Xavier Hanoulle

Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans.

Monitoring of the ethionamide pro-drug activation in mycobacteria by (1)H high resolution magic angle spinning NMR.

ELISE NMR: experimental liquid sealing of NMR samples.

Selective intracellular accumulation of the major metabolite issued from the activation of the prodrug ethionamide in mycobacteria.

A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes.

Structural and functional characterization of the interaction between cyclophilin B and a heparin-derived oligosaccharide.

Applications of diagonal chromatography for proteome-wide characterization of protein modifications and activity-based analyses.

Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry.

Sandwich-ELISE NMR: reducing the sample volume of NMR samples.

Graphical interpretation of Boolean operators for protein NMR assignments.

Tau aggregation in Alzheimer's disease: what role for phosphorylation?

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded.

Selective backbone labelling of ILV methyl labelled proteins.

Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B.

Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.

The domain 2 of the HCV NS5A protein is intrinsically unstructured.

DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A.

Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A.

Dissociation kinetics of a binary complex in solution by protein displacement.

Ranking high affinity ligands of low solubility by NMR spectroscopy.

A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication.

Proline Conformation in a Functional Tau Fragment.

Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment.