V
Violaine Moreau
Researcher at French Institute of Health and Medical Research
Publications - 57
Citations - 3501
Violaine Moreau is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Podosome & RHOA. The author has an hindex of 24, co-authored 52 publications receiving 3209 citations. Previous affiliations of Violaine Moreau include University of Bordeaux & Centre national de la recherche scientifique.
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Journal ArticleDOI
Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling.
Friedrich Frischknecht,Violaine Moreau,Sabine Röttger,Stefania Gonfloni,Inge Reckmann,Giulio Superti-Furga,Michael Way +6 more
TL;DR: It is suggested that vaccinia virus spreads by mimicking the signalling pathways that are normally involved in actin polymerization at the plasma membrane, including Nck and N-WASP.
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A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.
Violaine Moreau,Friedrich Frischknecht,Inge Reckmann,Renaud Vincentelli,Gwénaël Rabut,Donn M. Stewart,Michael Way +6 more
TL;DR: In this paper, the amino-terminal WH1 domain of N-WASP was found to be responsible for its recruitment to sites of actin polymerization during Cdc42-independent, actin-based motility of vaccinia virus.
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Ubiquitination Mediated by the Npi1p/Rsp5p Ubiquitin-protein Ligase Is Required for Endocytosis of the Yeast Uracil Permease
TL;DR: The data presented here show that uracil permease also undergoes basal turnover under normal growth conditions, and both basal and stress-stimulated turnover rates were greatly reduced in pep4 mutant cells having defective vacuolar protease activities.
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Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA.
TL;DR: Punctate filamentous actin structures appeared along the ventral plasma membrane of endothelial cells and were identified as the core of podosomes by the distinctive vinculin ring around the F-actin.
Journal ArticleDOI
The Saccharomyces cerevisiae Homologue of Human Wiskott–Aldrich Syndrome Protein Las17p Interacts with the Arp2/3 Complex
Ammar Madania,Pascal Dumoulin,Sandrine Grava,Hiroko Kitamoto,Claudia Schärer-Brodbeck,Alexandre Soulard,Violaine Moreau,Barbara Winsor +7 more
TL;DR: Two hybrid results suggest that Las17p interacts with actin, verprolin, Rvs167p and several other proteins including Src homology 3 (SH3) domain proteins, suggesting thatLas17p may integrate signals from different regulatory cascades destined for the Arp2/3p complex and the actin cytoskeleton.