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Fig. 1 | Clinical Epigenetics

Fig. 1

From: Histone acetyltransferases: challenges in targeting bi-substrate enzymes

Fig. 1

Lysine acetylation is balanced by histone acetyltransferases (HATs) and histone deacetylases (HDACs). Acetylation of lysine residues on the histone tails that protrude from the histone–DNA complex modifies the chromatin structure of the DNA, which allows transcription factors to bind. The transcription factors themselves can be acetylated, which influences promotor activity and specificity. Lysine acetylation of enzymes or nuclear receptors can influence their function. Bromodomain-containing proteins will bind to the acetylated lysine residues. Through lysine acetylations, HATs are involved in many different diseases such as cancer, inflammatory diseases, and neurological disorders. NR nuclear receptor, BRD bromodomain, NE nuclear enzyme, TF transcription factor

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