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Arnaud Ducruix
Researcher at Centre national de la recherche scientifique
Publications - 61
Citations - 2292
Arnaud Ducruix is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Crystal structure & Solubility. The author has an hindex of 23, co-authored 61 publications receiving 2210 citations.
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Relative effectiveness of various ions on the solubility and crystal growth of lysozyme.
TL;DR: Lysozyme thiocyanate and nitrate crystals belong to the monoclinic system, whereas all the others have a tetragonal lattice, and SCN- precipitates and crystallizes lysozyme at low concentration, whereas sulfate is ineffective even at high concentrations.
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GRB2 Links Signaling to Actin Assembly by Enhancing Interaction of Neural Wiskott-Aldrich Syndrome Protein (N-WASp) with Actin-related Protein (ARP2/3) Complex*
Marie-France Carlier,Pierre Nioche,Isabelle Broutin-L'Hermite,Rajaa Boujemaa,Christophe Le Clainche,Coumaran Egile,Christiane Garbay,Arnaud Ducruix,Philippe J. Sansonetti,Dominique Pantaloni +9 more
TL;DR: It is shown that Grb2 may activate Arp2/3 complex-mediated actin polymerization downstream from the receptor tyrosine kinase signaling pathway and shortens the delay preceding the onset of Escherichia coli actin-based reconstituted movement.
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Crystal structure of the mammalian Grb2 adaptor.
Sébastien Maignan,Jean-Pierre Guilloteau,Nadine Fromage,Bernadette Arnoux,Jerome Becquart,Arnaud Ducruix +5 more
TL;DR: The mammalian growth factor receptor-binding protein Grb2 is an adaptor that mediates activation of guanine nucleotide exchange on Ras and is a key element in the signal transduction pathway.
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The Grb2 adaptor.
TL;DR: The structure of Grb2, the precise motifs recognised by its SH2 and SH3 domains, the way Grb 2 performs its function, a possible regulation of its association with Sos, and its ability to complex with other proteins in vivo are discussed.
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No salting-in of lysozyme chloride observed at low ionic strength over a large range of pH
TL;DR: The solubility of lysozyme chloride seems to become independent of ionic strength at pH approximately 9.5, which is interpreted as a shift of the isoionic pH to an isoelectric pH due to chloride binding.