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Histone Deacetylases (HDAC) Targeted Library Selection

Histone Deacetylases (HDAC) Targeted Library Selection

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ChemDiv presents Histone Deacetylases (HDAC) Targeted Library Selection.

Histone deacetylases (HDAC) are a class of enzymes that remove acetyl groups (O=C-CH3) from an ε-N-acetyl lysine amino acid on a histone, allowing the histones to wrap the DNA more tightly. This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. Its action is opposite to that of histone acetyltransferase. HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins.

Publications
1. Luckhurst C.A., et al. Potent, Selective, and CNS Penetrant Tetrasubstituted Cyclopropane Class IIa Histone Deacetylase (HDAC) Inhibitors. ACS Med Chem Lett. 2015;7(1):34 39.

2. Luckhurst CA, et al. Development and characterization of a CNS penetrant benzhydryl hydroxamic acid class IIa histone deacetylase inhibitor. Bioorg Med Chem Lett. 2019;29(1):83 88.

3. Blum C.A., Jarpe M.B. Isoform Selective Histone Deacetylase (HDAC) Inhibitors in the Treatment of Cancer. Chapter 13, Medicinal Chemistry Reviews 2018; 53:245 264.

4. Wagner F.F., et al. Kinetic and structural insights into the binding of histone deacetylase 1 and 2 (HDAC1, 2) inhibitors. Bioorg . Med. Chem. 2016;24(18):4008 4015.

5. Ferreira de Freitas R., et al. Identification and Structure Activity Relationship of HDAC6 Zinc Finger Ubiquitin Binding Domain Inhibitors. J. Med. Chem. 2018;61(10):4517 4527.
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