Irina Bezsonova

USP1 inhibition promotes RAD18-dependent PCNA degradation and BRCA1 synthetic lethality

This paper identifies a PIP motif in RAD18 essential for PCNA ubiquitination and shows USP1 inhibition leads to synthetic lethality in BRCA1-deficient cells.

Mechanisms of USP7/MAGEL2 Complex Assembly and Its Mutational Disruption in Neurodevelopmental Diseases

This study investigates the assembly mechanism of the USP7/MAGEL2 complex and identifies mutations that disrupt its formation, linking it to neurodevelopmental diseases.

High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons

This paper uses high-pH NMR to identify hydrogen bonds and foldons in proteins, achieving higher accuracy than traditional methods.

PXL: a Nucleic Acid-Binding Module of Promyelocytic Leukemia Protein

This study identifies a novel nucleic acid-binding module, PXL, in PML-1 and shows it binds G-rich RNA/DNA and modulates the transcriptome.

DNA polymerase η is regulated by mutually exclusive mono-ubiquitination and mono-NEDDylation

This study shows DNA polymerase η is regulated by both mono-ubiquitination and mono-NEDDylation at the same lysine residues, with NEDDylation disrupting foci formation.

Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7)

This study identifies and characterizes MS-8, a small-molecule activator of USP7, showing it activates mutant USP7 in a cellular context and impacts downstream proteins.

Functional Spectrum of USP7 Pathogenic Variants in Hao-Fountain Syndrome: Insights into the Enzyme's Activity, Stability, and Allosteric Modulation

This study analyzes 11 USP7 variants in Hao-Fountain syndrome, showing they affect enzyme activity, stability, and substrate recognition, with some variants responsive to an allosteric activator.

The HSV-1 immediate early protein ICP22 is a J-like protein required for Hsc70 reorganization during lytic infection

This paper shows that HSV-1's ICP22 protein functions as a viral J-like co-chaperone that interacts with Hsc70 to manage protein aggregation during lytic infection.