Results 321 to 330 of about 223,415 (361)
Some of the next articles are maybe not open access.
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. Roth, J. Denu, C. Allis
semanticscholar +3 more sources
▪ 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. Roth, J. Denu, C. Allis
semanticscholar +3 more sources
Journal of Medicinal Chemistry, 2020
p300/CBP are ubiquitously expressed pleiotropic lysine acetyl transferases and play a key role as transcriptional co-activators that are essential for a multitude of cellular processes.
Yaxi Yang +13 more
semanticscholar +1 more source
p300/CBP are ubiquitously expressed pleiotropic lysine acetyl transferases and play a key role as transcriptional co-activators that are essential for a multitude of cellular processes.
Yaxi Yang +13 more
semanticscholar +1 more source
The CBP/p300 histone acetyltransferases function as plant-specific MEDIATOR subunits in Arabidopsis.
Journal of Integrative Plant Biology, 2020In eukaryotes, MEDIATOR is a conserved multi-subunit complex that links transcription factors and RNA polymerase II and that thereby facilitates transcriptional initiation.
Jing Guo +7 more
semanticscholar +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
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 ...
openaire +4 more sources
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
openaire +2 more sources
Roles of Histone Acetyltransferases and Deacetylases in the Retinal Development and Diseases
Molecular Neurobiology, 2023Jingjing Wang +8 more
semanticscholar +1 more source
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
openaire +4 more sources
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
openaire +2 more sources