More than 30 years ago, Vincent Allfrey proposed that histone acetylation was associated
with transcriptional activity in eukaryotic cells (Allfrey et al. 1964; Pogo et al. 1966) …

All four histones of the nucleosome core particle are subject to post-translational acetylation
of selected lysine residues in their amino-terminal domains. The modification is ubiquitous …

Histone acetylation is an important regulatory mechanism that controls transcription and
diverse nuclear processes. While great progress has been made in understanding how …

Eukaryotic DNA is packaged into chromatin by histone proteins, which assemble the DNA
into an organized, higher-order structure. The precise organization of chromatin is essential …

In eukaryotes, DNA is assembled with histones to form nucleosomes, the basic subunit of
chromatin structure. The wrapping of DNA around histone octamers to form nucleosomal …

Acetylation of internal lysine residues of core histone N‐terminal domains has been found
correlatively associated with transcriptional activation in eukaryotes for more than three …

Eukaryotic DNA is packaged into a nucleoprotein structure known as chromatin, which is
comprised of DNA, histones, and nonhistone proteins. Chromatin structure is highly …

Transcriptionally active DNA is packaged with histones that are post-translationally
acetylated on multiple lysines within their amino termini. While the majority of this acetylation …

What's Up and Down with Histone Deacetylation and Transcription?: Cell Skip to Main Content
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Recent advances highlight the involvement of histone acetyltransferases in transcriptional
activation and histone deacetylases in transcriptional repression. Transcription factors …