Results 1 to 10 of about 259,600 (294)

Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins [PDF]

open access: yesnpj Metabolic Health and Disease
Protein 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
doaj   +2 more sources

Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II [PDF]

open access: goldCell Reports, 2017
Summary: Acetyl coenzyme A (AcCoA), a key intermediate in mitochondrial metabolism, N-acetylates lysine residues, disrupting and, in some cases, regulating protein function.
Andrew M. James   +6 more
doaj   +2 more sources

Skeletal muscle alpha actin acetylation enhances myosin binding and increases calcium sensitivity [PDF]

open access: yesBiophysical Reports
Skeletal muscle alpha actin (ACTA1) is important for muscle contraction and relaxation, with historical studies focused on ACTA1 mutations in muscle dysfunction.
Samantha S. Romanick   +7 more
doaj   +2 more sources

Contribution of Nε-lysine Acetylation towards Regulation of Bacterial Pathogenesis

open access: yesmSystems, 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

Interplay between p300 and HDAC1 regulate acetylation and stability of Api5 to regulate cell proliferation

open access: yesScientific 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

Molecular Characterization and Clinical Relevance of Lysine Acetylation Regulators in Urological Cancers

open access: yesFrontiers 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
doaj   +1 more source

Acetylation-mediated suppression of transcription-independent memory: bidirectional modulation of memory by acetylation. [PDF]

open access: yesPLoS 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

Position-specific analysis and prediction for protein lysine acetylation based on multiple features. [PDF]

open access: yesPLoS ONE, 2012
Protein lysine acetylation is a type of reversible post-translational modification that plays a vital role in many cellular processes, such as transcriptional regulation, apoptosis and cytokine signaling.
Sheng-Bao Suo   +6 more
doaj   +1 more source

Acetylation-dependent coupling between G6PD activity and apoptotic signaling

open access: yesNature 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
doaj   +1 more source

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