Results 1 to 10 of about 191,770 (239)
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
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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
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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
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Position-specific analysis and prediction for protein lysine acetylation based on multiple features. [PDF]
PLoS 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
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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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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
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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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Acetylation of GATA4 on Lysine Residue K313 Promotes Osteoblastic Cells Growth
Cellular Physiology and Biochemistry, 2018 Background/Aims: GATA4, a protein related to osteoblast differentiation and mineralization, whose acetylation is essential for cardiac defects. Here, we aimed to explore the functional impacts of GATA4 acetylation on osteoporosis (OS).
Wenjun You, Lijuan Song, Kun Wang
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Protein Acetylation/Deacetylation: A Potential Strategy for Fungal Infection Control
Frontiers in Microbiology, 2020 Protein acetylation is a universal post-translational modification that fine-tunes the major cellular processes of many life forms. Although the mechanisms regulating protein acetylation have not been fully elucidated, this modification is finely tuned ...
Junzhu Chen +3 more
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