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Emilie Genin

Researcher at University of Bordeaux

Publications -  58
Citations -  2060

Emilie Genin is an academic researcher from University of Bordeaux. The author has contributed to research in topics: Catalysis & Cycloisomerization. The author has an hindex of 25, co-authored 57 publications receiving 1927 citations. Previous affiliations of Emilie Genin include University of Rennes & École Normale Supérieure.

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Dimerized linear mimics of a natural cyclopeptide (TMC-95A) are potent noncovalent inhibitors of the eukaryotic 20S proteasome.

TL;DR: The use of the multivalency inhibitor concept has produced highly efficient and selective noncovalent compounds (no inhibition of calpain and cathepsin) that have potential therapeutic advantages compared to covalent binders such as bortezomib and carfilzomib.
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CrAsH-quantum dot nanohybrids for smart targeting of proteins.

TL;DR: Smart nanohybrids prepared by conjugation of CrAsH to hydrosoluble and biocompatible quantum dots (QDs) were shown to bind efficiently and selectively to Cys-tagged proteins to allow extended monitoring of the target protein.
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Palladium(0)-Catalyzed Allylic Aminations: Kinetics and Mechanism of the Reaction of Secondary Amines with Cationic [(η3-allyl)PdL2]+ Complexes†

TL;DR: Fully established catalytic cycles are now proposed for the Pd-catalyzed allylic amination of (E)-PhCHCHCH CH(Ph)OAc by piperidine and morpholine with fully established rate and equilibrium constants determined in DMF.
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Cooperative Veratryle and Nitroindoline Cages for Two-Photon Uncaging in the NIR.

TL;DR: The interactions between the 2PA module and the caging moiety are found to promote cooperative effects on the2PA response while additional processes that enhance the uncaging efficiency are operative in well-oriented nitroindoline-derived dyads.
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1,2,4-Oxadiazoles identified by virtual screening and their non-covalent inhibition of the human 20S proteasome.

TL;DR: The cellular effects of the compounds validate their utility as potential pharmacological agents for anti-cancer pre-clinical studies and suggest an unusual binding of the inhibitor within the S5 binding pocket (β6 subunit).