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Registro:

Documento: Artículo
Título:Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]
Autor:de Lederkremer, R.M.; Frasch, A.C.C.
Filiación:Depto. de Quimica Organica, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires 1428, Argentina
Inst. de Invest. Biotecnologicas, Univ. Nacional de Gral. San Martin, INTI, Edificio 24, 1650 San Martin, Buenos Aires, Argentina
Palabras clave:glucose; lactitol; lactobionic acid; lactose; sialidase; sialidase inhibitor; anion exchange chromatography; concentration response; donor; enzyme activity; enzyme inhibition; enzyme substrate; letter; nonhuman; priority journal; quantitative analysis; reduction; sialylation; Trypanosoma cruzi; Trypanosoma; Trypanosoma cruzi
Año:2004
Volumen:14
Número:10
DOI: http://dx.doi.org/10.1093/glycob/cwh125
Título revista:Glycobiology
Título revista abreviado:Glycobiology
ISSN:09596658
CODEN:GLYCE
CAS:glucose, 50-99-7, 84778-64-3; lactitol, 585-86-4; lactobionic acid, 96-82-2; lactose, 10039-26-6, 16984-38-6, 63-42-3, 64044-51-5; sialidase, 9001-67-6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09596658_v14_n10_p_deLederkremer

Referencias:

  • Agusti, R., Paris, G., Ratier, L., Frasch, A.C., de Lederkremer, R.M., Lactose derivatives are inhibitors of Trypanosoma cruzi transsialidase activity toward conventional substrates in vitro and in vivo (2004) Glycobiology, 14, pp. 659-670
  • Amaya, M.F., Buschiazzo, A., Nguyen, T., Alzari, P.M., The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase (2003) J. Mol. Biol., 325, pp. 773-784
  • Buschiazzo, A., Tavares, G.A., Campetella, O., Spinelli, S., Cremona, M.L., Paris, G., Amaya, M.F., Alzari, P.M., Structural basis of sialyltransferase activity in trypanosomal sialidases (2000) EMBO J., 19, pp. 16-24
  • Buschiazzo, A., Amaya, M.F., Cremona, M.L., Frasch, A.C., Alzari, P.M., The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis (2002) Mol. Cell, 10, pp. 757-768

Citas:

---------- APA ----------
de Lederkremer, R.M. & Frasch, A.C.C. (2004) . Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]. Glycobiology, 14(10).
http://dx.doi.org/10.1093/glycob/cwh125
---------- CHICAGO ----------
de Lederkremer, R.M., Frasch, A.C.C. "Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]" . Glycobiology 14, no. 10 (2004).
http://dx.doi.org/10.1093/glycob/cwh125
---------- MLA ----------
de Lederkremer, R.M., Frasch, A.C.C. "Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]" . Glycobiology, vol. 14, no. 10, 2004.
http://dx.doi.org/10.1093/glycob/cwh125
---------- VANCOUVER ----------
de Lederkremer, R.M., Frasch, A.C.C. Relative efficacy of lactose-related donors for Trypanosoma cruzi trans-sialidase [2]. Glycobiology. 2004;14(10).
http://dx.doi.org/10.1093/glycob/cwh125