메뉴 건너뛰기




Volumn 49, Issue 1, 2006, Pages 426-435

Design, synthesis, and biological evaluation of phosphinopeptides against Trypanosoma cruzi targeting trypanothione biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

1 BUTYL [[(GAMMA GLUTAMYLLEUCYL)AMINO]METHYL]PHOSPHINATE; 1 PENTYL [[(GAMMA GLUTAMYLLEUCYL)AMINO]METHYL]PHOSPHINATE; PHOSPHINIC ACID DERIVATIVE; TRYPANOTHIONE; UNCLASSIFIED DRUG;

EID: 30444438035     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050922i     Document Type: Article
Times cited : (46)

References (57)
  • 1
    • 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
  • 2
    • 0033230579 scopus 로고    scopus 로고
    • Glutathione and trypanothione in parasitic hydroperoxide metabolism
    • Flohé, L.; Hecht, J.; Steinert, P. Glutathione and trypanothione in parasitic hydroperoxide metabolism. Free Radic. Biol. Med. 1999, 27, 966-984.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 966-984
    • Flohé, L.1    Hecht, J.2    Steinert, P.3
  • 3
    • 0034934234 scopus 로고    scopus 로고
    • Trypanothione as a target in the design of antitrypanosomal and antileishmanial agents
    • Augustyns, K.; Amssoms, A.; Yamani, A.; Rajan, P. K.; Haemers, A. Trypanothione as a target in the design of antitrypanosomal and antileishmanial agents. Curr. Pharm. Des. 2001, 7, 1117-1141.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1117-1141
    • Augustyns, K.1    Amssoms, A.2    Yamani, A.3    Rajan, P.K.4    Haemers, A.5
  • 6
    • 0021933665 scopus 로고
    • Identification of a novel, thiol-containing cofactor essential for glutathione reductase enzyme activity in trypanosomatids
    • Fairlamb, A. H.: Cerami, A. Identification of a novel, thiol-containing cofactor essential for glutathione reductase enzyme activity in trypanosomatids. Mol. Biochem. Parasitol. 1985, 14, 187-198.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 187-198
    • Fairlamb, A.H.1    Cerami, A.2
  • 7
    • 0023051830 scopus 로고
    • Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered 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 newly discovered 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
  • 8
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb, A. H. 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
  • 9
    • 0033200161 scopus 로고    scopus 로고
    • Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata
    • Montemartini, M.; Kalisz, H. M.; Hecht, H.-J.; Steinert, P., Flohé, L. Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata. Eur. J. Biochem. 1999, 264, 516-524.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 516-524
    • Montemartini, M.1    Kalisz, H.M.2    Hecht, H.-J.3    Steinert, P.4    Flohé, L.5
  • 10
    • 0034678059 scopus 로고    scopus 로고
    • Distinct mitochondrial and cytosolic enzymes mediate trypanothione- dependent peroxide metabolism in Trypanosoma cruzi
    • Wilkinson, S. R.: Temperton, N. J.: Mondragon, A.; Kelly, J. M. Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. J. Biol. Chem. 2000, 175, 8220-8225.
    • (2000) J. Biol. Chem. , vol.175 , pp. 8220-8225
    • Wilkinson, S.R.1    Temperton, N.J.2    Mondragon, A.3    Kelly, J.M.4
  • 11
    • 10444255569 scopus 로고    scopus 로고
    • Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity
    • Vickers, T. J.; Wyllie, S.; Fairlamb, A. H. Leishmania major elongation factor 1B complex has trypanothione S-transferase and peroxidase activity. J. Biol. Chem. 2004, 279, 49003-49009.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49003-49009
    • Vickers, T.J.1    Wyllie, S.2    Fairlamb, A.H.3
  • 12
    • 3042641848 scopus 로고    scopus 로고
    • Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B
    • Vickers, T. J.; Fairlamb A. H. Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B. J. Biol. Chem. 2004, 279, 27246-27256.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27246-27256
    • Vickers, T.J.1    Fairlamb, A.H.2
  • 13
    • 0030016346 scopus 로고    scopus 로고
    • Characterization of Trypanosoma brucei γ-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione (diglutathionylspermidine)
    • Lueder, D. V.; Phillips, M. A. Characterization of Trypanosoma brucei γ-glutamylcysteine synthetase, an essential enzyme in the biosynthesis of trypanothione (diglutathionylspermidine). J. Biol. Chem. 1996, 271, 17485-17490.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17485-17490
    • Lueder, D.V.1    Phillips, M.A.2
  • 14
    • 0021219926 scopus 로고
    • The effects of buthionine sulphoximine (BSO) on glutathione depletion and xenobiotic biotransformation
    • Drew, R.; Miners, J. O. The effects of buthionine sulphoximine (BSO) on glutathione depletion and xenobiotic biotransformation Biochem. Pharmacol. 1984, 33, 2989-2994.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 2989-2994
    • Drew, R.1    Miners, J.O.2
  • 15
    • 0035941059 scopus 로고    scopus 로고
    • Spermidine is essential for normal proliferation of trypanosomatid protozoa
    • González, N. S.; Huber, A.; Algranati, I. D. Spermidine is essential for normal proliferation of trypanosomatid protozoa. FEBS Lett. 2001, 508, 323-326.
    • (2001) FEBS Lett. , vol.508 , pp. 323-326
    • González, N.S.1    Huber, A.2    Algranati, I.D.3
  • 16
    • 0011740954 scopus 로고
    • Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells A
    • Kierszembaum, F.; Wirth, J. J.; McCann, P. P.; Sjoerdsma. Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells A. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 4278-4282.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4278-4282
    • Kierszembaum, F.1    Wirth, J.J.2    McCann, P.P.3    Sjoerdsma4
  • 17
    • 0031057528 scopus 로고    scopus 로고
    • Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes
    • Ariyanayagam, M. R.; Fairlamb, A. H. Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. Mol. Biochem. Parasitol. 1997, 84, 111-121.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 111-121
    • Ariyanayagam, M.R.1    Fairlamb, A.H.2
  • 18
    • 0033146548 scopus 로고    scopus 로고
    • Arginine decarboxylase in Trypanosoma cruzi, characteristics and kinetic properties
    • Hernández, S.; Schwarcz De Tarlovsky, M. Arginine decarboxylase in Trypanosoma cruzi, characteristics and kinetic properties Cell. Mol. Biol. 1999, 45, 383-391.
    • (1999) Cell. Mol. Biol. , vol.45 , pp. 383-391
    • Hernández, S.1    Schwarcz De Tarlovsky, M.2
  • 19
    • 0003140774 scopus 로고
    • Polyamine metabolism and function in mammalian-cells and protozoans
    • Pegg, A. E.; McCann, P. P. Polyamine metabolism and function in mammalian-cells and protozoans; ISI Atlas of Science 1988, 11-18.
    • (1988) ISI Atlas of Science , pp. 11-18
    • Pegg, A.E.1    McCann, P.P.2
  • 21
    • 0025273891 scopus 로고
    • Biosynthesis of the trypanosomatid metabolite trypanothione: Purification and characterization of trypanothione synthetase from Crithidia fasciculata
    • Henderson, G. B.; Yamaguchi, M.; Novoa, L.: Fairlamb, A. H.; Cerami, A. Biosynthesis of the trypanosomatid metabolite trypanothione: purification and characterization of trypanothione synthetase from Crithidia fasciculata. Biochemistry 1990, 29, 3924-3929.
    • (1990) Biochemistry , vol.29 , pp. 3924-3929
    • Henderson, G.B.1    Yamaguchi, M.2    Novoa, L.3    Fairlamb, A.H.4    Cerami, A.5
  • 22
    • 0027092987 scopus 로고
    • Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata
    • Smith, K.; Nadeau, K.; Bradley M.; Walsh, C.; Fairlamb, A. H. Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata. Prot. Sci. 1992, 1, 874-883.
    • (1992) Prot. Sci. , vol.1 , pp. 874-883
    • Smith, K.1    Nadeau, K.2    Bradley, M.3    Walsh, C.4    Fairlamb, A.H.5
  • 23
    • 0030994263 scopus 로고    scopus 로고
    • Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia fasciculata
    • Koening, K.; Menge, U.; Kiess, M.; Wray, V.; Flohé, L. Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia fasciculata. J. Biol. Chem. 1997, 18, 11908-11915.
    • (1997) J. Biol. Chem. , vol.18 , pp. 11908-11915
    • Koening, K.1    Menge, U.2    Kiess, M.3    Wray, V.4    Flohé, L.5
  • 24
    • 0029036040 scopus 로고
    • Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase
    • Bollinger, J. M.: Kwon, D. S.; Huisman, G. W.; Kolters, R.; Walsh, C. T. Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. J. Biol. Chem. 1995, 23, 14031-14041.
    • (1995) J. Biol. Chem. , vol.23 , pp. 14031-14041
    • Bollinger, J.M.1    Kwon, D.S.2    Huisman, G.W.3    Kolters, R.4    Walsh, C.T.5
  • 25
    • 0032582843 scopus 로고    scopus 로고
    • Cloning, expression and reconstitution of the trypanothione-dependent peroxidase system of Crithidia fasciculata
    • Tetaud, E.: Fairlamb, A. H. Cloning, expression and reconstitution of the trypanothione-dependent peroxidase system of Crithidia fasciculata. Mol Biochem Parasitol. 1998, 96, 111-123.
    • (1998) Mol Biochem Parasitol , vol.96 , pp. 111-123
    • Tetaud, E.1    Fairlamb, A.H.2
  • 26
    • 0037097023 scopus 로고    scopus 로고
    • Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata
    • Oza, S. L.; Ariyanayagam, M. R.; Fairlamb, A. H. Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. Biochem. J. 2002, 364, 679-686.
    • (2002) Biochem. J. , vol.364 , pp. 679-686
    • Oza, S.L.1    Ariyanayagam, M.R.2    Fairlamb, A.H.3
  • 27
    • 0037183969 scopus 로고    scopus 로고
    • A single enzyme catalyses formation of trypanothione from glutathione and spermidine in Trypanosoma cruzi
    • Oza, S. L; Tetaud, E.; Ariyanayagam, M. R.; Warnon, S. S.; Fairlamb, A. H. A single enzyme catalyses formation of trypanothione from glutathione and spermidine in Trypanosoma cruzi. J. Biol. Chem. 2002, 39, 35853-35861.
    • (2002) J. Biol. Chem. , vol.39 , pp. 35853-35861
    • Oza, S.L.1    Tetaud, E.2    Ariyanayagam, M.R.3    Warnon, S.S.4    Fairlamb, A.H.5
  • 29
    • 14844334895 scopus 로고    scopus 로고
    • Trypanothione synthesis in Crithidia revisited
    • Comini, M.; Menge, U.; Wissing, J.; Flohé, L. Trypanothione synthesis in Crithidia Revisited. J. Biol. Chem. 2005, 280, 6850-6860.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6850-6860
    • Comini, M.1    Menge, U.2    Wissing, J.3    Flohé, L.4
  • 31
    • 0041461862 scopus 로고    scopus 로고
    • Bis-(glutathionylspermidine) and other novel trypanothione analogues in Trypanosoma cruzi
    • Ariyanayagam, M. R.: Oza, S. L.; Mehlert, A.: Fairlamb, A. H. Bis-(glutathionylspermidine) and other novel trypanothione analogues in Trypanosoma cruzi. J. Biol. Chem. 2003, 278, 27612-2769.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27612-32769
    • Ariyanayagam, M.R.1    Oza, S.L.2    Mehlert, A.3    Fairlamb, A.H.4
  • 35
    • 0031054199 scopus 로고    scopus 로고
    • Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata
    • De Craecker, S.; Verbruggen, C.; Rajan, P. K.; Smith, K.; Haemers, A.; Fairlamb, A. H. Characterization of the peptide substrate specificity of glutathionylspermidine synthetase from Crithidia fasciculata. Mol. Biochem. Parasitol. 1997, 84, 25-32.
    • (1997) Mol. Biochem. Parasitol. , vol.84 , pp. 25-32
    • De Craecker, S.1    Verbruggen, C.2    Rajan, P.K.3    Smith, K.4    Haemers, A.5    Fairlamb, A.H.6
  • 36
    • 0028151598 scopus 로고
    • Vancomycin resistance: Structure of D-alanine: D-alanine ligase at 2.3 Å resolution
    • Fan, C.; Moews, P. C.; Walsh, C. T.: Knox, J. R. Vancomycin resistance: structure of D-alanine: D-alanine ligase at 2.3 Å resolution. Science 1994, 266, 439-443.
    • (1994) Science , vol.266 , pp. 439-443
    • Fan, C.1    Moews, P.C.2    Walsh, C.T.3    Knox, J.R.4
  • 37
    • 0028605351 scopus 로고
    • Mechanism-based inactivation of glutathione synthetase by phosphinic acid transition-state analogue
    • Hiratake, J.: Kato, H.: Oda, J. Mechanism-Based Inactivation of Glutathione Synthetase by Phosphinic Acid Transition-State Analogue. J. Am. Chem. Soc: 1994, 116, 12059-12060.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 12059-12060
    • Hiratake, J.1    Kato, H.2    Oda, J.3
  • 39
    • 0001241539 scopus 로고    scopus 로고
    • Investigations on new strategies for the facile synthesis of polyfunctionalized phosphinates: Phosphinopeptide analogues of glutathionylspermidine
    • Chen, S.; Coward, J. K. Investigations on New Strategies for the Facile Synthesis of Polyfunctionalized Phosphinates: Phosphinopeptide Analogues of Glutathionylspermidine. J. Org. Chem. 1998, 63, 502-509.
    • (1998) J. Org. Chem. , vol.63 , pp. 502-509
    • Chen, S.1    Coward, J.K.2
  • 40
    • 0031552157 scopus 로고    scopus 로고
    • Novel inhibitors of trypanothione biosynthesis: Synthesis and evaluation of a phosphinate analogue of glutathionyl spermidine (GSP), a potent, slow-binding inhibitor of GSP synthetase
    • Chen, S.; Lin, C.-H.: Walsh, C. T.; Coward, J. K. Novel inhibitors of trypanothione biosynthesis: synthesis and evaluation of a phosphinate analogue of glutathionyl spermidine (GSP), a potent, slow-binding inhibitor of GSP synthetase. Bioorg. Med. Chem. Lett. 1997, 7, 505-510.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 505-510
    • Chen, S.1    Lin, C.-H.2    Walsh, C.T.3    Coward, J.K.4
  • 43
    • 0034117242 scopus 로고    scopus 로고
    • Structure-activity study on the in Vitro antiprotozoal activity of glutathione derivatives
    • D'Silva, C.: Daunes, S.; Rock, P.; Yardley, V.; Croft, S. L. Structure-Activity Study on the In Vitro Antiprotozoal Activity of Glutathione Derivatives. J. Med. Chem. 2000, 43, 2072-2078.
    • (2000) J. Med. Chem. , vol.43 , pp. 2072-2078
    • D'Silva, C.1    Daunes, S.2    Rock, P.3    Yardley, V.4    Croft, S.L.5
  • 44
    • 0035974742 scopus 로고    scopus 로고
    • QSAR study on the contribution of Log P and Es to the in Vitro antiprotozoal. Activity of glutathione derivatives
    • Daunes, S.; D'Silva, C.; Kendrick, H.: Yardley, V.; Croft, S. L. QSAR Study on the Contribution of Log P and Es to the in Vitro Antiprotozoal. Activity of Glutathione Derivatives. J. Med. Chem. 2001, 44, 2976-2983.
    • (2001) J. Med. Chem. , vol.44 , pp. 2976-2983
    • Daunes, S.1    D'Silva, C.2    Kendrick, H.3    Yardley, V.4    Croft, S.L.5
  • 45
    • 3242738322 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of glutathione-like tripeptides against Trypanosoma cruzi
    • Ravaschino, E. L.; Docampo, R.; Rodriguez, J. B. Synthesis and Biological Evaluation of Glutathione-like Tripeptides against Trypanosoma cruzi. Arkivoc 2003, Part (x), 298-313.
    • (2003) Arkivoc , Issue.PART X , pp. 298-313
    • Ravaschino, E.L.1    Docampo, R.2    Rodriguez, J.B.3
  • 46
    • 0030727159 scopus 로고    scopus 로고
    • Design, synthesis, and biochemical evaluation of phosphonate and phosphonamidate analogues of glutathionylspermidine as inhibitors of glutathionylspermidine synthetase/amidase from Escherichia coli
    • Chen, S.: Lin, C.-H.: Kwon, D. S.: Walsh, C. T.; Coward, J. K. Design, Synthesis, and Biochemical Evaluation of Phosphonate and Phosphonamidate Analogues of Glutathionylspermidine as Inhibitors of Glutathionylspermidine Synthetase/Amidase from Escherichia coli. J. Med. Chem. 1997, 40, 3842-3850.
    • (1997) J. Med. Chem. , vol.40 , pp. 3842-3850
    • Chen, S.1    Lin, C.-H.2    Kwon, D.S.3    Walsh, C.T.4    Coward, J.K.5
  • 47
    • 0031029389 scopus 로고    scopus 로고
    • Dissection of glutathionylspermidine synthetase/amidase from Escherichia coli into autonomously folding and functional synthetase and amidase domains
    • Kwon, D. S.: Lin, C.-H.; Chen, S.; Coward, J. K.; Walsh, C. T.: Bollinger, J. M., Jr. Dissection of Glutathionylspermidine Synthetase/Amidase from Escherichia coli into Autonomously Folding and Functional Synthetase and Amidase Domains. J. Biol. Chem. 1997, 272, 2429-2436.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2429-2436
    • Kwon, D.S.1    Lin, C.-H.2    Chen, S.3    Coward, J.K.4    Walsh, C.T.5    Bollinger Jr., J.M.6
  • 48
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith, O. W.; Meister, A. Potent and Specific Inhibition of Glutathione Synthesis by Buthionine Sulfoximine (S-n-Butyl Homocysteine Sulfoximine). J. Biol. Chem. 1979, 254, 7558-7560.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 53
    • 0034030531 scopus 로고    scopus 로고
    • Design and synthesis of aryloxyethyl thiocyanate derivatives as potent inhibitors of Trypanosoma cruzi proliferation
    • Szajnman, S. H.; Yan, W.; Bailey, B. N.; Docampo, R.; Elhalem, E.; Rodriguez, J. B.; Design and Synthesis of Aryloxyethyl Thiocyanate Derivatives as Potent Inhibitors of Trypanosoma cruzi Proliferation. J. Med. Chem. 2000, 43, 1826-1840.
    • (2000) J. Med. Chem. , vol.43 , pp. 1826-1840
    • Szajnman, S.H.1    Yan, W.2    Bailey, B.N.3    Docampo, R.4    Elhalem, E.5    Rodriguez, J.B.6
  • 54
    • 0037194642 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of aryloxyethyl thiocyanate derivatives against Trypanosoma cruzi
    • Elhalem, E.; Bailey, B. N.: Docampo, R.; Ujváry, I.; Szajnman, S. H.; Rodriguez, J. B. Design, Synthesis and Biological Evaluation of Aryloxyethyl Thiocyanate Derivatives against Trypanosoma cruzi. J. Med. Chem. 2002, 45, 3984-3999.
    • (2002) J. Med. Chem. , vol.45 , pp. 3984-3999
    • Elhalem, E.1    Bailey, B.N.2    Docampo, R.3    Ujváry, I.4    Szajnman, S.H.5    Rodriguez, J.B.6
  • 55
    • 0038778632 scopus 로고    scopus 로고
    • Mechanism of action of 4-phenoxyphenoxy derivatives against Trypanosoma cruzi, the causative agent of Chagas disease
    • Urbina, J. A.; Concepcion, J. L.; Montalvetti, A.; Rodriguez, J. B.; Docampo, R. Mechanism of action of 4-phenoxyphenoxy derivatives against Trypanosoma cruzi, the causative agent of Chagas disease. Antimicrob. Agents Chemother. 2003, 47, 2047-2050.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2047-2050
    • Urbina, J.A.1    Concepcion, J.L.2    Montalvetti, A.3    Rodriguez, J.B.4    Docampo, R.5
  • 56
    • 0035953026 scopus 로고    scopus 로고
    • Bisphosphonates derived from fatty acids are potent growth inhibitors of Trypanosoma cruzi
    • Szajnman, S. H.; Bailey, B. N.; Docampo, R.; Rodriguez, J. B. Bisphosphonates Derived from Fatty Acids are Potent Growth Inhibitors of Trypanosoma cruzi. Bioorg. Med. Chem. Lett. 2001, 11, 789-792.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 789-792
    • Szajnman, S.H.1    Bailey, B.N.2    Docampo, R.3    Rodriguez, J.B.4
  • 57
    • 0041330424 scopus 로고    scopus 로고
    • Bisphosphonates derived from fatty acids are potent inhibitors of Trypanosoma cruzi farnesyl pyrophosphate synthase
    • Szajnman, S. H.; Montalvetti, A.; Wang, Y.; Docampo, R.; Rodriguez, J. B. Bisphosphonates Derived from Fatty Acids are Potent Inhibitors of Trypanosoma cruzi Farnesyl Pyrophosphate Synthase. Bioorg. Med. Chem. Lett. 2003, 13, 3231-3235.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 3231-3235
    • Szajnman, S.H.1    Montalvetti, A.2    Wang, Y.3    Docampo, R.4    Rodriguez, J.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.