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Anne Imberty

Researcher at University of Grenoble

Publications -  406
Citations -  20811

Anne Imberty is an academic researcher from University of Grenoble. The author has contributed to research in topics: Lectin & Binding site. The author has an hindex of 74, co-authored 381 publications receiving 18759 citations. Previous affiliations of Anne Imberty include Bar-Ilan University & Joseph Fourier University.

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Tetraphenylethylene-based glycoclusters with aggregation-induced emission (AIE) properties as high-affinity ligands of bacterial lectins

TL;DR: Evaluation in a cell-based anti-adhesive assay highlighted a limited decrease in adhesion for the fucosylated glycocluster, which confirmed that these TPE-based glycoclusters are indeed LecA and LecB high-affinity ligands.
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Importance of the polarity of the glycosaminoglycan chain on the interaction with FGF-1

TL;DR: It is concluded that the directionality of the GAG chain is essential for the binding and subsequent activation of FGF-1 and the relative biological activity of the compounds with regular substitution pattern can be inferred from their values of IC50.
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A recombinant fungal lectin for labeling truncated glycans on human cancer cells.

TL;DR: PVL binding is specific to cancer tissue and weak or no labeling is observed for healthy ones, except for stomach glands that present unique αGlcNAc-presenting mucins, which makes it a useful tool for labeling agalacto-glycans in cancer or other diseases.
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Combining fold recognition and exploratory data analysis for searching for glycosyltransferases in the genome of Mycobacterium tuberculosis.

TL;DR: Fold recognition was applied to the systematic analysis of the all sequences encoded by the genome of Mycoplasma tuberculosis H37Rv in order to identify new putative glycosyltransferases, and a clear relationship appeared between some sequences and some folds.
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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.