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Volumn 79, Issue 7, 2011, Pages 2764-2769

Spermidine synthase is required for virulence of Leishmania donovani

Author keywords

[No Author keywords available]

Indexed keywords

POLYAMINE; PUTRESCINE; SPERMIDINE SYNTHASE;

EID: 79959450164     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00073-11     Document Type: Article
Times cited : (40)

References (62)
  • 1
    • 0023085302 scopus 로고
    • Cytostatic effect of DL-alpha-difluoromethylornithine against Plasmodium falciparum and its reversal by diamines and spermidine
    • Assaraf, Y. G., J. Golenser, D. T. Spira, G. Messer, and U. Bachrach. 1987. Cytostatic effect of DL-alpha-difluoromethylornithine against Plasmodium falciparum and its reversal by diamines and spermidine. Parasitol. Res. 73: 313-318.
    • (1987) Parasitol. Res. , vol.73 , pp. 313-318
    • Assaraf, Y.G.1    Golenser, J.2    Spira, D.T.3    Messer, G.4    Bachrach, U.5
  • 2
    • 0026480583 scopus 로고
    • Cure of murine Trypanosoma brucei rhodesiense infections with an S-adenosylmethionine decarboxylase inhibitor
    • Bacchi, C. J., et al. 1992. Cure of murine Trypanosoma brucei rhodesiense infections with an S-adenosylmethionine decarboxylase inhibitor. Antimicrob. Agents Chemother. 36:2736-2740.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 2736-2740
    • Bacchi, C.J.1
  • 3
    • 67749142072 scopus 로고    scopus 로고
    • Trypanocidal activity of 8-methyl-′-{[(Z)-4-aminobut-2-enyl]-(methylamino)}adenosine (Genz-644131), an adenosylmethionine decarboxylase inhibitor
    • Bacchi, C. J., et al. 2009. Trypanocidal activity of 8-methyl-5′-{[(Z)-4-aminobut-2-enyl]-(methylamino)}adenosine (Genz-644131), an adenosylmethionine decarboxylase inhibitor. Antimicrob. Agents Chemother. 53: 3269-3272.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3269-3272
    • Bacchi, C.J.1
  • 5
    • 28444461786 scopus 로고    scopus 로고
    • Naturally occurring polyamines: interaction with macromolecules
    • Bachrach, U. 2005. Naturally occurring polyamines: interaction with macromolecules. Curr. Protein Pept. Sci. 6:559-566.
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 559-566
    • Bachrach, U.1
  • 6
    • 66149136395 scopus 로고    scopus 로고
    • Novel S-adenosylmethionine decarboxylase inhibitors for the treatment of human African trypanosomiasis
    • Barker, R. H., Jr., et al. 2009. Novel S-adenosylmethionine decarboxylase inhibitors for the treatment of human African trypanosomiasis. Antimicrob. Agents Chemother. 53:2052-2058.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2052-2058
    • Barker Jr., R.H.1
  • 8
    • 0025180260 scopus 로고
    • Cure of Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense infections in mice with an irreversible inhibitor of S-adenosylmethionine decarboxylase
    • Bitonti, A. J., et al. 1990. Cure of Trypanosoma brucei brucei and Trypanosoma brucei rhodesiense infections in mice with an irreversible inhibitor of S-adenosylmethionine decarboxylase. Antimicrob. Agents Chemother. 34: 1485-1490.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 1485-1490
    • Bitonti, A.J.1
  • 9
    • 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., J. A. Dumont, and P. P. McCann. 1986. Characterization of Trypanosoma brucei brucei S-adenosyl-L-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone). Biochem. J. 237:685-689.
    • (1986) Biochem. J. , vol.237 , pp. 685-689
    • Bitonti, A.J.1    Dumont, J.A.2    McCann, P.P.3
  • 10
    • 0029892549 scopus 로고    scopus 로고
    • Genetic susceptibility to leishmanial infections: studies in mice and man
    • Blackwell, J. M. 1996. Genetic susceptibility to leishmanial infections: studies in mice and man. Parasitology. 112(Suppl.):S67-S74.
    • (1996) Parasitology , vol.112 , Issue.SUPPL.
    • Blackwell, J.M.1
  • 11
    • 33744937343 scopus 로고    scopus 로고
    • A conditional mutant deficient in hypoxanthine-guanine phosphoribosyltransferase and xanthine phosphoribosyltransferase validates the purine salvage pathway of Leishmania donovani
    • Boitz, J. M., and B. Ullman. 2006. A conditional mutant deficient in hypoxanthine-guanine phosphoribosyltransferase and xanthine phosphoribosyltransferase validates the purine salvage pathway of Leishmania donovani. J. Biol. Chem. 281:16084-16089.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16084-16089
    • Boitz, J.M.1    Ullman, B.2
  • 12
    • 60549113705 scopus 로고    scopus 로고
    • Leishmania donovani ornithine decarboxylase is indispensable for parasite survival in the mammalian host
    • Boitz, J. M., et al. 2009. Leishmania donovani ornithine decarboxylase is indispensable for parasite survival in the mammalian host. Infect. Immun. 77:756-63.
    • (2009) Infect. Immun. , vol.77 , pp. 756-763
    • Boitz, J.M.1
  • 13
    • 0029149252 scopus 로고
    • Culture microtitration: a sensitive method for quantifying Leishmania infantum in tissues of infected mice
    • Buffet, P. A., A. Sulahian, Y. J. Garin, N. Nassar, and F. Derouin. 1995. Culture microtitration: a sensitive method for quantifying Leishmania infantum in tissues of infected mice. Antimicrob. Agents Chemother. 39:2167-2168.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2167-2168
    • Buffet, P.A.1    Sulahian, A.2    Garin, Y.J.3    Nassar, N.4    Derouin, F.5
  • 14
    • 0038639784 scopus 로고    scopus 로고
    • Eflornithine for the treatment of human African trypanosomiasis
    • Burri, C., and R. Brun. 2003. Eflornithine for the treatment of human African trypanosomiasis. Parasitol. Res. 90(Suppl. 1):S49-S52.
    • (2003) Parasitol. Res. , vol.90 , Issue.SUPPL. 1
    • Burri, C.1    Brun, R.2
  • 15
    • 69249245459 scopus 로고    scopus 로고
    • Polyamine catabolism and disease
    • Casero, R. A., and A. E. Pegg. 2009. Polyamine catabolism and disease. Biochem. J. 421:323-338.
    • (2009) Biochem. J. , vol.421 , pp. 323-338
    • Casero, R.A.1    Pegg, A.E.2
  • 16
    • 0018197931 scopus 로고
    • Effects of methylglyoxal bis(ganylhydrazone) on trypanosomatid flagellates: inhibition of growth and nucleoside incorporation in Trypanosoma brucei
    • Chang, K. P., R. F. Steiger, C. Dave, and Y. C. Cheng. 1978. Effects of methylglyoxal bis(ganylhydrazone) on trypanosomatid flagellates: inhibition of growth and nucleoside incorporation in Trypanosoma brucei. J. Protozool. 25:145-149.
    • (1978) J. Protozool. , vol.25 , pp. 145-149
    • Chang, K.P.1    Steiger, R.F.2    Dave, C.3    Cheng, Y.C.4
  • 17
    • 0032583153 scopus 로고    scopus 로고
    • Genetic nomenclature for Trypanosoma and Leishmania
    • Clayton, C., et al. 1998. Genetic nomenclature for Trypanosoma and Leishmania. Mol. Biochem. Parasitol. 97:221-224.
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 221-224
    • Clayton, C.1
  • 18
    • 0024999490 scopus 로고
    • Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine
    • Danzin, C., P. Marchal, and P. Casara. 1990. Irreversible inhibition of rat S-adenosylmethionine decarboxylase by 5′-([(Z)-4-amino-2-butenyl]methylamino)-5′-deoxyadenosine. Biochem. Pharmacol. 40:1499-1503.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1499-1503
    • Danzin, C.1    Marchal, P.2    Casara, P.3
  • 19
    • 1242294372 scopus 로고    scopus 로고
    • Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics
    • Debrabant, A., M. B. Joshi, P. F. Pimenta, and D. M. Dwyer. 2004. Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics. Int. J. Parasitol. 34:205-217.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 205-217
    • Debrabant, A.1    Joshi, M.B.2    Pimenta, P.F.3    Dwyer, D.M.4
  • 20
    • 0037625351 scopus 로고    scopus 로고
    • Current chemotherapy of human African trypanosomiasis
    • Docampo, R., and S. N. Moreno. 2003. Current chemotherapy of human African trypanosomiasis. Parasitol. Res. 90(Suppl. 1):S10-S13.
    • (2003) Parasitol. Res. , vol.90 , Issue.SUPPL. 1
    • Docampo, R.1    Moreno, S.N.2
  • 21
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the Kinetoplastida
    • Fairlamb, A. H., and A. Cerami. 1992. Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46:695-729.
    • (1992) Annu. Rev. Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 22
    • 33745199610 scopus 로고    scopus 로고
    • Animal models for vaccine studies for visceral leishmaniasis
    • Garg, R., and A. Dube. 2006. Animal models for vaccine studies for visceral leishmaniasis. Indian J. Med. Res. 123:439-454.
    • (2006) Indian J. Med. Res. , vol.123 , pp. 439-454
    • Garg, R.1    Dube, A.2
  • 23
    • 40049092026 scopus 로고    scopus 로고
    • An effect of parasite-encoded arginase on the outcome of murine cutaneous leishmaniasis
    • Gaur, U., et al. 2007. An effect of parasite-encoded arginase on the outcome of murine cutaneous leishmaniasis. J. Immunol. 179:8446-8453.
    • (2007) J. Immunol. , vol.179 , pp. 8446-8453
    • Gaur, U.1
  • 24
    • 0344325708 scopus 로고
    • Drug resistance in protozoa
    • W. C. Campbell and R. S. Rew (ed.) Plenum Press, New York, NY
    • Geary, T. G., S. A. Edgar, and J. D. Jensen. 1986. Drug resistance in protozoa, p. 209-236. In W. C. Campbell and R. S. Rew (ed.), Chemotherapy of parasitic diseases. Plenum Press, New York, NY.
    • (1986) Chemotherapy of parasitic diseases , pp. 209-236
    • Geary, T.G.1    Edgar, S.A.2    Jensen, J.D.3
  • 25
    • 0025282471 scopus 로고
    • Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation
    • Ghoda, L., M. A. Phillips, K. E. Bass, C. C. Wang, and P. Coffino. 1990. Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation. J. Biol. Chem. 265:11823-11826.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11823-11826
    • Ghoda, L.1    Phillips, M.A.2    Bass, K.E.3    Wang, C.C.4    Coffino, P.5
  • 26
    • 0024600672 scopus 로고
    • Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation
    • Ghoda, L., T. van Daalen Wetters, M. Macrae, D. Ascherman, and P. Coffino. 1989. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science 243:1493-1495.
    • (1989) Science , vol.243 , pp. 1493-1495
    • Ghoda, L.1    van Daalen Wetters, T.2    Macrae, M.3    Ascherman, D.4    Coffino, P.5
  • 27
    • 0021249073 scopus 로고
    • Inhibition of growth of Giardia lamblia by difluoromethylornithine, a specific inhibitor of polyamine biosynthesis
    • Gillin, F. D., D. S. Reiner, and P. P. McCann. 1984. Inhibition of growth of Giardia lamblia by difluoromethylornithine, a specific inhibitor of polyamine biosynthesis. J. Protozool. 31:161-163.
    • (1984) J. Protozool. , vol.31 , pp. 161-163
    • Gillin, F.D.1    Reiner, D.S.2    McCann, P.P.3
  • 28
    • 0034073186 scopus 로고    scopus 로고
    • Blasticidin resistance: a new independent marker for stable transfection of Leishmania
    • Goyard, S., and S. M. Beverley. 2000. Blasticidin resistance: a new independent marker for stable transfection of Leishmania. Mol. Biochem. Parasitol. 08:249-252.
    • (2000) Mol. Biochem. Parasitol. , vol.108 , pp. 249-252
    • Goyard, S.1    Beverley, S.M.2
  • 29
    • 0141560355 scopus 로고    scopus 로고
    • An in vitro system for developmental and genetic studies of Leishmania donovani phosphoglycans
    • Goyard, S., et al. 2003. An in vitro system for developmental and genetic studies of Leishmania donovani phosphoglycans. Mol. Biochem. Parasitol. 130:31-2.
    • (2003) Mol. Biochem. Parasitol. , vol.130 , pp. 31-42
    • Goyard, S.1
  • 30
    • 0024942714 scopus 로고
    • In vivo effect of eflornithine (DFMO) and some related compounds on Leishmania infantum preliminary communication
    • Gradoni, L., M. A. Iorio, M. Gramiccia, and S. Orsini. 1989. In vivo effect of eflornithine (DFMO) and some related compounds on Leishmania infantum preliminary communication. Farmaco 44:1157-1166.
    • (1989) Farmaco , vol.44 , pp. 1157-1166
    • Gradoni, L.1    Iorio, M.A.2    Gramiccia, M.3    Orsini, S.4
  • 31
    • 17644403556 scopus 로고    scopus 로고
    • Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major
    • Hasne, M. P., and B. Ullman. 2005. Identification and characterization of a polyamine permease from the protozoan parasite Leishmania major. J. Biol. Chem. 280:15188-15194.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15188-15194
    • Hasne, M.P.1    Ullman, B.2
  • 32
    • 30944463252 scopus 로고    scopus 로고
    • Animal disease models generated by genetic engineering of polyamine metabolism
    • Janne, J., et al. 2005. Animal disease models generated by genetic engineering of polyamine metabolism. J. Cell. Mol. Med. 9:865-882.
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 865-882
    • Janne, J.1
  • 33
    • 1542284582 scopus 로고    scopus 로고
    • Genetic approaches to the cellular functions of polyamines in mammals
    • Janne, J., L. Alhonen, M. Pietila, and T. A. Keinanen. 2004. Genetic approaches to the cellular functions of polyamines in mammals. Eur. J. Biochem. 71:877-894.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 877-894
    • Janne, J.1    Alhonen, L.2    Pietila, M.3    Keinanen, T.A.4
  • 34
    • 0033525089 scopus 로고    scopus 로고
    • Ornithine decarboxylase gene deletion mutants of Leishmania donovani
    • Jiang, Y., et al. 1999. Ornithine decarboxylase gene deletion mutants of Leishmania donovani. J. Biol. Chem. 274:3781-3788.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3781-3788
    • Jiang, Y.1
  • 35
    • 0022864572 scopus 로고
    • Effects of DL-alpha-difluoromethylornithine on Leishmania donovani promastigotes
    • Kaur, K., K. Emmett, P. P. McCann, A. Sjoerdsma, and B. Ullman. 1986. Effects of DL-alpha-difluoromethylornithine on Leishmania donovani promastigotes. J. Protozool. 33:518-521.
    • (1986) J. Protozool. , vol.33 , pp. 518-521
    • Kaur, K.1    Emmett, K.2    McCann, P.P.3    Sjoerdsma, A.4    Ullman, B.5
  • 36
    • 0029617291 scopus 로고
    • Strategies for immune intervention in visceral leishmaniasis
    • Kaye, P. M., P. Gorak, M. Murphy, and S. Ross. 1995. Strategies for immune intervention in visceral leishmaniasis. Ann. Trop. Med. Parasitol. 89(Suppl.): 5-81.
    • (1995) Ann. Trop. Med. Parasitol. , vol.89 , Issue.SUPPL. , pp. 75-81
    • Kaye, P.M.1    Gorak, P.2    Murphy, M.3    Ross, S.4
  • 37
    • 0011179878 scopus 로고
    • Inhibition of Leishmania species by alpha-difluoromethylornithine
    • D. T. Hart (ed.) Plenum Press, New York, NY
    • Keithly, J. S., and A. H. Fairlamb. 1987. Inhibition of Leishmania species by alpha-difluoromethylornithine, p. 749-756. In D. T. Hart (ed.), Leishmaniasis: the current status and new strategies for control, vol. 163. Plenum Press, New York, NY.
    • (1987) Leishmaniasis: the current status and new strategies for control , vol.163 , pp. 749-756
    • Keithly, J.S.1    Fairlamb, A.H.2
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0004713598 scopus 로고
    • Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E C. 4. 1. 1. 17) by substrate and product analogues
    • Metcalf, B. W., et al. 1978. Catalytic irreversible inhibition of mammalian ornithine decarboxylase (E.C. 4.1.1.17) by substrate and product analogues. J. Am. Chem. Soc. 100:2551-2553.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 2551-2553
    • Metcalf, B.W.1
  • 40
    • 34247579197 scopus 로고    scopus 로고
    • Chemotherapy of leishmaniasis: past, present and future
    • Mishra, J., A. Saxena, and S. Singh. 2007. Chemotherapy of leishmaniasis: past, present and future. Curr. Med. Chem. 14:1153-1169.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1153-1169
    • Mishra, J.1    Saxena, A.2    Singh, S.3
  • 41
    • 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., P. Kapoor, and R. Madhubala. 1996. Characterization of alpha-difluoromethylornithine resistant Leishmania donovani and its susceptibility to other inhibitors of the polyamine biosynthetic pathway. Pharmacol. Res. 34:43-46.
    • (1996) Pharmacol. Res. , vol.34 , pp. 43-46
    • Mukhopadhyay, R.1    Kapoor, P.2    Madhubala, R.3
  • 42
    • 0027733717 scopus 로고
    • Effect of a bis(benzyl)polyamine analogue, and DL-alpha-difluoromethylornithine on parasite suppression and cellular polyamine levels in golden hamster during Leishmania donovani infection
    • Mukhopadhyay, R., and R. Madhubala. 1993. Effect of a bis(benzyl)polyamine analogue, and DL-alpha-difluoromethylornithine on parasite suppression and cellular polyamine levels in golden hamster during Leishmania donovani infection. Pharmacol. Res. 28:359-365.
    • (1993) Pharmacol. Res. , vol.28 , pp. 359-365
    • Mukhopadhyay, R.1    Madhubala, R.2
  • 43
    • 76249084931 scopus 로고    scopus 로고
    • Infection with arginase-deficient Leishmania major reveals a parasite number-dependent and cytokine-independent regulation of host cellular arginase activity and disease pathogenesis
    • Muleme, H. M., et al. 2009. Infection with arginase-deficient Leishmania major reveals a parasite number-dependent and cytokine-independent regulation of host cellular arginase activity and disease pathogenesis. J. Immunol. 183:8068-8076.
    • (2009) J. Immunol. , vol.183 , pp. 8068-8076
    • Muleme, H.M.1
  • 44
    • 0031658033 scopus 로고    scopus 로고
    • Visceral leishmaniasis in the BALB/c mouse: a comparison of the efficacy of a nonionic surfactant formulation of sodium stibogluconate with those of three proprietary formulations of amphotericin B
    • Mullen, A. B., A. J. Baillie, and K. C. Carter. 1998. Visceral leishmaniasis in the BALB/c mouse: a comparison of the efficacy of a nonionic surfactant formulation of sodium stibogluconate with those of three proprietary formulations of amphotericin B. Antimicrob. Agents Chemother. 42:2722-2725.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2722-2725
    • Mullen, A.B.1    Baillie, A.J.2    Carter, K.C.3
  • 45
    • 79951676877 scopus 로고    scopus 로고
    • Oral putrescine restores virulence of ornithine decarboxylase-deficient Leishmania donovani in mice
    • Olenyik, T., C. Gilroy, and B. Ullman. 2011. Oral putrescine restores virulence of ornithine decarboxylase-deficient Leishmania donovani in mice. Mol. Biochem. Parasitol. 176:109-111.
    • (2011) Mol. Biochem. Parasitol. , vol.176 , pp. 109-111
    • Olenyik, T.1    Gilroy, C.2    Ullman, B.3
  • 46
    • 0028067923 scopus 로고
    • Formation of functional cross-species heterodimers of ornithine decarboxylase
    • Osterman, A., N. V. Grishin, L. N. Kinch, and M. A. Phillips. 1994. Formation of functional cross-species heterodimers of ornithine decarboxylase. Biochemistry 33:13662-13667.
    • (1994) Biochemistry , vol.33 , pp. 13662-13667
    • Osterman, A.1    Grishin, N.V.2    Kinch, L.N.3    Phillips, M.A.4
  • 48
    • 60649087303 scopus 로고    scopus 로고
    • Leishmania major lacking arginase (ARG) are auxotrophic for polyamines but retain infectivity to susceptible BALB/c mice
    • Reguera, R. M., R. Balana-Fouce, M. Showalter, S. Hickerson, and S. M. Beverley. 2009. Leishmania major lacking arginase (ARG) are auxotrophic for polyamines but retain infectivity to susceptible BALB/c mice. Mol. Biochem. Parasitol. 165:48-56.
    • (2009) Mol. Biochem. Parasitol. , vol.165 , pp. 48-56
    • Reguera, R.M.1    Balana-Fouce, R.2    Showalter, M.3    Hickerson, S.4    Beverley, S.M.5
  • 49
    • 0028819048 scopus 로고
    • Fluorinated analogues of L-ornithine are powerful inhibitors of ornithine decarboxylase and cell growth of Leishmania infantum promastigotes
    • Reguera, R. M., R. B. Fouce, J. C. Cubria, M. L. Bujidos, and D. Ordonez. 1995. Fluorinated analogues of L-ornithine are powerful inhibitors of ornithine decarboxylase and cell growth of Leishmania infantum promastigotes. Life Sci. 56:223-230.
    • (1995) Life Sci , vol.56 , pp. 223-230
    • Reguera, R.M.1    Fouce, R.B.2    Cubria, J.C.3    Bujidos, M.L.4    Ordonez, D.5
  • 50
    • 0035400392 scopus 로고    scopus 로고
    • Genetic analysis of spermidine synthase from Leishmania donovani
    • Roberts, S. C., et al. 2001. Genetic analysis of spermidine synthase from Leishmania donovani. Mol. Biochem. Parasitol. 115:217-226.
    • (2001) Mol. Biochem. Parasitol. , vol.115 , pp. 217-226
    • Roberts, S.C.1
  • 52
    • 2542428547 scopus 로고    scopus 로고
    • Arginase plays a pivotal role in polyamine precursor metabolism in Leishmania
    • Roberts, S. C., et al. 2004. Arginase plays a pivotal role in polyamine precursor metabolism in Leishmania. Characterization of gene deletion mutants. J. Biol. Chem. 279:23668-23678.
    • (2004) Characterization of gene deletion mutants. J. Biol. Chem. , vol.279 , pp. 23668-23678
    • Roberts, S.C.1
  • 53
    • 33846605975 scopus 로고    scopus 로고
    • Leishmania donovani polyamine biosynthetic enzyme overproducers as tools to investigate the mode of action of cytotoxic polyamine analogs
    • Roberts, S. C., et al. 2007. Leishmania donovani polyamine biosynthetic enzyme overproducers as tools to investigate the mode of action of cytotoxic polyamine analogs. Antimicrob. Agents Chemother. 51:438-445.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 438-445
    • Roberts, S.C.1
  • 54
    • 0037884861 scopus 로고    scopus 로고
    • Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania
    • Robinson, K. A., and S. M. Beverley. 2003. Improvements in transfection efficiency and tests of RNA interference (RNAi) approaches in the protozoan parasite Leishmania. Mol. Biochem. Parasitol. 128:217-228.
    • (2003) Mol. Biochem. Parasitol. , vol.128 , pp. 217-228
    • Robinson, K.A.1    Beverley, S.M.2
  • 55
    • 0030754481 scopus 로고    scopus 로고
    • Alpha-difluoromethylornithine-resistant cell lines obtained after one-step selection of Leishmania mexicana promastigote cultures
    • Sanchez, C. P., et al. 1997. Alpha-difluoromethylornithine-resistant cell lines obtained after one-step selection of Leishmania mexicana promastigote cultures. Biochem. J. 324(Pt 3):847-853.
    • (1997) Biochem. J. , vol.324 , Issue.PART 3 , pp. 847-853
    • Sanchez, C.P.1
  • 56
    • 0001054364 scopus 로고
    • Clinical aspects of inhibition of ornithine decarboxylase with emphasis on therapeutic trials of eflornithine (DFMO) in cancer and protozoan diseases
    • P. P. McCann, A. E. Pegg, and A. Sjoerdsma (ed.)Academic Press, Orlando, FL
    • Schechter, P. J., J. L. R. Barlow, and A. Sjoerdsma. 1987. Clinical aspects of inhibition of ornithine decarboxylase with emphasis on therapeutic trials of eflornithine (DFMO) in cancer and protozoan diseases, p. 345-364. In P. P. McCann, A. E. Pegg, and A. Sjoerdsma (ed.), Inhibition of polyamine metabolism: biological significance and basis for new therapies. Academic Press, Orlando, FL.
    • (1987) Inhibition of polyamine metabolism: biological significance and basis for new therapies , pp. 345-364
    • Schechter, P.J.1    Barlow, J.L.R.2    Sjoerdsma, A.3
  • 58
    • 0019972095 scopus 로고
    • The trypanocidal activity of various aromatic bisguanylhydrazones in vivo
    • Ulrich, P., R. W. Grady, and A. Cerami. 1982. The trypanocidal activity of various aromatic bisguanylhydrazones in vivo. Drug Dev. Res. 2:219-228.
    • (1982) Drug Dev. Res. , vol.2 , pp. 219-228
    • Ulrich, P.1    Grady, R.W.2    Cerami, A.3
  • 59
    • 0022194481 scopus 로고
    • Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-alpha-difluoromethylornithine), an inhibitor of ornithine decarboxylase; first field trial
    • Van Nieuwenhove, S., et al. 1985. Treatment of gambiense sleeping sickness in the Sudan with oral DFMO (DL-alpha-difluoromethylornithine), an inhibitor of ornithine decarboxylase; first field trial. Trans. R. Soc. Trop. Med. Hyg. 79:692-698.
    • (1985) Trans. R. Soc. Trop. Med. Hyg. , vol.79 , pp. 692-698
    • Van Nieuwenhove, S.1
  • 60
    • 15744396294 scopus 로고    scopus 로고
    • Immunopathogenesis of infection with the visceralizing Leishmania species
    • Wilson, M. E., S. M. Jeronimo, and R. D. Pearson. 2005. Immunopathogenesis of infection with the visceralizing Leishmania species. Microb. Pathog. 8:147-160.
    • (2005) Microb. Pathog. , vol.38 , pp. 147-160
    • Wilson, M.E.1    Jeronimo, S.M.2    Pearson, R.D.3
  • 61
    • 34447554595 scopus 로고    scopus 로고
    • Structure and mechanism of spermidine synthases
    • Wu, H., et al. 2007. Structure and mechanism of spermidine synthases. Biochemistry 46:8331-8339.
    • (2007) Biochemistry , vol.46 , pp. 8331-8339
    • Wu, H.1
  • 62
    • 66149158543 scopus 로고    scopus 로고
    • RNA interferencemediated silencing in ornithine decarboxylase and spermidine synthase genes in Trypanosoma brucei provides insight into regulation of polyamine biosynthesis
    • Xiao, Y., D. E. McCloskey, and M. A. Phillips. 2009. RNA interferencemediated silencing in ornithine decarboxylase and spermidine synthase genes in Trypanosoma brucei provides insight into regulation of polyamine biosynthesis. Eukaryot. Cell 8:747-755.
    • (2009) Eukaryot. Cell , vol.8 , pp. 747-755
    • Xiao, Y.1    McCloskey, D.E.2    Phillips, M.A.3


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