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Correction for Luo et al., An acetyltransferase moonlights as a regulator of the RNA binding repertoire of the RNA chaperone Hfq in <i>Escherichia coli</i>. [PDF]
Proc Natl Acad Sci U S Aeuropepmc +1 more source
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Histone acetyltransferase complexes: one size doesn't fit all
Nature Reviews Molecular Cell Biology, 2007Jerry L Workman
exaly +2 more sources
Gut, 2023
Objective The protein post-translational modification (PTM) in host cells can be rewritten by bacterial enzymes and represents an unprecedented mechanism in the communication between intestinal flora and the host.
Yi Jiang +8 more
semanticscholar +1 more source
Objective The protein post-translational modification (PTM) in host cells can be rewritten by bacterial enzymes and represents an unprecedented mechanism in the communication between intestinal flora and the host.
Yi Jiang +8 more
semanticscholar +1 more source
Choline acetyltransferase and carnitine acetyltransferase in the placenta of the mouse
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1977Abstract 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.
Susan K. McCarthy, Frank Welsch
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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
openaire +2 more sources
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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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
openaire +5 more sources
Human acetyltransferase polymorphisms
Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, 1997Conjugation 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.
Hillary J Chen +7 more
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A snapshot of carnitine acetyltransferase
Trends in Biochemical Sciences, 2003Carnitine 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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