Results 181 to 190 of about 76,328 (190)
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Identification of Lysine-Acetylated Mitochondrial Proteins and Their Acetylation Sites
2015The (ε)N-acetylation of lysine side chains is a highly conserved posttranslational modification of both prokaryotic and eukaryotic proteins. Lysine acetylation not only occurs on histones in the nucleus but also on many mitochondrial proteins in plants and animals.
Hartl, M., König, A., Finkemeier, I.
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Lysine Succinylation and Acetylation in Pseudomonas aeruginosa
Journal of Proteome Research, 2018Pseudomonas aeruginosa is a multi-drug-resistant human opportunistic pathogen largely involved in nosocomial infections. Unfortunately, effective antibacterial agents are lacking. Exploring its physiology at the post-translational modifications (PTMs) level may contribute to the renewal of combat tactics.
Gaviard, Charlotte +5 more
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Mitochondria Lysine Acetylation and Phenotypic Control
2019Mitochondria have a central role in cellular metabolism and reversible post-translational modifications regulate activity of mitochondrial proteins. Thanks to advances in proteomics, lysine acetylation has arisen as an important post-translational modification in the mitochondrion.
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PLMLA: prediction of lysine methylation and lysine acetylation by combining multiple features
Molecular BioSystems, 2012Post-translational lysine methylation and acetylation are two major modifications of lysine residues. They play critical roles in various biological processes, especially in gene regulation. Identification of protein methylation and acetylation sites would be a foundation for understanding their modification dynamics and molecular mechanism.
Shao-Ping, Shi +5 more
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Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions
ACS Chemical Biology, 2014Bromodomains are protein modules that bind to acetylated lysine residues. Their interaction with histone proteins suggests that they function as "readers" of histone lysine acetylation, a component of the proposed "histone code". Bromodomain-containing proteins are often found as components of larger protein complexes with roles in fundamental cellular
Michael, Brand +10 more
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Properties of Troponin C Acetylated at Lysine Residues
Biochemistry, 1995We have studied the properties of rabbit skeletal troponin C (TnC) fully acetylated at its lysine residues (AcTnC). Acetylation causes a decrease in thermal stability of both domains of TnC in the absence of Ca2+. At 25 degrees C, the acetylated C-terminal domain of TnC is almost completely unfolded and the melting temperature of the N-terminal domain ...
Z, Grabarek, Y, Mabuchi, J, Gergely
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Computational Prediction of Lysine Acetylation Proteome-Wide
2012Several studies have contributed to our knowledge of the enzymology underlying acetylation, including focused efforts to understand the molecular mechanism of substrate recognition by several acetyltransferases; however, conventional experiments to determine intrinsic features of substrate site specificity have proven challenging.
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