메뉴 건너뛰기




Volumn 1, Issue 4, 1998, Pages 266-278

Drug resistance in Leishmania: similarities and differences to other organisms

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0002940232     PISSN: 13687646     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1368-7646(98)80007-1     Document Type: Review
Times cited : (26)

References (157)
  • 1
    • 0026543392 scopus 로고
    • Estimation of population at risk of infection and number of cases of leishmaniasis
    • Ashford R.W., Desjeux P., and deRaadt P. Estimation of population at risk of infection and number of cases of leishmaniasis. Parasitol. Today 8 (1992) 104-105
    • (1992) Parasitol. Today , vol.8 , pp. 104-105
    • Ashford, R.W.1    Desjeux, P.2    deRaadt, P.3
  • 2
    • 0027241626 scopus 로고
    • Visceral infection caused by Leishmania tropica in veterans of Operation Desert Storm
    • Magill A.J., Grogl M., Gasser Jr. R.A., et al. Visceral infection caused by Leishmania tropica in veterans of Operation Desert Storm. N Engl J Med 328 19 (1993) 1383-1387
    • (1993) N Engl J Med , vol.328 , Issue.19 , pp. 1383-1387
    • Magill, A.J.1    Grogl, M.2    Gasser Jr., R.A.3
  • 3
    • 0027255738 scopus 로고
    • Mechanisms of drug resistance in Leishmania
    • Ouellette M., and Papadopoulou B. Mechanisms of drug resistance in Leishmania. Parasitol Today 9 5 (1993) 150-153
    • (1993) Parasitol Today , vol.9 , Issue.5 , pp. 150-153
    • Ouellette, M.1    Papadopoulou, B.2
  • 4
    • 0030950966 scopus 로고    scopus 로고
    • Leishmania and human immunodeficiency virus coinfection: the first 10 years
    • Alvar J., Canavate C., Gutierrez-Solar B., et al. Leishmania and human immunodeficiency virus coinfection: the first 10 years. Clin Microbiol Rev 10 2 (1997) 298-319
    • (1997) Clin Microbiol Rev , vol.10 , Issue.2 , pp. 298-319
    • Alvar, J.1    Canavate, C.2    Gutierrez-Solar, B.3
  • 5
    • 0028933795 scopus 로고
    • The regulation of immunity to Leishmania major
    • Reiner S.L., and Locksley R.M. The regulation of immunity to Leishmania major. Annu Rev Immunol 13 (1995) 151-177
    • (1995) Annu Rev Immunol , vol.13 , pp. 151-177
    • Reiner, S.L.1    Locksley, R.M.2
  • 6
    • 0027249951 scopus 로고
    • Practical progress and new drugs for changing patterns of leishmaniasis
    • Olliaro P.L., and Bryceson A. Practical progress and new drugs for changing patterns of leishmaniasis. Parasitol Today 9 (1993) 323-328
    • (1993) Parasitol Today , vol.9 , pp. 323-328
    • Olliaro, P.L.1    Bryceson, A.2
  • 7
    • 0030940539 scopus 로고    scopus 로고
    • Human leishmaniasis: clinical, diagnostic, and chemotherapeutic developments in the last 10 years
    • Berman J.D. Human leishmaniasis: clinical, diagnostic, and chemotherapeutic developments in the last 10 years. Clin Infect Dis 24 4 (1997) 684-703
    • (1997) Clin Infect Dis , vol.24 , Issue.4 , pp. 684-703
    • Berman, J.D.1
  • 8
    • 0028822932 scopus 로고
    • New mechanisms of drug resistance in parasitic protozoa
    • Borst P., and Ouellette M. New mechanisms of drug resistance in parasitic protozoa. Annu Rev Microbiol 49 (1995) 427-460
    • (1995) Annu Rev Microbiol , vol.49 , pp. 427-460
    • Borst, P.1    Ouellette, M.2
  • 9
    • 0026769377 scopus 로고
    • Drug resistance in leishmaniasis: its implication in systemic chemotherapy of cutaneous and mucocutaneous disease
    • Grogl M., Thomason T.N., and Franke E.D. Drug resistance in leishmaniasis: its implication in systemic chemotherapy of cutaneous and mucocutaneous disease. Am J Trop Med Hyg 47 1 (1992) 117-126
    • (1992) Am J Trop Med Hyg , vol.47 , Issue.1 , pp. 117-126
    • Grogl, M.1    Thomason, T.N.2    Franke, E.D.3
  • 10
    • 0030009650 scopus 로고    scopus 로고
    • Pentamidine uptake in Leishmania donovani and Leishmania amazonensis promastigotes and axenic amastigotes
    • Pt2
    • Pt2. Basselin M., Lawrence F., and Robert-Gero M. Pentamidine uptake in Leishmania donovani and Leishmania amazonensis promastigotes and axenic amastigotes. Biochem J 315 (1996) 631-634
    • (1996) Biochem J , vol.315 , pp. 631-634
    • Basselin, M.1    Lawrence, F.2    Robert-Gero, M.3
  • 11
    • 0031105745 scopus 로고    scopus 로고
    • Effects of pentamidine on polyamine level and biosynthesis in wild-type, pentamidine-treated, and pentamidine-resistant Leishmania
    • Basselin M., Badet-Denisot M.A., Lawrence F., and Robert-Gero M. Effects of pentamidine on polyamine level and biosynthesis in wild-type, pentamidine-treated, and pentamidine-resistant Leishmania. Exp Parasitol 85 3 (1997) 274-282
    • (1997) Exp Parasitol , vol.85 , Issue.3 , pp. 274-282
    • Basselin, M.1    Badet-Denisot, M.A.2    Lawrence, F.3    Robert-Gero, M.4
  • 12
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb A.H., and Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 46 (1992) 695-729
    • (1992) Annu Rev Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 13
    • 0028072555 scopus 로고
    • Amphotericin versus sodium stibogluconate in first-line treatment of Indian Kala-azar
    • Mishra M., Biswas U.K., Jha A.M., and Khan A.B. Amphotericin versus sodium stibogluconate in first-line treatment of Indian Kala-azar. Lancet 344 8937 (1994) 1599-1600
    • (1994) Lancet , vol.344 , Issue.8937 , pp. 1599-1600
    • Mishra, M.1    Biswas, U.K.2    Jha, A.M.3    Khan, A.B.4
  • 14
    • 0024004690 scopus 로고
    • Chemotherapy for leishmaniasis: biochemical mechanisms, clinical efficacy, and future strategies
    • Berman J.D. Chemotherapy for leishmaniasis: biochemical mechanisms, clinical efficacy, and future strategies. Rev Infect Dis 10 3 (1988) 560-586
    • (1988) Rev Infect Dis , vol.10 , Issue.3 , pp. 560-586
    • Berman, J.D.1
  • 15
    • 0029064954 scopus 로고
    • Ribosomes of Leishmania are a target for the aminoglycosides
    • Maarouf M., Lawrence F., Croft S.L., and Robert-Gero M. Ribosomes of Leishmania are a target for the aminoglycosides. Parasitol Res 81 5 (1995) 421-425
    • (1995) Parasitol Res , vol.81 , Issue.5 , pp. 421-425
    • Maarouf, M.1    Lawrence, F.2    Croft, S.L.3    Robert-Gero, M.4
  • 16
    • 0031149815 scopus 로고    scopus 로고
    • In vivo interference of paromomycin with mitochondrial activity of Leishmania
    • Maarouf M., de Kouchkovsky Y., Brown S., et al. In vivo interference of paromomycin with mitochondrial activity of Leishmania. Exp Cell Res 232 2 (1997) 339-348
    • (1997) Exp Cell Res , vol.232 , Issue.2 , pp. 339-348
    • Maarouf, M.1    de Kouchkovsky, Y.2    Brown, S.3
  • 17
    • 0031939452 scopus 로고    scopus 로고
    • Topical paromomycin/methylbenzethonium chloride plus parenteral meglumine antimonate as treatment for American cutaneous leishmaniasis: controlled study
    • Soto J., Fuya P., Herrera R., and Berman J. Topical paromomycin/methylbenzethonium chloride plus parenteral meglumine antimonate as treatment for American cutaneous leishmaniasis: controlled study. Clin Infect Dis 26 1 (1998) 56-58
    • (1998) Clin Infect Dis , vol.26 , Issue.1 , pp. 56-58
    • Soto, J.1    Fuya, P.2    Herrera, R.3    Berman, J.4
  • 18
    • 0031080430 scopus 로고    scopus 로고
    • Molecular and biochemical studies on the hypoxanthine-guanine phosphoribosyltransferases of the pathogenic haemoflagellates
    • Ullman B., and Carter D. Molecular and biochemical studies on the hypoxanthine-guanine phosphoribosyltransferases of the pathogenic haemoflagellates. Int J Parasitol 27 2 (1997) 203-213
    • (1997) Int J Parasitol , vol.27 , Issue.2 , pp. 203-213
    • Ullman, B.1    Carter, D.2
  • 19
    • 0027172259 scopus 로고
    • Scott P.T-cell and cytokine responses in leishmaniasis
    • Reed S.G. Scott P.T-cell and cytokine responses in leishmaniasis. Curr Opin Immunol 5 4 (1993) 524-531
    • (1993) Curr Opin Immunol , vol.5 , Issue.4 , pp. 524-531
    • Reed, S.G.1
  • 20
    • 0029451961 scopus 로고
    • The development of effector T cell subsets in murine Leishmania major infection
    • discussion
    • discussion. Locksley R.M., Wakil A.E., Corry D.B., et al. The development of effector T cell subsets in murine Leishmania major infection. Ciba Found Symp 195 (1995) 110-117
    • (1995) Ciba Found Symp , vol.195 , pp. 110-117
    • Locksley, R.M.1    Wakil, A.E.2    Corry, D.B.3
  • 21
    • 0029451961 scopus 로고
    • The development of effector T cell subsets in murine Leishmania major infection
    • Locksley R.M., Wakil A.E., Corry D.B., et al. The development of effector T cell subsets in murine Leishmania major infection. Ciba Found Symp 195 (1995) 117-122
    • (1995) Ciba Found Symp , vol.195 , pp. 117-122
    • Locksley, R.M.1    Wakil, A.E.2    Corry, D.B.3
  • 22
    • 0025139949 scopus 로고
    • Treatment of visceral leishmaniasis with pentavalent antimony and interferon gamma [see comments]
    • Badaro R., Falcoff E., Badaro F.S., et al. Treatment of visceral leishmaniasis with pentavalent antimony and interferon gamma [see comments]. N Engl J Med 322 1 (1990) 16-21
    • (1990) N Engl J Med , vol.322 , Issue.1 , pp. 16-21
    • Badaro, R.1    Falcoff, E.2    Badaro, F.S.3
  • 23
    • 0028844536 scopus 로고
    • Effect of treatment with interferon-gamma alone in visceral leishmaniasis
    • Sundar S., and Murray H.W. Effect of treatment with interferon-gamma alone in visceral leishmaniasis. J Infect Dis 172 6 (1995) 1627-1629
    • (1995) J Infect Dis , vol.172 , Issue.6 , pp. 1627-1629
    • Sundar, S.1    Murray, H.W.2
  • 24
    • 0025678398 scopus 로고
    • Quantitative in vitro drug potency and drug susceptibility evaluation of Leishmania spp. from patients unresponsive to pentavalent antimony therapy
    • Jackson J.E., Tally J.D., Ellis W.Y., et al. Quantitative in vitro drug potency and drug susceptibility evaluation of Leishmania spp. from patients unresponsive to pentavalent antimony therapy. Am J Trop Med Hyg 43 5 (1990) 464-480
    • (1990) Am J Trop Med Hyg , vol.43 , Issue.5 , pp. 464-480
    • Jackson, J.E.1    Tally, J.D.2    Ellis, W.Y.3
  • 25
    • 0029841913 scopus 로고    scopus 로고
    • Trypanothione overproduction and resistance to antimonials and arsenicals in Leishmania
    • Mukhopadhyay R., Dey S., Xu N., et al. Trypanothione overproduction and resistance to antimonials and arsenicals in Leishmania. Proc Natl Acad Sci U S A 93 19 (1996) 10383-10387
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.19 , pp. 10383-10387
    • Mukhopadhyay, R.1    Dey, S.2    Xu, N.3
  • 26
    • 0030924243 scopus 로고    scopus 로고
    • Co-amplification of the gamma-glutamylcysteine synthetase gene gshl/it and of the ABC transporter gene pgpA in arsenite-resistant Leishmania tarentolae
    • Grondin K., Haimeur A., Mukhopadhyay R., et al. Co-amplification of the gamma-glutamylcysteine synthetase gene gshl/it and of the ABC transporter gene pgpA in arsenite-resistant Leishmania tarentolae. Embo J 16 11 (1997) 3057-3065
    • (1997) Embo J , vol.16 , Issue.11 , pp. 3057-3065
    • Grondin, K.1    Haimeur, A.2    Mukhopadhyay, R.3
  • 27
    • 0031282335 scopus 로고    scopus 로고
    • Efflux systems and increased trypanothione levels in arsenite-resistant Leishmania
    • Legare D., Papadopoulou B., Roy G., et al. Efflux systems and increased trypanothione levels in arsenite-resistant Leishmania. Exp Parasitol 87 3 (1997) 275-282
    • (1997) Exp Parasitol , vol.87 , Issue.3 , pp. 275-282
    • Legare, D.1    Papadopoulou, B.2    Roy, G.3
  • 28
    • 0002328486 scopus 로고    scopus 로고
    • ABC transporters in Leishmania and their role in drug resistance
    • Ouellette M., Légaré D., Haimeur A., et al. ABC transporters in Leishmania and their role in drug resistance. Drug Res. Updates 1 (1998) 43-48
    • (1998) Drug Res. Updates , vol.1 , pp. 43-48
    • Ouellette, M.1    Légaré, D.2    Haimeur, A.3
  • 29
    • 0031861799 scopus 로고    scopus 로고
    • Gene amplification in Leishmania tarentolae selected for resistance to sodium stibogluconate
    • in press
    • in press. Haimeur A., and Ouellette M. Gene amplification in Leishmania tarentolae selected for resistance to sodium stibogluconate. Antimicrob. Agents Chemother. (1998)
    • (1998) Antimicrob. Agents Chemother.
    • Haimeur, A.1    Ouellette, M.2
  • 30
    • 0029554288 scopus 로고
    • Resistance mechanisms to arsenicals and antimonials
    • Rosen B.P. Resistance mechanisms to arsenicals and antimonials. J Basic Clin Physiol Pharmacol 6 3-4 (1995) 251-263
    • (1995) J Basic Clin Physiol Pharmacol , vol.6 , Issue.3-4 , pp. 251-263
    • Rosen, B.P.1
  • 31
    • 0027500261 scopus 로고
    • Arsenical-resistant trypanosomes lack an unusual adenosine transporter [published erratum appears in Nature 1993 Jan 28; 361 (6410): 374]
    • Carter N.S., and Fairlamb A.H. Arsenical-resistant trypanosomes lack an unusual adenosine transporter [published erratum appears in Nature 1993 Jan 28; 361 (6410): 374]. Nature 361 6408 (1993) 173-176
    • (1993) Nature , vol.361 , Issue.6408 , pp. 173-176
    • Carter, N.S.1    Fairlamb, A.H.2
  • 32
    • 77949778073 scopus 로고    scopus 로고
    • (Yu VL, ed. Antimicrobial Chemotherapy; vol in press), Williams and Wilkins
    • (Yu VL, ed. Antimicrobial Chemotherapy; vol in press). Ouellette M., and Pépin J. Pentamidine (1998), Williams and Wilkins
    • (1998) Pentamidine
    • Ouellette, M.1    Pépin, J.2
  • 33
    • 0030603960 scopus 로고    scopus 로고
    • Effects of cationic diamidines on polyamine content and uptake on Leishmania infantum in in vitro cultures
    • Calonge M., Johnson R., Balana-Fouce R., and Ordonez D. Effects of cationic diamidines on polyamine content and uptake on Leishmania infantum in in vitro cultures. Biochem Pharmacol 52 6 (1996) 835-841
    • (1996) Biochem Pharmacol , vol.52 , Issue.6 , pp. 835-841
    • Calonge, M.1    Johnson, R.2    Balana-Fouce, R.3    Ordonez, D.4
  • 34
    • 0030953686 scopus 로고    scopus 로고
    • Altered transport properties of pentamidine-resistant Leishmania donovani and L. amazonensis promastigotes
    • Basselin M., Lawrence F., and Robert-Gero M. Altered transport properties of pentamidine-resistant Leishmania donovani and L. amazonensis promastigotes. Parasitol Res 83 5 (1997) 413-418
    • (1997) Parasitol Res , vol.83 , Issue.5 , pp. 413-418
    • Basselin, M.1    Lawrence, F.2    Robert-Gero, M.3
  • 35
    • 0022454288 scopus 로고
    • Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone)
    • Bitonti A.J., Dumont J.A., and McCann P.P. Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone). Biochem J 237 3 (1986) 685-689
    • (1986) Biochem J , vol.237 , Issue.3 , pp. 685-689
    • Bitonti, A.J.1    Dumont, J.A.2    McCann, P.P.3
  • 36
    • 0027436769 scopus 로고
    • Polyamine and pentamidine metabolism in African trypanosomes
    • Berger B.J., Carter N.S., and Fairlamb A.H. Polyamine and pentamidine metabolism in African trypanosomes. Acta Trop 54 3-4 (1993) 215-224
    • (1993) Acta Trop , vol.54 , Issue.3-4 , pp. 215-224
    • Berger, B.J.1    Carter, N.S.2    Fairlamb, A.H.3
  • 37
    • 0030902239 scopus 로고    scopus 로고
    • Axenically cultured amastigote forms as an in vitro model for investigation of antileishmanial agents
    • Sereno D., and Lemesre J.L. Axenically cultured amastigote forms as an in vitro model for investigation of antileishmanial agents. Antimicrob Agents Chemother 41 5 (1997) 972-976
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.5 , pp. 972-976
    • Sereno, D.1    Lemesre, J.L.2
  • 38
    • 25444520813 scopus 로고    scopus 로고
    • Alterations in membrane fluidity, lipid metabolism, mitochondrial activity, and lipophosphoglycan expression in pentamidine-resistant Leishmania
    • Basselin M., and Robert-Gero M. Alterations in membrane fluidity, lipid metabolism, mitochondrial activity, and lipophosphoglycan expression in pentamidine-resistant Leishmania. Parasitol Res 84 1 (1998) 78-83
    • (1998) Parasitol Res , vol.84 , Issue.1 , pp. 78-83
    • Basselin, M.1    Robert-Gero, M.2
  • 39
    • 0029898712 scopus 로고    scopus 로고
    • Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes
    • Pt 2
    • Pt 2. Le Quesne S.A., and Fairlamb A.H. Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes. Biochem J 316 (1996) 481-486
    • (1996) Biochem J , vol.316 , pp. 481-486
    • Le Quesne, S.A.1    Fairlamb, A.H.2
  • 40
    • 0027437962 scopus 로고
    • Effects of antagonists of polyamine metabolism on African trypanosomes
    • Bacchi C.J., and Yarlett N. Effects of antagonists of polyamine metabolism on African trypanosomes. Acta Trop 54 3-4 (1993) 225-236
    • (1993) Acta Trop , vol.54 , Issue.3-4 , pp. 225-236
    • Bacchi, C.J.1    Yarlett, N.2
  • 41
    • 0028875686 scopus 로고
    • Uptake of diamidine drugs by the P2 nucleoside transporter in melarsen- sensitive and - resistant Trypanosoma bruceibrucei
    • Carter N.S., Berger B.J., and Fairlamb A.H. Uptake of diamidine drugs by the P2 nucleoside transporter in melarsen- sensitive and - resistant Trypanosoma bruceibrucei. J Biol Chem 270 47 (1995) 28153-28157
    • (1995) J Biol Chem , vol.270 , Issue.47 , pp. 28153-28157
    • Carter, N.S.1    Berger, B.J.2    Fairlamb, A.H.3
  • 42
    • 0028909819 scopus 로고
    • Characterisation of pentamidine-resistant Trypanosoma brucei brucei
    • Berger B.J., Carter N.S., and Fairlamb A.H. Characterisation of pentamidine-resistant Trypanosoma brucei brucei. Mol Biochem Parasitol 69 2 (1995) 289-298
    • (1995) Mol Biochem Parasitol , vol.69 , Issue.2 , pp. 289-298
    • Berger, B.J.1    Carter, N.S.2    Fairlamb, A.H.3
  • 44
    • 0026734403 scopus 로고
    • Characterisation of melarsen-resistant Trypanosoma brucei brucei with respect to cross-resistance to other drugs and trypanothione metabolism
    • Fairlamb A.H., Carter N.S., Cunningham M., and Smith K. Characterisation of melarsen-resistant Trypanosoma brucei brucei with respect to cross-resistance to other drugs and trypanothione metabolism. Mol Biochem Parasitol 53 1-2 (1992) 213-222
    • (1992) Mol Biochem Parasitol , vol.53 , Issue.1-2 , pp. 213-222
    • Fairlamb, A.H.1    Carter, N.S.2    Cunningham, M.3    Smith, K.4
  • 45
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann P.P., and Pegg A.E. Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Ther 54 2 (1992) 195-215
    • (1992) Pharmacol Ther , vol.54 , Issue.2 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 46
    • 77949868030 scopus 로고    scopus 로고
    • (Yu VL, ed. Antimicrobial Chemotherapy; vol in press), Williams and Wilkins, New York
    • (Yu VL, ed. Antimicrobial Chemotherapy; vol in press). Ouellette M., and Pépin J. Eflornithine (1998), Williams and Wilkins, New York
    • (1998) Eflornithine
    • Ouellette, M.1    Pépin, J.2
  • 47
    • 0022439474 scopus 로고
    • Adenine phosphoribosyltransferase-deficient Leishmania donovani
    • Pt B
    • Pt B. Kaur K., Iovannisci D.M., and Ullman B. Adenine phosphoribosyltransferase-deficient Leishmania donovani. Adv Exp Med Biol 195 (1986) 553-557
    • (1986) Adv Exp Med Biol , vol.195 , pp. 553-557
    • Kaur, K.1    Iovannisci, D.M.2    Ullman, B.3
  • 48
    • 0023433861 scopus 로고
    • Plasmodium falciparum and Plasmodium berghei: effects of ornithine decarboxylase inhibitors on erythrocytic schizogony
    • Bitonti A.J., McCann P.P., and Sjoerdsma A. Plasmodium falciparum and Plasmodium berghei: effects of ornithine decarboxylase inhibitors on erythrocytic schizogony. Exp Parasitol 64 2 (1987) 237-243
    • (1987) Exp Parasitol , vol.64 , Issue.2 , pp. 237-243
    • Bitonti, A.J.1    McCann, P.P.2    Sjoerdsma, A.3
  • 49
    • 0028344420 scopus 로고
    • Effect of antioxidants on the growth and polyamine levels of Leishmania donovani
    • Mukhopadhyay R., and Madhubala R. Effect of antioxidants on the growth and polyamine levels of Leishmania donovani. Biochem Pharmacol 47 4 (1994) 611-615
    • (1994) Biochem Pharmacol , vol.47 , Issue.4 , pp. 611-615
    • Mukhopadhyay, R.1    Madhubala, R.2
  • 50
    • 77949821080 scopus 로고    scopus 로고
    • Polyamine metabolism in Trypanosomes
    • Hide G., Mottram J.C., Coombs G.H., and Ph H. (Eds)
    • Fairlamb A.H., and Sa L.Q. Polyamine metabolism in Trypanosomes. In: Hide G., Mottram J.C., Coombs G.H., and Ph H. (Eds). CAB International (1997)
    • (1997) CAB International
    • Fairlamb, A.H.1    Sa, L.Q.2
  • 51
    • 0029894593 scopus 로고    scopus 로고
    • Procyclic Trypanosoma brucei cell lines deficient in ornithine decarboxylase activity
    • Li F., Hua S.B., Wang C.C., and Gottesdiener K.M. Procyclic Trypanosoma brucei cell lines deficient in ornithine decarboxylase activity. Mol Biochem Parasitol 78 1-2 (1996) 227-236
    • (1996) Mol Biochem Parasitol , vol.78 , Issue.1-2 , pp. 227-236
    • Li, F.1    Hua, S.B.2    Wang, C.C.3    Gottesdiener, K.M.4
  • 52
    • 0030824384 scopus 로고    scopus 로고
    • Alterations in ornithine decarboxylase characteristics account for tolerance of Trypanosoma brucei rhodesiense to D,L- alpha-difluoromethylornithine
    • Iten M., Mett H., Evans A., et al. Alterations in ornithine decarboxylase characteristics account for tolerance of Trypanosoma brucei rhodesiense to D,L- alpha-difluoromethylornithine. Antimicrob Agents Chemother 41 9 (1997) 1922-1925
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.9 , pp. 1922-1925
    • Iten, M.1    Mett, H.2    Evans, A.3
  • 53
    • 0025138660 scopus 로고
    • Alpha-difluoromethylornithine resistance in Leishmania donovani is associated with increased ornithine decarboxylase activity
    • Coons T., Hanson S., Bitonti A.J., et al. Alpha-difluoromethylornithine resistance in Leishmania donovani is associated with increased ornithine decarboxylase activity. Mol Biochem Parasitol 39 1 (1990) 77-89
    • (1990) Mol Biochem Parasitol , vol.39 , Issue.1 , pp. 77-89
    • Coons, T.1    Hanson, S.2    Bitonti, A.J.3
  • 54
    • 0030184887 scopus 로고    scopus 로고
    • Characterization of alpha-difluoromethylornithine resistant Leishmania donovani and its susceptibility to other inhibitors of the polyamine biosynthetic pathway
    • Mukhopadhyay R., Kapoor P., and Madhubala R. Characterization of alpha-difluoromethylornithine resistant Leishmania donovani and its susceptibility to other inhibitors of the polyamine biosynthetic pathway. Pharmacol Res 34 1-2 (1996) 43-46
    • (1996) Pharmacol Res , vol.34 , Issue.1-2 , pp. 43-46
    • Mukhopadhyay, R.1    Kapoor, P.2    Madhubala, R.3
  • 55
    • 0026453347 scopus 로고
    • Unstable amplification of two extrachromosomal elements in alpha-difluoromethylornithine-resistant Leishmania donovani
    • Hanson S., Beverley S.M., Wagner W., and Ullman B. Unstable amplification of two extrachromosomal elements in alpha-difluoromethylornithine-resistant Leishmania donovani. Mol Cell Biol 12 12 (1992) 5499-5507
    • (1992) Mol Cell Biol , vol.12 , Issue.12 , pp. 5499-5507
    • Hanson, S.1    Beverley, S.M.2    Wagner, W.3    Ullman, B.4
  • 56
    • 0030754481 scopus 로고    scopus 로고
    • Alpha-difluoromethylornithine-resistant cell lines obtained after one- step selection of Leishmania mexicana promastigote cultures
    • Pt 3
    • Pt 3. Sanchez C.P., Mucci J., Gonzalez N.S., et al. Alpha-difluoromethylornithine-resistant cell lines obtained after one- step selection of Leishmania mexicana promastigote cultures. Biochem J 324 (1997) 847-853
    • (1997) Biochem J , vol.324 , pp. 847-853
    • Sanchez, C.P.1    Mucci, J.2    Gonzalez, N.S.3
  • 57
    • 0023219692 scopus 로고
    • Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei. Implications for enzyme turnover and selective difluoromethylornithine inhibition
    • Phillips M.A., Coffino P., and Wang C.C. Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei. Implications for enzyme turnover and selective difluoromethylornithine inhibition. J Biol Chem 262 18 (1987) 8721-8727
    • (1987) J Biol Chem , vol.262 , Issue.18 , pp. 8721-8727
    • Phillips, M.A.1    Coffino, P.2    Wang, C.C.3
  • 58
    • 0023431045 scopus 로고
    • Biochemical changes associated with alpha-difluoromethylornithine uptake and resistance in Trypanosoma brucei
    • Bellofatto V., Fairlamb A.H., Henderson G.B., and Cross G.A. Biochemical changes associated with alpha-difluoromethylornithine uptake and resistance in Trypanosoma brucei. Mol Biochem Parasitol 25 3 (1987) 227-238
    • (1987) Mol Biochem Parasitol , vol.25 , Issue.3 , pp. 227-238
    • Bellofatto, V.1    Fairlamb, A.H.2    Henderson, G.B.3    Cross, G.A.4
  • 59
    • 0022992801 scopus 로고
    • Effects of ketoconazole on sterol biosynthesis by Leishmania mexicana mexicana amastigotes in murine macrophage tumor cells
    • Berman J.D., Goad L.J., Beach D.H., and Holz Jr. G.G. Effects of ketoconazole on sterol biosynthesis by Leishmania mexicana mexicana amastigotes in murine macrophage tumor cells. Mol Biochem Parasitol 20 1 (1986) 85-92
    • (1986) Mol Biochem Parasitol , vol.20 , Issue.1 , pp. 85-92
    • Berman, J.D.1    Goad, L.J.2    Beach, D.H.3    Holz Jr., G.G.4
  • 60
    • 0024507364 scopus 로고
    • Perturbation of sterol biosynthesis by itraconazole and ketoconazole in Leishmania mexicana mexicana infected macrophages
    • Hart D.T., Lauwers W.J., Willemsens G., et al. Perturbation of sterol biosynthesis by itraconazole and ketoconazole in Leishmania mexicana mexicana infected macrophages. Mol Biochem Parasitol 33 2 (1989) 123-134
    • (1989) Mol Biochem Parasitol , vol.33 , Issue.2 , pp. 123-134
    • Hart, D.T.1    Lauwers, W.J.2    Willemsens, G.3
  • 61
    • 0022482179 scopus 로고
    • Amphotericin B-induced oxidative damage and killing of Candida albicans
    • Sokol-Anderson M.L., Brajtburg J., and Medoff G. Amphotericin B-induced oxidative damage and killing of Candida albicans. J Infect Dis 154 1 (1986) 76-83
    • (1986) J Infect Dis , vol.154 , Issue.1 , pp. 76-83
    • Sokol-Anderson, M.L.1    Brajtburg, J.2    Medoff, G.3
  • 62
    • 0023867621 scopus 로고
    • Influence of amphotericin B on the transport of phosphate, sulphate and potassium ions across the human erythrocyte membrane
    • Abu-Salah K.M., Sedrani S.H., Tobia A.S., and Gambo H.A. Influence of amphotericin B on the transport of phosphate, sulphate and potassium ions across the human erythrocyte membrane. Acta Haematol 79 2 (1988) 77-80
    • (1988) Acta Haematol , vol.79 , Issue.2 , pp. 77-80
    • Abu-Salah, K.M.1    Sedrani, S.H.2    Tobia, A.S.3    Gambo, H.A.4
  • 63
    • 0024205042 scopus 로고
    • The polyene antibiotic amphotericin B inhibits the Na+/K+ pump of human erythrocytes
    • Vertut-Doi A., Hannaert P., and Bolard J. The polyene antibiotic amphotericin B inhibits the Na+/K+ pump of human erythrocytes. Biochem Biophys Res Commun 157 2 (1988) 692-697
    • (1988) Biochem Biophys Res Commun , vol.157 , Issue.2 , pp. 692-697
    • Vertut-Doi, A.1    Hannaert, P.2    Bolard, J.3
  • 64
    • 0030065722 scopus 로고    scopus 로고
    • Binding and uptake of liposomes containing a poly(ethylene glycol) derivative of cholesterol (stealth liposomes) by the macrophage cell line J774: influence of PEG content and its molecular weight
    • Vertut-Doi A., Ishiwata H., and Miyajima K. Binding and uptake of liposomes containing a poly(ethylene glycol) derivative of cholesterol (stealth liposomes) by the macrophage cell line J774: influence of PEG content and its molecular weight. Biochim Biophys Acta 1278 1 (1996) 19-28
    • (1996) Biochim Biophys Acta , vol.1278 , Issue.1 , pp. 19-28
    • Vertut-Doi, A.1    Ishiwata, H.2    Miyajima, K.3
  • 65
    • 0029008058 scopus 로고
    • Treatment of kala-azar in Brazil with Amphocil (amphotericin B cholesterol dispersion) for 5 days
    • Dietze R., Fagundes S.M., Brito E.F., et al. Treatment of kala-azar in Brazil with Amphocil (amphotericin B cholesterol dispersion) for 5 days. Trans R Soc Trop Med Hyg 89 3 (1995) 309-311
    • (1995) Trans R Soc Trop Med Hyg , vol.89 , Issue.3 , pp. 309-311
    • Dietze, R.1    Fagundes, S.M.2    Brito, E.F.3
  • 66
    • 0030006792 scopus 로고    scopus 로고
    • Comparison of three treatment regimens with liposomal amphotericin B (AmBisome) for visceral leishmaniasis in India: a randomized dose-finding study
    • Thakur C.P., Pandey A.K., Sinha G.P., et al. Comparison of three treatment regimens with liposomal amphotericin B (AmBisome) for visceral leishmaniasis in India: a randomized dose-finding study. Trans R Soc Trop Med Hyg 90 3 (1996) 319-322
    • (1996) Trans R Soc Trop Med Hyg , vol.90 , Issue.3 , pp. 319-322
    • Thakur, C.P.1    Pandey, A.K.2    Sinha, G.P.3
  • 67
  • 68
    • 0031035553 scopus 로고    scopus 로고
    • Isolation and characterization of fluconazole- and amphotericin B- resistant Candida albicans from blood of two patients with leukemia
    • Nolte F.S., Parkinson T., Falconer D.J., et al. Isolation and characterization of fluconazole- and amphotericin B- resistant Candida albicans from blood of two patients with leukemia. Antimicrob Agents Chemother 41 1 (1997) 196-199
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.1 , pp. 196-199
    • Nolte, F.S.1    Parkinson, T.2    Falconer, D.J.3
  • 69
    • 0026000270 scopus 로고
    • Amphotericin B: an introduction
    • Warnock D.W. Amphotericin B: an introduction. J Antimicrob Chemother 28 Suppl B (1991) 27-38
    • (1991) J Antimicrob Chemother , vol.28 , Issue.SUPPL. B , pp. 27-38
    • Warnock, D.W.1
  • 71
    • 0028793725 scopus 로고
    • Mechanisms of resistance to azole antifungal agents in Candida albicans isolates from AIDS patients involve specific multidrug transporters
    • Sanglard D., Kuchler K., Ischer F., et al. Mechanisms of resistance to azole antifungal agents in Candida albicans isolates from AIDS patients involve specific multidrug transporters. Antimicrob Agents Chemother 39 11 (1995) 2378-2386
    • (1995) Antimicrob Agents Chemother , vol.39 , Issue.11 , pp. 2378-2386
    • Sanglard, D.1    Kuchler, K.2    Ischer, F.3
  • 73
    • 0025788737 scopus 로고
    • Antifungal therapy and the new azole compounds
    • Hay R.J. Antifungal therapy and the new azole compounds. J Antimicrob Chemother 28 Suppl A (1991) 35-46
    • (1991) J Antimicrob Chemother , vol.28 , Issue.SUPPL. A , pp. 35-46
    • Hay, R.J.1
  • 74
    • 0030921232 scopus 로고    scopus 로고
    • Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites
    • Suppl
    • Suppl. Urbina J.A. Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites. Parasitology 114 (1997) S91-S99
    • (1997) Parasitology , vol.114
    • Urbina, J.A.1
  • 75
    • 0023765496 scopus 로고
    • Effects of antimycotic azoles on growth and sterol biosynthesis of Leishmania promastigotes
    • Beach D.H., Goad L.J., and Holz Jr. G.G. Effects of antimycotic azoles on growth and sterol biosynthesis of Leishmania promastigotes. Mol Biochem Parasitol 31 2 (1988) 149-162
    • (1988) Mol Biochem Parasitol , vol.31 , Issue.2 , pp. 149-162
    • Beach, D.H.1    Goad, L.J.2    Holz Jr., G.G.3
  • 76
    • 0029844998 scopus 로고    scopus 로고
    • Naturally azole-resistant Leishmania braziliensis promastigotes are rendered susceptible in the presence of terbinafine: comparative study with azole-susceptible Leishmania mexicana promastigotes [published erratum appears in Antimicrob Agents Chemother 1997 Feb; 41 (2): 496]
    • Rangel H., Dagger F., Hernandez A., et al. Naturally azole-resistant Leishmania braziliensis promastigotes are rendered susceptible in the presence of terbinafine: comparative study with azole-susceptible Leishmania mexicana promastigotes [published erratum appears in Antimicrob Agents Chemother 1997 Feb; 41 (2): 496]. Antimicrob Agents Chemother 40 12 (1996) 2785-2791
    • (1996) Antimicrob Agents Chemother , vol.40 , Issue.12 , pp. 2785-2791
    • Rangel, H.1    Dagger, F.2    Hernandez, A.3
  • 77
    • 0030757227 scopus 로고    scopus 로고
    • Increased mRNA levels of ERG16, CDR, and MDRI correlate with increases in azole resistance in Candida albicans isolates from a patient infected with human immunodeficiency virus
    • White T.C. Increased mRNA levels of ERG16, CDR, and MDRI correlate with increases in azole resistance in Candida albicans isolates from a patient infected with human immunodeficiency virus. Antimicrob Agents Chemother 41 7 (1997) 1482-1487
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.7 , pp. 1482-1487
    • White, T.C.1
  • 78
    • 0030792602 scopus 로고    scopus 로고
    • The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14alpha demethylase in Candida albicans
    • White T.C. The presence of an R467K amino acid substitution and loss of allelic variation correlate with an azole-resistant lanosterol 14alpha demethylase in Candida albicans. Antimicrob Agents Chemother 41 7 (1997) 1488-1494
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.7 , pp. 1488-1494
    • White, T.C.1
  • 79
    • 0031938057 scopus 로고    scopus 로고
    • Amino acid substitutions in the cytochrome P-450 lanosterol 14alpha- demethylase (CYP51A1) from azole-resistant Candida albicans clinical isolates contribute to resistance to azole antifungal agents [In Process Citation]
    • Sanglard D., Ischer F., Koymans L., and Bille J. Amino acid substitutions in the cytochrome P-450 lanosterol 14alpha- demethylase (CYP51A1) from azole-resistant Candida albicans clinical isolates contribute to resistance to azole antifungal agents [In Process Citation]. Antimicrob Agents Chemother 42 2 (1998) 241-253
    • (1998) Antimicrob Agents Chemother , vol.42 , Issue.2 , pp. 241-253
    • Sanglard, D.1    Ischer, F.2    Koymans, L.3    Bille, J.4
  • 80
    • 0027948398 scopus 로고
    • Molecular mechanisms of drug resistance in fungi
    • Vanden Bossche H., Marichal P., and Odds F.C. Molecular mechanisms of drug resistance in fungi. Trends Microbiol 2 10 (1994) 393-400
    • (1994) Trends Microbiol , vol.2 , Issue.10 , pp. 393-400
    • Vanden Bossche, H.1    Marichal, P.2    Odds, F.C.3
  • 81
    • 0028300587 scopus 로고
    • Effect of ketoconazole on lethal action of amphotericin B on Leishmania mexicana promastigotes
    • Ramos H., Saint-Pierre-Chazalet M., Bolard J., and Cohen B.E. Effect of ketoconazole on lethal action of amphotericin B on Leishmania mexicana promastigotes. Antimicrob Agents Chemother 38 5 (1994) 1079-10784
    • (1994) Antimicrob Agents Chemother , vol.38 , Issue.5 , pp. 1079-10784
    • Ramos, H.1    Saint-Pierre-Chazalet, M.2    Bolard, J.3    Cohen, B.E.4
  • 82
    • 0026076280 scopus 로고
    • Purine analogs as chemotherapeutic agents in leishmaniasis and American trypanosomiasis
    • Marr J.J. Purine analogs as chemotherapeutic agents in leishmaniasis and American trypanosomiasis. J Lab Clin Med 118 2 (1991) 111-119
    • (1991) J Lab Clin Med , vol.118 , Issue.2 , pp. 111-119
    • Marr, J.J.1
  • 83
    • 0031049914 scopus 로고    scopus 로고
    • Inefficacy of allopurinol as monotherapy for Colombian cutaneous leishmaniasis. A randomized, controlled trial
    • Velez I., Agudelo S., Hendrickx E., et al. Inefficacy of allopurinol as monotherapy for Colombian cutaneous leishmaniasis. A randomized, controlled trial. Ann Intern Med 126 3 (1997) 232-236
    • (1997) Ann Intern Med , vol.126 , Issue.3 , pp. 232-236
    • Velez, I.1    Agudelo, S.2    Hendrickx, E.3
  • 84
    • 0030803896 scopus 로고    scopus 로고
    • Genetic analysis of purine metabolism in Leishmania donovani
    • Hwang H.Y., and Ullman B. Genetic analysis of purine metabolism in Leishmania donovani. J Biol Chem 272 31 (1997) 19488-194896
    • (1997) J Biol Chem , vol.272 , Issue.31 , pp. 19488-194896
    • Hwang, H.Y.1    Ullman, B.2
  • 85
    • 0028046723 scopus 로고
    • Toxoplasma gondii: characterization of a mutant resistant to 6-thioxanthine
    • Pfefferkorn E.R., and Borotz S.E. Toxoplasma gondii: characterization of a mutant resistant to 6-thioxanthine. Exp Parasitol 79 3 (1994) 374-382
    • (1994) Exp Parasitol , vol.79 , Issue.3 , pp. 374-382
    • Pfefferkorn, E.R.1    Borotz, S.E.2
  • 86
    • 0021129833 scopus 로고
    • Genetic analysis of nucleoside transport in Leishmania donovani
    • Iovannisci D.M., Kaur K., Young L., and Ullman B. Genetic analysis of nucleoside transport in Leishmania donovani. Mol Cell Biol 4 6 (1984) 1013-1019
    • (1984) Mol Cell Biol , vol.4 , Issue.6 , pp. 1013-1019
    • Iovannisci, D.M.1    Kaur, K.2    Young, L.3    Ullman, B.4
  • 87
    • 0021245052 scopus 로고
    • Formycin B resistance in Leishmania
    • Rainey P., and Santi D.V. Formycin B resistance in Leishmania. Biochem Pharmacol 33 8 (1984) 1374-1374
    • (1984) Biochem Pharmacol , vol.33 , Issue.8 , pp. 1374-1374
    • Rainey, P.1    Santi, D.V.2
  • 88
    • 0023151184 scopus 로고
    • Two high affinity nucleoside transporters in Leishmania donovani
    • Aronow B., Kaur K., McCartan K., and Ullman B. Two high affinity nucleoside transporters in Leishmania donovani. Mol Biochem Parasitol 22 1 (1987) 29-37
    • (1987) Mol Biochem Parasitol , vol.22 , Issue.1 , pp. 29-37
    • Aronow, B.1    Kaur, K.2    McCartan, K.3    Ullman, B.4
  • 89
    • 0023678663 scopus 로고
    • Nucleoside uptake in Trypanosoma cruzi: analysis of a mutant resistant to tubercidin
    • Finley R.W., Cooney D.A., and Dvorak J.A. Nucleoside uptake in Trypanosoma cruzi: analysis of a mutant resistant to tubercidin. Mol Biochem Parasitol 31 2 (1988) 133-140
    • (1988) Mol Biochem Parasitol , vol.31 , Issue.2 , pp. 133-140
    • Finley, R.W.1    Cooney, D.A.2    Dvorak, J.A.3
  • 90
    • 0027323171 scopus 로고
    • Molecular biology studies of tubercidin resistance in Trypanosoma cruzi
    • Nozaki T., and Dvorak J.A. Molecular biology studies of tubercidin resistance in Trypanosoma cruzi. Parasitol Res 79 6 (1993) 451-455
    • (1993) Parasitol Res , vol.79 , Issue.6 , pp. 451-455
    • Nozaki, T.1    Dvorak, J.A.2
  • 91
    • 0024706538 scopus 로고
    • Purine base transport in wild-type and mycophenolic acid-resistant Tritrichomonas foetus
    • Hedstrom L., and Wang C.C. Purine base transport in wild-type and mycophenolic acid-resistant Tritrichomonas foetus. Mol Biochem Parasitol 35 3 (1989) 219-227
    • (1989) Mol Biochem Parasitol , vol.35 , Issue.3 , pp. 219-227
    • Hedstrom, L.1    Wang, C.C.2
  • 92
    • 0030050830 scopus 로고    scopus 로고
    • Alteration to one of three adenosine transporters is associated with resistance to cymelarsan in Trypanosoma evansi
    • Ross C.A., and Barns A.M. Alteration to one of three adenosine transporters is associated with resistance to cymelarsan in Trypanosoma evansi. Parasitol Res 82 2 (1996) 183-188
    • (1996) Parasitol Res , vol.82 , Issue.2 , pp. 183-188
    • Ross, C.A.1    Barns, A.M.2
  • 93
    • 0028805035 scopus 로고
    • A diamidine-resistant Trypanosoma equiperdum clone contains a P2 purine transporter with reduced substrate affinity
    • Barrett M.P., Zhang Z.Q., Denise H., et al. A diamidine-resistant Trypanosoma equiperdum clone contains a P2 purine transporter with reduced substrate affinity. Mol Biochem Parasitol 73 1-2 (1995) 223-229
    • (1995) Mol Biochem Parasitol , vol.73 , Issue.1-2 , pp. 223-229
    • Barrett, M.P.1    Zhang, Z.Q.2    Denise, H.3
  • 94
    • 0027181088 scopus 로고
    • Reduced purine accumulation is encoded on an amplified DNA in Leishmania mexicana amazonensis resistant to toxic nucleosides
    • Kerby B.R., and Detke S. Reduced purine accumulation is encoded on an amplified DNA in Leishmania mexicana amazonensis resistant to toxic nucleosides. Mol Biochem Parasitol 60 2 (1993) 171-185
    • (1993) Mol Biochem Parasitol , vol.60 , Issue.2 , pp. 171-185
    • Kerby, B.R.1    Detke, S.2
  • 95
    • 0031574141 scopus 로고    scopus 로고
    • Identification of a transcription factor like protein at the TOR locus in Leishmania mexicana amazonensis
    • Detke S. Identification of a transcription factor like protein at the TOR locus in Leishmania mexicana amazonensis. Mol Biochem Parasitol 90 2 (1997) 505-511
    • (1997) Mol Biochem Parasitol , vol.90 , Issue.2 , pp. 505-511
    • Detke, S.1
  • 96
    • 0026657269 scopus 로고
    • Stable amplification of a linear extrachromosomal DNA in mycophenolic acid-resistant Leishmania donovani
    • Wilson K., Beverley S.M., and Ullman B. Stable amplification of a linear extrachromosomal DNA in mycophenolic acid-resistant Leishmania donovani. Mol Biochem Parasitol 55 1-2 (1992) 197-206
    • (1992) Mol Biochem Parasitol , vol.55 , Issue.1-2 , pp. 197-206
    • Wilson, K.1    Beverley, S.M.2    Ullman, B.3
  • 97
    • 0028046144 scopus 로고
    • Amplification of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number
    • Wilson K., Berens R.L., Sifri C.D., and Ullman B. Amplification of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number. J Biol Chem 269 46 (1994) 28979-28987
    • (1994) J Biol Chem , vol.269 , Issue.46 , pp. 28979-28987
    • Wilson, K.1    Berens, R.L.2    Sifri, C.D.3    Ullman, B.4
  • 98
    • 0019179251 scopus 로고
    • Dihydrofolate reductase: thymidylate synthase, a bifunctional polypeptide from Crithidia fasciculata
    • Ferone R., and Roland S. Dihydrofolate reductase: thymidylate synthase, a bifunctional polypeptide from Crithidia fasciculata. Proc Natl Acad Sci U S A 77 10 (1980) 5802-5806
    • (1980) Proc Natl Acad Sci U S A , vol.77 , Issue.10 , pp. 5802-5806
    • Ferone, R.1    Roland, S.2
  • 99
    • 77949788207 scopus 로고    scopus 로고
    • Antifolate resistance mechanisms from bacteria to cancer cells with emphasis on parasites
    • in press. Rosen B.P., and Mobashery S. (Eds), Plenum Publishing Corporation, New York
    • in press. Ouellette M., Leblanc É., Kündig C., and Papadopoulou B. Antifolate resistance mechanisms from bacteria to cancer cells with emphasis on parasites. In: Rosen B.P., and Mobashery S. (Eds). Resolving the antibiotic paradox (1998), Plenum Publishing Corporation, New York
    • (1998) Resolving the antibiotic paradox
    • Ouellette, M.1    Leblanc, É.2    Kündig, C.3    Papadopoulou, B.4
  • 100
    • 0022606608 scopus 로고
    • Adaptation of the Indochina I/CDC strain of Plasmodium falciparum to the squirrel monkey (Saimiri sciureus)
    • Campbell C.C., Collins W.E., Milhous W.K., et al. Adaptation of the Indochina I/CDC strain of Plasmodium falciparum to the squirrel monkey (Saimiri sciureus). Am J Trop Med Hyg 35 3 (1986) 472-475
    • (1986) Am J Trop Med Hyg , vol.35 , Issue.3 , pp. 472-475
    • Campbell, C.C.1    Collins, W.E.2    Milhous, W.K.3
  • 101
    • 0031963057 scopus 로고    scopus 로고
    • Kenyan Plasmodium falciparum field isolates: correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain
    • Nzila-Mounda A., Mberu E.K., Sibley C.H., et al. Kenyan Plasmodium falciparum field isolates: correlation between pyrimethamine and chlorcycloguanil activity in vitro and point mutations in the dihydrofolate reductase domain. Antimicrob Agents Chemother 42 1 (1998) 164-169
    • (1998) Antimicrob Agents Chemother , vol.42 , Issue.1 , pp. 164-169
    • Nzila-Mounda, A.1    Mberu, E.K.2    Sibley, C.H.3
  • 102
    • 0030946111 scopus 로고    scopus 로고
    • The roles of pteridine reductase I and dihydrofolate reductase- thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major
    • Nare B., Hardy L.W., and Beverley S.M. The roles of pteridine reductase I and dihydrofolate reductase- thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major. J Biol Chem 272 21 (1997) 13883-13891
    • (1997) J Biol Chem , vol.272 , Issue.21 , pp. 13883-13891
    • Nare, B.1    Hardy, L.W.2    Beverley, S.M.3
  • 103
    • 0008614282 scopus 로고
    • Overproduction of a bifunctional thymidylate synthetase-dihydrofolate reductase and DNA amplification in methotrexate-resistant Leishmania tropica
    • Coderre J.A., Beverley S.M., Schimke R.T., and Santi D.V. Overproduction of a bifunctional thymidylate synthetase-dihydrofolate reductase and DNA amplification in methotrexate-resistant Leishmania tropica. Proc Natl Acad Sci U S A 80 8 (1983) 2132-2136
    • (1983) Proc Natl Acad Sci U S A , vol.80 , Issue.8 , pp. 2132-2136
    • Coderre, J.A.1    Beverley, S.M.2    Schimke, R.T.3    Santi, D.V.4
  • 104
    • 0021210054 scopus 로고
    • Unstable DNA amplifications in methotrexate-resistant Leishmania consist of extrachromosomal circles which relocalize during stabilization
    • Beverley S.M., Coderre J.A., Santi D.V., and Schimke R.T. Unstable DNA amplifications in methotrexate-resistant Leishmania consist of extrachromosomal circles which relocalize during stabilization. Cell 38 2 (1984) 431-439
    • (1984) Cell , vol.38 , Issue.2 , pp. 431-439
    • Beverley, S.M.1    Coderre, J.A.2    Santi, D.V.3    Schimke, R.T.4
  • 105
    • 0028308713 scopus 로고
    • Isolation and characherization of a mutant dihydrofolate reductase-thymidylate synthase from methotrexate-resistant Leishmania cells
    • Arrebola R., Olmo A., Reche P., et al. Isolation and characherization of a mutant dihydrofolate reductase-thymidylate synthase from methotrexate-resistant Leishmania cells. J Biol Chem 269 14 (1994) 10590-10596
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10590-10596
    • Arrebola, R.1    Olmo, A.2    Reche, P.3
  • 107
    • 0027351189 scopus 로고
    • Karnofsky memorial lecture. Ode to methotrexate
    • Bertino J.R. Karnofsky memorial lecture. Ode to methotrexate. J Clin Oncol 11 1 (1993) 5-14
    • (1993) J Clin Oncol , vol.11 , Issue.1 , pp. 5-14
    • Bertino, J.R.1
  • 108
    • 0029944197 scopus 로고    scopus 로고
    • In search of dihydrofolate reductase
    • Huennekens F.M. In search of dihydrofolate reductase. Protein Sci 5 6 (1996) 1201-1208
    • (1996) Protein Sci , vol.5 , Issue.6 , pp. 1201-1208
    • Huennekens, F.M.1
  • 109
    • 0000854414 scopus 로고
    • Amino acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum
    • Cowman A.F., Morry M.J., Biggs B.A., Cross G.A., and Foote S.J. Amino acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum. Proc Natl Acad Sci U S A 85 23 (1988) 9109-9113
    • (1988) Proc Natl Acad Sci U S A , vol.85 , Issue.23 , pp. 9109-9113
    • Cowman, A.F.1    Morry, M.J.2    Biggs, B.A.3    Cross, G.A.4    Foote, S.J.5
  • 110
    • 0031570732 scopus 로고    scopus 로고
    • Pterin and folate reduction by the Leishmania tarentolae H locus short- chain dehydrogenase/reductase PTRI
    • Wang J., Leblanc E., Chang C.F., et al. Pterin and folate reduction by the Leishmania tarentolae H locus short- chain dehydrogenase/reductase PTRI. Arch Biochem Biophys 342 2 (1997) 197-202
    • (1997) Arch Biochem Biophys , vol.342 , Issue.2 , pp. 197-202
    • Wang, J.1    Leblanc, E.2    Chang, C.F.3
  • 111
    • 0023200218 scopus 로고
    • Reductions in methotrexate and folate influx in methotrexate-resistant lines of Leishmania major are independent of R or H region amplification
    • Ellenberger T.E., and Beverley S.M. Reductions in methotrexate and folate influx in methotrexate-resistant lines of Leishmania major are independent of R or H region amplification. J Biol Chem 262 28 (1987) 13501-13506
    • (1987) J Biol Chem , vol.262 , Issue.28 , pp. 13501-13506
    • Ellenberger, T.E.1    Beverley, S.M.2
  • 112
    • 0027296408 scopus 로고
    • Frequent amplification of a short chain dehydrogenase gene as part of circular and linear amplicons in methotrexate resistant Leishmania
    • Papadopoulou B., Roy G., and Ouellette M. Frequent amplification of a short chain dehydrogenase gene as part of circular and linear amplicons in methotrexate resistant Leishmania. Nucleic Acids Res 21 18 (1993) 4305-4312
    • (1993) Nucleic Acids Res , vol.21 , Issue.18 , pp. 4305-4312
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 113
    • 0029128486 scopus 로고
    • Co-existence of circular and multiple linear amplicons in methotrexate- resistant Leishmania
    • Olmo A., Arrebola R., Bernier V., et al. Co-existence of circular and multiple linear amplicons in methotrexate- resistant Leishmania. Nucleic Acids Res 23 15 (1995) 2856-2864
    • (1995) Nucleic Acids Res , vol.23 , Issue.15 , pp. 2856-2864
    • Olmo, A.1    Arrebola, R.2    Bernier, V.3
  • 114
    • 0026779424 scopus 로고
    • A novel antifolate resistance gene on the amplified H circle of Leishmania
    • Papadopoulou B., Roy G., and Ouellette M. A novel antifolate resistance gene on the amplified H circle of Leishmania. Embo J 11 10 (1992) 3601-3608
    • (1992) Embo J , vol.11 , Issue.10 , pp. 3601-3608
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 115
    • 0026459643 scopus 로고
    • A member of the aldoketo reductase family confers methotrexate resistance in Leishmania
    • Callahan H.L., and Beverley S.M. A member of the aldoketo reductase family confers methotrexate resistance in Leishmania. J Biol Chem 267 34 (1992) 24165-24168
    • (1992) J Biol Chem , vol.267 , Issue.34 , pp. 24165-24168
    • Callahan, H.L.1    Beverley, S.M.2
  • 116
    • 0028308557 scopus 로고
    • Changes in folate and pterin metabolism after disruption of the Leishmania H locus short chain dehydrogenase gene
    • Papadopoulou B., Roy G., Mourad W., et al. Changes in folate and pterin metabolism after disruption of the Leishmania H locus short chain dehydrogenase gene. J Biol Chem 269 10 (1994) 7310-7315
    • (1994) J Biol Chem , vol.269 , Issue.10 , pp. 7310-7315
    • Papadopoulou, B.1    Roy, G.2    Mourad, W.3
  • 117
    • 0027996240 scopus 로고
    • PTRI: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major
    • Bello A.R., Nare B., Freedman D., et al. PTRI: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major. Proc Natl Acad Sci U S A 91 24 (1994) 11442-11446
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.24 , pp. 11442-11446
    • Bello, A.R.1    Nare, B.2    Freedman, D.3
  • 118
    • 0032005249 scopus 로고    scopus 로고
    • Residues involved in co-factor and substrate binding of the short-chain dehydrogenase/reductase PTRI producing methotrexate resistance in Leishmania
    • Leblanc E., Papadopoulou B., Bernatchez C., and Ouellette M. Residues involved in co-factor and substrate binding of the short-chain dehydrogenase/reductase PTRI producing methotrexate resistance in Leishmania. Eur J Biochem 251 3 (1998) 768-774
    • (1998) Eur J Biochem , vol.251 , Issue.3 , pp. 768-774
    • Leblanc, E.1    Papadopoulou, B.2    Bernatchez, C.3    Ouellette, M.4
  • 119
    • 0031282556 scopus 로고    scopus 로고
    • Biochemical and Genetic Tests for Inhibitors of Leishmania Pteridine Pathways
    • Hardy L.W., Matthews W., Nare B., and Beverley S.M. Biochemical and Genetic Tests for Inhibitors of Leishmania Pteridine Pathways. Exp Parasitol 87 3 (1997) 158-170
    • (1997) Exp Parasitol , vol.87 , Issue.3 , pp. 158-170
    • Hardy, L.W.1    Matthews, W.2    Nare, B.3    Beverley, S.M.4
  • 120
    • 0031574462 scopus 로고    scopus 로고
    • A pteridine reductase gene ptrl contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi
    • Robello C., Navarro P., Castanys S., and Gamarro F. A pteridine reductase gene ptrl contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi. Mol Biochem Parasitol 90 2 (1997) 525-535
    • (1997) Mol Biochem Parasitol , vol.90 , Issue.2 , pp. 525-535
    • Robello, C.1    Navarro, P.2    Castanys, S.3    Gamarro, F.4
  • 121
    • 0022476965 scopus 로고
    • Impaired drug uptake in methotrexate resistant Crithidia fasciculata without changes in dihydrofolate reductase activity or gene amplification
    • Dewes H., Ostergaard H.L., and Simpson L. Impaired drug uptake in methotrexate resistant Crithidia fasciculata without changes in dihydrofolate reductase activity or gene amplification. Mol Biochem Parasitol 19 2 (1986) 149-161
    • (1986) Mol Biochem Parasitol , vol.19 , Issue.2 , pp. 149-161
    • Dewes, H.1    Ostergaard, H.L.2    Simpson, L.3
  • 122
    • 0023938349 scopus 로고
    • Methotrexate-resistant Leishmania donovani genetically deficient in the folate-methotrexate transporter
    • Kaur K., Coons T., Emmett K., and Ullman B. Methotrexate-resistant Leishmania donovani genetically deficient in the folate-methotrexate transporter. J Biol Chem 263 15 (1988) 7020-7028
    • (1988) J Biol Chem , vol.263 , Issue.15 , pp. 7020-7028
    • Kaur, K.1    Coons, T.2    Emmett, K.3    Ullman, B.4
  • 123
    • 0027451936 scopus 로고
    • Frequent amplification of a short chain dehydrogenase gene in methotrexate resistant Leishmania
    • Papadopoulou B., and Ouellette M. Frequent amplification of a short chain dehydrogenase gene in methotrexate resistant Leishmania. Adv Exp Med Biol 338 (1993) 559-562
    • (1993) Adv Exp Med Biol , vol.338 , pp. 559-562
    • Papadopoulou, B.1    Ouellette, M.2
  • 124
    • 0028285518 scopus 로고
    • P-glycoprotein overexpression in methotrexate-resistant Leishmania tropica
    • Gamarro F., Chiquero M.J., Amador M.V., et al. P-glycoprotein overexpression in methotrexate-resistant Leishmania tropica. Biochem Pharmacol 47 11 (1994) 1939-1947
    • (1994) Biochem Pharmacol , vol.47 , Issue.11 , pp. 1939-1947
    • Gamarro, F.1    Chiquero, M.J.2    Amador, M.V.3
  • 125
    • 0002573211 scopus 로고
    • Transport of antifolates and antimonials in drug-resistant Leishmania
    • Georgopapadakou N. (Ed), Marcel Dekker, Inc, New York
    • Ouellette M., Papadopoulou B., Haimeur A., et al. Transport of antifolates and antimonials in drug-resistant Leishmania. In: Georgopapadakou N. (Ed). Drug Transport in Antimicrobial and anticancer chemotherapy (1995), Marcel Dekker, Inc, New York 377-402
    • (1995) Drug Transport in Antimicrobial and anticancer chemotherapy , pp. 377-402
    • Ouellette, M.1    Papadopoulou, B.2    Haimeur, A.3
  • 126
    • 0025936205 scopus 로고
    • Biopterin conversion to reduced folates by Leishmania donovani promastigotes
    • Beck J.T., and Ullman B. Biopterin conversion to reduced folates by Leishmania donovani promastigotes. Mol Biochem Parasitol 49 1 (1991) 21-28
    • (1991) Mol Biochem Parasitol , vol.49 , Issue.1 , pp. 21-28
    • Beck, J.T.1    Ullman, B.2
  • 127
    • 0030921824 scopus 로고    scopus 로고
    • New approaches to Leishmania chemotherapy: pteridine reductase I (PTRI) as a target and modulator of antifolate sensitivity
    • Suppl
    • Suppl. Nare B., Luba J., Hardy L.W., and Beverley S. New approaches to Leishmania chemotherapy: pteridine reductase I (PTRI) as a target and modulator of antifolate sensitivity. Parasitology 114 (1997) S101-S110
    • (1997) Parasitology , vol.114
    • Nare, B.1    Luba, J.2    Hardy, L.W.3    Beverley, S.4
  • 128
    • 0027938665 scopus 로고
    • An amplified DNA element in Leishmania encodes potential integral membrane and nucleotide-binding proteins
    • Myler P.J., Lodes M.J., Merlin G., et al. An amplified DNA element in Leishmania encodes potential integral membrane and nucleotide-binding proteins. Mol Biochem Parasitol 66 1 (1994) 11-20
    • (1994) Mol Biochem Parasitol , vol.66 , Issue.1 , pp. 11-20
    • Myler, P.J.1    Lodes, M.J.2    Merlin, G.3
  • 129
    • 0030813914 scopus 로고    scopus 로고
    • LDI amplifications in Leishmania
    • Segovia M., and Ortiz G. LDI amplifications in Leishmania. Parasitol Today 13 (1997) 342-348
    • (1997) Parasitol Today , vol.13 , pp. 342-348
    • Segovia, M.1    Ortiz, G.2
  • 130
    • 0030948473 scopus 로고    scopus 로고
    • Defective transport is a common mechanism of acquired methotrexate resistance in acute lymphocytic leukemia and is associated with decreased reduced folate carrier expression
    • Gorlick R., Goker E., Trippett T., et al. Defective transport is a common mechanism of acquired methotrexate resistance in acute lymphocytic leukemia and is associated with decreased reduced folate carrier expression. Blood 89 3 (1997) 1013-1018
    • (1997) Blood , vol.89 , Issue.3 , pp. 1013-1018
    • Gorlick, R.1    Goker, E.2    Trippett, T.3
  • 131
    • 0030828391 scopus 로고    scopus 로고
    • Comparison of aminosidine (paromomycin) and sodium stibogluconate for treatment of canine leishmaniasis
    • Poli A., Sozzi S., Guidi G., et al. Comparison of aminosidine (paromomycin) and sodium stibogluconate for treatment of canine leishmaniasis. Vet Parasitol 71 4 (1997) 263-271
    • (1997) Vet Parasitol , vol.71 , Issue.4 , pp. 263-271
    • Poli, A.1    Sozzi, S.2    Guidi, G.3
  • 132
    • 0028606767 scopus 로고
    • Paromomycin resistance in Leishmania tropica: lack of correlation with mutation in the small subunit ribosomal RNA gene
    • Fong D., Chan M.M., Rodriguez R., et al. Paromomycin resistance in Leishmania tropica: lack of correlation with mutation in the small subunit ribosomal RNA gene. Am J Trop Med Hyg 51 6 (1994) 758-766
    • (1994) Am J Trop Med Hyg , vol.51 , Issue.6 , pp. 758-766
    • Fong, D.1    Chan, M.M.2    Rodriguez, R.3
  • 133
    • 0025878924 scopus 로고
    • Leishmania major: resistance of promastigotes to paromomycin, and susceptibility of amastigotes to paromomycin-methylbenzethonium chloride ointment
    • el-On J., Sulitzeanu A., and Schnur L.F. Leishmania major: resistance of promastigotes to paromomycin, and susceptibility of amastigotes to paromomycin-methylbenzethonium chloride ointment. Ann Trop Med Parasitol 85 3 (1991) 323-328
    • (1991) Ann Trop Med Parasitol , vol.85 , Issue.3 , pp. 323-328
    • el-On, J.1    Sulitzeanu, A.2    Schnur, L.F.3
  • 134
    • 0028142090 scopus 로고
    • On the introduction of genetically modified Leishmania outside the laboratory
    • Gueiros-Filho F.J., and Beverley S.M. On the introduction of genetically modified Leishmania outside the laboratory. Exp Parasitol 78 4 (1994) 425-428
    • (1994) Exp Parasitol , vol.78 , Issue.4 , pp. 425-428
    • Gueiros-Filho, F.J.1    Beverley, S.M.2
  • 135
    • 0026720137 scopus 로고
    • Multidrug resistance in Leishmania donovani is conferred by amplification of a gene homologous to the mammalian mdr1 gene
    • Henderson D.M., Sifri C.D., Rodgers M., et al. Multidrug resistance in Leishmania donovani is conferred by amplification of a gene homologous to the mammalian mdr1 gene. Mol Cell Biol 12 6 (1992) 2855-2865
    • (1992) Mol Cell Biol , vol.12 , Issue.6 , pp. 2855-2865
    • Henderson, D.M.1    Sifri, C.D.2    Rodgers, M.3
  • 136
    • 0027178549 scopus 로고
    • Cloning and functional analysis of an extrachromosomally amplified multidrug resistance-like gene in Leishmania enriettii
    • Chow L.M., Wong A.K., Ullman B., and Wirth D.F. Cloning and functional analysis of an extrachromosomally amplified multidrug resistance-like gene in Leishmania enriettii. Mol Biochem Parasitol 60 2 (1993) 195-208
    • (1993) Mol Biochem Parasitol , vol.60 , Issue.2 , pp. 195-208
    • Chow, L.M.1    Wong, A.K.2    Ullman, B.3    Wirth, D.F.4
  • 137
    • 0029565603 scopus 로고
    • Leishmania amazonensis: Multidrug resistance in vinblastine-resistant promastigotes is associated with rhodamine 123 efflux, DNA amplification, and RNA overexpression of a Leishmania mdr1 gene
    • Gueiros-Filho F.J., Viola J.P., Gomes F.C., et al. Leishmania amazonensis: Multidrug resistance in vinblastine-resistant promastigotes is associated with rhodamine 123 efflux, DNA amplification, and RNA overexpression of a Leishmania mdr1 gene. Exp Parasitol 81 4 (1995) 480-490
    • (1995) Exp Parasitol , vol.81 , Issue.4 , pp. 480-490
    • Gueiros-Filho, F.J.1    Viola, J.P.2    Gomes, F.C.3
  • 138
    • 0344333486 scopus 로고    scopus 로고
    • Altered drug membrane permeability in a multidrug-resistant Leishmania tropica line
    • Chiquero M.J., Perez-Victoria J.M., O'Valle F., et al. Altered drug membrane permeability in a multidrug-resistant Leishmania tropica line. Biochem Pharmacol 55 2 (1998) 131-139
    • (1998) Biochem Pharmacol , vol.55 , Issue.2 , pp. 131-139
    • Chiquero, M.J.1    Perez-Victoria, J.M.2    O'Valle, F.3
  • 139
    • 0028922077 scopus 로고
    • Multidrug resistance and P-glycoproteins in parasitic protozoa
    • Ullman B. Multidrug resistance and P-glycoproteins in parasitic protozoa. J Bioenerg Biomembr 27 1 (1995) 77-84
    • (1995) J Bioenerg Biomembr , vol.27 , Issue.1 , pp. 77-84
    • Ullman, B.1
  • 140
    • 77949811743 scopus 로고
    • Amplification of the ABC transporter gene pgpA and of other metal resistance genes in Leishmania tarentolae and their study by gene transfection and gene disruption
    • in press. vol ABC Transporters: Biochemical, cellular, and molecular aspects). Ambudkar S.V., and Gottesman M.M. (Eds), Academic Press, San Diego
    • in press. vol ABC Transporters: Biochemical, cellular, and molecular aspects). Ouellette M., Haimeur A., Grondin K., et al. Amplification of the ABC transporter gene pgpA and of other metal resistance genes in Leishmania tarentolae and their study by gene transfection and gene disruption. In: Ambudkar S.V., and Gottesman M.M. (Eds). Methods Enzymol (1988), Academic Press, San Diego
    • (1988) Methods Enzymol
    • Ouellette, M.1    Haimeur, A.2    Grondin, K.3
  • 141
    • 0026709847 scopus 로고
    • The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-I-phosphate transferase gene that can be used as a dominant selectable marker in transfection
    • Liu X., and Chang K.P. The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-I-phosphate transferase gene that can be used as a dominant selectable marker in transfection. Mol Cell Biol 12 9 (1992) 4112-4122
    • (1992) Mol Cell Biol , vol.12 , Issue.9 , pp. 4112-4122
    • Liu, X.1    Chang, K.P.2
  • 142
    • 0026072572 scopus 로고
    • Gene amplification in Leishmania
    • Beverley S.M. Gene amplification in Leishmania. Annu Rev Microbiol 45 (1991) 417-444
    • (1991) Annu Rev Microbiol , vol.45 , pp. 417-444
    • Beverley, S.M.1
  • 143
    • 0026022969 scopus 로고
    • Direct and inverted DNA repeats associated with P-glycoprotein gene amplification in drug resistant Leishmania
    • Ouellette M., Hettema E., Wust D., et al. Direct and inverted DNA repeats associated with P-glycoprotein gene amplification in drug resistant Leishmania. Embo J 10 4 (1991) 1009-1016
    • (1991) Embo J , vol.10 , Issue.4 , pp. 1009-1016
    • Ouellette, M.1    Hettema, E.2    Wust, D.3
  • 144
    • 0029975465 scopus 로고    scopus 로고
    • Formation of extrachromosomal circular amplicons with direct or inverted duplications in drug-resistant Leishmania tarentolae
    • Grondin K., Roy G., and Ouellette M. Formation of extrachromosomal circular amplicons with direct or inverted duplications in drug-resistant Leishmania tarentolae. Mol Cell Biol 16 7 (1996) 3587-3595
    • (1996) Mol Cell Biol , vol.16 , Issue.7 , pp. 3587-3595
    • Grondin, K.1    Roy, G.2    Ouellette, M.3
  • 145
    • 0028070305 scopus 로고
    • Autonomous replication of bacterial DNA plasmid oligomers in Leishmania
    • Papadopoulou B., Roy G., and Ouellette M. Autonomous replication of bacterial DNA plasmid oligomers in Leishmania. Mol Biochem Parasitol 65 1 (1994) 39-49
    • (1994) Mol Biochem Parasitol , vol.65 , Issue.1 , pp. 39-49
    • Papadopoulou, B.1    Roy, G.2    Ouellette, M.3
  • 146
    • 0027992487 scopus 로고
    • An episome of Trypanosoma brucei can exist as an extrachromosomal element in a broad range of trypanosomatids but shows different requirements for stable replication
    • Patnaik P.K., Bellofatto V., Hartree D., and Cross G.A. An episome of Trypanosoma brucei can exist as an extrachromosomal element in a broad range of trypanosomatids but shows different requirements for stable replication. Mol Biochem Parasitol 66 1 (1994) 153-156
    • (1994) Mol Biochem Parasitol , vol.66 , Issue.1 , pp. 153-156
    • Patnaik, P.K.1    Bellofatto, V.2    Hartree, D.3    Cross, G.A.4
  • 147
    • 0024366276 scopus 로고
    • Antifolate drug selection results in duplication and rearrangement of chromosome 7 in Plasmodium chabaudi
    • Cowman A.F., and Lew A.M. Antifolate drug selection results in duplication and rearrangement of chromosome 7 in Plasmodium chabaudi. Mol Cell Biol 9 11 (1989) 5182-5188
    • (1989) Mol Cell Biol , vol.9 , Issue.11 , pp. 5182-5188
    • Cowman, A.F.1    Lew, A.M.2
  • 148
    • 0024574074 scopus 로고
    • The importance of circular DNA in mammalian gene amplification
    • Wahl G.M. The importance of circular DNA in mammalian gene amplification. Cancer Res 49 6 (1989) 1333-1340
    • (1989) Cancer Res , vol.49 , Issue.6 , pp. 1333-1340
    • Wahl, G.M.1
  • 149
    • 0031041891 scopus 로고    scopus 로고
    • Analysis of post-transcriptional regulation operating on transcription products of the tandemly linked Leishmania infantum hsp 70 genes
    • Quijada L., Soto M., Alonso C., and Requena J.M. Analysis of post-transcriptional regulation operating on transcription products of the tandemly linked Leishmania infantum hsp 70 genes. J Biol Chem 272 7 (1997) 4493-4499
    • (1997) J Biol Chem , vol.272 , Issue.7 , pp. 4493-4499
    • Quijada, L.1    Soto, M.2    Alonso, C.3    Requena, J.M.4
  • 150
    • 0028114097 scopus 로고
    • A regulatory role for the 5′ and 3′ untranslated regions in differential expression of hsp83 in Leishmania
    • Aly R., Argaman M., Halman S., and Shapira M. A regulatory role for the 5′ and 3′ untranslated regions in differential expression of hsp83 in Leishmania. Nucleic Acids Res 22 15 (1994) 2922-2929
    • (1994) Nucleic Acids Res , vol.22 , Issue.15 , pp. 2922-2929
    • Aly, R.1    Argaman, M.2    Halman, S.3    Shapira, M.4
  • 151
    • 0031035013 scopus 로고    scopus 로고
    • Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain
    • Svensson F., Ceriani C., Wallstrom E.L., et al. Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain. Proc Natl Acad Sci U S A 94 2 (1997) 397-402
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.2 , pp. 397-402
    • Svensson, F.1    Ceriani, C.2    Wallstrom, E.L.3
  • 152
    • 0028156734 scopus 로고
    • Complete developmental cycle of Leishmania mexicana in axenic culture
    • Pt 1
    • Pt 1. Bates P.A. Complete developmental cycle of Leishmania mexicana in axenic culture. Parasitology 108 (1994) 1-9
    • (1994) Parasitology , vol.108 , pp. 1-9
    • Bates, P.A.1
  • 153
    • 0029031644 scopus 로고
    • In vitro antileishmanial properties of tri- and pentavalent antimonial preparations
    • Roberts W.L., Berman J.D., and Rainey P.M. In vitro antileishmanial properties of tri- and pentavalent antimonial preparations. Antimicrob Agents Chemother 39 6 (1995) 1234-1239
    • (1995) Antimicrob Agents Chemother , vol.39 , Issue.6 , pp. 1234-1239
    • Roberts, W.L.1    Berman, J.D.2    Rainey, P.M.3
  • 155
    • 0030952921 scopus 로고    scopus 로고
    • Pentostam induces resistance to antimony and the preservative chlorocresol in Leishmania donovani promastigotes and axenically grown amastigotes
    • Ephros M., Waldman E., and Zilberstein D. Pentostam induces resistance to antimony and the preservative chlorocresol in Leishmania donovani promastigotes and axenically grown amastigotes. Antimicrob Agents Chemother 41 5 (1997) 1064-1068
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.5 , pp. 1064-1068
    • Ephros, M.1    Waldman, E.2    Zilberstein, D.3
  • 156
    • 0030881960 scopus 로고    scopus 로고
    • In vitro life cycle of pentamidine-resistant amastigotes: stability of the chemoresistant phenotypes is dependent on the level of resistance induced
    • Sereno D., and Lemesre J.L. In vitro life cycle of pentamidine-resistant amastigotes: stability of the chemoresistant phenotypes is dependent on the level of resistance induced. Antimicrob Agents Chemother 41 9 (1997) 1898-1903
    • (1997) Antimicrob Agents Chemother , vol.41 , Issue.9 , pp. 1898-1903
    • Sereno, D.1    Lemesre, J.L.2
  • 157
    • 0027987981 scopus 로고
    • Leishmania resistant to sodium stibogluconate: drug-associated macrophage-dependent killing
    • Ibrahim M.E., Hag-Ali M., el-Hassan A.M., et al. Leishmania resistant to sodium stibogluconate: drug-associated macrophage-dependent killing. Parasitol Res 80 7 (1994) 569-574
    • (1994) Parasitol Res , vol.80 , Issue.7 , pp. 569-574
    • Ibrahim, M.E.1    Hag-Ali, M.2    el-Hassan, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.