Isabelle Becher

This study reveals that phage T7 kinase broadly phosphorylates host and phage proteins, disabling bacterial defense systems through widespread phosphorylation.

The paper maps virus-host protein contact sites during influenza A virus infection, revealing new interactions and paraspeckle disassembly as a novel infection mechanism.

The paper shows NLRP3 activators disrupt the AP2 complex and impair plasma membrane signaling, leading to inflammation and cell death.

This study uses multi-omics and biophysical phosphoproteomics to analyze BRAFV600E signaling, identifying ETV3 as a new downstream regulator and revealing mechanisms of drug resistance.

This paper introduces HT-PELSA, a high-throughput adaptation of a peptide-centric local stability assay, enabling sensitive protein-ligand profiling in diverse biological samples.

The paper evaluates methods for inferring kinase-driven signaling pathways using phosphoproteomics data and kinase-substrate networks, finding that literature-curated networks with network propagation best recover ground truth interactions.

The paper introduces mito-TPP, a thermal proteome profiling workflow for studying mitochondrial protein interactions and proteoforms, detecting over 180 proteins with multiple proteoform groups.

The paper identifies an ancient relaxant-inflammatory response in sponges during deflation, driven by actomyosin relaxation and associated with inflammation-like states.

The paper introduces a high-throughput glycoproteomics method to quantify brain glycoproteome changes induced by gut microbiome composition.

The paper assesses the impact of phosphorylation on protein thermal stability using phospho-TPP in HeLa cells, finding that phosphorylation affects stability less than previously reported.

The paper develops a statistical method to analyze thermal proteome profiles and identifies off-target drug interactions in epigenetic drugs.