Results 51 to 60 of about 94,143 (143)
Systematic analysis of the lysine succinylome in the model medicinal mushroom Ganoderma lucidum
Background Ganoderma lucidum, one of the best-known medicinal mushrooms in the world, produces more than 400 different bioactive compounds. However, the regulation of these bioactive compounds biosynthesis is still unclear.
Guangyuan Wang +4 more
doaj +1 more source
GPSuc: Global Prediction of Generic and Species-specific Succinylation Sites by aggregating multiple sequence features. [PDF]
Lysine succinylation is one of the dominant post-translational modification of the protein that contributes to many biological processes including cell cycle, growth and signal transduction pathways.
Md Mehedi Hasan, Hiroyuki Kurata
doaj +1 more source
This review elucidates how cancer cell metabolic reprogramming—across glucose, lipid, amino acid, and nucleotide pathways—remodels the tumor microenvironment to suppress anti‐tumor immunity and promote immune escape. Targeting these metabolic axes offers promising strategies to overcome immunotherapy resistance and enhance cancer treatment.
Guoqing Xiang +5 more
wiley +1 more source
Lysine succinylation precisely controls normal erythropoiesis
Lysine succinylation (Ksu) has recently emerged as a protein modification that regulates diverse functions in various biological processes. However, the systemically and precise role of lysine succinylation in erythropoiesis remains to be fully ...
Bin Hu +19 more
doaj +1 more source
Metabolic reprogramming and epigenetic remodeling are critical features of tumorigenesis. The process of metabolic reprogramming causes metabolites like Succinyl-CoA to accumulate.
Dan Liu +5 more
doaj +1 more source
Aspirin‐Derived Salicyl‐CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2
Aspirin‐derived salicyl‐CoA serves as a previously unrecognized acyl donor for protein lysine salicylation. This study identifies histone lysine salicylation as a reversible epigenetic modification regulated by CBP and SIRT2, expanding the biochemical actions of aspirin beyond its canonical acetylation‐dependent mechanisms and providing a new framework
Facai Zhang +15 more
wiley +1 more source
Summary: Succinylation is a post-translational protein acylation modification that converts the cationic lysine side chain to an anion with large potential impacts on protein structure and function. Here we characterize the epigenome-wide distribution of
John Smestad +3 more
doaj +1 more source
AARS2‐SIRT5‐Driven DLD K445 Lactylation Promotes Cuproptosis Resistance in Glioblastoma Stem Cells
Lactylation of DLD at K445 by AARS2 suppresses PDH complex activity and reduces DLAT lipoylation, thereby conferring cuproptosis resistance in glioblastoma stem cells. SIRT5‐mediated delactylation restores PDH function and enhances cuproptosis sensitivity.
Mingtian Ding +12 more
wiley +1 more source
Protein post-translational modification (PTM) is an efficient biological mechanism to regulate protein structure and function, but its role in plant responses to heavy metal stress is poorly understood.
Xiong Li +7 more
doaj +1 more source
CD112 Lactylation Drives Dual Immune Evasion From CD8+ T Cells and NK Cells
AARS2 functions as an intracellular lactate sensor and lactyltransferase, catalyzing CD112 K412 lactylation to block ubiquitination‐dependent degradation and stabilize CD112. This pathway suppresses CD8+ T‐cell and NK‐cell cytotoxicity, enabling dual immune evasion.
Zhuoshuo Xu +6 more
wiley +1 more source

