Results 281 to 290 of about 438,961 (309)
Some of the next articles are maybe not open access.

Acetylome profiling reveals extensive involvement of lysine acetylation in the conversion of muscle to meat.

Journal of Proteomics, 2019
Protein lysine acetylation is an post-translational modification that regulates gene expression, metabolism, cell signaling, and diseases, but its implication in the postmortem (PM) meat quality development is basically unclear.
Shengwang Jiang   +4 more
semanticscholar   +1 more source

Lysine acetylation contributes todevelopment, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus.

Environmental Microbiology, 2019
Aspergillus flavus (A. flavus) is a pathogenic fungus that produces carcinogenic aflatoxins, posing a great threat to crops, animals and humans. Lysine acetylation is one of the most important reversible post-translational modifications, and plays a ...
Guang Yang   +9 more
semanticscholar   +1 more source

Mechanism and Kinetics of Acetyl-Lysine Binding to Bromodomains

Journal of Chemical Theory and Computation, 2013
Bromodomains are four-helix bundle proteins that specifically recognize acetylation of lysine side chains on histones. The available X-ray structures of bromodomain/histone tail complexes show that the conserved Asn residue in the loop between helices B and C is involved in a hydrogen bond with the acetyl-lysine side chain.
Magno, Andrea   +2 more
openaire   +4 more sources

Proteomic analysis reveals that lysine acetylation mediates the effect of antemortem stress on postmortem meat quality development.

Food Chemistry, 2019
To explore the involvement of protein lysine acetylation in the conversion of muscle to meat, a quantitative analysis of the acetylome in postmortem porcine muscle with or without antemortem stress was conducted.
Bing Zhou   +4 more
semanticscholar   +1 more source

PLMLA: prediction of lysine methylation and lysine acetylation by combining multiple features

Molecular BioSystems, 2012
Abstract Post-translational lysine methylation and acetylation are two major modifications of lysine residues. They play critical roles in various biological processes, especially in gene regulation. Identification of protein methylation and acetylation sites would be a foundation for understanding their modification dynamics and ...
Shao-Ping, Shi   +5 more
openaire   +2 more sources

Characterizing lysine acetylation of Escherichia coli type II citrate synthase

The FEBS Journal, 2019
The citrate synthase (CS) catalyzes the first reaction of the tricarboxylic acid cycle, playing an important role in central metabolism. The acetylation of lysine residues in the Escherichia coli Type II CS has been identified at multiple sites by ...
Suryawanshi Venkat Shivaji   +5 more
semanticscholar   +1 more source

Deep learning based prediction of reversible HAT/HDAC-specific lysine acetylation

Briefings Bioinform., 2019
Protein lysine acetylation regulation is an important molecular mechanism for regulating cellular processes and plays critical physiological and pathological roles in cancers and diseases.
Kai Yu   +8 more
semanticscholar   +1 more source

Analysis of Protein Lysine Acetylation In Vitro and In Vivo

Current Protocols in Protein Science, 2008
AbstractProtein lysine acetylation, referring to acetylation of the ɛ‐amino group of a lysine residue, has recently emerged as an important post‐translational modification for regulating protein functions in various organisms. Like phosphorylation, lysine acetylation is a rapidly reversible and precisely controlled covalent modification that serves as ...
Nadine, Pelletier   +2 more
openaire   +2 more sources

Mitochondria Lysine Acetylation and Phenotypic Control

2019
Mitochondria have a central role in cellular metabolism and reversible post-translational modifications regulate activity of mitochondrial proteins. Thanks to advances in proteomics, lysine acetylation has arisen as an important post-translational modification in the mitochondrion.
openaire   +2 more sources

Properties of Troponin C Acetylated at Lysine Residues

Biochemistry, 1995
We have studied the properties of rabbit skeletal troponin C (TnC) fully acetylated at its lysine residues (AcTnC). Acetylation causes a decrease in thermal stability of both domains of TnC in the absence of Ca2+. At 25 degrees C, the acetylated C-terminal domain of TnC is almost completely unfolded and the melting temperature of the N-terminal domain ...
Z, Grabarek, Y, Mabuchi, J, Gergely
openaire   +2 more sources

Home - About - Disclaimer - Privacy