B
B de Néchaud
Researcher at Collège de France
Publications - 7
Citations - 492
B de Néchaud is an academic researcher from Collège de France. The author has contributed to research in topics: Microtubule & Tubulin. The author has an hindex of 7, co-authored 7 publications receiving 475 citations.
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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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Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335.
TL;DR: Results obtained in Paramecium strongly suggest that both axonemal and cytoplasmic tubulin are glutamylated, and suggests that tubulin glut amylation came out early in the course of eukaryotic evolution and has been widely exploited in various cellular strategies.
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Expression of glial fibrillary acidic protein and vimentin in mouse lens epithelial cells during development in vivo and during proliferation and differentiation in vitro: comparison with the developmental appearance of GFAP in the mouse central nervous system.
TL;DR: Analysis of glial fibrillary acidic protein (GFAP) and vimentin in mouse lens epithelial cells (MLEC) during ontogenesis revealed a two‐step developmental expression similar to that observed in astrocytcs.
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Stable and metastable cytoskeletal polymers carried by slow axonal transport
TL;DR: The proteins carried by the slow axonal transport in the rat sciatic motor axons were radiolabeled by injecting 35S-methionine into the spinal cord, and the distribution of their solubility through the 2 main components of slow transport (SCa and SCb) was considered.
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Plasma protein adsorption to artificial ligament fibers
TL;DR: Suggestions that low fibrinogen adsorption might be due to the preferential adsorbent of Apo-1 are supported, which may favor fibroblast adherence, growth, and tissue repair.