C
C. Hirth
Researcher at Centre national de la recherche scientifique
Publications - 25
Citations - 2065
C. Hirth is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Binding site & Receptor. The author has an hindex of 10, co-authored 25 publications receiving 2004 citations.
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The delta-opioid receptor: isolation of a cDNA by expression cloning and pharmacological characterization.
TL;DR: A random primed expression cDNA library was constructed from the RNA of NG 108-15 cells that encodes a 371-amino acid-residue protein presenting all the structural characteristics of receptors that interact with guanine nucleotide-binding proteins.
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Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
Michal Harel,Isabelle J. Schalk,L Ehret-Sabatier,Françoise Bouet,Maurice Goeldner,C. Hirth,Paul H. Axelsen,Israel Silman,Joel L. Sussman +8 more
TL;DR: The structural and chemical data show the important role of aromatic groups as binding sites for quaternary ligands in Torpedo acetylcholinesterase, and provide complementary evidence assigning Trp-84 and Phe-330 to the "anionic" subsite of the active site andtrp-279 to the 'peripheral' anionic site.
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A photoaffinity ligand of the acetylcholine-binding site predominantly labels the region 179–207 of the α-subunit on native acetylcholine receptor from Torpedo marmorata
Michael Dennis,Jérôme Giraudat,Florence Kotzyba-Hibert,Maurice Goeldner,C. Hirth,Jui-Yoa Chang,Jui-Yoa Chang,Jean-Pierre Changeux +7 more
TL;DR: The acetylcholine‐binding site on the native AChR may involve several distinct portions of the α‐chain, with the region α 179–207 making a major contribution to the site.
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Sequence determination of a peptide fragment from electric eel acetylcholinesterase, involved in the binding of quaternary ammonium
TL;DR: Specific photoaffinity labelling of purified electric eel acetylcholinesterase by 3H‐labelled p‐(N,N‐dimethyl‐amino) benzenediazonium fluoroborate allows the identification of a labelled peptide fragment which is described as being involved in the binding of quaternary ammonium ions on this enzyme.
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Topography of toxin-acetylcholine receptor complexes by using photoactivatable toxin derivatives.
TL;DR: The molecular environment of a snake neurotoxin interacting with the high- and low-affinity binding sites of the nicotinic acetylcholine receptor (AcChoR) is defined by photocoupling reactions using three toxin derivatives with photoactivatable moieties on Lys-15, Lys-47, and Lys-51.