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Regulation of Choline Acetyltransferase
1989Publisher Summary This chapter presents the studies related to choline acetyltransferase (ChAT) and cholinergic biology into a more comprehensive neurobiological context. The recent results of biochemical, immunological, molecular biological, arid immunocytochemical studies of ChAT and its regulation are discussed.
J E Vaughn, P M Salvaterra
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Nomenclature for N-acetyltransferases
Pharmacogenetics, 1995A consolidated classification system is described for prokaryotic and eukaryotic N-acetyltransferases in accordance with the international rules for gene nomenclature. The root symbol (NAT) specifically identifies the genes that code for the N-acetyltransferases, and NAT* loci encoding proteins with similar function are distinguished by Arabic numerals.
Kostas P. Vatsis +12 more
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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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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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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 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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Immunohistochemistry of Choline Acetyltransferase
1979Publisher Summary This chapte discusses the problems related to immunohistochemistry of choline acetyltransferase (ChAT)-containing systems in the brain and spinal cord. The synthetic enzyme ChAT is a definitive marker for cholinergic neurons and their processes.
Patrick L. McGeer +3 more
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CBP, a transcriptional coactivator and acetyltransferase
Biochemistry and Cell Biology, 2001The CREB binding protein (CBP) was first identified as a protein that specifically binds to the active phosphorylated form of the cyclic-AMP response element binding protein (CREB). CBP was initially defined as a transcriptional coactivator that, as a result of its large size and multiple protein binding domain modules, may function as a molecular ...
Michael J. Hendzel, Kirk J. McManus
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Regulation of Arylamine N-Acetyltransferases
Current Drug Metabolism, 2008Acetylation catalysed by the arylamine N-acetyltransferases (NATs; 2.3.1.5) is a major biotransformation pathway for arylamine and hydrazine drugs, as well as many carcinogens that we are exposed to on a daily basis. These compounds can either be detoxified by NATs or bioactivated to metabolites that have the potential to cause toxicity such as cancer.
Butcher, Neville J. +2 more
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Chloramphenicol Acetyltransferase Assay
Cold Spring Harbor Protocols, 2010INTRODUCTIONWhen 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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Automation of a chloramphenicol acetyltransferase assay
Analytical Biochemistry, 1990Accurate quantification of chloramphenicol acetyltransferase (CAT) enzyme activity in a large number of samples has been achieved through robotization of a CAT assay on a laboratory workstation (Biomek 1000). The basic principle of this CAT assay relies on the selective diffusion of [3H]acetylchloramphenicol into a water-immiscible liquid scintillation
Daniel Astinotti +2 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.
Yujun George Zheng, Jiang Wu
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