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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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Proceedings ArticleDOI

Alpha-(2,6)-sialyltransferase catalyzed sialylations of conformationally constrained oligosaccharides

TL;DR: It is demonstrated that conformationally restricted oligosaccharides can act as acceptors for glycosyltransferases and correlations of the conformational properties of N-acetyl lactosamine and several preorganized derivatives suggest that preorganization of acceptors in conformations that are favorable for recognition by a transferase may improve catalytic efficiencies.
Journal ArticleDOI

Adsorption characterization of various modified β-cyclodextrins onto TEMPO-oxidized cellulose nanofibril membranes and cryogels

TL;DR: In this article, the authors developed toCNF cryogels containing various types of β-Cyclodextrins derivatives by physical adsorption, and the results were consistent with the estimated binding capacity.
Posted ContentDOI

A pore-forming β-trefoil lectin with specificity for the tumor-related glycosphingolipid Gb3

TL;DR: SaroL-1 from the lower eukaryote Salpingoeca rosetta was predicted to contain both β-trefoil and aerolysin-like pore-forming domain, with a stronger affinity for cancer-related α-galactosylated epitopes such as glycosphingolipid Gb3 embedded in giant unilamellar vesicles or cell membranes.
Journal ArticleDOI

Targeting a Multidrug-Resistant Pathogen: First Generation Antagonists of Burkholderia cenocepacia’s BC2L-C Lectin

TL;DR: Rational design and synthesis of bifunctional C- or N-fucosides, generated by connecting these fragments to a fucoside core using a panel of rationally selected linkers are reported.
Journal ArticleDOI

Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations.

TL;DR: Two distinct structures of AA(Gly)B, a dual-specificity blood group synthase, are described in complex with a UDP-galactose derivative in which the O6'' atom is protected by a 2-nitrobenzyl group, paving the way for kinetic crystallography experiments aiming at trapping and characterizing reaction-intermediate states in the mechanism of enzymatic glycosyl transfer.