A. Buschiazzo, G. A. Tavares, O. Campetella, S. Spinelli, M. L. Cremona et al.,

P. M. Alzari, Structural basis of sialyltransferase activity in trypanosomal sialidases, EMBO J, vol.19, pp.16-24, 2000.

A. C. Frasch, Trans-Sialidase, Sapa Amino Acid Repeats and the Relationship between Trypanosoma cruzi and the Mammalian Host, Parasitology, vol.108, pp.37-44, 1994.

S. Schenkman, D. Eichinger, M. E. Pereira, and V. Nussenzweig, Structural and Functional Properties of Trypanosoma Trans-Sialidase, Annu. ReV. Microbiol, vol.48, pp.499-523, 1994.

P. Scudder, J. P. Doom, M. Chuenkova, I. D. Manger, and M. E. Pereira, Enzymatic Characterization of -D-Galactoside R-2,3-Trans-Sialidase from Trypanosoma cruzi, J. Biol. Chem, vol.268, pp.9886-9891, 1993.

M. Ribeirao, V. L. Pereirachioccola, D. Eichinger, M. M. Rodrigues, and S. Schenkman, Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi transsialidase, Glycobiology, vol.7, pp.1237-1246, 1997.

J. S. Yang, S. Schenkman, and B. A. Horenstein, Primary C-13 and -secondary H-2 KIEs for trans-sialidase. A snapshot of nucleophilic participation during catalysis, Biochemistry, vol.39, pp.5902-5910, 2000.

M. F. Amaya, A. G. Watts, I. Damager, A. Wehenkel, T. Nguyen et al., Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase, Structure, vol.12, pp.775-784, 2004.

A. G. Watts, I. Damager, M. L. Amaya, A. Buschiazzo, P. Alzari et al., Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: Tyrosine is the catalytic nucleophile, J. Am. Chem. Soc, vol.125, pp.7532-7533, 2003.

A. Buschiazzo, M. F. Amaya, M. L. Cremona, A. C. Frasch, A. et al., The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis, Mol. Cell, vol.10, pp.757-768, 2002.

G. Paris, M. L. Cremona, M. F. Amaya, A. Buschiazzo, S. Giambiagi et al., Probing molecular function of trypanosomal sialidases: Single point mutations can change substrate specificity and increase hydrolytic activity, Glycobiology, vol.11, pp.305-311, 2001.

Z. Gyorgydeak, L. Szilagyi, Z. Dinya, J. , and J. , Practical route to the anomeric methyl (5-acetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-D-galacto-non-2-ulopyranosyl) onate azides, Carbohydr. Res, vol.291, pp.183-187, 1996.

M. Engstler, J. W. Talhouk, R. E. Smith, and R. Schauer, Chemical synthesis of 4-trifluoromethylumbelliferyl-R-D-N-acetylneuraminic acid glycoside and its use for the fluorometric detection of poorly expressed natural and recombinant sialidases, Anal. Biochem, vol.250, pp.176-180, 1997.

R. W. Myers, R. T. Lee, Y. C. Lee, G. H. Thomas, L. W. Reynolds et al., Synthesis of 4-Methylumbelliferyl R-Ketoside of N-Acetylneuraminic Acid and Its Use in a Fluorometric Assay for Neuraminidase, Anal. Biochem, vol.101, pp.166-174, 1980.

H. D. Ly and S. G. Withers, Mutagenesis of glycosidases, Annu. ReV. Biochem, vol.68, pp.487-522, 1999.

A. M. Macleod, T. Lindhorst, S. G. Withers, and R. A. Warren, The Acid/Base Catalyst in the Exoglucanase/Xylanase from Cellulomonas fimi Is Glutamic Acid 127: Evidence from Detailed Kinetic Studies of Mutants, Biochemistry, vol.33, pp.6371-6376, 1994.

A. M. Macleod, D. Tull, K. Rupitz, R. A. Warren, and S. G. Withers, Mechanistic consequences of mutation of active site carboxylates in a retaining -1,4-glycanase from Cellulomonas fimi, Biochemistry, vol.35, pp.13165-13172, 1996.

M. Gross and J. E. Folk, Mapping of Active Sites of Transglutaminases. 1. Activity of Guinea-Pig Liver Enzyme toward Aliphatic Amides, J. Biol. Chem, vol.248, pp.1301-1306, 1973.

W. J. Arion and R. C. Nordlie, Liver Microsomal Glucose 6-Phosphatase, Inorganic Pyrophosphatase, and Pyrophosphate-Glucose Phosphotransferase. II. Kinetic Studies, J. Biol. Chem, vol.239, pp.2752-2757, 1964.

D. C. Prasher, M. C. Carr, D. H. Ives, T. C. Tsai, and P. A. Frey, Nucleoside Phosphotransferase from Barley: Characterization and Evidence for Ping Pong Kinetics Involving Phosphoryl Enzyme, J. Biol. Chem, vol.257, pp.4931-4939, 1982.

S. Newstead, J. N. Watson, T. L. Knoll, A. J. Bennet, T. et al., Structure and mechanism of action of an inverting mutant sialidase, Biochemistry, vol.44, pp.9117-9122, 2005.