Results 21 to 30 of about 204,757 (287)

Acetylation of WRN protein regulates its stability by inhibiting ubiquitination. [PDF]

PLoS ONE, 2010
WRN is a multi-functional protein involving DNA replication, recombination and repair. WRN acetylation has been demonstrated playing an important role in response to DNA damage.
Kai Li, Rui Wang, Enerlyn Lozada, Wei Fan, David K Orren, Jianyuan Luo   +5 more
doaj   +1 more source

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

Biophysical 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, Luis Godoy, Adrian Lopez, Allison Matsumura, Kiana Boc, Travis J. Stewart, Josh E. Baker, Bradley S. Ferguson   +7 more
doaj   +1 more source

Progress of Acetylation Modification in Plants

Agronomy
Protein acetylation, a conserved post-translational modification, is collaboratively catalyzed by acetyltransferases and deacetylases and is widespread in plants.
Ruiqi Li, Xuezhong Li, Ying He, Xiaoyuan Chen, Jing Li, Chuxiong Zhuang   +5 more
doaj   +1 more source

Lysine acetylation regulates the interaction between proteins and membranes

Nature Communications, 2021
Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates the function of membrane proteins.
Alan K. Okada, Kazuki Teranishi, Mark R. Ambroso, Jose Mario Isas, Elena Vazquez-Sarandeses, Joo-Yeun Lee, Arthur Alves Melo, Priyatama Pandey, Daniel Merken, Leona Berndt, Michael Lammers, Oliver Daumke, Karen Chang, Ian S. Haworth, Ralf Langen   +14 more
doaj   +1 more source

How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?

Frontiers in Neuroscience, 2022
N-α-acetylation is a frequently occurring post-translational modification in eukaryotic proteins. It has manifold physiological consequences on the regulation and function of several proteins, with emerging studies suggesting that it is a global ...
Aditya Iyer, Arshdeep Sidhu, Vinod Subramaniam   +2 more
doaj   +1 more source

Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation

Nature 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, Rajat Gupta, Linda Baldus, David Lyon, Takeo Narita, Michael Lammers, Chunaram Choudhary, Brian T. Weinert   +7 more
doaj   +1 more source

Influence of N^ε-Lysine Acetylation on the Formation of Protein Aggregates and Antibiotic Persistence in E. coli

Molecules
Numerous studies indicate that reversible Nε-lysine acetylation in bacteria may play a key role in the regulation of metabolic processes, transcription and translation, biofilm formation, virulence, and drug resistance.
Karolina Stojowska-Swędrzyńska, Dorota Kuczyńska-Wiśnik, Ewa Laskowska   +2 more
doaj   +1 more source

Acetylation of AMPA Receptors Regulates Receptor Trafficking and Rescues Memory Deficits in Alzheimer's Disease

iScience, 2020
Summary: In Alzheimer's disease (AD), decreases in the amount and synaptic localization of AMPA receptors (AMPARs) result in weakened synaptic activity and dysfunction in synaptic plasticity, leading to impairments in cognitive functions.
Margaret O'Connor, Yang-Ping Shentu, Guan Wang, Wen-Ting Hu, Zhen-Dong Xu, Xiao-Chuan Wang, Rong Liu, Heng-Ye Man   +7 more
doaj   +1 more source

Redox state and the sirtuin deacetylases are major factors that regulate the acetylation status of the stress protein NQO1

Frontiers in Pharmacology, 2022
The stress induced protein NQO1 can participate in a wide range of biological pathways which are dependent upon the interaction of NQO1 with protein targets.
David Siegel, Peter S. Harris, Cole R. Michel, Cole R. Michel, Rafael de Cabo, Kristofer S. Fritz, David Ross   +6 more
doaj   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

FEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source