Results 221 to 230 of about 83,086 (267)
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Determination of Protein Lysine Deacetylation
Current Protocols in Protein Science, 2008AbstractHistone deacetylases (HDACs) are members of a diverse family of enzymes that catalyze the removal of an acetyl moiety from an acetyl‐lysine‐containing substrate. HDACs target a variety of substrates, including histone and nonhistone proteins, to mediate alterations in protein localization, stability, and activity.
Danielle J P, Ellis +2 more
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Deacetylation of phenacetin by liver esterase
Biochemical Pharmacology, 1965Abstract Microsomal liver esterase cleaves the amide bond of the phenacetin molecule in vitro yielding p -phenetidine and acetic acid as reaction products. Some kinetic data of this reaction are reported. N-acetyl- p -aminobenzoic acid, being more polar than acetanilide, is hydrolysed about 1000 times slower by the isolated enzyme.
E, Bernhammer, K, Krisch
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Deacetylation of Phenylthioacetate in the Presence of Oximes
Acta Pharmacologica et Toxicologica, 1973Abstract: In the presence of oximes phenylthioacetate is deacetylated and acetylated oximes formed. By measuring the velocity of this transacetylation reaction for a number of oximes in vitro, the slopes are found to differ in a way which resembles the variance in the potency of the oximes in vivo as reactivators for cholinesterases inhibited by alkyl
P, Fèvre Honoré, O, Karlog
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Chemical Acetylation and Deacetylation
2013Lysine acetylation is an important posttranslational modification known to alter protein structure and function. Understanding the mechanisms involved in regulating protein acetylation remains a key factor in elucidating what role this modification plays in numerous disease pathologies.
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Science Signaling, 2009
Proper regulation of acetylation of the nuclear receptor FXR is lost in metabolic disease.
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Proper regulation of acetylation of the nuclear receptor FXR is lost in metabolic disease.
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Histone Deacetylation as a Target for Radiosensitization
2006Due to an increase in the understanding of molecular radiobiology, strategies for enhancing tumor radiosensitivity have begun to focus on targeting the molecules and processes that regulate cellular radioresponse. Toward this end, histone acetylation has begun to receive considerable attention as a potential target for radiosensitization.
David, Cerna +2 more
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Kinetics of N-acetylprocainamide deacetylation
Clinical Pharmacology and Therapeutics, 1980The kinetics of N-acetylprocainamide (NAPA) deacetylation to procainamide (PA) were determined in a normal subject using NAPA-13C, labeled in the acetyl group. The deacetylation clearance of NAPA (ClD) was found to be 6.5 ml/min whereas total NAPA elimination clearance was 231 ml/min, so that 2.8% of the administered NAPA-13C was metabolized by ...
G P, Stec +5 more
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Histone Acetylation and Histone Deacetylation
Molecular Biotechnology, 2002Regulation of inflammatory gene transcription is controlled, at least in part, by the degree of local unwinding of nucleosomal DNA. This unwinding is regulated by histone acetylation--increased acetylation results in a more loosely wound structure allowing access of basal transcription factors and RNA polymerase II.
Kazuhiro, Ito, Ian M, Adcock
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Histone acetylation and deacetylation in yeast
Nature Reviews Molecular Cell Biology, 2003Histone acetylation and deacetylation in the yeast Saccharomyces cerevisiae occur by targeting acetyltransferase and deacetylase enzymes to gene promoters and, in an untargeted and global manner, by affecting most nucleosomes. Recently, new roles for histone acetylation have been uncovered, not only in transcription but also in DNA replication, repair ...
Siavash K, Kurdistani +1 more
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Enzymatic deacetylation of galactoglucomannans
Applied Microbiology and Biotechnology, 1993Several hemicellulolytic microorganisms were screened for their capability of liberating acetyl side groups from native softwood galactoglucomannan. All the microorganisms tested were found to produce an extracellular acetyl glucomannan esterase(s). The highest activity was detected in Schizophyllum commune culture filtrate.
Puls, Jürgen +4 more
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