메뉴 건너뛰기




Volumn 6, Issue 4, 2010, Pages 195-210

Targets for Anti-T. Cruzi Drugs in the Post-Genomic Era

Author keywords

Chagas'disease; Drugs development; Enzymatic inhibitors

Indexed keywords

2 DIFLUOROMETHYL 4 NITROPHENYL 3,5 DIDEOXY DEXTRO GLYCERO ALPHA DEXTRO GALACTO 2 NONULOPYRANOSID ACID; ANTHRAQUINONE DERIVATIVE; ANTITRYPANOSOMAL AGENT; BENZIMIDAZOLE; BENZNIDAZOLE; CYCLIC AMP PHOSPHODIESTERASE; DIPYRIDAMOLE; ETAZOLATE; GUANOSINE TRIPHOSPHATASE; HYDROXAMIC ACID DERIVATIVE; IMAZODAN; ISOQUINOLINE DERIVATIVE; MEVALONIC ACID; MILRINONE; N ACETYLNEURAMINIC ACID; NIFURTIMOX; PAPAVERINE; PHOSPHODIESTERASE INHIBITOR; PROTEIN FARNESYLTRANSFERASE INHIBITOR; RISEDRONIC ACID; ROLIPRAM; THEOPHYLLINE; TIPIFARNIB; TREQUINSIN; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; VINPOCETINE; ZAPRINAST;

EID: 79954445625     PISSN: 15734080     EISSN: None     Source Type: Journal    
DOI: 10.2174/157340810794578533     Document Type: Article
Times cited : (6)

References (130)
  • 1
    • 0000921923 scopus 로고
    • Nova entidade morbida do homen. Resumo geral dos estudos etiológicos e clínicos
    • Chagas, C. Nova entidade morbida do homen. Resumo geral dos estudos etiológicos e clínicos. Mem. Inst. Oswaldo Cruz, 1911, 3, 219-275.
    • (1911) Mem. Inst. Oswaldo Cruz , vol.3 , pp. 219-275
    • Chaga, C.1
  • 2
    • 79954430346 scopus 로고    scopus 로고
    • http://www.who.org/.
  • 3
    • 0032463396 scopus 로고    scopus 로고
    • The Southern Cone initiative against Chagas disease
    • Schofield, C.J.; Dias, J.C. The Southern Cone initiative against Chagas disease. Adv. Parasitol., 1999, 42, 1-27.
    • (1999) Adv. Parasitol , vol.42 , pp. 1-27
    • Schofield, C.J.1    Dias, J.C.2
  • 4
    • 79954432026 scopus 로고    scopus 로고
    • Available at, Accessed December 19
    • Available at http://www.who.int/tdrold/publications/tdrnews/news63/chagas.htm (Accessed December 19, 2010).
    • (2010)
  • 6
    • 77953989938 scopus 로고    scopus 로고
    • Series of acute Chagas' disease cases attended at a tertiary-level clinic in Manaus, State of Amazonas, from 1980 to 2006
    • Monteiro, W.M.; das Graças Vale Barbosa, M.; de Ornelas Toledo, M.J.; Fé, F.A.; Ferreira Fé, N. Series of acute Chagas' disease cases attended at a tertiary-level clinic in Manaus, State of Amazonas, from 1980 to 2006. Rev. Soc. Bras. Med. Trop., 2010, 43, 207-210.
    • (2010) Rev. Soc. Bras. Med. Trop , vol.43 , pp. 207-210
    • Monteiro, W.M.1    das Graças, V.B.M.2    de ornelas, T.M.J.3    Fé, F.A.4    Ferreira, F.N.5
  • 7
    • 77954007945 scopus 로고    scopus 로고
    • Clinic and epidemiological study on Chagas disease in the Serra Azul district of Mateus Leme, central-western region of the State of Minas Gerais, Brazil
    • Marques da Silva, E.; da Costa Rocha, M.O.; Silva, R.C.; do Carmo Paixão, G.; Buzzati, H.; Nogueira Santos, A.; do Carmo Pereira Nunes, M. Clinic and epidemiological study on Chagas disease in the Serra Azul district of Mateus Leme, central-western region of the State of Minas Gerais, Brazil. Rev. Soc. Bras. Med. Trop., 2010, 43, 178-181.
    • (2010) Rev. Soc. Bras. Med. Trop , vol.43 , pp. 178-181
    • da Silva, E.M.1    da Costa, R.M.O.2    Silva, R.C.3    do Carmo, P.G.4    Buzzati, H.5    Nogueira, S.A.6    do Carmo, P.N.M.7
  • 8
    • 77949851114 scopus 로고    scopus 로고
    • Prevalence of Chagas disease among pregnant women in the southern region of rio grande do sul
    • Bergmann Araújo, A.; Delpizzo Castagno, V.; Gallina, T.; Aires Berne, M.E. Prevalence of Chagas disease among pregnant women in the southern region of Rio Grande do Sul. Rev. Soc. Bras. Med. Trop., 2009, 42, 732-733.
    • (2009) Rev. Soc. Bras. Med. Trop , vol.42 , pp. 732-733
    • Bergmann, A.A.1    Delpizzo, C.V.2    Gallina, T.3    Aires, B.M.E.4
  • 10
    • 77954016922 scopus 로고    scopus 로고
    • Analysis on the food source of Panstrongylus megistus (Hemiptera, Reduviidae, Triatominae) and its present importance as a vector for Trypanosoma cruzi, in the State of Minas Gerais
    • Marreiro Villela, M.; Cortiço Corrêa Rodrigues, V.L.; Casanova, C.; Pinto, J.C. Dias. Analysis on the food source of Panstrongylus megistus (Hemiptera, Reduviidae, Triatominae) and its present importance as a vector for Trypanosoma cruzi, in the State of Minas Gerais. Rev. Soc. Bras. Med. Trop., 2010, 43, 125-128.
    • (2010) Rev. Soc. Bras. Med. Trop , vol.43 , pp. 125-128
    • Marreiro, V.M.1    Cortiço, C.R.V.L.2    Casanova, C.3    Pinto, D.J.C.4
  • 12
    • 77952531258 scopus 로고    scopus 로고
    • Mexican Trypanosoma cruzi T. cruzi I strains with different degrees of virulence induce diverse humoral and cellular immune responses in a murine experimental infection model
    • Espinoza, B.; Rico, T., Sosa, S.; Oaxaca, E.; Vizcaino-Castillo, A.; Caballero, M.L.; Martínez, I. Mexican Trypanosoma cruzi T. cruzi I strains with different degrees of virulence induce diverse humoral and cellular immune responses in a murine experimental infection model. J. Biomed. Biotechnol., 2010, 2010, 890672.
    • (2010) J. Biomed. Biotechnol , vol.2010 , pp. 890672
    • Espinoza, B.1    Rico, T.2    Sosa, S.3    Oaxaca, E.4    Vizcaino-Castillo, A.5    Caballero, M.L.6    Martínez, I.7
  • 13
    • 0036835130 scopus 로고    scopus 로고
    • Chemotherapy of Chagas' disease: Status and new developments
    • Cerecetto, H.; González, M. Chemotherapy of Chagas' disease: status and new developments. Curr. Top. Med. Chem., 2002, 2, 1187-213.
    • (2002) Curr. Top. Med. Chem , vol.2 , pp. 1187-1213
    • Cerecetto, H.1    González, M.2
  • 14
    • 33748669644 scopus 로고    scopus 로고
    • Toxic side effects of drugs used to treat Chagas' disease (American Trypanosomiasis)
    • Castro, J.A.; Montalto de Mecca, M.; Bartel, L.C. Toxic side effects of drugs used to treat Chagas' disease (American Trypanosomiasis). Hum. Exp. Toxicol., 2006, 25, 471-479.
    • (2006) Hum. Exp. Toxicol , vol.25 , pp. 471-479
    • Castro, J.A.1    de Mecca, M.M.2    Bartel, L.C.3
  • 15
    • 36349037267 scopus 로고    scopus 로고
    • An overview of Chagas disease treatment
    • Jannin, J.; Villa, L. An overview of Chagas disease treatment. Mem. Inst. Oswaldo Cruz, 2007, 102, 95-97.
    • (2007) Mem. Inst. Oswaldo Cruz , vol.102 , pp. 95-97
    • Jannin, J.1    Villa, L.2
  • 17
    • 68949220484 scopus 로고    scopus 로고
    • The BENEFIT trial: Testing the hypothesis that trypanocidal therapy is beneficial for patients with chronic Chagas heart disease
    • Marin-Neto, J.A.; Rassi, A.; Avezum, A.; Mattos, A.C.; Rassi, A. The BENEFIT trial: testing the hypothesis that trypanocidal therapy is beneficial for patients with chronic Chagas heart disease. Mem. Inst. Oswaldo Cruz, 2009, 104, 319-324.
    • (2009) Mem. Inst. Oswaldo Cruz , vol.104 , pp. 319-324
    • Marin-Neto, J.A.1    Rassi, A.2    Avezum, A.3    Mattos, A.C.4    Rassi, A.5
  • 18
    • 45549100534 scopus 로고    scopus 로고
    • Rationale and design of a randomized placebo-controlled trial assessing the effects of etiologic treatment in Chagas' cardiomyopathy: The BENznidazole Evaluation For Interrupting Trypanosomiasis (BENEFIT)
    • Marin-Neto, J.A.; Rassi, A.; Morillo, C.A.; Avezum, A.; Connolly, S.J.; Sosa-Estani, S.; Rosas, F.; Yusuf, S. Rationale and design of a randomized placebo-controlled trial assessing the effects of etiologic treatment in Chagas' cardiomyopathy: The BENznidazole Evaluation For Interrupting Trypanosomiasis (BENEFIT). Am. Heart J., 2008, 156, 37-43.
    • (2008) Am. Heart J , vol.156 , pp. 37-43
    • Marin-Neto, J.A.1    Rassi, A.2    Morillo, C.A.3    Avezum, A.4    Connolly, S.J.5    Sosa-Estani, S.6    Rosas, F.7    Yusuf, S.8
  • 20
    • 17344379918 scopus 로고    scopus 로고
    • Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox
    • Murta, S.M.; Gazzinelli, R.T.; Brener, Z.; Romanha, A.J. Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox. Mol. Biochem. Parasitol., 1998, 93, 203-214.
    • (1998) Mol. Biochem. Parasitol , vol.93 , pp. 203-214
    • Murta, S.M.1    Gazzinelli, R.T.2    Brener, Z.3    Romanha, A.J.4
  • 21
    • 0023192059 scopus 로고
    • Genotoxicity studies with two antichagasic drugs
    • Nagel, R. Genotoxicity studies with two antichagasic drugs. Mutat. Res., 1987, 191, 17-20.
    • (1987) Mutat. Res , vol.191 , pp. 17-20
    • Nagel, R.1
  • 26
    • 22744459375 scopus 로고    scopus 로고
    • Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis
    • Meiering, S.; Inhoff, O.; Mies, J.; Vincek, A.; Garcia, G.; Kramer, B.; Dormeyer, M.; Krauth-Siegel, R.L. Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis. J. Med. Chem., 2005, 48, 4793-4802.
    • (2005) J. Med. Chem , vol.48 , pp. 4793-4802
    • Meiering, S.1    Inhoff, O.2    Mies, J.3    Vincek, A.4    Garcia, G.5    Kramer, B.6    Dormeyer, M.7    Krauth-Siegel, R.L.8
  • 29
    • 56449128034 scopus 로고    scopus 로고
    • Structure-activity relationships for a class of selective inhibitors of the major cysteine protease from trypanosoma cruzi
    • Guido, R.V.; Trossini, G.H.; Castilho, M.S.; Oliva, G.; Ferreira, E.I.; Andricopulo, A.D. Structure-activity relationships for a class of selective inhibitors of the major cysteine protease from Trypanosoma cruzi. J. Enzyme Inhib. Med. Chem., 2008, 23, 964-973.
    • (2008) J. Enzyme Inhib. Med. Chem , vol.23 , pp. 964-973
    • Guido, R.V.1    Trossini, G.H.2    Castilho, M.S.3    Oliva, G.4    Ferreira, E.I.5    Andricopulo, A.D.6
  • 30
    • 69249202661 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships for a series of inhibitors of cruzain from Trypanosoma cruzi: Molecular modeling, CoMFA and CoMSIA studies
    • Trossini, G.H.; Guido, R.V.; Oliva, G.; Ferreira, E.I.; Andricopulo, A.D. Quantitative structure-activity relationships for a series of inhibitors of cruzain from Trypanosoma cruzi: molecular modeling, CoMFA and CoMSIA studies. J. Mol. Graph. Model, 2009, 28, 3-11.
    • (2009) J. Mol. Graph. Model , vol.28 , pp. 3-11
    • Trossini, G.H.1    Guido, R.V.2    Oliva, G.3    Ferreira, E.I.4    Andricopulo, A.D.5
  • 32
    • 61449562202 scopus 로고    scopus 로고
    • Trypanosoma cruzi targets for new chemotherapeutic approaches
    • Soeiro, M.N.; de Castro, S.L. Trypanosoma cruzi targets for new chemotherapeutic approaches. Expert Opin Ther Targets, 2009, 13, 105-121.
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 105-121
    • Soeiro, M.N.1    de Castro, S.L.2
  • 33
    • 77953082627 scopus 로고    scopus 로고
    • Specific chemotherapy of Chagas disease: Relevance, current limitations and new approaches
    • Urbina, J.A. Specific chemotherapy of Chagas disease: Relevance, current limitations and new approaches. Acta Trop., 2010, 115, 55- 68.
    • (2010) Acta Trop , vol.115 , pp. 55-68
    • Urbina, J.A.1
  • 34
    • 69049116505 scopus 로고    scopus 로고
    • Ergosterol biosynthesis and drug development for Chagas disease
    • Urbina, J.A. Ergosterol biosynthesis and drug development for Chagas disease. Mem. Inst. Oswaldo Cruz, 2009, 104, 311-318.
    • (2009) Mem. Inst. Oswaldo Cruz , vol.104 , pp. 311-318
    • Urbina, J.A.1
  • 36
    • 59649119617 scopus 로고    scopus 로고
    • Pentafluorosulfanyl as a novel building block for enzyme inhibitors: Trypanothione reductase inhibition and antiprotozoal activities of diarylamines
    • Stump, B.; Eberle, C.; Schweizer, W.B.; Marcel Kaiser, M.; Brun, R.; Krauth-Siegel, R.L.; Lentz, D.; Diederich, F. Pentafluorosulfanyl as a novel building block for enzyme inhibitors: Trypanothione reductase inhibition and antiprotozoal activities of diarylamines. ChemBioChem, 2009, 10, 79-83.
    • (2009) ChemBioChem , vol.10 , pp. 79-83
    • Stump, B.1    Eberle, C.2    Schweizer, W.B.3    Marcel, K.M.4    Brun, R.5    Krauth-Siegel, R.L.6    Lentz, D.7    Diederich, F.8
  • 37
    • 73449144111 scopus 로고    scopus 로고
    • Synthesis, inhibition potency, binding mode, and antiprotozoal activities of fluorescent inhibitors of trypanothione reductase based on mepacrine-conjugated diaryl sulfide scaffolds
    • Eberle, C.; Burkhard, J.A.; Stump, B.; Kaiser, M.; Brun, R.; Krauth-Siegel, R.S.; Diederich, F. Synthesis, inhibition potency, binding mode, and antiprotozoal activities of fluorescent inhibitors of trypanothione reductase based on mepacrine-conjugated diaryl sulfide scaffolds. ChemMedChem, 2009, 4, 2034-2044.
    • (2009) ChemMedChem , vol.4 , pp. 2034-2044
    • Eberle, C.1    Burkhard, J.A.2    Stump, B.3    Kaiser, M.4    Brun, R.5    Krauth-Siegel, R.S.6    Diederich, F.7
  • 38
    • 71549158851 scopus 로고    scopus 로고
    • Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi
    • Jones, D.C.; Ariza, A.; Chow, W.-H.A.; Oza, S.L.; Fairlamb, A.H. Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi. Mol. Biochem. Parasitol., 2010, 169, 12-19.
    • (2010) Mol. Biochem. Parasitol , vol.169 , pp. 12-19
    • Jones, D.C.1    Ariza, A.2    Chow, W.-H.A.3    Oza, S.L.4    Fairlamb, A.H.5
  • 39
    • 77952171991 scopus 로고    scopus 로고
    • Synthetic medicinal chemistry in Chagas' disease: Compounds at the final stage of hit-to-lead phase
    • Cerecetto, H.; González, M. Synthetic medicinal chemistry in Chagas' disease: compounds at the final stage of Hit-to-Lead phase. Pharmaceuticals, 2010, 3, 810-838.
    • (2010) Pharmaceuticals , vol.3 , pp. 810-838
    • Cerecetto, H.1    González, M.2
  • 40
    • 27744577599 scopus 로고    scopus 로고
    • Biogenesis, molecular regulation and function of plant isoprenoids
    • Bouvier, F.; Rahier, A.; Camara, B. Biogenesis, molecular regulation and function of plant isoprenoids. Prog. Lipid Res., 2005, 44, 357-429.
    • (2005) Prog. Lipid Res , vol.44 , pp. 357-429
    • Bouvier, F.1    Rahier, A.2    Camara, B.3
  • 41
    • 58549107780 scopus 로고    scopus 로고
    • Intracellular location of the early steps of the isoprenoid biosynthetic pathway in the trypanosomatids Leishmania major and Trypanosoma brucei
    • Carrero-Lérida, J.; Pérez-Moreno, G.; Castillo-Acosta, V.M.; Ruiz-Pérez, L.M.; González-Pacanowska, D. Intracellular location of the early steps of the isoprenoid biosynthetic pathway in the trypanosomatids Leishmania major and Trypanosoma brucei. Int. J. Parasitol., 2009, 39, 307-314.
    • (2009) Int. J. Parasitol , vol.39 , pp. 307-314
    • Carrero-Lérida, J.1    Pérez-Moreno, G.2    Castillo-Acosta, V.M.3    Ruiz-Pérez, L.M.4    González-Pacanowska, D.5
  • 43
    • 4644370323 scopus 로고    scopus 로고
    • Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
    • Reid, T.S.; Terry, K.L. Casey, P.J.;Beese, L.S. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J. Mol. Biol., 2004, 343, 417-433.
    • J. Mol. Biol
    • Reid, T.S.1    Terry, K.L.2    Casey, P.J.3    Beese, L.S.4
  • 44
    • 34247482458 scopus 로고    scopus 로고
    • C-Terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins
    • Gillespie, J.R.; Yokoyamab, K.; Lu, K.; Eastman, R.T.; Bollinger, J.G.; Van Voorhis, W.C.; Gelb, M.H.; Buckner, F.S. C-Terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins. Mol. Biochem. Parasitol., 2007, 153, 115-124.
    • (2007) Mol. Biochem. Parasitol , vol.153 , pp. 115-124
    • Gillespie, J.R.1    Yokoyamab, K.2    Lu, K.3    Eastman, R.T.4    Bollinger, J.G.5    van Voorhis, W.C.6    Gelb, M.H.7    Buckner, F.S.8
  • 45
    • 0032500692 scopus 로고    scopus 로고
    • Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics
    • Yokoyama, K.; Trobridge, P.; Buckner, F.S.; Van Voorhis, W.C.; Stuart, K.D.; Gelb, M.H. Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics. J. Biol. Chem., 1998, 273, 26497-26505.
    • (1998) J. Biol. Chem , vol.273 , pp. 26497-26505
    • Yokoyama, K.1    Trobridge, P.2    Buckner, F.S.3    van Voorhis, W.C.4    Stuart, K.D.5    Gelb, M.H.6
  • 47
    • 23944466866 scopus 로고    scopus 로고
    • The protein farnesyltransferase inhibitor Tipifarnib as a new lead for the development of drugs against Chagas disease
    • Hucke, O.; Gelb, M.H.; Verlinde, C.L.M.J.; Buckner, F.S. The protein farnesyltransferase inhibitor Tipifarnib as a new lead for the development of drugs against Chagas disease. J. Med. Chem., 2005, 48, 5415-5418.
    • (2005) J. Med. Chem , vol.48 , pp. 5415-5418
    • Hucke, O.1    Gelb, M.H.2    Verlinde, C.L.M.J.3    Buckner, F.S.4
  • 48
    • 64349102737 scopus 로고    scopus 로고
    • Lepesheva, Gelb, M.H.; Buckner, F.S. Rational modification of a candidate cancer drug for use against Chagas disease
    • Kraus, J.M.; Verlinde, C.L.M.J.; Karimi, M.; Galina I. Lepesheva, Gelb, M.H.; Buckner, F.S. Rational modification of a candidate cancer drug for use against Chagas disease. J. Med. Chem., 2009, 52, 1639-1647.
    • (2009) J. Med. Chem , vol.52 , pp. 1639-1647
    • Kraus, J.M.1    Verlinde, C.L.M.J.2    Karimi, M.3    Galina, I.4
  • 50
    • 71749114204 scopus 로고    scopus 로고
    • Isoquinoline-based analogs of the cancer drug clinical candidate tipifarnib as anti-Trypanosoma cruzi agents
    • Chennamaneni, N.K.; Arif, J.; Buckner, F.S.; Gelb, M.H. Isoquinoline-based analogs of the cancer drug clinical candidate tipifarnib as anti-Trypanosoma cruzi agents. Bioorg. Med. Chem. Lett., 2009, 19, 6582-6584.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 6582-6584
    • Chennamaneni, N.K.1    Arif, J.2    Buckner, F.S.3    Gelb, M.H.4
  • 51
    • 0038268177 scopus 로고    scopus 로고
    • Farnesyl pyrophosphate synthase is an essential enzyme in Trypanosoma brucei. In vitro RNA interference and in vivo inhibition studies
    • Montalvetti, A., Fernandez, A., Sanders, J.M., Ghosh, S., Van Brussel, E., Oldfield, E., Docampo, R. Farnesyl pyrophosphate synthase is an essential enzyme in Trypanosoma brucei. In vitro RNA interference and in vivo inhibition studies. J. Biol. Chem., 2003, 278, 17075-17083.
    • (2003) J. Biol. Chem , vol.278 , pp. 17075-17083
    • Montalvetti, A.1    Fernandez, A.2    Sanders, J.M.3    Ghosh, S.4    van Brussel, E.5    Oldfield, E.6    Docampo, R.7
  • 53
    • 42749083092 scopus 로고    scopus 로고
    • Farnesyl diphosphate synthase localizes to the cytoplasm of Trypanosoma cruzi and
    • Ferella, M.; Li, Z.-H.; Andersson, B.; Docampo, R. Farnesyl diphosphate synthase localizes to the cytoplasm of Trypanosoma cruzi and T. brucei. Exp. Parasitol., 2008, 119, 308-312.
    • (2008) T. Brucei. Exp. Parasitol , vol.119 , pp. 308-312
    • Ferella, M.1    Li, Z.-H.2    Andersson, B.3    Docampo, R.4
  • 54
    • 0033527417 scopus 로고    scopus 로고
    • Nitrogen-containing bisphosphonates as carbocation transition state analogs for isoprenoid biosynthesis
    • Martin, M.B.; Arnold, W.; Heath, H.T.; Urbina, J.A.; Oldfield, E. Nitrogen-containing bisphosphonates as carbocation transition state analogs for isoprenoid biosynthesis. Biochem. Biophys. Res. Commun., 1999, 263, 754-758.
    • (1999) Biochem. Biophys. Res. Commun , vol.263 , pp. 754-758
    • Martin, M.B.1    Arnold, W.2    Heath, H.T.3    Urbina, J.A.4    Oldfield, E.5
  • 60
    • 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
  • 61
    • 25444525132 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 1-amino-1, 1- bisphosphonates derived from fatty acids against Trypanosoma cruzi targeting farnesyl pyrophosphate synthase
    • Szajnman, S.H.; Ravaschino, E.L.; Docampo, R.; Rodriguez, J.B. Synthesis and biological evaluation of 1-amino-1,1- bisphosphonates derived from fatty acids against Trypanosoma cruzi targeting farnesyl pyrophosphate synthase. Bioorg. Med. Chem. Lett., 2005, 15, 4685-4690.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 4685-4690
    • Szajnman, S.H.1    Ravaschino, E.L.2    Docampo, R.3    Rodriguez, J.B.4
  • 62
    • 41249085709 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 2- alkylaminoethyl-1, 1-bisphosphonic acids against Trypanosoma cruzi and Toxoplasma gondii targeting farnesyl diphosphate synthase
    • Szajnman, S.H.; García Liñares, G.E.; Li, Z.H.; Jiang, C.; Galizzi, M.; Bontempi, E.J.; Ferella, M.; Moreno, S.N.; Docampo, R.; Rodriguez, J.B. Synthesis and biological evaluation of 2-alkylaminoethyl-1,1-bisphosphonic acids against Trypanosoma cruzi and Toxoplasma gondii targeting farnesyl diphosphate synthase. Bioorg. Med. Chem., 2008, 16, 3283-3290.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 3283-3290
    • Szajnman, S.H.1    Garcíaliñares, G.E.2    Li, Z.H.3    Jiang, C.4    Galizzi, M.5    Bontempi, E.J.6    Ferella, M.7    Moreno, S.N.8    Docampo, R.9    Rodriguez, J.B.10
  • 67
    • 0022268757 scopus 로고
    • Calmodulin and Ca2+-dependent cyclic AMP phosphodiesterase activity in Trypanosoma cruzi
    • Téllez-Iñón, M. T.; Ulloa, R. M.; Torreula, M.; Torres, H. N. Calmodulin and Ca2+-dependent cyclic AMP phosphodiesterase activity in Trypanosoma cruzi. Mol. Biochem. Parasitol., 1985, 17, 143-153.
    • (1985) Mol. Biochem. Parasitol , vol.17 , pp. 143-153
    • Téllez-Iñón, M.T.1    Ulloa, R.M.2    Torreula, M.3    Torres, H.N.4
  • 68
    • 1542374655 scopus 로고    scopus 로고
    • Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi
    • D'Angelo, M.A.; Sanguineti, S.; Reece, J.M.; Birnbaumer, L.; Torres, H.N.; Flawiá, M.M. Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi. Biochem. J., 2004, 378, 63-72.
    • (2004) Biochem. J , vol.378 , pp. 63-72
    • D'angelo, M.A.1    Sanguineti, S.2    Reece, J.M.3    Birnbaumer, L.4    Torres, H.N.5    Flawiá, M.M.6
  • 70
    • 28044464526 scopus 로고    scopus 로고
    • TcPDE4, a novel membrane-associated cAMP-specific phosphodiesterase from Trypanosoma cruzi
    • Alonso, G.D.; Schoijet, A.C.; Torres, H.N.; Flawiá, M.M. TcPDE4, a novel membrane-associated cAMP-specific phosphodiesterase from Trypanosoma cruzi. Mol. Biochem. Parasitol., 2006, 145, 40-49.
    • (2006) Mol. Biochem. Parasitol , vol.145 , pp. 40-49
    • Alonso, G.D.1    Schoijet, A.C.2    Torres, H.N.3    Flawiá, M.M.4
  • 71
    • 33846339421 scopus 로고    scopus 로고
    • TcrPDEA1, a cAMP-specific phosphodiesterase with atypical pharmacological properties from trypanosoma Cruzi
    • Alonso, G.D.; Schoijet, A.C.; Torres, H.N.; Flawiá, M.M. TcrPDEA1, a cAMP-specific phosphodiesterase with atypical pharmacological properties from Trypanosoma cruzi. Mol. Biochem. Parasitol., 2007, 152, 72-79.
    • (2007) Mol. Biochem. Parasitol , vol.152 , pp. 72-79
    • Alonso, G.D.1    Schoijet, A.C.2    Torres, H.N.3    Flawiá, M.M.4
  • 72
    • 77956131207 scopus 로고    scopus 로고
    • Chemical validation of phosphodiesterase C as a chemotherapeutic target in Trypanosoma cruzi, the etiological agent of Chagas' disease
    • King-Keller, S.; Li, M.; Smith, A.; Zheng, S.; Kaur, G.; Yang, X.; Wang, B.; Docampo, R. Chemical validation of phosphodiesterase C as a chemotherapeutic target in Trypanosoma cruzi, the etiological agent of Chagas' disease. Antimicrob. Agents Chemother., 2010, 54, 3738-3745.
    • (2010) Antimicrob. Agents Chemother , vol.54 , pp. 3738-3745
    • King-Keller, S.1    Li, M.2    Smith, A.3    Zheng, S.4    Kaur, G.5    Yang, X.6    Wang, B.7    Docampo, R.8
  • 73
    • 54949087530 scopus 로고    scopus 로고
    • Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification
    • Irigoín, F.; Cibils, L.; Comini, M.A.; Wilkinson, S.R.; Flohé, L.; Radi, R. Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification. Free Radic. Biol. Med., 2008, 45, 733-742.
    • (2008) Free Radic. Biol. Med , vol.45 , pp. 733-742
    • Irigoín, F.1    Cibils, L.2    Comini, M.A.3    Wilkinson, S.R.4    Flohé, L.5    Radi, R.6
  • 74
    • 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, 277, 35853-35861.
    • (2002) J. Biol. Chem , vol.277 , pp. 35853-35861
    • Oza, S.L.1    Tetaud, E.2    Ariyanayagam, M.R.3    Warnon, S.S.4    Fairlamb, A.H.5
  • 75
    • 13444280474 scopus 로고    scopus 로고
    • Dithiol proteins as guardians of the intracellular redox milieu in parasites: Old and new drug targets in trypanosomes and malaria-causing plasmodia
    • Krauth-Siegel, R. L.; Bauer, H.; Schirmer, R. H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. Angew. Chem. Int. Ed. Engl., 2005, 44, 690-715.
    • (2005) Angew. Chem. Int. Ed. Engl , vol.44 , pp. 690-715
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 77
    • 47749111316 scopus 로고    scopus 로고
    • Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities
    • Fyfe, P. K.; Oza, S. L.; Fairlamb, A. H.; Hunter, W. N. Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. J. Biol. Chem., 2008, 283, 17672-17680.
    • (2008) J. Biol. Chem , vol.283 , pp. 17672-17680
    • Fyfe, P.K.1    Oza, S.L.2    Fairlamb, A.H.3    Hunter, W.N.4
  • 78
    • 0031451002 scopus 로고    scopus 로고
    • Polyamine derivatives as inhibitors of trypanothione reductase and assessment of their trypanocidal activities
    • O'Sullivan, M.C.; Zhou, Q.; Li, Z.; Durham, T.B.; Rattendi, D.; Lane, S.; Bacchi, C.J. Polyamine derivatives as inhibitors of trypanothione reductase and assessment of their trypanocidal activities. Bioorg. Med. Chem., 1997, 5, 2145-2155.
    • (1997) Bioorg. Med. Chem , vol.5 , pp. 2145-2155
    • O'Sullivan, M.C.1    Zhou, Q.2    Li, Z.3    Durham, T.B.4    Rattendi, D.5    Lane, S.6    Bacchi, C.J.7
  • 80
    • 40749087168 scopus 로고    scopus 로고
    • Imidazolidines as new anti-trypanosoma cruzi agents: Biological evaluation and structure-activity relationships
    • Caterina, M.C.; Perillo, I.A.; Boiani, L.; Pezaroglo, H.; Cerecetto, H.; González, M.; Salerno, A. Imidazolidines as new anti- Trypanosoma cruzi agents: Biological evaluation and structure- activity relationships. Bioorg. Med. Chem., 2008, 16, 2226-2234.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 2226-2234
    • Caterina, M.C.1    Perillo, I.A.2    Boiani, L.3    Pezaroglo, H.4    Cerecetto, H.5    González, M.6    Salerno, A.7
  • 81
    • 33646178978 scopus 로고    scopus 로고
    • Novel alkylpolyaminoguanidines and alkylpolyaminobiguanides with potent antitrypanosomal activity
    • Bi, X.; Lopez, C.; Bacchi, C.J.; Rattendi, D.; Woster, P.M. Novel alkylpolyaminoguanidines and alkylpolyaminobiguanides with potent antitrypanosomal activity. Bioorg. Med. Chem. Lett., 2006, 16, 3229-3232.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 3229-3232
    • Bi, X.1    Lopez, C.2    Bacchi, C.J.3    Rattendi, D.4    Woster, P.M.5
  • 82
    • 70350381791 scopus 로고    scopus 로고
    • Dissecting the essentiality of the bifunctional trypanothione synthetase-amidase in Trypanosoma brucei using chemical and genetic methods
    • Wyllie, S.; Oza, S.L.; Patterson, S.; Spinks, D.; Thompson, S.; Fairlamb, A.H. Dissecting the essentiality of the bifunctional trypanothione synthetase-amidase in Trypanosoma brucei using chemical and genetic methods. Mol. Microbiol., 2009, 74, 529-540.
    • (2009) Mol. Microbiol , vol.74 , pp. 529-540
    • Wyllie, S.1    Oza, S.L.2    Patterson, S.3    Spinks, D.4    Thompson, S.5    Fairlamb, A.H.6
  • 85
    • 0019089331 scopus 로고
    • Folding and association of triose phosphate isomerase from rabbit muscle
    • Zabori, S.; Rudolph, R.; Jaenicke, R. Folding and association of triose phosphate isomerase from rabbit muscle. Z. Naturforsch., 1980, 35C, 999-1004.
    • (1980) Z. Naturforsch , vol.35 C , pp. 999-1004
    • Zabori, S.1    Rudolph, R.2    Jaenicke, R.3
  • 87
    • 0036582008 scopus 로고    scopus 로고
    • The interfaces of oligomeric proteins as targets for drug design against enzymes from parasites
    • Pérez-Montfort, R.; de Gómez-Puyou, M.T.; Gómez-Puyou, A. The interfaces of oligomeric proteins as targets for drug design against enzymes from parasites. Curr. Top. Med. Chem., 2002, 2, 457-470.
    • (2002) Curr. Top. Med. Chem , vol.2 , pp. 457-470
    • Pérez-Montfort, R.1    de Gómez-Puyou, M.T.2    Gómez-Puyou, A.3
  • 93
    • 0035501756 scopus 로고    scopus 로고
    • Structure-based inhibitor screening: A family of sulfonated dye inhibitors for malaria parasite triosephosphate isomerase
    • Joubert, F.; Neitz, A. W. H.; Louw, A. I. Structure-based inhibitor screening: A family of sulfonated dye inhibitors for malaria parasite triosephosphate isomerase. Proteins, 2001, 45, 136-143.
    • (2001) Proteins , vol.45 , pp. 136-143
    • Joubert, F.1    Neitz, A.W.H.2    Louw, A.I.3
  • 95
    • 0017939092 scopus 로고
    • Formas moleculares de α-hidroxiácido deshidrogenasa en trypanosoma Cruzi
    • Gerez de Burgos, N.M.; Blanco, A.; Segura, E.L. 1978. Formas moleculares de α-hidroxiácido deshidrogenasa en Trypanosoma cruzi. Medicina (Buenos Aires), 1978, 38, 151-154.
    • (1978) Medicina (Buenos Aires) , vol.1978 , Issue.38 , pp. 151-154
    • de Burgos, N.M.G.1    Blanco, A.2    Segura, E.L.3
  • 96
    • 0038351812 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma cruzi α- hydroxyacid dehydrogenase-isozyme II by N-isopropyl oxamate and its effect on intact epimastigotes
    • Elizondo, S.; Chena, M.A.; Rodríguez-Páez, L.; Nogueda, B.; Baeza, I.; Wong, C. Inhibition of Trypanosoma cruzi α- hydroxyacid dehydrogenase-isozyme II by N-isopropyl oxamate and its effect on intact epimastigotes. J. Enzyme Inhib. Med. Chem., 2003, 3, 265-271.
    • (2003) J. Enzyme Inhib. Med. Chem , vol.3 , pp. 265-271
    • Elizondo, S.1    Chena, M.A.2    Rodríguez-Páez, L.3    Nogueda, B.4    Baeza, I.5    Wong, C.6
  • 98
    • 0023103912 scopus 로고
    • Subcellular localization of leucin amino transferase and α-hydroxyacid dehydrogenase in Trypanosoma cruzi
    • Montamat, E.E.; Arauzo, S.S.; Blanco, A. Subcellular localization of leucin amino transferase and α-hydroxyacid dehydrogenase in Trypanosoma cruzi. Mol. Biochem. Parasitol., 1987, 22, 185-193.
    • (1987) Mol. Biochem. Parasitol , vol.22 , pp. 185-193
    • Montamat, E.E.1    Arauzo, S.S.2    Blanco, A.3
  • 99
    • 0023812367 scopus 로고
    • Subcellular localization of branched-chain aminoacid amino transferase and lactate dehydrogenase C4 in rat and mouse spermatozoa
    • Montamat, E.E.; Vermouth, N.T.; Blanco, A. Subcellular localization of branched-chain aminoacid amino transferase and lactate dehydrogenase C4 in rat and mouse spermatozoa. Biochem. J., 1988, 255, 1053-1056.
    • (1988) Biochem. J , vol.255 , pp. 1053-1056
    • Montamat, E.E.1    Vermouth, N.T.2    Blanco, A.3
  • 101
    • 18444405242 scopus 로고    scopus 로고
    • Trypanocidal activity of N-isopropyl oxamate on cultured epimastigotes and murine trypanosomiasis using different Trypanosoma cruzi strains
    • Chena, M.A.; Elizondo, S.; Rodríguez-Páez, L.; Nogueda, B.; Baeza, I.; Wong, C. Trypanocidal activity of N-isopropyl oxamate on cultured epimastigotes and murine trypanosomiasis using different Trypanosoma cruzi strains. J. Enzyme Inhib. Med. Chem., 2005, 20, 189-197.
    • (2005) J. Enzyme Inhib. Med. Chem , vol.20 , pp. 189-197
    • Chena, M.A.1    Elizondo, S.2    Rodríguez-Páez, L.3    Nogueda, B.4    Baeza, I.5    Wong, C.6
  • 102
    • 34247131722 scopus 로고    scopus 로고
    • In vitro and in vivo trypanocidal activity of the ethyl esters of N-allyl and N-propyl oxamates using different Trypanosoma cruzi strains
    • Aguirre-Alvarado, C.; Zaragoza-Martínez, F.; Rodríguez-Páez, L.; Nogueda, B.; Baeza, I.; Wong, C. In vitro and in vivo trypanocidal activity of the ethyl esters of N-allyl and N-propyl oxamates using different Trypanosoma cruzi strains. J. Enzyme Inhib. Med. Chem., 2007, 22, 227-233.
    • (2007) J. Enzyme Inhib. Med. Chem , vol.22 , pp. 227-233
    • Aguirre-Alvarado, C.1    Zaragoza-Martínez, F.2    Rodríguez-Páez, L.3    Nogueda, B.4    Baeza, I.5    Wong, C.6
  • 104
    • 53849148575 scopus 로고    scopus 로고
    • Structural insights into sialic acid enzymology
    • Buschiazzo, A.; Alzari, P.M. Structural insights into sialic acid enzymology. Curr. Op. Chem. Biol., 2008, 12, 565-572.
    • (2008) Curr. Op. Chem. Biol , vol.12 , pp. 565-572
    • Buschiazzo, A.1    Alzari, P.M.2
  • 105
    • 0027984541 scopus 로고
    • Structural and functional properties of Trypanosoma trans-sialidase
    • Schenkman, S. Structural and functional properties of Trypanosoma trans-sialidase. Annu. Rev. Microbiol., 1994, 48, 499-523.
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 499-523
    • Schenkman, S.1
  • 106
    • 0031054705 scopus 로고    scopus 로고
    • Removal of sialic acid from mucin-like surface molecules of Trypanosoma cruzi metacyclic trypomastigotes enhances parasite-host cell interaction
    • Yoshida, N.; Dorta, M.L.; Ferreira, A.T.; Oshiro, M.E.M.; Mortara, M.A.; Acosta-Serrano, A.; Favoreto, S. Removal of sialic acid from mucin-like surface molecules of Trypanosoma cruzi metacyclic trypomastigotes enhances parasite-host cell interaction. Mol. Biochem. Parasitol., 1997, 84, 57-67.
    • (1997) Mol. Biochem. Parasitol , vol.84 , pp. 57-67
    • Yoshida, N.1    Dorta, M.L.2    Ferreira, A.T.3    Oshiro, M.E.M.4    Mortara, M.A.5    Acosta-Serrano, A.6    Favoreto, S.7
  • 108
    • 77956209421 scopus 로고    scopus 로고
    • CD8+ T cells specific for immunodominant trans-sialidase epitopes contribute to control of Trypanosoma cruzi infection but are not required for resistance
    • Rosenberg, C.S.; Martin, D.L.; Tarleton, R.L. CD8+ T cells specific for immunodominant trans-sialidase epitopes contribute to control of Trypanosoma cruzi infection but are not required for resistance. J. Immunol., 2010, 185, 560-568.
    • (2010) J. Immunol , vol.185 , pp. 560-568
    • Rosenberg, C.S.1    Martin, D.L.2    Tarleton, R.L.3
  • 109
    • 77956266766 scopus 로고    scopus 로고
    • Identification of glycoproteins targeted by Trypanosoma cruzi trans-sialidase, a virulence factor that disturbs lymphocyte glycosylation
    • Muiá, R.P.; Yu, H.; Prescher, J.A.; Hellman, U.; Chen, X.; Bertozzi, C.R.; Campetella, O. Identification of glycoproteins targeted by Trypanosoma cruzi trans-sialidase, a virulence factor that disturbs lymphocyte glycosylation. Glycobiology, 2010, 20, 833-842.
    • (2010) Glycobiology , vol.20 , pp. 833-842
    • Muiá, R.P.1    Yu, H.2    Prescher, J.A.3    Hellman, U.4    Chen, X.5    Bertozzi, C.R.6    Campetella, O.7
  • 110
    • 39149119608 scopus 로고    scopus 로고
    • Rational drug design in parasitology: Trans-sialidase as a case study for Chagas disease
    • Neres, J.; Bryce, R.A.; Douglas, K.T. Rational drug design in parasitology: trans-sialidase as a case study for Chagas disease. Drug Discov. Today, 2008, 13, 110-117.
    • (2008) Drug Discov. Today , vol.13 , pp. 110-117
    • Neres, J.1    Bryce, R.A.2    Douglas, K.T.3
  • 111
    • 0034234658 scopus 로고    scopus 로고
    • Functional Diversity in the trans-sialidase and mucin families in Trypanosoma cruzi
    • Frasch, A.C.C. Functional Diversity in the trans-sialidase and mucin families in Trypanosoma cruzi. Parasitol. Today, 2000, 16, 282-286.
    • (2000) Parasitol. Today , vol.16 , pp. 282-286
    • Frasch, A.C.C.1
  • 112
    • 0028915520 scopus 로고
    • Trypanosoma cruzi transsialidase gene lacking C-terminal repeats and expressed in epimastigote forms
    • Briones, M.; Egima, C.; Schenkman, S. Trypanosoma cruzi transsialidase gene lacking C-terminal repeats and expressed in epimastigote forms. Mol. Biochem. Parasitol., 1995, 70, 9-17.
    • (1995) Mol. Biochem. Parasitol , vol.70 , pp. 9-17
    • Briones, M.1    Egima, C.2    Schenkman, S.3
  • 113
    • 0032171720 scopus 로고    scopus 로고
    • Natural human immunity to trypanosomes
    • Tomlinson, S.; Raper, J. Natural human immunity to trypanosomes. Parasitol. Today, 1998, 14, 354-359.
    • (1998) Parasitol. Today , vol.14 , pp. 354-359
    • Tomlinson, S.1    Raper, J.2
  • 115
    • 0035929141 scopus 로고    scopus 로고
    • A ligand that Trypanosoma cruzi uses to bind to mammalian cells to initiate infection
    • Villalta, F.; Smith, C.M.; Ruiz-Ruano, A.; Lima, M.F. A ligand that Trypanosoma cruzi uses to bind to mammalian cells to initiate infection. FEBS Lett., 2001, 505, 383-388.
    • (2001) FEBS Lett , vol.505 , pp. 383-388
    • Villalta, F.1    Smith, C.M.2    Ruiz-Ruano, A.3    Lima, M.F.4
  • 116
    • 11144293485 scopus 로고    scopus 로고
    • The trans-sialidase from Trypanosoma cruzi induces thrombocytopenia during acute Chagas' disease by reducing the platelet sialic acid contents
    • Tribulatti, M.V.; Mucci, J.; Van Rooijen, N.; Leguizamón, M.S.; Campetella, O. The trans-sialidase from Trypanosoma cruzi induces thrombocytopenia during acute Chagas' disease by reducing the platelet sialic acid contents. Infect. Immun., 2005, 73, 201-207.
    • (2005) Infect. Immun , vol.73 , pp. 201-207
    • Tribulatti, M.V.1    Mucci, J.2    van Rooijen, N.3    Leguizamón, M.S.4    Campetella, O.5
  • 118
    • 34250215985 scopus 로고    scopus 로고
    • Galactosephosphonates as mimetics of the sialyltransfer by trypanosomal sialidases
    • Busse, H.; Hakoda, M.; Stanley, M.; Streicher, H. Galactosephosphonates as mimetics of the sialyltransfer by trypanosomal sialidases. J. Carbohydr. Chem., 2007, 26, 159-194.
    • (2007) J. Carbohydr. Chem , vol.26 , pp. 159-194
    • Busse, H.1    Hakoda, M.2    Stanley, M.3    Streicher, H.4
  • 121
    • 70350557049 scopus 로고    scopus 로고
    • Development of new and selective Trypanosoma cruzi trans-sialidase inhibitors from sulfonamide chalcones and their derivatives
    • Kim, J.H.; Ryu, H.W.; Shim, J.H.; Park, K.H.; Withers, S.G. Development of new and selective Trypanosoma cruzi trans-sialidase inhibitors from sulfonamide chalcones and their derivatives. ChemBioChem, 2009, 10, 2475-2479.
    • (2009) ChemBioChem , vol.10 , pp. 2475-2479
    • Kim, J.H.1    Ryu, H.W.2    Shim, J.H.3    Park, K.H.4    Withers, S.G.5
  • 124
    • 77952270262 scopus 로고    scopus 로고
    • Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase
    • Mitchell, F.L.; Miles, S.M.; Neres J.; Bichenkova, E.V.; Bryce, R.A. Tryptophan as a molecular shovel in the glycosyl transfer activity of Trypanosoma cruzi trans-sialidase. Biophys. J., 2010, 98, L38-L40.
    • (2010) Biophys. J , vol.98
    • Mitchell, F.L.1    Miles, S.M.2    Neres, J.3    Bichenkova, E.V.4    Bryce, R.A.5
  • 125
    • 1642306973 scopus 로고    scopus 로고
    • The Selenophosphate synthetase gene from leishmania major
    • Jayakumar, P. C.; Musande, V. V.; Shouche, Y. S.; Patole, M. S. The Selenophosphate synthetase gene from Leishmania major. DNA Seq., 2004, 15, 66-70.
    • (2004) DNA Seq , vol.15 , pp. 66-70
    • Jayakumar, P.C.1    Musande, V.V.2    Shouche, Y.S.3    Patole, M.S.4
  • 126
    • 33748537719 scopus 로고    scopus 로고
    • Selenium metabolism in Trypanosoma: Characterization of selenoproteomes and identification of a Kinetoplastida-specific selenoprotein
    • Lobanov, A. V.; Gromer, S.; Salinas, G.; Gladyshev, V. N. Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a Kinetoplastida-specific selenoprotein. Nucleic Acids Res., 2006, 34, 4012-4024.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4012-4024
    • Lobanov, A.V.1    Gromer, S.2    Salinas, G.3    Gladyshev, V.N.4
  • 130
    • 33646847486 scopus 로고    scopus 로고
    • TcRho1, the Trypanosoma cruzi Rho homologue, regulates cell-adhesion properties: Evidence for a conserved function
    • Barbosa de Melo, L.D.B.; Eisele, N.; Nepomuceno-Silva, J.L.; Gazos Lopes, U. TcRho1, the Trypanosoma cruzi Rho homologue, regulates cell-adhesion properties: Evidence for a conserved function. Biochem. Biophys. Res. Commun., 2006, 345, 617-622.
    • (2006) Biochem. Biophys. Res. Commun , vol.345 , pp. 617-622
    • de Melo, B.L.D.B.1    Eisele, N.2    Nepomuceno-Silva, J.L.3    Gazos, L.U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.