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Referencias:

• Agusti, R., Couto, A.S., Campetella, O.E., Frasch, A.C.C., de Lederkremer, R.M., The trans-sialidase of Trypanosoma cruzi is anchored by two different lipids (1997) Glycobiology, 7, pp. 731-735
• Agusti, R., Couto, A.S., Campetella, O., Frasch, A.C., de Lederkremer, R.M., Structure of the glycosylphosphatidylinositol-anchor of the trans-sialidase from Trypanosoma cruzi metacyclic trypomastigote forms (1998) Mol Biochem Parasitol, 97, pp. 123-131
• Agusti, R., Paris, G., Ratier, L., Frasch, A.C., de Lederkremer, R.M., Lactose derivatives are inhibitors of Trypanosoma cruzi trans-sialidase activity toward conventional substrates in vitro and in vivo (2004) Glycobiology, 14, pp. 659-670
• Agusti, R., Giorgi, M.E., Mendoza, V.M., Gallo-Rodriguez, C., de Lederkremer, R.M., Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose (2007) Bioorg Med Chem, 15, pp. 2611-2616
• Alvarez, P., Buscaglia, C.A., Campetella, O., Improving protein pharmacokinetics by genetic fusion to simple amino acid sequences (2004) J Biol Chem, 279, pp. 3375-3381
• Blejer, J.L., Sartor, P.A., Bottasso, O., Salamone, H.J., Leguizamón, M.S., Transsialidase inhibition assay for the detection of Trypanosoma cruzi infection in blood donor samples from Argentina (2008) Vox Sang, 95, pp. 189-196
• Buscaglia, C.A., Alfonso, J., Campetella, O., Frasch, A.C., Tandem amino acid repeats from Trypanosoma cruzi shed antigens increase the half-life of proteins in blood (1999) Blood, 93, pp. 2025-2032
• Buschiazzo, A., Frasch, A.C., Campetella, O., Medium scale production and purication to homogeneity of a recombinant trans-sialidase from Trypanosoma cruzi (1996) Cell Mol Biol (Noisy-le-grand), 42, pp. 703-710
• 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
• Ferrero-Garcia, M.A., Trombetta, S.E., Sanchez, D.O., Reglero, A., Frasch, A.C., Parodi, A.J., The action of Trypanosoma cruzi trans-sialidase on glycolipids and glycoproteins (1993) Eur J Biochem, 213, pp. 765-771
• Frasch, A.C., Functional diversity in the trans-sialidase and mucin families in Trypanosoma cruzi (2000) Parasitol Today, 16, pp. 282-286
• Kinoshita, M., Inagake, K., Kawabata, A., Kuroda, R., Oda, Y., Kakehi, K., Fluorometric determination of mucin-type glycoproteins by the galactose oxidase-peroxidase method (2000) Anal Biochem, 284, pp. 87-92
• Kuhn, R., Baer, H.H., Seeliger, A., Zur Methylierung Von N-Acetylglucosamin-Derivaten (1958) Lieb Ann, 611, pp. 236-241
• de Lederkremer, R.M., Agusti, R., Glycobiology of Trypanosoma cruzi (2009) Adv Carbohydr Chem Biochem, 62, pp. 311-366
• Lee, S.G., Kim, B.G., Development of spectrophotometric method for monitoring trans-sialidase reaction and its application (2000) Biotechnol Lett, 22, pp. 819-823
• Leguizamón, M.S., Campetella, O.E., González Cappa, S.M., Frasch, A.C., Mice infected with Trypanosoma cruzi produce antibodies against the enzymatic domain of trans-sialidase that inhibit its activity (1994) Infect Immun, 62, pp. 3441-3446
• Leguizamón, M.S., Campetella, O., Russomando, G., Almiron, M., Guillen, I., González Cappa, S.M., Frasch, A.C., Antibodies inhibiting Trypanosoma cruzi trans-sialidase activity in sera from human infections (1994) J Infect Dis, 170, pp. 1570-1574
• Leguizamón, M.S., Russomando, G., Luquetti, A., Rassi, A., Almiron, M., GonzálezCappa, S.M., Frasch, A.C., Campetella, O., Long-lasting antibodies de-tected by a trans-sialidase inhibition assay of sera from parasite-free, serologically cured chagasic patients (1997) J Infect Dis, 175, pp. 1272-1275
• Leguizamón, M.S., Mocetti, E., Garcia Rivello, H., Argibay, P., Campetella, O., Trans-sialidase from Trypanosoma cruzi induces apoptosis in cells from the immune system in vivo (1999) J Infect Dis, 180, pp. 1398-1402
• Lineweaver, G., Burk, D., The determination of enzyme dissociation constants (1934) J Am Chem Soc, 56, pp. 658-666
• Mohanty, J.G., Jaffe, J.S., Schulman, E.S., Raible, D.G., A highly sensitive uorescent micro-assay of H2O2 release from activated human leukocytes using a dihydroxyphenoxazine derivative (1997) J Immunol Methods, 202, pp. 133-141
• Mucci, J., Hidalgo, A., Mocetti, E., Argibay, P.F., Leguizamón, M.S., Campetella, O., Thymocyte depletion in Trypanosoma cruzi infection is mediated by trans-sialidase-induced apoptosis on nurse cells complex (2002) Proc Natl Acad Sci USA, 99, pp. 3896-3901
• Mucci, J., Mocetti, E., Leguizamón, M.S., Campetella, O., A sexual dimorphism in intrathymic sialylation survey is revealed by the trans-sialidase from Trypanosoma cruzi (2005) J Immunol, 174, pp. 4545-4550
• Mucci, J., Risso, M.G., Leguizamón, M.S., Frasch, A.C., Campetella, O., The trans-sialidase from Trypanosoma cruzi triggers apoptosis by target cell sialylation (2006) Cell Microbiol, 8, pp. 1086-1095
• Nagamune, K., Acosta-Serrano, A., Uemura, H., Brun, R., Kunz-Renggli, C., Maeda, Y., Ferguson, M.A., Kinoshita, T., Surface sialic acids taken from the host allow trypanosome survival in tsetse y vectors (2004) J Exp Med, 199, pp. 1445-1450
• Nayak, D.P., Reichl, U., Neuraminidase activity assays for monitoring MDCK cell culture derived inuenza virus (2004) J Virol Methods, 122, pp. 9-15
• Neres, J., Buschiazzo, A., Alzari, P.M., Walsh, L., Douglas, K.T., Continuous uorimetric assay for high-throughput screening of inhibitors of trans-sialidase from Trypanosoma cruzi (2006) Anal Biochem, 357, pp. 302-304
• Neres, J., Brewer, M.L., Ratier, L., Botti, H., Buschiazzo, A., Edwards, P.N., Mortenson, P.N., Frasch, A.C., Discovery of novel inhibitors of Trypanosoma cruzi trans-sialidase from in silico screening (2009) Bioorg Med Chem Lett, 19, pp. 589-596
• Pereira-Chioccola, V.L., Acosta-Serrano, A., Correia de Almeida, I., Ferguson, M.A., Souto-Padron, T., Rodrigues, M.M., Travassos, L.R., Schenkman, S., Mucin-like molecules form a negatively charged coat that protects Trypanosoma cruzi trypomastigotes from killing by human anti-alphagalactosyl antibodies (2000) J Cell Sci, 113, pp. 1299-1307
• Piochon, M., Legault, J., Gauthier, C., Pichette, A., Synthesis and cytotoxicity evaluation of natural α-bisabolol β-D-fucopyranoside and analogues (2009) Phytochemistry, 70, pp. 228-236
• Ratier, L., Urrutia, M., Paris, G., Zarebski, L., Frasch, A.C., Goldbaum, F.A., Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies (2008) PLoS One, 3, pp. e3524
• Ribeirão, M., Pereira-Chioccola, V.L., Eichinger, D., Rodrigues, M.M., Schenkman, S., Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase (1997) Glycobiology, 7, pp. 1237-1246
• Risso, M.G., Pitcovsky, T.A., Caccuri, R.L., Campetella, O., Leguizamón, M.S., Immune system pathogenesis is prevented by the neutralization of the systemic trans-sialidase from Trypanosoma cruzi during severe infections (2007) Parasitology, 134, pp. 503-510
• Ross, A.J., Ivanova, I.A., Ferguson, M.A.J., Nikolaev, A.V., Parasite glycoconjugates. Part 11. Preparation of phosphodisaccharide synthetic probes, substrate analogues for the elongating α-D-mannopyranosylphosphate transferase in the Leishmania (2001) J Chem Soc Perkin Trans, 1, pp. 72-81
• Schenkman, S., Jiang, M.S., Hart, G.W., Nussenzweig, V., A novel cell surface trans-sialidase of Trypanosoma cruzi generates a stage-specic epitope required for invasion of mammalian cells (1991) Cell, 65, pp. 1117-1125
• Schrader, S., Tiralongo, E., Paris, G., Yoshino, T., Schauer, R., A nonradioactive 96-well plate assay for screening of trans-sialidase activity (2003) Anal Biochem, 322, pp. 139-147
• Schrader, S., Schauer, R., Nonradioactive trans-sialidase screening assay (2007) Methods in Molecular Biology. Glycobiology Protocols., 347, pp. 93-107. , Brockhausen I, editor., Totowa, NJ: Humana Press, Inc
• Tiralongo, E., Schrader, S., Lange, H., Lemke, H., Tiralongo, J., Schauer, R., Two trans-sialidase forms with different sialic acid transfer and sialidase activities from Trypanosoma congolense (2003) J Biol Chem, 278, pp. 23301-23310
• Tomlinson, S., Pontes de Carvalho, L.C., Vandekerckhove, F., Nussenzweig, V., Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement (1994) J Immunol, 153, pp. 3141-3147
• Veh, R.W., Michalski, J., Corfield, A.P., Sander-Wewer, M., Gies, D., Schauer, R., New chromatographic system for the rapid analysis and preparation of colostrum sialyloligosaccharides (1981) J Chromatogr A, 212, pp. 313-322
• Williamson, Y.M., Gowrisankar, R., Longo, D.L., Facklam, R., Gipson, I.K., Ades, E.P., Carlone, G.M., Sampson, J.S., Adherence of nontypeable Streptococcus pneumoniae to human conjunctival epithelial cells (2008) Microb Pathogen, 44, pp. 175-185

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