Results 281 to 290 of about 73,046 (329)

Amelioration of Memory Deficits in a Transgenic Mouse Model of Alzheimer’s Disease by Manipulation of the Histone Acetyltransferase p300/CBP Associated Factor (PCAF)

, 2019
Samantha D. Creighton
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Anserine, a Histidine-Containing Dipeptide, Suppresses Pressure Overload-Induced Systolic Dysfunction by Inhibiting Histone Acetyltransferase Activity of p300 in Mice. [PDF]

Int J Mol Sci
Sunagawa Y, Tsukabe R, Irokawa Y, Funamoto M, Suzuki Y, Yamada M, Shimizu S, Katanasaka Y, Hamabe-Horiike T, Kawase Y, Naruta R, Shimizu K, Mori K, Hosomi R, Komiyama M, Hasegawa K, Morimoto T.   +16 more
europepmc   +1 more source

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Histone Acetyltransferases

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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Histone acetyltransferase complexes

Seminars in Cell & Developmental Biology, 1999
Modification 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, 2020
Lysine 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, 2001
Histone 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, 2008
Histone 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, 2009
Drugs 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, TAMBARO FP, MAI A, ALTUCCI, Lucia   +3 more
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Histone acetyltransferases: function, structure, and catalysis

Current Opinion in Genetics & Development, 2001
Histone 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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MYST-family histone acetyltransferases: beyond chromatin

Cellular and Molecular Life Sciences, 2010
Covalently 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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