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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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Discovery of Highly Potent, Selective, and Orally Efficacious p300/CBP Histone Acetyltransferases Inhibitors.

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
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ArylamineN-acetyltransferases

Expert Opinion on Drug Metabolism & Toxicology, 2007
Arylamine N-acetyltransferases (NATs), known as drug- and carcinogen-metabolising enzymes, have had historic roles in cellular metabolism, carcinogenesis and pharmacogenetics, including epidemiological studies of disease susceptibility. NAT research in the past 5 years builds on that history and additionally paves the way for establishing the following
Sim, Edith   +2 more
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Human acetyltransferase polymorphisms

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 1997
Conjugation of primary amino and hydroxylamino groups with acetate, catalyzed by acetyl CoA-dependent arylamine acetyltransferase (NAT) enzymes, may play an important role in the intricate series of metabolic pathways that produce or prevent toxicity following exposure to homo- and heterocyclic arylamine and hydrazine xenobiotics.
D M, Grant   +7 more
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Choline Acetyltransferase

CRC Critical Reviews in Biochemistry, 1977
Acetylcholine is essential to neural function. It synthesis is catalyzed by choline acetyltransferase, the enzyme responsible for the acetylation of choline by acetyl coenzye A, a reaction favored slightly thermodymodynamically and not at all kinetically. An analytically pure enzyme still has not been obtained; however, method of purification have been
Henry G. Mautner, David Nachmansohn
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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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N-Acetyltransferases, O-Acetyltransferases, and N, O-Acetyltransferases: Enzymology and Bioactivation

1994
Publisher Summary Acetyltransferases play a central role in the metabolic disposition, detoxication, and bioactivation of a diverse group of drugs—carcinogens and other xenobiotics. Acetylation is a major metabolic pathway for primary aromatic amines (arylamines, ArNH) and hydrazines.
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Chloramphenicol Acetyltransferase Assay

Cold Spring Harbor Protocols, 2010
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
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ACETYLCHOLINE AND CHOLINE ACETYLTRANSFERASE

Neurochemistry International, 1980
The thermodynamics and kinetics of the alcoholysis of thiolesters are discussed and related to choline acetyltransferase. The conformation and rotational barriers of acetylcholine are described as is the specific inability of choline to induce depolarization. Evidence is presented for the involvement of imidazole and the non-involvement of thiol groups
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