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Solange Monier

Researcher at Curie Institute

Publications -  10
Citations -  766

Solange Monier is an academic researcher from Curie Institute. The author has contributed to research in topics: Golgi apparatus & Endosome. The author has an hindex of 9, co-authored 10 publications receiving 721 citations. Previous affiliations of Solange Monier include University of Rennes.

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Characterization of Novel Rab6‐Interacting Proteins Involved in Endosome‐to‐TGN Transport

TL;DR: The data suggest that Rab6IP2s is involved in the pathway regulated by Rab6A′, which is ubiquitously expressed, mostly cytosolic and found in high molecular mass complexes in brain cytosol, and recruited on Golgi membranes in a Rab6:GTP‐dependent manner.
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The Mammalian Passenger Protein TD-60 Is an RCC1 Family Member with an Essential Role in Prometaphase to Metaphase Progression

TL;DR: The human passenger protein TD-60 is purified and cloned and it is reported that it is a member of the RCC1 family and that it binds preferentially the nucleotide-free form of the small G protein Rac1, which suggests that like other passenger proteins, TD- 60 is involved in regulation of cell cleavage.
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Recombinant antibodies to the small GTPase Rab6 as conformation sensors.

TL;DR: An approach, based on antibody phage display, to generate molecular conformation sensors that could be applied to other molecules that can be locked in a particular conformation in vitro is reported.
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ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function

TL;DR: This study indicates that Sec7 domain-containing GEFs control intracellular membrane compartment structure and function through the regulation of specific ARF proteins in mammalian cells.
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Rab6-interacting Protein 1 Links Rab6 and Rab11 Function

TL;DR: Fluorescence resonance energy transfer analysis using fluorescence lifetime imaging shows that the overexpression of R6IP1 promotes an interaction between Rab11A and Rab6 in living cells, and proposes that R 6IP1 may couple Rab6 and Rab11 function throughout the cell cycle.