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

Distinct binding of viral proteins to the same region on the nucleosome surface can result in contrasting changes to higher-order chromatin structure in the host cell.

Genomic landmarks, known generically as ‘CpG islands’, program chromatin structure via their richness in the dinucleotide CG and their skewed composition of DNA bases.

An extensive interface between the proteins RBBP4 and MTA1 defines the three-dimensional architecture of the core NuRD complex and determines the recruitment of the complex to chromatin.

The structure of the chromatin remodeller CHD4 bound to a nucleosome reveals differences to the known Chd1-nucleosome complex and maps cancer mutations.

The human leukemia virus HTLV-1 causes abnormal chromatin looping in tens of thousands of infected T cell clones in each host, and abnormal host transcription both flanking the integrated provirus and at distant loci in cis.

Structural models of the chromatin remodeling enzyme Chd1 in solution and when bound to chromatin indicate that conformational changes to both the enzyme and the nucleosome occur upon nucleotide dependent engagement.

Heterochromatin proteins like the SIR complex in budding yeast use different mechanisms for recruitment to nucleation sites and long-range spread to create a domain of transcriptional silencing.

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.

A new method using permeabilized cells and recombinant histones enables to analyze histone incorporations at the DNA sequence level.