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The Histone deacetylase IIb family consists of HDAC6 and HDAC10, two zinc-dependent enzymes mainly functioning as deacetylases for both histone and non-histone proteins. HDAC6 possesses two independent catalytic domains and is localized primarily in the cytoplasm, where it participates in microtubule deacetylation, protein trafficking, and stress responses. HDAC10 contains one catalytic domain and shuttles between the nucleus and cytoplasm, with roles in DNA repair and autophagy. Both are considered promising therapeutic targets due to their involvement in cancer progression and neurodegenerative conditions. Selectivity challenges and off-target effects are important considerations in drug development for these enzymes[1][2][3][6].
Inhibition of HDAC catalytic activity; Zinc-binding group targeting (HDAC inhibitors act via zinc chelation at the active site); Regulation of acetylation status of histones and non-histone proteins
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