@article { ISI:000221490200008,
	title = {Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase},
	journal = {STRUCTURE},
	volume = {12},
	number = {5},
	year = {2004},
	month = {MAY},
	pages = {775-784},
	abstract = {Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the pathogenesis of a number of diseases. However, extensive studies of viral and microbial sialidases have failed to provide a comprehensive picture of their mechanistic properties, in part because the structures of competent enzyme-substrate complexes and reaction intermediates have never been described. Here we report these structures for the Trypanosoma cruzi traps-sialidase (TcTS), showing that catalysis by sialidases occurs via a similar mechanism to that of other retaining glycosidases, but with some intriguing differences that may have evolved in response to the substrate structure.},
	issn = {0969-2126},
	doi = {10.1016/j.str.2004.02.036},
	author = {Amaya, MF and Watts, AG and Damager, I and Wehenkel, A and Nguyen, T and Buschiazzo, A and Paris, G and Frasch, AC and Withers, SG and Alzari, PM}
}
