L
Luc Brunsveld
Researcher at Eindhoven University of Technology
Publications - 220
Citations - 11024
Luc Brunsveld is an academic researcher from Eindhoven University of Technology. The author has contributed to research in topics: Supramolecular chemistry & Chemistry. The author has an hindex of 49, co-authored 200 publications receiving 9528 citations. Previous affiliations of Luc Brunsveld include DSM & Max Planck Society.
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Chiral Dihydrobenzofuran Acids Show Potent Retinoid X Receptor–Nuclear Receptor Related 1 Protein Dimer Activation
Henrik Sundén,Anja Schäfer,Anja Schäfer,Marcel Scheepstra,Seppe Leysen,Marcus Malo,Jian-Nong Ma,Ethan S. Burstein,Christian Ottmann,Luc Brunsveld,Roger Olsson,Roger Olsson,Roger Olsson +12 more
TL;DR: The enantioselective synthesis and SAR of sterically constricted benzofurans at RXR and the X-ray structure shows enantiomeric discrimination where 9a optimally addresses the ligand binding pocket of RXR.
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Orthosteric and Allosteric Dual Targeting of the Nuclear Receptor RORγt with a Bitopic Ligand.
TL;DR: In this paper, a chemical biology approach was used to develop a bitopic ligand for the RORγt nuclear receptor (NR), enabling concomitant engagement of both binding pockets.
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Combining Supramolecular Chemistry with Biology
TL;DR: In this paper, a tutorial review focuses on the possibilities of the marriage of synthetic supramolecular architectures and biological systems, and highlights that synthetic supersamolecular elements are for example ideal platforms for the recognition and modulation of proteins and cells.
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Solution structure of a cucurbit[8]uril induced compact supramolecular protein dimer
TL;DR: SAXS data reveal the formation of a well ordered protein dimer, notwithstanding being connected by a reversible and flexible peptide linker, and highlight the supramolecular induced interplay of the proteins, analogous to covalently linked proteins.
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The intramolecular allostery of GRB2 governing its interaction with SOS1 is modulated by phosphotyrosine ligands.
Neda S. Kazemein Jasemi,Christian Herrmann,Eva Magdalena Estirado,Lothar Gremer,Lothar Gremer,Dieter Willbold,Dieter Willbold,Luc Brunsveld,Radovan Dvorsky,Mohammad Reza Ahmadian +9 more
TL;DR: In this paper, it was shown that HER2 pYP-bound SH2 potentiates GRB2 SH3 domain interactions with SOS1 (an allosteric mechanism), and the SH2 domain blocks cSH3, enabling nSH3 to bind SOS1 first before cSH 3 follows (an avidity-based mechanism).