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Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins [PDF]
npj Metabolic Health and DiseaseProtein acetylation is a fundamental regulatory mechanism occurring primarily on lysine amino acids. Here we report systematic in vivo characterization of cysteine S-acetylation as a widespread post-translational modification in mammalian tissues.
E. Keith Keenan +4 more
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KAT6A acetyltransferase accelerates colorectal cancer progression through upregulating BRD1 protein expression via acetylation modification. [PDF]
Cancer Cell IntLiang Y, Shen Y, Liang S, Wu S, Feng X.
europepmc +2 more sources
Contribution of Nε-lysine Acetylation towards Regulation of Bacterial Pathogenesis
mSystems, 2021 Nε-lysine acetylation is an important, dynamic regulatory posttranslational modification (PTM) that is common in bacteria. Protein acetylomes have been characterized for more than 30 different species, and it is known that acetylation plays important ...
Jackson Luu, Valerie J. Carabetta
doaj +1 more source
Scientific Reports, 2021 Api5, is a known anti-apoptotic and nuclear protein that is responsible for inhibiting cell death in serum-starved conditions. The only known post-translational modification of Api5 is acetylation at lysine 251 (K251).
Virender Kumar Sharma, Mayurika Lahiri
doaj +1 more source
Frontiers in Oncology, 2021 BackgroundLysine acetylation and deacetylation are posttranslational modifications that are able to link extracellular signals to intracellular responses. However, knowledge regarding the status of lysine regulators in urological cancers is still unknown.
Jian Zhang +4 more
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Acetylation-mediated suppression of transcription-independent memory: bidirectional modulation of memory by acetylation. [PDF]
PLoS ONE, 2012 Learning induced changes in protein acetylation, mediated by histone acetyl transferases (HATs), and the antagonistic histone deacetylases (HDACs) play a critical role in memory formation. The status of histone acetylation affects the interaction between
Katja Merschbaecher +2 more
doaj +1 more source
Acetyl-CoA Carboxylase Regulates Global Histone Acetylation [PDF]
Journal of Biological Chemistry, 2012 Histone acetylation depends on intermediary metabolism for supplying acetyl-CoA in the nucleocytosolic compartment. However, because nucleocytosolic acetyl-CoA is also used for de novo synthesis of fatty acids, histone acetylation and synthesis of fatty acids compete for the same acetyl-CoA pool.
Luciano, Galdieri, Ales, Vancura
openaire +2 more sources
Acetylation-dependent coupling between G6PD activity and apoptotic signaling
Nature Communications, 2023 Lysine acetylation has been discovered in thousands of non-histone human proteins, including most metabolic enzymes. Deciphering the functions of acetylation is key to understanding how metabolic cues mediate metabolic enzyme regulation and cellular ...
Fang Wu +7 more
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N-terminal acetylation can stabilize proteins independent of their ubiquitination
Scientific Reports, 2023 The majority of proteins in mammalian cells are modified by covalent attachment of an acetyl-group to the N-terminus (Nt-acetylation). Paradoxically, Nt-acetylation has been suggested to inhibit as well as to promote substrate degradation.
Bert van de Kooij +6 more
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mSystems, 2016 N ε-Lysine acetylation has been recognized as a ubiquitous regulatory posttranslational modification that influences a variety of important biological processes in eukaryotic cells.
Valerie J. Carabetta +4 more
doaj +1 more source