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Volumn 2011, Issue 1, 2011, Pages

Trypanosoma cruzi coexpressing ornithine decarboxylase and green fluorescence proteins as a tool to study the role of polyamines in chagas disease pathology

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; ORNITHINE; ORNITHINE DECARBOXYLASE; POLYAMINE;

EID: 84859803382     PISSN: 20900406     EISSN: 20900414     Source Type: Journal    
DOI: 10.4061/2011/657460     Document Type: Article
Times cited : (14)

References (68)
  • 1
    • 34547654456 scopus 로고    scopus 로고
    • Targeting the polyamine biosynthetic enzymes: A promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis
    • DOI 10.1007/s00726-007-0537-9, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Heby O., Persson L., Rentala M., Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis. Amino Acids 2007 33 2 359 366 2-s2.0-34547654456 10.1007/s00726-007-0537-9 (Pubitemid 47222983)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 359-366
    • Heby, O.1    Persson, L.2    Rentala, M.3
  • 3
    • 27244448634 scopus 로고    scopus 로고
    • Opinion: The Trypanosoma cruzi - Host-cell interplay: Location, invasion, retention
    • DOI 10.1038/nrmicro1249, PII N1249
    • Andrade L. O., Andrews N. W., Opinion: the Trypanosoma cruzi - host-cell interplay: location, invasion, retention. Nature Reviews Microbiology 2005 3 10 819 823 2-s2.0-27244448634 10.1038/nrmicro1249 (Pubitemid 41518742)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.10 , pp. 819-823
    • Andrade, L.O.1    Andrews, N.W.2
  • 4
    • 0035340990 scopus 로고    scopus 로고
    • The life cycle of Trypanosoma cruzi revisited
    • DOI 10.1016/S0020-7519(01)00153-9, PII S0020751901001539
    • Tyler K. M., Engman D. M., The life cycle of Trypanosoma cruzi revisited. International Journal for Parasitology 2001 31 5-6 472 481 2-s2.0-0035340990 10.1016/S0020-7519(01)00153-9 (Pubitemid 32382045)
    • (2001) International Journal for Parasitology , vol.31 , Issue.5-6 , pp. 472-481
    • Tyler, K.M.1    Engman, D.M.2
  • 5
    • 0142105416 scopus 로고    scopus 로고
    • Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes
    • DOI 10.1093/emboj/cdg518
    • Kohl L., Robinson D., Bastin P., Novel roles for the flagellum in cell morphogenesis and cytokinesis of trypanosomes. The EMBO Journal 2003 22 20 5336 5346 2-s2.0-0142105416 10.1093/emboj/cdg518 (Pubitemid 37279944)
    • (2003) EMBO Journal , vol.22 , Issue.20 , pp. 5336-5346
    • Kohl, L.1    Robinson, D.2    Bastin, P.3
  • 6
    • 58149398242 scopus 로고    scopus 로고
    • The autophagic pathway is a key component in the lysosomal dependent entry of Trypanosoma cruzi into the host cell
    • 2-s2.0-58149398242
    • Romano P. S., Arboit M. A., Vázquez C. L., Colombo M. I., The autophagic pathway is a key component in the lysosomal dependent entry of Trypanosoma cruzi into the host cell. Autophagy 2009 5 1 6 18 2-s2.0-58149398242
    • (2009) Autophagy , vol.5 , Issue.1 , pp. 6-18
    • Romano, P.S.1    Arboit, M.A.2    Vázquez, C.L.3    Colombo, M.I.4
  • 8
    • 0033763977 scopus 로고    scopus 로고
    • The use of the green fluorescent protein to monitor and improve transfection in Trypanosoma cruzi
    • 2-s2.0-0033763977 10.1016/S0166-6851(00)00309-1
    • Ramirez M. I., Yamauchi L. M., De Freitas L. H. G., Uemura H., Schenkman S., The use of the green fluorescent protein to monitor and improve transfection in Trypanosoma cruzi. Molecular and Biochemical Parasitology 2000 111 1 235 240 2-s2.0-0033763977 10.1016/S0166-6851(00)00309-1
    • (2000) Molecular and Biochemical Parasitology , vol.111 , Issue.1 , pp. 235-240
    • Ramirez, M.I.1    Yamauchi, L.M.2    De Freitas, L.H.G.3    Uemura, H.4    Schenkman, S.5
  • 9
    • 0018829957 scopus 로고
    • Stimulation of deoxyribonucleic acid replication fork movement by spermidine analogs in polyamine-deficient Escherichia coli
    • Geiger L. E., Morris D. R., Stimulation of deoxyribonucleic acid replication fork movement by spermidine analogs in polyamine-deficient Escherichia coli. Journal of Bacteriology 1980 141 3 1192 1198 2-s2.0-0018829957 (Pubitemid 10076143)
    • (1980) Journal of Bacteriology , vol.141 , Issue.3 , pp. 1192-1198
    • Geiger, L.E.1    Morris, D.R.2
  • 10
    • 0019784427 scopus 로고
    • Initiation, elongation and termination of polypeptide synthesis in cell-free systems from polyamine-deficient bacteria
    • Algranati I. D., Goldemberg S. H., Initiation, elongation and termination of polypeptide synthesis in cell-free systems from polyamine-deficient bacteria. Biochemical and Biophysical Research Communications 1981 103 1 8 15 2-s2.0-0019784427 (Pubitemid 12211067)
    • (1981) Biochemical and Biophysical Research Communications , vol.103 , Issue.1 , pp. 8-15
    • Algranati, I.D.1    Goldemberg, S.H.2
  • 12
    • 0345688128 scopus 로고    scopus 로고
    • A perspective of polyamine metabolism
    • DOI 10.1042/BJ20031327
    • Wallace H. M., Fraser A. V., Hughes A., A perspective of polyamine metabolism. Biochemical Journal 2003 376 1 1 14 2-s2.0-0345688128 10.1042/BJ20031327 (Pubitemid 37487199)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 1-14
    • Wallace, H.M.1    Fraser, A.V.2    Hughes, A.3
  • 14
    • 0002960266 scopus 로고
    • Inhibition of polyamine metabolism: Biological significance and bases for new therapies
    • Orlando, Fla, USA Academic Press
    • Bacchi C. J., McCann P. P., McCann P. P., Pegg A. E., Sjoerdsma A., Inhibition of polyamine metabolism: biological significance and bases for new therapies. Polyamines 1987 Orlando, Fla, USA Academic Press 317 344
    • (1987) Polyamines , pp. 317-344
    • Bacchi, C.J.1    McCann, P.P.2    McCann, P.P.3    Pegg, A.E.4    Sjoerdsma, A.5
  • 15
    • 77953064754 scopus 로고    scopus 로고
    • Polyamine metabolism in Trypanosoma cruzi: Studies on the expression and regulation of heterologous genes involved in polyamine biosynthesis
    • 2-s2.0-77953064754 10.1007/s00726-009-0425-6
    • Algranati I. D., Polyamine metabolism in Trypanosoma cruzi: studies on the expression and regulation of heterologous genes involved in polyamine biosynthesis. Amino Acids 2010 38 2 645 651 2-s2.0-77953064754 10.1007/s00726-009-0425-6
    • (2010) Amino Acids , vol.38 , Issue.2 , pp. 645-651
    • Algranati, I.D.1
  • 16
    • 0019194217 scopus 로고
    • Polyamine metabolism: A potential therapeutic target in trypanosomes
    • Bacchi C. J., Nathan H. C., Hutner S. H., Polyamine metabolism: a potential therapeutic target in trypanosomes. Science 1980 210 4467 332 334 2-s2.0-0019194217 (Pubitemid 11208468)
    • (1980) Science , vol.210 , Issue.4467 , pp. 332-334
    • Bacchi, C.J.1    Nathan, H.C.2    Hutner, S.H.3
  • 17
    • 0026660462 scopus 로고
    • Efficacy and toxicity of eflornithine for treatment of Trypanosoma brucei gambiense sleeping sickness
    • 2-s2.0-0026660462 10.1016/0140-6736(92)92180-N
    • Milord F., Pépin J., Loko L., Ethier L., Mpia B., Efficacy and toxicity of eflornithine for treatment of Trypanosoma brucei gambiense sleeping sickness. The Lancet 1992 340 8820 652 655 2-s2.0-0026660462 10.1016/0140-6736(92)92180-N
    • (1992) The Lancet , vol.340 , Issue.8820 , pp. 652-655
    • Milord, F.1    Pépin, J.2    Loko, L.3    Ethier, L.4    Mpia, B.5
  • 18
    • 0033578253 scopus 로고    scopus 로고
    • Eflornithine for African sleeping sickness
    • 2-s2.0-0033578253
    • Sjoerdsma A., Schechter P. J., Eflornithine for African sleeping sickness. The Lancet 1999 354 9174 254 2-s2.0-0033578253
    • (1999) The Lancet , vol.354 , Issue.9174 , pp. 254
    • Sjoerdsma, A.1    Schechter, P.J.2
  • 19
    • 0022450919 scopus 로고
    • Recent advances in the biochemistry of polyamines in eukaryocytes
    • Pegg A. E., Recent advances in the biochemistry of polyamines in eukaryocytes. Biochemical Journal 1986 234 2 249 262 2-s2.0-0022450919 (Pubitemid 16049822)
    • (1986) Biochemical Journal , vol.234 , Issue.2 , pp. 249-262
    • Pegg, A.E.1
  • 20
    • 0041461862 scopus 로고    scopus 로고
    • Bis(glutathionyl)spermine and other novel trypanothione analogues in Trypanosoma cruzi
    • DOI 10.1074/jbc.M302750200
    • Ariyanayagam M. R., Oza S. L., Mehlert A., Fairlamb A. H., Bis(glutathionyl)spermine and other novel trypanothione analogues in Trypanosoma cruzi. Journal of Biological Chemistry 2003 278 30 27612 27619 2-s2.0-0041461862 10.1074/jbc.M302750200 (Pubitemid 36899947)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27612-27619
    • Ariyanayagam, M.R.1    Oza, S.L.2    Mehlert, A.3    Fairlamb, A.H.4
  • 21
    • 0026788035 scopus 로고
    • Polyamines as a chemotaxonomic marker in bacterial systematics
    • 2-s2.0-0026788035
    • Hamana K., Matsuzaki S., Polyamines as a chemotaxonomic marker in bacterial systematics. Critical Reviews in Microbiology 1992 18 4 261 283 2-s2.0-0026788035
    • (1992) Critical Reviews in Microbiology , vol.18 , Issue.4 , pp. 261-283
    • Hamana, K.1    Matsuzaki, S.2
  • 23
    • 0018088697 scopus 로고
    • Polyamines in rapid growth and cancer
    • Janne J., Poso H., Raina A., Polyamines in rapid growth and cancer. Biochimica et Biophysica Acta 1978 473 3-4 241 293 2-s2.0-0018088697 (Pubitemid 8304209)
    • (1978) Biochimica et Biophysica Acta , vol.473 , Issue.3-4 , pp. 241-293
    • Janne, J.1    Poso, H.2    Raina, A.3
  • 24
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg A. E., Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Research 1988 48 4 759 774 2-s2.0-0023881236 (Pubitemid 18061860)
    • (1988) Cancer Research , vol.48 , Issue.4 , pp. 759-774
    • Pegg, A.E.1
  • 25
    • 0022531132 scopus 로고
    • Biosynthesis and metabolism of arginine in bacteria
    • Cunin R., Glansdorff N., Pierard A., Stalon V., Biosynthesis and metabolism of arginine in bacteria. Microbiological Reviews 1986 50 3 314 352 2-s2.0-0022531132 (Pubitemid 16017072)
    • (1986) Microbiological Reviews , vol.50 , Issue.3 , pp. 314-352
    • Cunin, R.1    Glansdorff, N.2    Pierard, A.3    Stalon, V.4
  • 26
    • 0000450238 scopus 로고
    • L-arginine carboxy-lyase of higher plants and its relation to potassium nutrition
    • 2-s2.0-0000450238
    • Smith T. A., L-arginine carboxy-lyase of higher plants and its relation to potassium nutrition. Phytochemistry 1963 2 3 241 252 2-s2.0-0000450238
    • (1963) Phytochemistry , vol.2 , Issue.3 , pp. 241-252
    • Smith, T.A.1
  • 27
    • 33645098156 scopus 로고    scopus 로고
    • Expression of arginine decarboxylase in brain regions and neuronal cells
    • 2-s2.0-33645098156 10.1111/j.1471-4159.2005.03544.x
    • Iyo A. H., Zhu M. Y., Ordway G. A., Regunathan S., Expression of arginine decarboxylase in brain regions and neuronal cells. Journal of Neurochemistry 2006 96 4 1042 1050 2-s2.0-33645098156 10.1111/j.1471-4159.2005.03544.x
    • (2006) Journal of Neurochemistry , vol.96 , Issue.4 , pp. 1042-1050
    • Iyo, A.H.1    Zhu, M.Y.2    Ordway, G.A.3    Regunathan, S.4
  • 28
    • 1642450643 scopus 로고    scopus 로고
    • Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine
    • DOI 10.1016/j.bbagen.2003.11.006
    • Zhu M. Y., Iyo A., Piletz J. E., Regunathan S., Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochimica et Biophysica Acta 2004 1670 2 156 164 2-s2.0-1642450643 10.1016/j.bbagen.2003.11. 006 (Pubitemid 38115860)
    • (2004) Biochimica et Biophysica Acta - General Subjects , vol.1670 , Issue.2 , pp. 156-164
    • Zhu, M.-Y.1    Iyo, A.2    Piletz, J.E.3    Regunathan, S.4
  • 31
    • 0020406954 scopus 로고
    • 1-acetyltransferase from rat liver
    • Della Ragione F., Pegg A. E., Purification and characterization of spermidine/spermine N-acetyltransferase from rat liver. Biochemistry 1982 21 24 6152 6158 2-s2.0-0020406954 (Pubitemid 13141618)
    • (1982) Biochemistry , vol.21 , Issue.24 , pp. 6152-6158
    • Della Ragione, F.1    Pegg, A.E.2
  • 32
    • 0037442525 scopus 로고    scopus 로고
    • Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion
    • DOI 10.1042/BJ20021779
    • Vujcic S., Liang P., Diegelman P., Kramer D. L., Porter C. W., Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochemical Journal 2003 370 1 19 28 2-s2.0-0037442525 10.1042/BJ20021779 (Pubitemid 36259415)
    • (2003) Biochemical Journal , vol.370 , Issue.1 , pp. 19-28
    • Vujcic, S.1    Liang, P.2    Diegelman, P.3    Kramer, D.L.4    Porter, C.W.5
  • 33
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • 2-s2.0-0026793462
    • Fairlamb A. H., Cerami A., Metabolism and functions of trypanothione in the kinetoplastida. Annual Review of Microbiology 1992 46 695 729 2-s2.0-0026793462
    • (1992) Annual Review of Microbiology , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 34
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb A. H., Blackburn P., Ulrich P., Chait B. T., Cerami A., Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 1985 227 4693 1485 1487 2-s2.0-0022002912 (Pubitemid 15146992)
    • (1985) Science , vol.227 , Issue.4693 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3
  • 35
    • 0021933665 scopus 로고
    • Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids
    • DOI 10.1016/0166-6851(85)90037-4
    • Fairlamb A. H., Cerami A., Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids. Molecular and Biochemical Parasitology 1985 14 2 187 198 2-s2.0-0021933665 (Pubitemid 15174629)
    • (1985) Molecular and Biochemical Parasitology , vol.14 , Issue.2 , pp. 187-198
    • Fairlamb, A.H.1    Cerami, A.2
  • 36
    • 0035941059 scopus 로고    scopus 로고
    • Spermidine is essential for normal proliferation of trypanosomatid protozoa
    • DOI 10.1016/S0014-5793(01)03091-5, PII S0014579301030915
    • González N. S., Huber A., Algranati I. D., Spermidine is essential for normal proliferation of trypanosomatid protozoa. FEBS Letters 2001 508 3 323 326 2-s2.0-0035941059 10.1016/S0014-5793(01)03091-5 (Pubitemid 33135463)
    • (2001) FEBS Letters , vol.508 , Issue.3 , pp. 323-326
    • Gonzalez, N.S.1    Huber, A.2    Algranati, I.D.3
  • 37
    • 0034685624 scopus 로고    scopus 로고
    • Polyamines: Mysterious modulators of cellular functions
    • DOI 10.1006/bbrc.2000.2601
    • Igarashi K., Kashiwagi K., Polyamines: mysterious modulators of cellular functions. Biochemical and Biophysical Research Communications 2000 271 3 559 564 2-s2.0-0034685624 10.1006/bbrc.2000.2601 (Pubitemid 30444667)
    • (2000) Biochemical and Biophysical Research Communications , vol.271 , Issue.3 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 38
    • 0033049344 scopus 로고    scopus 로고
    • Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme
    • DOI 10.1016/S0014-5793(99)00804-2, PII S0014579399008042
    • Carrillo C., Cejas S., González N. S., Algranati I. D., Trypanosoma cruzi epimastigotes lack ornithine decarboxylase but can express a foreign gene encoding this enzyme. FEBS Letters 1999 454 3 192 196 2-s2.0-0033049344 10.1016/S0014-5793(99)00804-2 (Pubitemid 29304598)
    • (1999) FEBS Letters , vol.454 , Issue.3 , pp. 192-196
    • Carrillo, C.1    Cejas, S.2    Gonzalez, N.S.3    Algranati, I.D.4
  • 40
    • 0031057528 scopus 로고    scopus 로고
    • Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes
    • DOI 10.1016/S0166-6851(96)02788-0, PII S0166685196027880
    • Ariyanayagam M. R., Fairlamb A. H., Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. Molecular and Biochemical Parasitology 1997 84 1 111 121 2-s2.0-0031057528 10.1016/S0166-6851(96)02788-0 (Pubitemid 27090511)
    • (1997) Molecular and Biochemical Parasitology , vol.84 , Issue.1 , pp. 111-121
    • Ariyanayagam, M.R.1    Fairlamb, A.H.2
  • 41
    • 0141787976 scopus 로고    scopus 로고
    • Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes
    • DOI 10.1111/j.1550-7408.2003.tb00141.x
    • Carrillo C., Cejas S., Huber A., González N. S., Algranati I. D., Lack of arginine decarboxylase in Trypanosoma cruzi epimastigotes. Journal of Eukaryotic Microbiology 2003 50 5 312 316 2-s2.0-0141787976 10.1111/j.1550-7408. 2003.tb00141.x (Pubitemid 37144034)
    • (2003) Journal of Eukaryotic Microbiology , vol.50 , Issue.5 , pp. 312-316
    • Carrillo, C.1    Cejas, S.2    Huber, A.3    Gonzalez, N.S.4    Algranati, I.D.5
  • 42
  • 43
    • 0027198139 scopus 로고
    • Inhibition of S-adenosyl-L-methionine (AdoMet) decarboxylase by the decarboxylated AdoMet analog 5'-{[(Z)-4-amino-2-butenyl]methylamino}-5'- deoxyadenosine (MDL 73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell
    • Yakubu M. A., Majumder S., Kierszenbaum F., Inhibition of S-adenosyl-L-methionine (AdoMet) decarboxylase by the decarboxylated AdoMet analog 5'-{[(Z)-4-amino-2-butenyl]methylamino}-5'-deoxyadenosine (MDL 73811) decreases the capacities of Trypanosoma cruzi to infect and multiply within a mammalian host cell. Journal of Parasitology 1993 79 4 525 532 2-s2.0-0027198139 (Pubitemid 23249739)
    • (1993) Journal of Parasitology , vol.79 , Issue.4 , pp. 525-532
    • Yakubu, M.A.1    Majumder, S.2    Kierszenbaum, F.3
  • 44
    • 0011740954 scopus 로고
    • Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells
    • DOI 10.1073/pnas.84.12.4278
    • Kierszenbaum F., Wirth J. J., McCann P. P., Sjoerdsma A., Arginine decarboxylase inhibitors reduce the capacity of Trypanosoma cruzi to infect and multiply in mammalian host cells. Proceedings of the National Academy of Sciences of the United States of America 1987 84 12 4278 4282 2-s2.0-0011740954 (Pubitemid 17090917)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.12 , pp. 4278-4282
    • Kierszenbaum, F.1    Wirth, J.J.2    McCann, P.P.3    Sjoerdsma, A.4
  • 45
    • 0023227549 scopus 로고
    • Impairment of macrophage function by inhibitors of ornithine decarboxylase activity
    • Kierszenbaum F., Wirth J. J., McCann P. P., Sjoerdsma A., Impairment of macrophage function by inhibitors of ornithine decarboxylase activity. Infection and Immunity 1987 55 10 2461 2464 2-s2.0-0023227549 (Pubitemid 17136326)
    • (1987) Infection and Immunity , vol.55 , Issue.10 , pp. 2461-2464
    • Kierszenbaum, F.1    Wirth, J.J.2    McCann, P.P.3    Sjoerdsma, A.4
  • 46
    • 79951676877 scopus 로고    scopus 로고
    • Oral putrescine restores virulence of ornithine decarboxylase-deficient Leishmania donovani in mice
    • ullmanb@ohsu.edu 10.1016/j.molbiopara.2010.12.004
    • Olenyik T., Gilroy C., Ullman B., ullmanb@ohsu.edu Oral putrescine restores virulence of ornithine decarboxylase-deficient Leishmania donovani in mice. Molecular and Biochemical Parasitology 2011 176 2 109 111 10.1016/j.molbiopara.2010.12.004
    • (2011) Molecular and Biochemical Parasitology , vol.176 , Issue.2 , pp. 109-111
    • Olenyik, T.1    Gilroy, C.2    Ullman, B.3
  • 47
    • 0037192115 scopus 로고    scopus 로고
    • Metabolic pathway analysis in trypanosomes and malaria parasites
    • DOI 10.1098/rstb.2001.1040
    • Fairlamb A. H., Metabolic pathway analysis in trypanosomes and malaria parasites. Philosophical Transactions of the Royal Society B 2002 357 1417 101 107 2-s2.0-0037192115 10.1098/rstb.2001.1040 (Pubitemid 34147269)
    • (2002) Philosophical Transactions of the Royal Society B: Biological Sciences , vol.357 , Issue.1417 , pp. 101-107
    • Fairlamb, A.H.1
  • 49
    • 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
    • DOI 10.1073/pnas.94.2.397
    • Svensson F., Ceriani C., Wallström E. L., Kockum I., Algranati I. D., Heby O., Persson LO., Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain. Proceedings of the National Academy of Sciences of the United States of America 1997 94 2 397 402 2-s2.0-0031035013 10.1073/pnas.94.2.397 (Pubitemid 27053643)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.2 , pp. 397-402
    • Svensson, F.1    Ceriani, C.2    Wallstrom, E.L.3    Kockum, I.4    Algranati, I.D.5    Heby, O.6    Persson, L.7
  • 50
    • 0343416375 scopus 로고    scopus 로고
    • PRIBOTEX expression vector: A pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants
    • DOI 10.1016/S0378-1119(97)00348-X, PII S037811199700348X
    • Martínez-Calvillo S., López I., Hernández R., pRIBOTEX expression vector: a pTEX derivative for a rapid selection of Trypanosoma cruzi transfectants. Gene 1997 199 1-2 71 76 2-s2.0-0343416375 10.1016/S0378-1119(97)00348-X (Pubitemid 27448203)
    • (1997) Gene , vol.199 , Issue.1-2 , pp. 71-76
    • Martinez-Calvillo, S.1    Lopez, I.2    Hernandez, R.3
  • 51
    • 0037498106 scopus 로고    scopus 로고
    • Integration of expression vectors into the ribosomal locus of Trypanosoma cruzi
    • DOI 10.1016/S0378-1119(03)00502-X
    • Lorenzi H. A., Vazquez M. P., Levin M. J., Integration of expression vectors into the ribosomal locus of Trypanosoma cruzi. Gene 2003 310 1-2 91 99 2-s2.0-0037498106 10.1016/S0378-1119(03)00502-X (Pubitemid 36703303)
    • (2003) Gene , vol.310 , Issue.1-2 , pp. 91-99
    • Lorenzi, H.A.1    Vazquez, M.P.2    Levin, M.J.3
  • 52
    • 84755161369 scopus 로고    scopus 로고
    • Polyamine biosynthesis in Phytomonas: Biochemical characterisation of a very unstable ornithine decarboxylase
    • 2-s2.0-77952102754 10.1016/j.ijpara.2010.04.003
    • Marcora M. S., Cejas S., González N. S., Carrillo C., Algranati I. D., Polyamine biosynthesis in Phytomonas: biochemical characterisation of a very unstable ornithine decarboxylase. International Journal for Parasitology 2010 40 1389 1394 2-s2.0-77952102754 10.1016/j.ijpara.2010.04.003
    • (2010) International Journal for Parasitology , vol.40 , pp. 1389-1394
    • Marcora, M.S.1    Cejas, S.2    González, N.S.3    Carrillo, C.4    Algranati, I.D.5
  • 53
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • 2-s2.0-0017184389
    • Bradford M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 1976 72 1-2 248 254 2-s2.0-0017184389
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 54
    • 0030754481 scopus 로고    scopus 로고
    • α-Difluoromethylornithine-resistant cell lines obtained after one-step selection of Leishmania mexicana promastigote cultures
    • Sánchez C. P., Mucci J., González N. S., Ochoa A., Zakin M. M., Algranati I. D., α -difluoromethylornithine-resistant cell lines obtained after one-step selection of Leishmania mexicana promastigote cultures. Biochemical Journal 1997 324 3 847 853 2-s2.0-0030754481 (Pubitemid 27285543)
    • (1997) Biochemical Journal , vol.324 , Issue.3 , pp. 847-853
    • Sanchez, C.P.1    Mucci, J.2    Gonzalez, N.S.3    Ochoa, A.4    Zakin, M.M.5    Algranati, I.D.6
  • 55
    • 0021933036 scopus 로고
    • Stage specific gene expression precedes morphological changes during Trypanosoma cruzi metacyclogenesis
    • DOI 10.1016/0166-6851(85)90108-2
    • Contreras V. T., Morel C. M., Goldenberg S., Stage specific gene expression precedes morphological changes during Trypanosoma cruzi metacyclogenesis. Molecular and Biochemical Parasitology 1985 14 1 83 96 2-s2.0-0021933036 (Pubitemid 15171432)
    • (1985) Molecular and Biochemical Parasitology , vol.14 , Issue.1 , pp. 83-96
    • Contreras, V.T.1    Morel, C.M.2    Goldenberg, S.3
  • 56
    • 0032833130 scopus 로고    scopus 로고
    • Expression of serum amyloid A3 mRNA by inflammatory macrophages exposed to membrane glycoconjugates from Trypanosoma cruzi
    • Ferreira L. R. P., Silva A. M., Michailowsky V., Reis L. F. L., Gazzinelli R. T., Expression of serum amyloid A3 mRNA by inflammatory macrophages exposed to membrane glycoconjugates from Trypanosoma cruzi. Journal of Leukocyte Biology 1999 66 4 593 600 2-s2.0-0032833130 (Pubitemid 29489886)
    • (1999) Journal of Leukocyte Biology , vol.66 , Issue.4 , pp. 593-600
    • Ferreira, L.R.P.1    Silva, A.M.2    Michailowsky, V.3    Reis, L.F.L.4    Gazzinelli, R.T.5
  • 57
    • 0035339822 scopus 로고    scopus 로고
    • Enzymes of carbohydrate metabolism as potential drug targets
    • PII S0020751901001552
    • Opperdoes F. R., Michels P. A. M., Enzymes of carbohydrate metabolism as potential drug targets. International Journal for Parasitology 2001 31 5-6 482 490 2-s2.0-0035339822 (Pubitemid 32382046)
    • (2001) International Journal for Parasitology , vol.31 , Issue.5-6 , pp. 482-490
    • Opperdoes, F.R.1    Michels, P.A.M.2
  • 58
    • 35448955196 scopus 로고    scopus 로고
    • Trypanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites
    • DOI 10.1016/j.bbagen.2007.08.013, PII S030441650700181X
    • Carrillo C., González N. S., Algranati I. D., Trypanosoma cruzi as a model system to study the expression of exogenous genes coding for polyamine biosynthetic enzymes. Induction of DFMO resistance in transgenic parasites. Biochimica et Biophysica Acta 2007 1770 12 1605 1611 2-s2.0-35448955196 10.1016/j.bbagen.2007.08.013 (Pubitemid 47633818)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.12 , pp. 1605-1611
    • Carrillo, C.1    Gonzalez, N.S.2    Algranati, I.D.3
  • 60
    • 0026603431 scopus 로고
    • Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation
    • 2-s2.0-0026603431 10.1016/0014-5793(92)80253-D
    • Ceriani C., González N. S., Algranati I. D., Ornithine decarboxylase from Crithidia fasciculata is metabolically unstable and resistant to polyamine down-regulation. FEBS Letters 1992 301 3 261 264 2-s2.0-0026603431 10.1016/0014-5793(92)80253-D
    • (1992) FEBS Letters , vol.301 , Issue.3 , pp. 261-264
    • Ceriani, C.1    González, N.S.2    Algranati, I.D.3
  • 61
    • 77449126859 scopus 로고    scopus 로고
    • Arginase in parasitic infections: Macrophage activation, immunosuppression, and intracellular signals
    • 683485 2-s2.0-77449126859
    • Stempin C. C., Dulgerian L. R., Garrido V. V., Cerban F. M., Arginase in parasitic infections: macrophage activation, immunosuppression, and intracellular signals. Journal of Biomedicine and Biotechnology 2010 2010 10 683485 2-s2.0-77449126859
    • (2010) Journal of Biomedicine and Biotechnology , vol.2010 , pp. 10
    • Stempin, C.C.1    Dulgerian, L.R.2    Garrido, V.V.3    Cerban, F.M.4
  • 62
    • 3142757951 scopus 로고    scopus 로고
    • L-arginine metabolism during interaction of Trypanosoma cruzi with host cells
    • DOI 10.1016/j.pt.2004.05.010, PII S1471492204001527
    • Peluffo G., Piacenza L., Irigoín F., Alvarez M. N., Radi R., L-arginine metabolism during interaction of Trypanosoma cruzi with host cells. Trends in Parasitology 2004 20 8 363 369 2-s2.0-3142757951 10.1016/j.pt.2004.05. 010 (Pubitemid 38916525)
    • (2004) Trends in Parasitology , vol.20 , Issue.8 , pp. 363-369
    • Peluffo, G.1    Piacenza, L.2    Irigoin, F.3    Alvarez, M.N.4    Radi, R.5
  • 64
    • 33744951504 scopus 로고    scopus 로고
    • Regulation of ornithine decarboxylase
    • DOI 10.1074/jbc.R500031200
    • Pegg A. E., Regulation of ornithine decarboxylase. Journal of Biological Chemistry 2006 281 21 14529 14532 2-s2.0-33744951504 10.1074/jbc.R500031200 (Pubitemid 43855154)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14529-14532
    • Pegg, A.E.1
  • 65
    • 0033146548 scopus 로고    scopus 로고
    • Arginine decarboxylase in Trypanosoma cruzi, characteristics and kinetic properties
    • 2-s2.0-0033146548
    • Hernández S., Schwarcz de Tarlovsky S., Arginine decarboxylase in Trypanosoma cruzi, characteristics and kinetic properties. Cellular and Molecular Biology 1999 45 4 383 391 2-s2.0-0033146548
    • (1999) Cellular and Molecular Biology , vol.45 , Issue.4 , pp. 383-391
    • Hernández, S.1    Schwarcz De Tarlovsky, S.2
  • 66
    • 0035912807 scopus 로고    scopus 로고
    • L-arginine-dependent suppression of apoptosis in Trypanosoma cruzi: Contribution of the nitric oxide and polyamine pathways
    • DOI 10.1073/pnas.121520398
    • Piacenza L., Peluffo G., Radi R., L-arginine-dependent suppression of apoptosis in Trypanosoma cruzi: contribution of the nitric oxide and polyamine pathways. Proceedings of the National Academy of Sciences of the United States of America 2001 98 13 7301 7306 2-s2.0-0035912807 10.1073/pnas.121520398 (Pubitemid 32567943)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.13 , pp. 7301-7306
    • Piacenza, L.1    Peluffo, G.2    Radi, R.3
  • 67
    • 0029898712 scopus 로고    scopus 로고
    • Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes
    • Le Quesne S. A., Fairlamb A. H., Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes. Biochemical Journal 1996 316 2 481 486 2-s2.0-0029898712 (Pubitemid 26182145)
    • (1996) Biochemical Journal , vol.316 , Issue.2 , pp. 481-486
    • Le Quesne, S.A.1    Fairlamb, A.H.2
  • 68
    • 0026842163 scopus 로고
    • Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi
    • 2-s2.0-0026842163
    • Majumder S., Wirth J. J., Bitonti A. J., McCann P. P., Kierszenbaum F., Biochemical evidence for the presence of arginine decarboxylase activity in Trypanosoma cruzi. Journal of Parasitology 1992 78 2 371 374 2-s2.0-0026842163
    • (1992) Journal of Parasitology , vol.78 , Issue.2 , pp. 371-374
    • Majumder, S.1    Wirth, J.J.2    Bitonti, A.J.3    McCann, P.P.4    Kierszenbaum, F.5


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