Frédéric H.‐T. Allain

A qualitative and quantitative framework for the characterization of protein-RNA interactions by cross-linking mass spectrometry (XL-MS)

This paper introduces a XL-MS workflow combining DDA and PRM for quantitative characterization of protein-RNA interactions, applied to TDP-43 and FOX1 complexes.

Monomeric TDP-43 binds GU-rich RNA via its NTD but only its oligomers block cryptic exon inclusion

This study shows that the NTD of TDP-43 binds UG-rich RNA on monomers, while oligomerization is essential for repressing cryptic exons.

Phosphorylation tunes electrostatically driven protein-RNA interactions

This study quantifies how phosphorylation modulates electrostatic interactions between charged IDPs and RNA, showing that phosphorylation reduces binding affinity linearly with net charge.

Multiplexed analysis of multicomponent biomolecular condensates without any tag

This paper introduces a non-invasive NMR method to study multiple components in biomolecular condensates without tags, demonstrating its effectiveness with FUS and hnRNPC1 samples.

LLPS REDIFINE allows the biophysical characterization of multicomponent condensates without tags or labels

The paper introduces REDIFINE, a label-free method to characterize multicomponent biomolecular condensates using diffusion NMR, revealing insights into their biophysical properties and dynamics.

The diversity of splicing modifiers acting on A-1 bulged 5'-splice sites reveals rules to guide rational design

This study identifies common pharmacophores in splicing modifiers targeting A-1 bulged 5'-splice sites using structural and computational methods.

The solution structure of Dead End bound to AU-rich RNA reveals an unprecedented mode of tandem RRM-RNA recognition required for mRNA regulation

This study determines the solution structure of DND1 bound to AU-rich RNA, revealing a novel tandem RRM-RNA recognition mechanism essential for mRNA regulation.

The cancer-associated RBM39 bridges the pre-mRNA, U1 and U2 snRNPs to regulate alternative splicing

This study identifies RBM39's role in autoregulating its own pre-mRNA splicing through interactions with U1 and U2 snRNPs, offering insights for alternative cancer therapies.

Phase separation of hnRNP A1 upon specific RNA-binding observed by magnetic resonance

The paper investigates how hnRNP A1 interacts with specific RNA and undergoes phase separation, using magnetic resonance techniques to observe structural changes and droplet formation.