Matthieu Schapira

The paper shows that BAY-805 induces USP21-KLHL12 association, recruiting USP21 to COPII vesicles and impairing large cargo transport.

The paper uses machine learning-augmented virtual screening to discover a novel series of Mac1 inhibitors for SARS-CoV-2 NSP3, validated by experimental assays and crystallography.

The paper develops a chemical probe targeting the USP16 zinc-finger ubiquitin-binding domain and evaluates its selectivity and activity in cellular assays.

This study introduces E-ASMS, a method to detect weak binders and assess enantioselectivity, identifying 16 binders across 12 human protein targets with confirmed binding mechanisms.

The paper identifies a small molecule ligand for the HTT-HAP40 complex using AS-MS and validates its binding through multiple techniques, highlighting a druggable interface for HD therapeutics.

The paper introduces kNN-AS, an adaptive sampling method that uses k-nearest neighbour graphs to efficiently explore conformational space, showing state-of-the-art performance on artificial and protein systems.

The paper evaluates computational hit-finding methods for targeting the WDR domain of LRRK2, a Parkinson's disease protein, finding that diverse strategies yielded weakly potent compounds.

The paper develops a resource for discovering ligands for WDR proteins using experimental and computational methods, leading to the identification of drug-like ligands for 9 out of 20 targets.

The paper introduces PFI-7, a chemical probe that inhibits GID4 Pro/N-degron interactions, revealing non-degradative roles of the CTLH complex in human cells.

The paper assesses current chemical coverage of the human Reactome, finding that 3% of proteins are targeted by chemical probes, but they cover 53% of pathways due to pathway overlap.

This paper benchmarks PROTAC docking and virtual screening tools to evaluate their ability to predict ternary complexes and distinguish active from inactive PROTACs.

The paper systematically surveys the human proteome to identify non-catalytic drug binding pockets on protein-modifying enzymes for proximity pharmacology opportunities.

The paper reviews PDB structures of human proteins bound to drug-like ligands to map the druggable genome, identifying 46 druggable domains across 3440 proteins.

The paper presents a chemical probe collection for studying protein methyltransferases, showing their utility in modulating epigenetic marks and affecting T cell differentiation.