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Article

Loop interactions and dynamics tune the enzymatic activity of the human histone deacetylase 8.

Journal of the American Chemical Society - 27 Nov 2013

Kunze Micha B A, Wright David W, Werbeck Nicolas D, Kirkpatrick John, Coveney Peter V, Hansen D Flemming

Abstract excerpt

The human histone deacetylase 8 (HDAC8) is a key hydrolase in gene regulation and has been identified as a drug target for the treatment of several cancers. Previously the HDAC8 enzyme has been extensively studied using biochemical techniques, X-ray crystallography, and computational methods. Those investigations have yielded detailed information about the active site and have demonstrated that the substrate...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 24171457
DOI: 10.1021/ja408184x
PMCID: PMC3926704

Genes

HDAC8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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