fromm, H. J. Use of competitive inhibitors to study substrate binding order. In Contemporary Enzyme Kinetics and Mechanism; Purich, D. L., Ed.; Academic Press: New York, 1983; p 243.
    • (1983) Contemporary Enzyme Kinetics and Mechanism , pp. 243
    • Fromm, H.J.1
  • 30
    • 0025752362 scopus 로고
    • Mutational Analysis of Parasite Trypanothione Reductase: Acquisition of Glutathione Reductase Activity in a Triple Mutant
    • Sullivan, F. X.; Sobolov, S. B.; Bradley, M.; Walsh, C. T. Mutational Analysis of Parasite Trypanothione Reductase: Acquisition of Glutathione Reductase Activity in a Triple Mutant. Biochemistry 1991, 30, 2761-2767.
    • (1991) Biochemistry , vol.30 , pp. 2761-2767
    • Sullivan, F.X.1    Sobolov, S.B.2    Bradley, M.3    Walsh, C.T.4
  • 31
    • 0026642472 scopus 로고
    • Kinetic isotope effect analysis of the reaction catalyzed by Trypanosoma congolense trypanothione reductase
    • Leichus, B. N.; Bradley, M.; Nadeau, K.; Walsh, C. T.; Blanchard, J. S. Kinetic isotope effect analysis of the reaction catalyzed by Trypanosoma congolense trypanothione reductase. Biochemistry 1992, 31, 6414-6420.
    • (1992) Biochemistry , vol.31 , pp. 6414-6420
    • Leichus, B.N.1    Bradley, M.2    Nadeau, K.3    Walsh, C.T.4    Blanchard, J.S.5
  • 32
    • 0028921346 scopus 로고
    • Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase
    • Borges, A.; Cunningham, M. L.; Tovar, J.; Fairlamb, A. H. Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase. Eur. J. Biochem. 1995, 228, 745-752.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 745-752
    • Borges, A.1    Cunningham, M.L.2    Tovar, J.3    Fairlamb, A.H.4
  • 33
    • 0027432023 scopus 로고
    • The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: Enzyme kinetic properties of α-glutamyl-modified substrate analogues
    • El-Waer, A. F.; Smith, K.; McKie, J. H.; Benson, T. J.; Fairlamb, A. H.; Douglas, K. T. The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzyme kinetic properties of α-glutamyl-modified substrate analogues. Biochim. Biophys. Acta 1993, 1203, 93-98.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 93-98
    • El-Waer, A.F.1    Smith, K.2    McKie, J.H.3    Benson, T.J.4    Fairlamb, A.H.5    Douglas, K.T.6
  • 34
    • 0023695894 scopus 로고
    • Fast purification of a functional elongator tRNAmet expressed from a synthetic gene in vivo
    • Meinnel, T.; Mechulam, Y.; Fayat, G. Fast purification of a functional elongator tRNAmet expressed from a synthetic gene in vivo. Nucl. Acids Res. 1988, 16(16), 8095-8096.
    • (1988) Nucl. Acids Res. , vol.16 , Issue.16 , pp. 8095-8096
    • Meinnel, T.1    Mechulam, Y.2    Fayat, G.3
  • 36
    • 0016210428 scopus 로고
    • Human glutathione reductase: Purification of the crystalline enzyme from erythrocytes
    • Worthington, D. J.; Rosemeyer, M. A. Human glutathione reductase: Purification of the crystalline enzyme from erythrocytes. Eur. J. Biochem. 1974, 48, 167-177.
    • (1974) Eur. J. Biochem. , vol.48 , pp. 167-177
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 37
    • 0023644992 scopus 로고
    • Refined structure of glutathione reductase at 1.54 Å resolution
    • Karplus, P. A.; Schulz, G. E. Refined structure of glutathione reductase at 1.54 Å resolution. J. Mol. Biol. 1987, 195, 701-729.
    • (1987) J. Mol. Biol. , vol.195 , pp. 701-729
    • Karplus, P.A.1    Schulz, G.E.2
  • 38
    • 33947445466 scopus 로고
    • Some phenothiazine derivatives. The course of the Friedel-Crafts reaction
    • Baltzly, R.; Harfenist, M.; Webb, F. J. Some phenothiazine derivatives. The course of the Friedel-Crafts reaction. J. Am. Chem. Soc. 1946, 68, 2673-2678.
    • (1946) J. Am. Chem. Soc. , vol.68 , pp. 2673-2678
    • Baltzly, R.1    Harfenist, M.2    Webb, F.J.3
  • 39
    • 15144356015 scopus 로고
    • Studies in the sulfone series. V. 2,8-Diaminophenithiazine-5-oxide
    • Michels, J. G.; Amstutz, E. D. Studies in the sulfone series. V. 2,8-Diaminophenithiazine-5-oxide. J. Am. Chem. Soc. 1950, 72, 888-892.
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 888-892
    • Michels, J.G.1    Amstutz, E.D.2
  • 40
    • 15144353251 scopus 로고
    • Hypercube, Inc., UnPub
    • Hyperchem 4.0, Hypercube, Inc., 1995 (UnPub).
    • (1995) Hyperchem 4.0
  • 41
    • 0024948840 scopus 로고
    • Continuous cultivation of Trypanosoma brucei bloodstream forms in a medium containing a low concentration of serum protein without feeder cell layers
    • Hirumi, H.; Hirumi, K. Continuous cultivation of Trypanosoma brucei bloodstream forms in a medium containing a low concentration of serum protein without feeder cell layers. J. Antimicrob. Chemother. 1989, 75, 985-989.
    • (1989) J. Antimicrob. Chemother. , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 42
    • 0021590709 scopus 로고
    • An in vitro system for determining the activity of compounds against the intracellular amastigote form of Leishmania donovani
    • Neal, R. A.; Croft, S. L. An in vitro system for determining the activity of compounds against the intracellular amastigote form of Leishmania donovani. J. Antimicrob. Chemother. 1984, (14): 463-475.
    • (1984) J. Antimicrob. Chemother. , Issue.14 , pp. 463-475
    • Neal, R.A.1    Croft, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.