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Epigenetic Modulation Using Small Molecules - Targeting Histone Acetyltransferases in Disease
Current Medicinal Chemistry, 2017 Histone acetyltransferases (HATs) are epigenetic drivers that catalyze the acetyl transfer from acetyl-CoA to lysines of both histone and non-histone substrates and thereby induce transcription either by chromatin remodeling or direct transcription ...
André Richters, Angela N Koehler
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The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Cell, 1996 p300/CBP is a transcriptional adaptor that integrates signals from many sequence-specific activators via direct interactions. Various cellular and viral factors target p300/CBP to modulate transcription and/or cell cycle progression. One such factor, the
Vasily Ogryzko +2 more
exaly +2 more sources
Modulation of the activity of histone acetyltransferases by long chain alkylidenemalonates (LoCAMs)
Bioorganic and Medicinal Chemistry, 2011 A novel class of KAT modulators (long chain alkylidenemalonates, LoCAMs) has been identified. Variations of the alkyl chain length can change the activity profile from inhibition of both KAT3A/KAT2B (as derivative 2a) to the peculiar profile of ...
Ciro Milite +2 more
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Annual Review of Biochemistry, 2001
▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
openaire +2 more sources
Histone acetyltransferase complexes
Seminars in Cell & Developmental Biology, 1999Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases.
P A, Grant, S L, Berger
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Fluorescent reporters of the histone acetyltransferase
Analytical Biochemistry, 2008Histone acetyltransferases (HATs) are important chromatin modifying enzymes that catalyze acetylation of specific lysine residues in histone and nonhistone substrates. They participate in multiple cellular processes such as transcriptional regulation and signal transduction.
Jiang, Wu, Yujun George, Zheng
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Histone acetyltransferases: function, structure, and catalysis
Current Opinion in Genetics and Development, 2001Histone acetyltransferases (HATs) directly link chromatin modification to gene activation. Recent structure/function studies provide insights into HAT catalysis and histone binding, and genetic studies suggest cross-talk between acetylation and other histone modifications.
Ronen Marmorstein, Sharon Y Roth
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Structure and function of histone acetyltransferases
Cellular and Molecular Life Sciences, 2001Histone acetyltranferase (HAT) enzymes are the catalytic subunit of large multisubunit HAT complexes that acetylate the epsilon-amino group of specific lysine residues on histone tails to promote transcriptional activation. Recent structural and functional studies on the divergent HAT enzymes Gcn5/PCAF, Esa1 and Hat1 have provided new insights into the
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