Anthony K. L. Leung

The paper shows influenza A virus infection increases global ADP-ribosylation, which inhibits viral replication, and identifies PARP1 as the main enzyme involved, with NS1 counteracting this effect.

The paper shows PAR induces a conformational switch in FUS, enabling sustained condensation through N-terminal PrLD interactions after PAR degradation.

This study shows interferon induces ADP-ribosylation in p62 bodies via PARP14, requiring ubiquitin activation and proteasome activity.

This study identifies FA-induced DNA-protein crosslinks (DPCs) and discovers that FEN1 repairs them via PARylation, revealing a novel PARP1-FEN1 pathway for DPC repair.

The paper identifies a deficient PAR response in Huntington disease patients, suggesting a potential therapeutic target for early intervention.

This study shows that reducing PAR-binding in ZAPS enhances antiviral activity against alphaviruses by disrupting replication complex formation and viral transcript levels.

This paper demonstrates that inhibiting PARP1 and Tankyrases in human pluripotent stem cells reprograms them to a totipotent state with lineage-specific gene expression and proteomic changes, mimicking early embryonic development.

This study investigates PARP13's role in transcriptome regulation during basal and antiviral states, finding it shifts target localization but not binding preferences and supports ISGylation-related gene expression.

The paper introduces a PAR photoaffinity probe to identify PAR-binding proteins, revealing novel binders and demonstrating length-selective PAR binding.

ADPriboDB v2.0 updates a database of ADP-ribosylated proteins with 9,097 entries, including 6,708 new proteins, and links ADP-ribosylation to SARS-CoV-2 protein interactions and other post-translational modifications.

nearBynding characterizes RBP binding preferences relative to RNA structure using CLIP-seq data without peak-calling.