Results 11 to 20 of about 341,133 (297)

SIRT7-mediated deacetylation of XRCC6 at lysine 591 drives breast cancer progression [PDF]

open access: yesFrontiers in Oncology
RationaleThe acetylation level of XRCC6 is significantly decreased in clinical breast cancer tissues compared with paracancerous tissues; however, the relationship between this alteration and the occurrence and development of breast cancer remains ...
Jie Yin   +15 more
doaj   +2 more sources

Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

open access: yesNature Communications, 2019
Many human proteins are regulated by lysine acetylation, but the degree of acetylation at individual sites is poorly characterized. Here, the authors measure acetylation stoichiometry in the HeLa cell proteome, providing a resource to assess mechanistic ...
Bogi Karbech Hansen   +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

The acetylation of insulin [PDF]

open access: yesBiochemical Journal, 1971
The acetylation of the free amino groups of insulin was studied by reaction of the hormone with N-hydroxysuccinimide acetate at pH6.9 and 8.5. The products formed were separated by chromatography on DEAE-Sephadex and were characterized by isoelectric focusing, by end-group analysis, by the incorporation of [3H]acetyl groups in the molecule, and by ...
D G, Lindsay, S, Shall
openaire   +2 more sources

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

N-terminal acetylation can stabilize proteins independent of their ubiquitination

open access: yesScientific 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
doaj   +1 more source

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