scispace - formally typeset
C

Cédric Atmanene

Researcher at University of Strasbourg

Publications -  19
Citations -  545

Cédric Atmanene is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Protein subunit & Protein ligand. The author has an hindex of 13, co-authored 19 publications receiving 520 citations. Previous affiliations of Cédric Atmanene include International Pentecostal Holiness Church & Centre national de la recherche scientifique.

Papers
More filters
Journal ArticleDOI

Native MS: an 'ESI' way to support structure- and fragment-based drug discovery.

TL;DR: A description of the general approach and an overview of the possible characterization of ligand-binding properties are provided, as well as how native MS supports structure- and fragment-based drug research is discussed.
Journal ArticleDOI

Extending mass spectrometry contribution to therapeutic monoclonal antibody lead optimization: characterization of immune complexes using noncovalent ESI-MS.

TL;DR: Investigations focused on mAb:Ag complexes revealed that, similarly to murine mAb, humanized mAb 6F4 binds selectively up to four antigen molecules with a similar affinity, confirming in this way the reliability of the humanization process.
Journal ArticleDOI

One Question, Multiple Answers: Biochemical and Biophysical Screening Methods Retrieve Deviating Fragment Hit Lists.

TL;DR: While the combined results of these screening methods retrieve 10 of the 11 crystal structures originally predicted by the biochemical assay, the mutual overlap of individual hit lists is surprisingly low, highlighting that each technique operates on different biophysical principles and conditions.
Journal ArticleDOI

An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction.

TL;DR: Noncovalent mass spectrometry was used to confirm the dimeric oligomerization state of Tgt in solution and evidence the binding stoichiometry of the complex formed between Tgt and its full-length substrate tRNA and the effect of inhibitor binding was investigated, thus providing thebinding stoichiometries of TGT:inhibitor complexes and showing competitive interactions in the presence of tRNA.