CORDIS Project
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This project investigates the reversible modification of histones to regulate gene expression through dynamic covalent chemistry. By exploring aldehyde interactions, it aims to develop new methods for protein functionalization that can impact cellular processes and disease mechanisms.
Nature makes use of covalent additions of functional groups to proteins for regulating essential processes like cellular signalling and protein folding/degradation.
Most of these post-translational modifications (PTMs) are enzymatically-reversible, with the coupled catalytic processes being fulfilled by antagonistic enzymes (e.g., methylase-demethylase pair).
This dynamic behaviour allows for the correct metabolic equilibrium, as an unbalanced PTM-machinery is indicative of some severe diseases.…
UNIVERSITE DE STRASBOURG
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