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The Growing Landscape of Lysine Acetylation Links Metabolism and Cell Signalling
Nature Reviews Molecular Cell Biology, 2014 Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased ...
Chunaram Choudhary +2 more
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Lysine Acetylation and Cancer: A Proteomics Perspective
Journal of Proteomics, 2017Lysine acetylation is a reversible modification controlled by two groups of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (KDACs). Acetylated lysine residues are recognized by bromodomains, a family of evolutionarily conserved domains.
Sergio Encarnación, Jeovanis Gil
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Targeting bromodomains: epigenetic readers of lysine acetylation
Nature Reviews Drug Discovery, 2014 Lysine acetylation is a key mechanism that regulates chromatin structure; aberrant acetylation levels have been linked to the development of several diseases.
P. Filippakopoulos, S. Knapp
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Protein Lysine Acetylation and Its Role in Different Human Pathologies: A Proteomic Approach
Expert Review of Proteomics, 2021Introduction Lysine acetylation is a reversible post-translational modification (PTM) regulated through the action of specific types of enzymes: lysine acetyltransferases (KATs) and lysine deacetylases (HDACs), in addition to bromodomains, which are a ...
Sergio Encarnación +1 more
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Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
Science, 2009 Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation’s cellular roles.
C. Choudhary +7 more
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Trifluoroacetyl Lysine as a Bromodomain Binding Mimic of Lysine Acetylation
ACS Chemical Biology, 2022Genetic code expansion has proven invaluable to the elucidation of functions of defined protein modifications through the site-specific incorporation of noncanonical amino acids. The use of nonhydrolyzable derivatives of post-translational modifications can greatly increase site stoichiometry and half-life.
Gregory M. Miller +4 more
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Protein Lysine Acetylation by p300/CBP [PDF]
Chemical Reviews, 2015 Since their discovery in the 1980s and 1990s, the human protein lysine acetyltransferase encoded by the paralogous p300 and CBP genes has received much interest. p300/CBP functions in regulating the expression of genes controlling several basic cellular processes, such as proliferation and homeostasis, and plays a role in a variety of human diseases ...
Philip A Cole, Beverley M Rabbitts
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Science, 2009
A proteomic-scale analysis of protein acetylation suggests that it is an important biological regulatory mechanism.
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A proteomic-scale analysis of protein acetylation suggests that it is an important biological regulatory mechanism.
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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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