PARP-7 is a mono(ADP-ribosyl) transferase that directs an extensive ADP-ribosylated proteome to control microtubule stability, and regulate ovarian cancer cell growth and motility.

A combined chemical genetics, proximity labeling, and ADP-ribose site mapping approach shows that PARP-7 mono-ADP-ribosylates immune-relevant proteins on cysteine amino acids.

Identification of PARP1 trapping as the major contributor of PARP1 inhibitor-induced innate immune response.

The polymerase activity of PARP1 is converted to hydrolase activity upon binding of Histone Parylation Factor 1 (HPF1) with nucleosome activators.

As the first fully genetically encoded method, PARIS allows cell-specific, long-term, repeated measurements of gap junctional coupling with high spatiotemporal resolution, facilitating its study in both health and disease.

Basal ganglia output neurons use the NALCN leak channel to maintain their characteristic tonic firing, and this channel is important for the modulation of firing by metabolic or receptor-mediated signals.

Tyrosine phosphorylation of the intracellular domain of LRP1 serves as a molecular switch to regulate cellular cholesterol homeostasis through nuclear hormone receptor-mediated regulation of the cellular cholesterol exporter ABCA1.

Upon genotoxic stress, the FBXL10-RNF68-RNF2 ubiquitin ligase complex mono-ubiquitylates histone H2A and mediates H2A/H2A.Z exchange to repress transcription and ensures proper high fidelity homologous recombination repair.

Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.

In depth characterization of gene expression in the mouse hypothalamus will facilitate understanding of the molecular pathways that affect metabolic traits and discovers new genes associated with these pathways.