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Histone acetyltransferase (HAT) inhibitors target the writers of lysine acetylation on histones and other proteins. Acetylation neutralizes the positive charge of histone tails and favors transcription. In 1996 a Tetrahymena HAT was found to be related to a yeast transcriptional regulator, which linked histone acetylation to gene activation. In the same year the coactivators p300 and CREB-binding protein (CBP) were shown to be histone acetyltransferases. C646, found in 2010 by virtual ligand screening, is a selective inhibitor of the p300/CBP HAT domain. MG149 and NU 9056 target lysine acetyltransferase 5 (KAT5, Tip60), and garcinol is a natural product with broad HAT inhibition. SGC-CBP30 and I-CBP112 bind the CBP/p300 bromodomain rather than the catalytic site.