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Histone acetyltransferases: function, structure, and catalysis
Current Opinion in Genetics & 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.
R, Marmorstein, S Y, Roth
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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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Assays for Validating Histone Acetyltransferase Inhibitors
Journal of Visualized Experiments, 2020Lysine acetyltransferases (KATs) catalyze acetylation of lysine residues on histones and other proteins to regulate chromatin dynamics and gene expression. KATs, such as CBP/p300, are under intense investigation as therapeutic targets due to their critical role in tumorigenesis of diverse cancers.
Aaron R, Waddell, Daiqing, Liao
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Structure of histone acetyltransferases.
Journal of molecular biology, 2001Histone acetyltranferase (HAT) enzymes are the catalytic subunits of multisubunit protein complexes that acetylate specific lysine residues on the N-terminal regions of the histone components of chromatin to promote gene activation. These enzymes, which now include more than 20 members, fall into distinct families that generally have high sequence ...
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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 acetyltransferase inhibitors and preclinical studies
Expert Opinion on Therapeutic Patents, 2009Drugs able to regulate the histone modifier enzymes are very promising tools for the treatment of several diseases, such as cancer. Histone acetyltransferase (HAT) inhibitors are compounds able to inhibit the catalytic activity of HATs reported to be active in cancer, or in several other diseases, such as Alzheimer (AD), diabetes and hyperlipidaemia ...
MANZO F +3 more
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MYST-family histone acetyltransferases: beyond chromatin
Cellular and Molecular Life Sciences, 2010Covalently modifying a protein has proven to be a powerful mechanism of functional regulation. N-epsilon acetylation of lysine residues was initially discovered on histones and has been studied extensively in the context of chromatin and DNA metabolism, such as transcription, replication and repair.
Vasileia, Sapountzi, Jacques, Côté
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Histone acetyltransferase activity in rat hepatomas
Journal of Cancer Research and Clinical Oncology, 1989In view of various reports describing differences in histone acetylation between normal rat liver and hepatomas, the behaviour of histone acetyltransferase (EC 2.3.1.48) activity was elucidated in normal rat liver and in a spectrum of well-characterized rat hepatomas of slow, intermediate and rapid growth rates.
H H, Grunicke +5 more
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The MYST Family of Histone Acetyltransferases
2003Multiple chromatin modifying proteins and multisubunit complexes have been characterized in recent years. Histone acetyltransferase (HAT) activities have been the most thoroughly studied, both biochemically and functionally. This review sums up the current knowledge on a specific group of proteins that is extremely well conserved throughout evolution ...
R T, Utley, J, Côté
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Histone acetyltransferases and histone deacetylases of Physarum polycephalum
Cell Biology International Reports, 1992Abstract DEAE-Sepharose chromatography of plasmodial extracts of the myxomycete Physarum polycephalum reveals the presence of multiple histone acetyltransferases and histone deacetylases. Five putative histone acetyltransferases and histone deacetylases.
G BROSCH +5 more
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