B
Bernard Eddé
Researcher at Collège de France
Publications - 33
Citations - 3462
Bernard Eddé is an academic researcher from Collège de France. The author has contributed to research in topics: Tubulin & Microtubule. The author has an hindex of 26, co-authored 33 publications receiving 3229 citations. Previous affiliations of Bernard Eddé include Pierre-and-Marie-Curie University & McGill University.
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Journal ArticleDOI
Posttranslational glutamylation of alpha-tubulin
TL;DR: A posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445) could play a role in regulating microtubule dynamics.
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Centriole Disassembly In Vivo and Its Effect on Centrosome Structure and Function in Vertebrate Cells
TL;DR: The results suggest that a posttranslational modification of tubulin is critical for long-term stability of centriolar microtubules and demonstrate that in animal cells, centrioles are instrumental in organizing centrosomal components into a structurally stable organelle.
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Tubulin Polyglutamylase Enzymes Are Members of the TTL Domain Protein Family
Carsten Janke,Krzysztof Rogowski,Dorota Wloga,Catherine Regnard,Andrey V. Kajava,Jean-Marc Strub,Nevzat Temurak,Juliette van Dijk,Dominique Boucher,Alain Van Dorsselaer,Swati Suryavanshi,Jacek Gaertig,Bernard Eddé +12 more
TL;DR: The neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase–like protein, TTLL1, a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates.
Journal Article
Distribution of glutamylated alpha and beta-tubulin in mouse tissues using a specific monoclonal antibody, GT335.
A Wolff,B de Néchaud,D. Chillet,H Mazarguil,E Desbruyeres,Stéphane Audebert,Bernard Eddé,François Gros,Philippe Denoulet +8 more
TL;DR: Results indicate that, in addition to alpha and beta' (class III)-tubulin, other beta-tubulin isotypes are also glutamylated, and this antibody has been used to analyze the cell and tissue distributions of glutamelated tubulin.
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A targeted multienzyme mechanism for selective microtubule polyglutamylation.
TL;DR: A multienzyme mechanism of polyglutamylation is proposed that can explain how the diversity ofpolyglutamate side chains of variable lengths on selected types of MTs is controlled at the molecular level.