Results 201 to 210 of about 30,339 (261)
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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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Choline acetyltransferase and carnitine acetyltransferase in the placenta of the mouse

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1977
Abstract 1. The major 1-14C-acetyl labelled metabolite as identified by high voltage electrophoresis and thin layer chromatography was 1-14C-acetylcarnitine when crude or dialyzed mouse placenta homogenates were incubated in the absence or presence of exogenous 1-carnitine respectively and with 1-14C-acetylcoenzyme A. 2.
F, Welsch, S K, McCarthy
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A snapshot of carnitine acetyltransferase

Trends in Biochemical Sciences, 2003
Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I
Rona R, Ramsay, James H, Naismith
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Acetyltransferases and susceptibility to chemicals

Toxicology Letters, 1992
Arylamine chemicals inflict a number of toxicities including cancer. Metabolic activation (i.e., oxidation) is required in order to elicit the toxic actions. Acetylation is an important step in the metabolic activation and deactivation of arylamines. N-acetylation forms the amide derivative which is often nontoxic.
D W, Hein   +7 more
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The phosphorylation of choline acetyltransferase

Neurochemical Research, 1989
Human placental Choline Acetyltransferase (ChAT) has been shown to be phosphorylated in vitro by kinases present in rat brain. Phosphorylation occurs at a single site with the exclusive phosphoamino acid being serine. ChAT phosphorylation was shown to be calcium, and not cyclic nucleotide, dependent and was inhibited by inhibitors of calcium/calmodulin
G, Bruce, L B, Hersh
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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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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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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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