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Laura Ratier

Researcher at National University of General San Martín

Publications -  6
Citations -  294

Laura Ratier is an academic researcher from National University of General San Martín. The author has contributed to research in topics: Sialic acid & Trypanosoma cruzi. The author has an hindex of 6, co-authored 6 publications receiving 283 citations. Previous affiliations of Laura Ratier include National Scientific and Technical Research Council.

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Journal ArticleDOI

A sialidase mutant displaying trans-sialidase activity.

TL;DR: The results show that the presence of a sugar acceptor binding-site, the fine-tuning of protein-substrate interactions and the flexibility of crucial active site residues are all important to achieve transglycosidase activity from the TrSA sialidase scaffold.
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Lactose derivatives are inhibitors of Trypanosoma cruzi trans-sialidase activity toward conventional substrates in vitro and in vivo.

TL;DR: The acceptor substrate specificity of lactose derivatives was studied by high pH anion-exchange chromatography with pulse amperometric detection and lactitol, which was the best of the ones tested, effectively inhibited the transfer of sialic acid to N-acetyllactosamine.
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Discovery of novel inhibitors of Trypanosoma cruzi trans-sialidase from in silico screening

TL;DR: Attempts to obtain crystal structures of these compounds with TcTS proved unsuccessful but provided evidence of ligand binding at the active site, including the 3-benzothiazol-2-yl-4-phenyl-but-3-enoic acid scaffold.
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Relevance of the diversity among members of the Trypanosoma cruzi trans-sialidase family analyzed with camelids single-domain antibodies.

TL;DR: The results suggest that the presence of a large and diverse trans-sialidase family might be required to prevent the inhibitory response against this essential enzyme and might thus constitute a novel strategy of T. cruzi to evade the host immune system.
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Synthesis of PEGylated lactose analogs for inhibition studies on T.cruzi trans-sialidase

TL;DR: In this paper, a covalent conjugation of polyethylene glycol (PEG) with lactose, lactobionolactone and benzyl β-D-galactopyranosyl- (1→6)-2-amino-2-deoxy-α-Dglucopyranoide (1) with the hope of improving the bioavailability, though retaining their inhibitory properties.