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UMR8576,
CNRS,
UMR8576, CNRS
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Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans.
Journal of molecular biology Sep, 2004 | Pubmed ID: 15313617
Monitoring of the ethionamide pro-drug activation in mycobacteria by (1)H high resolution magic angle spinning NMR.
Biochemical and biophysical research communications Jun, 2005 | Pubmed ID: 15850780
ELISE NMR: experimental liquid sealing of NMR samples.
Journal of magnetic resonance (San Diego, Calif. : 1997) Aug, 2006 | Pubmed ID: 16709462
Selective intracellular accumulation of the major metabolite issued from the activation of the prodrug ethionamide in mycobacteria.
The Journal of antimicrobial chemotherapy Oct, 2006 | Pubmed ID: 16895935
A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes.
Journal of proteome research Dec, 2006 | Pubmed ID: 17137346
Structural and functional characterization of the interaction between cyclophilin B and a heparin-derived oligosaccharide.
The Journal of biological chemistry Nov, 2007 | Pubmed ID: 17855358
Applications of diagonal chromatography for proteome-wide characterization of protein modifications and activity-based analyses.
The FEBS journal Dec, 2007 | Pubmed ID: 18021238
Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry.
Biochemical and biophysical research communications May, 2008 | Pubmed ID: 18298951
Sandwich-ELISE NMR: reducing the sample volume of NMR samples.
Journal of magnetic resonance (San Diego, Calif. : 1997) Jul, 2008 | Pubmed ID: 18455452
Graphical interpretation of Boolean operators for protein NMR assignments.
Journal of biomolecular NMR Sep, 2008 | Pubmed ID: 18762868
Tau aggregation in Alzheimer's disease: what role for phosphorylation?
Prion Jan-Mar, 2007 | Pubmed ID: 19164903
Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded.
Biochemical and biophysical research communications Apr, 2009 | Pubmed ID: 19249289
Selective backbone labelling of ILV methyl labelled proteins.
Journal of biomolecular NMR Apr, 2009 | Pubmed ID: 19288066
Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B.
The Journal of biological chemistry May, 2009 | Pubmed ID: 19297321
Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.
Biochemistry Jun, 2010 | Pubmed ID: 20423153
The domain 2 of the HCV NS5A protein is intrinsically unstructured.
Protein and peptide letters Aug, 2010 | Pubmed ID: 20450484
DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A.
PloS one Oct, 2010 | Pubmed ID: 21060866
Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
Molecular bioSystems May, 2011 | Pubmed ID: 21327254
Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.
The Journal of biological chemistry Jun, 2011 | Pubmed ID: 21489988
Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A.
The Journal of biological chemistry Dec, 2012 | Pubmed ID: 23152499
Dissociation kinetics of a binary complex in solution by protein displacement.
Angewandte Chemie (International ed. in English) Nov, 2013 | Pubmed ID: 24123878
Ranking high affinity ligands of low solubility by NMR spectroscopy.
ACS medicinal chemistry letters Jun, 2011 | Pubmed ID: 24900335
A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication.
The Journal of biological chemistry Jul, 2015 | Pubmed ID: 26085105
Proline Conformation in a Functional Tau Fragment.
Journal of molecular biology Jan, 2016 | Pubmed ID: 26655856
Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment.
Frontiers in molecular biosciences , 2016 | Pubmed ID: 27668217
Lille University
Clément Danis*,1,2,
Clément Despres*,1,
Luiza M. Bessa1,
Idir Malki1,
Hamida Merzougui1,
Isabelle Huvent1,
Haoling Qi1,
Guy Lippens1,
François-Xavier Cantrelle1,
Robert Schneider1,
Xavier Hanoulle1,
Caroline Smet-Nocca1,
Isabelle Landrieu1
1UMR8576, CNRS, Lille University,
2UMR-S1172, INSERM CNRS, Lille University
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