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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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Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands for Burkholderia ambifaria lectin (BambL)
Sakonwan Kuhaudomlarp,Linda Cerofolini,Sabrina Santarsia,Emilie Gillon,Silvia Fallarini,Grazia Lombardi,Maxime Denis,Stefano Giuntini,Carolina Valori,Marco Fragai,Anne Imberty,Alessandro Dondoni,Cristina Nativi +12 more
TL;DR: Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen Burkholderia ambifaria, proved high affinity and unprecedented immune modulatory properties towards macrophages activation.
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Three-dimensional structure analysis of the crystalline moiety of A-starch
TL;DR: In this article, the authors used electron diffraction on single, micron-sized crystals and deconvolution of X-ray powder patterns into individual peaks to obtain the threedimensional structure analysis of the A-type polymorph of starch.
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Multivalent thioglycopeptoids via photoclick chemistry: potent affinities towards LecA and BC2L-A lectins.
Cécile Caumes,Emilie Gillon,Bertrand Legeret,Bertrand Legeret,Claude Taillefumier,Claude Taillefumier,Anne Imberty,Sophie Faure,Sophie Faure +8 more
TL;DR: A tetrameric cyclic β-peptoid scaffold showing efficient binding potency for bacterial lectins LecA and BC2L-A has been revealed by ITC experiments.
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Biophysical characterization and structural determination of the potent cytotoxic Psathyrella asperospora lectin.
João P. Ribeiro,Mohamed Ali Abol Hassan,Razina Rouf,Evelin Tiralongo,Tom W. May,Christopher J. Day,Anne Imberty,Joe Tiralongo,Annabelle Varrot +8 more
TL;DR: The structure of PAL was resolved by X‐ray crystallography, elucidating both the protein's amino acid sequence as well as the molecular basis rationalizing its binding specificity, and binding preference towards N‐acetylglucosamine and, to a lesser extent, towards sialic acid.