B
Bernard Rossi
Researcher at French Institute of Health and Medical Research
Publications - 120
Citations - 5168
Bernard Rossi is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Tyrosine kinase & Insulin receptor. The author has an hindex of 39, co-authored 120 publications receiving 5068 citations. Previous affiliations of Bernard Rossi include University of Nice Sophia Antipolis.
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Journal ArticleDOI
Tyrosine Phosphorylation of IκB-α Activates NF-κB without Proteolytic Degradation of IκB-α
Véronique Imbert,Rudolf A. Rupec,Antonia Livolsi,Heike L. Pahl,E. Britta-Mareen Traenckner,Christoph Mueller-Dieckmann,Dariush Farahifar,Bernard Rossi,Patrick Auberger,Patrick A. Baeuerle,Jean-François Peyron +10 more
TL;DR: In this article, the authors reported an alternative mechanism of NF-κB activation by using tyrosine-phosphorylation of IκB-α in the presence of pervanadate.
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Characterization of a natural inhibitor of the insulin receptor tyrosine kinase: cDNA cloning, purification, and anti-mitogenic activity
Patrick Auberger,Laurence Falquerho,Jean Olivier Contreres,Gilles Pagès,Ginette Le Cam,Bernard Rossi,Alphonse Le Cam +6 more
TL;DR: In additon, pp63 antagonized the growth-promoting action of insulin in FaO cells but did not affect hormone-mediated increase in amino acid transport capacity or tyrosine aminotransferase induction in these cells.
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Receptor-mediated phosphorylation of the hepatic insulin receptor: Evidence that the Mr 95,000 receptor subunit is its own kinase
TL;DR: It is shown that an insulin-stimulated phosphorylation site and an ATP-binding site coexist on the beta subunit of the insulin receptor, indicating that the insulin receptors acts as its own protein kinase.
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Saccharomyces boulardii preserves the barrier function and modulates the signal transduction pathway induced in enteropathogenic Escherichia coli-infected T84 cells.
TL;DR: It is demonstrated that S. boulardii exerts a protective effect on epithelial cells after EPEC adhesion by modulating the signaling pathway induced by bacterial infection.
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Signal transduction involved in MCP-1–mediated monocytic transendothelial migration
TL;DR: Coordinated action of distinct signal pathways is required to produce a full response to MCP-1 in terms of monocytic locomotion, and the results underscore the major implication of Go/Gi proteins and nonreceptor tyrosine kinases in the early MCP