Tools
Tools
Ganesan, A. 
ORCID: https://orcid.org/0000-0003-4862-7999
(2020)
Targeting the Zinc-Dependent Histone Deacetylases (HDACs) for Drug Discovery.
In:
Topics in Medicinal Chemistry.
Topics in Medicinal Chemistry
.
Springer, pp. 1-27.
ISBN 978-3-030-42981-2
Abstract
In humans, the zinc-dependent histone deacetylases (HDACs) are a family of 11 nonredundant isoforms that catalyze the dynamic reversal of posttranslationally modified acyl-lysine residues back to lysine. At the epigenetic level, HDACs have a critical gene silencing effect, promoting the compaction of histone tails with DNA to prevent transcription. In addition, HDACs deacylate many nonhistone substrates in diverse cellular compartments to profoundly influence protein structure and function. While the action of HDACs is indispensable to normal physiology, their abnormal overexpression is linked to the majority of human diseases. Consequently, the inhibition of HDACs has become a valuable target for therapeutic applications. Numerous potent small molecules are known, of both natural product and synthetic origin, that inhibit HDACs, primarily by reversibly interacting with the zinc cation within the enzyme active site. At the present time, five such HDAC inhibitors have received regulatory approval for the treatment of hematological cancers. This review focuses on the typical zinc-binding groups employed in HDAC inhibitors and the major advances within each class in terms of potency, isoform selectivity, and clinical applications.
| Item Type: | Book Section |
|---|---|
| Uncontrolled Keywords: | anticancer drugs,epigenetics,histone deacetylases,zinc metalloenzymes,molecular medicine,drug discovery,sdg 3 - good health and well-being ,/dk/atira/pure/subjectarea/asjc/1300/1313 |
| Faculty \ School: | Faculty of Science > School of Pharmacy (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Groups > Chemical Biology and Medicinal Chemistry (former - to 2021) |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 12 May 2020 00:17 |
| Last Modified: | 25 Sep 2024 10:42 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/75120 |
| DOI: | 10.1007/7355_2019_68 |
Actions (login required)
 |
View Item |