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Lenka Šnajdrová

Researcher at Masaryk University

Publications -  23
Citations -  877

Lenka Šnajdrová is an academic researcher from Masaryk University. The author has contributed to research in topics: Population & Cancer registry. The author has an hindex of 6, co-authored 23 publications receiving 755 citations. Previous affiliations of Lenka Šnajdrová include Centre national de la recherche scientifique & Joseph Fourier University.

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Journal ArticleDOI

Structures and mechanisms of glycosyltransferases

TL;DR: The 3D-Glycosyltransferase database is created to gather structural information concerning this class of enzymes and to accommodate the growing number of crystal structures.
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High affinity fucose binding of Pseudomonas aeruginosa lectin PA-IIL: 1.0 A resolution crystal structure of the complex combined with thermodynamics and computational chemistry approaches.

TL;DR: Calculations of partial charges indicated that extensive delocalization of charges between the calcium ions, the side chains of the protein‐binding site and the carbohydrate ligand is responsible for the high enthalpy of binding and therefore for the unusually high affinity observed for this unique mode of carbohydrate recognition.
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Complex Reporting of the COVID-19 Epidemic in the Czech Republic: Use of an Interactive Web-Based App in Practice.

TL;DR: The online interactive overview of the current spread of CO VID-19 in the Czech Republic was launched on March 11, 2020 and has immediately become the primary communication channel employed by the health care sector to present the current situation regarding the COVID-19 epidemic.
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Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity.

TL;DR: Evidence is collected supporting the 〈β2–α2〉 loop in the N-domain as likely to be involved in diacylglycerol binding in MGD, and the monotopic insertion of MGD in one membrane leaflet of the plastid envelope occurs very likely at the level of hydrophobic amino acids of theN-terminal domain.
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Molecular dynamics study of Pseudomonas aeruginosa lectin‐II complexed with monosaccharides

TL;DR: The results of a series of 10‐ns molecular dynamics simulations on Pseudomonas aeruginosa lectin‐II (PA‐IIL) and its complexes with four different monosaccharides are presented and it suggests that the high density peaks of the solvent around the binding site in the free protein could be the tool to predict hydroxyl group orientation of the sugar in the protein/sugar complexes.