Results 281 to 290 of about 391,128 (337)
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The CBP co-activator is a histone acetyltransferase
Nature, 1996The CBP protein acts as a transcriptional adaptor for many different transcription factors by directly contacting DNA-bound activators. One mechanism by which CBP is thought to stimulate transcription is by recruiting the histone acetyltransferase (HAT) P/CAF to the promoter. Here we show that CBP has intrinsic HAT activity.
Andrew J. Bannister, T. Kouzarides
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Histone Acetyltransferase Complexes and Their Link to Transcription
Critical Reviews in Eukaryotic Gene Expression, 1999Early studies revealing the relationship between the state of histone acetylation and gene transcription were largely indirect. Increasing information regarding the enzymes that catalyze transcription linked acetylation is beginning to clarify this issue.
LeAnn J Howe +2 more
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, 2020
A kind of novel heterojunction structure with black TiO2 and WS2 was prepared with matched energy band and significantly improved visible-light-driven photoelectrochemical activity.
Yan Chen +6 more
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A kind of novel heterojunction structure with black TiO2 and WS2 was prepared with matched energy band and significantly improved visible-light-driven photoelectrochemical activity.
Yan Chen +6 more
semanticscholar +1 more source
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
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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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On the ubiquitous presence of histone acetyltransferase B in eukaryotes [PDF]
FEBS Letters, 1985 Histone acetyltransferase B activity has been found in pea (Pisun sativum) seedlings. The enzyme has been partially purified and it has been found that it is highly specific for H4.
Gerardo López-Rodas +2 more
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Hypothetical protein Rv3423.1 of Mycobacterium tuberculosis is a histone acetyltransferase [PDF]
The FEBS Journal, 2016 We isolated an 8 kDa mycobacterial hypothetical protein, Rv3423.1, from the chromatin of human macrophages infected with Mycobacterium tuberculosis H37Rv.
L. Jose +9 more
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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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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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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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