Results 91 to 100 of about 438,961 (309)
AMB Express, 2017 Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes.
Guangyuan Wang +4 more
doaj +1 more source
FEBS Open Bio, EarlyView.KDAC6 has been associated with cell motility and actin structures, but specific domain contributions are not established. The two catalytic domains have differential effects on motility and F‐actin regulation, affecting cortical F‐actin density, motility, stress fibers, and cell spreading.
Taylor V. Joseph +7 more
wiley +1 more source
Identification of Novel Protein Lysine Acetyltransferases in
mBio, 2018 Posttranslational modifications, such as Nε-lysine acetylation, regulate protein function. Nε-lysine acetylation can occur either nonenzymatically or enzymatically.
David G. Christensen +8 more
doaj +1 more source
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT Background Hereditary Spastic Paraplegia (HSP) comprises a group of rare genetic diseases characterized by length‐dependent axonal degeneration of the corticospinal tracts and dorsal columns, whose main clinical feature is spastic gait. Pathogenic variants in the SPG4 gene cause Spastic Paraplegia Type 4 (SPG4‐HSP), the most common form of HSP.
Gaia Fattorini +12 more
wiley +1 more source
PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
Nature Communications, 2019 p53 acetylation is indispensable for its transcriptional activity and tumor suppressive function. However, the identity of reader protein(s) for p53 acetylation remains elusive. PBRM1, the second most highly mutated tumor suppressor gene in kidney cancer,
Wei-Jia Cai +12 more
semanticscholar +1 more source
Advanced Functional Materials, EarlyView.Schematic illustration of LNP‐MPG nuclei‐targeting delivery of HMW‐FGF2 promoting histone acetylation to regulate the fate of DPSCs and treat spinal cord injury. LNPs components include pHMW‐FGF2 plasmid, DSPC, Dlin‐MC3‐DMA, cholesterol, and PEG2000, and are modified with MPG to form HMW‐FGF2@LNP‐MPG (HLM). HLM nuclei‐targets DPSCs to deliver HMW‐FGF2,
Heng Zhou +6 more
wiley +1 more source
Beyond Histones: New Substrate Proteins of Lysine Deacetylases in Arabidopsis Nuclei
Frontiers in Plant Science, 2018 The reversible acetylation of lysine residues is catalyzed by the antagonistic action of lysine acetyltransferases and deacetylases, which can be considered as master regulators of their substrate proteins.
Magdalena Füßl +11 more
doaj +1 more source
Aspirin-NHS Ester Mediated Acetylation of Lysine Residues in β-Conglycinin: Implications for Cancer Research in NF-κB [PDF]
Post-translational modifications (PTMs) represent a dynamic and intricate layer of cellular regulation that significantly contributes to the diversification of protein functions (1).
Syon, Schlecht +2 more
core +1 more source
Genetically Programmed Shape‐Morphing of Engineered Living Materials
Advanced Functional Materials, EarlyView.Here, bacterial and mammalian engineered living materials (ELMs) are presented, in which living cells direct genetically programmed and enzymatically mediated shape‐morphing. The resulting deformation and shape‐recovery can be actuated in a genetically controlled manner by an ELM incorporating out‐of‐equilibrium counteracting biochemical reactions with
Jan Becker +7 more
wiley +1 more source
Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli
, 2018 Protein lysine acetylation is a widely conserved posttranslational modification in all three domains of life. Lysine acetylation frequently occurs in aminoacyl-tRNA synthetases (aaRSs) from many organisms.
Dieter Söll +3 more
core +1 more source