J
Jean-Claude Mani
Researcher at Centre national de la recherche scientifique
Publications - 58
Citations - 2824
Jean-Claude Mani is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Monoclonal antibody & Epitope. The author has an hindex of 26, co-authored 58 publications receiving 2785 citations.
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Journal ArticleDOI
A peptide mimetic of an anti-CD4 monoclonal antibody by rational design
Florence Casset,Florence Roux,Patrick Mouchet,Cédric Bès,Thierry Chardès,Claude Granier,Jean-Claude Mani,Martine Pugnière,Daniel Laune,Bernard Pau,Michel Kaczorek,Roger Lahana,Anthony R. Rees +12 more
TL;DR: Using peptide mapping to determine 'active' antigen recognition residues, molecular modeling, and a molecular dynamics trajectory analysis, a peptide mimic of an anti-CD4 antibody is developed, containing antigen contact residues from multiple CDRs.
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Extracellular ATP and cell signalling.
Journal ArticleDOI
Systematic exploration of the antigen binding activity of synthetic peptides isolated from the variable regions of immunoglobulins.
Daniel Laune,Franck Molina,Gaëlle Ferrières,Jean-Claude Mani,Pascale Cohen,Dominique Simon,Thierry Bernardi,Martine Piechaczyk,Bernard Pau,Claude Granier +9 more
TL;DR: Peptides enclosing one or several of the complementarity determining region (CDR) residues had antigen binding activity, although the most active peptides were not necessarily those bearing the greatest number of CDR residues.
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Streptabody, a high avidity molecule made by tetramerization of in vivo biotinylated, phage display-selected scFv fragments on streptavidin.
Cloutier Sylvain,S. Couty,Alexey Terskikh,L. Marguerat,V. Crivelli,M. Pugnières,Jean-Claude Mani,H.-J. Leisinger,Jean-Pierre Mach,David Deperthes +9 more
TL;DR: An easy way to increase the functional affinity (avidity) of single chain variable fragments (scFvs) by tetramerization on streptavidin, following their site-specific biotinylation by the enzyme BirA is described.
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Human cardiac troponin I: precise identification of antigenic epitopes and prediction of secondary structure
Gaëlle Ferrières,Charles Calzolari,Jean-Claude Mani,Daniel Laune,Sylvie Marie-France Trinquier,Michel Laprade,Catherine Larue,Bernard Pau,Claude Granier +8 more
TL;DR: The view is that hcTnI is not a globular protein but probably adopts an extended conformation, allowing a large part of the amino acid sequence of this molecule to be recognized by the immune system.