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Jean-Claude Huet

Researcher at Institut national de la recherche agronomique

Publications -  98
Citations -  4407

Jean-Claude Huet is an academic researcher from Institut national de la recherche agronomique. The author has contributed to research in topics: Elicitin & Peptide sequence. The author has an hindex of 38, co-authored 98 publications receiving 4229 citations. Previous affiliations of Jean-Claude Huet include École pratique des hautes études & Pasteur Institute.

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Structure and activity of proteins from pathogenic fungi Phytophthora eliciting necrosis and acquired resistance in tobacco.

TL;DR: Both cryptogein and capsicein protect tobacco against invasion by the pathogen Phytophthora nicotianac, the agent of the tobacco black shank, that is unable to produce such an elicitor.
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Evidence of an odorant-binding protein in the human olfactory mucus: location, structural characterization, and odorant-binding properties.

TL;DR: By measuring the displacement of several fluorescent probes, it is shown that hOBP(IIa)(alpha) is able to bind numerous odorants of diverse chemical structures, with a higher affinity for aldehydes and large fatty acids.
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Role of Ser-652 and Lys-692 in the protease activity of infectious bursal disease virus VP4 and identification of its substrate cleavage sites.

TL;DR: The results suggest that VP4 cleaves multiple (Thr/Ala)-X-Ala downward arrowAla motifs, delineating the birnavirus protease as a new type of viral serine protease.
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Characterization of a chemosensory protein (ASP3c) from honeybee (Apis mellifera L.) as a brood pheromone carrier

TL;DR: This is the first report on a natural pheromonal ligand bound by a recombinant CSP with a measured affinity constant, and the cloning of a honeybee CSP gene called ASP3c is reported.
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High homology between a trophoblastic protein (trophoblastin) isolated from ovine embryo and α-interferons

TL;DR: The sequence data reveal a significant homology between oTPB and bovine interferons α of class II: 64% of the amino acids are identical and 75% are homologous and these alignments occur at the N‐terminal amino acid sequence and proceed without deletion.