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Histone deacetylases 1, 2, 3, and 4 are part of a family of zinc-dependent enzymes that remove acetyl groups from lysine residues on histone and non-histone proteins, leading to condensation of chromatin and transcriptional silencing. HDAC1, HDAC2, and HDAC3 are classified as Class I HDACs, predominantly located in the nucleus and highly involved in corepressor complexes regulating transcription and cell cycle progression. HDAC4 belongs to Class IIa and shuttles between the nucleus and cytoplasm, playing specific roles in tissue development, especially in muscle and bone. Abnormal activity or expression of these enzymes is implicated in the development and progression of numerous diseases, including various cancers and neurodegenerative conditions, making them key drug targets for HDAC inhibitors. When using this grouping for data structuring, it is advisable to treat each HDAC isoform as an individual molecular target for accurate annotation and downstream applications.
Inhibition of HDAC activity leading to increased acetylation of histones and non-histone proteins; Chromatin relaxation and enhanced transcription of tumor suppressor genes; Induction of cell cycle arrest, apoptosis, and differentiation in cancer cells
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