Lactobacillus plantarum regulates host uric acid metabolism via its own nucleoside hydrolase iunH.

A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

The important oncogene KRasG13C can be targeted by covalently binding nucleotide-analogues, resulting in a locked protein that can no longer induce oncogenic signaling.

Studies of the substrate selectivity of concentrative nucleoside transporters provide proof of principle for structure-based improvement of drug delivery by these transporters.

Cryo-EM structures capture different conformational states of chromatin remodeler-nucleosome complexes.

Computational analysis of MNase-seq data reveals that alternatively positioned nucleosomes are prevalent in both yeast and human cells and create significant heterogeneity within cell populations.

NMR spectroscopy, dCypher assays, and CUT&RUN demonstrate that occlusion of the histone tails in the nucleosome context alters histone PTM specificity for a tandem of reader domains.

Disruption of the nucleosome DNA entry-exit site causes readthrough transcription of terminators, decreased nucleosome occupancy, and pervasive noncoding transcription, demonstrating this nucleosomal region protects the genome against inappropriate transcription.

Analysis of conformational heterogeneity in cryo-EM data by a recently developed deep learning method reveals the structure and dynamics of the oncogenic chromatin remodeler ALC1 bound to a poly-ADP-ribosylated nucleosome.

The unwrapping two turns of DNA on Chd1-bound nucleosomes cause the histone H3 tail and ubiquitin to be re-positioned.