Results 51 to 60 of about 94,143 (143)

Systematic analysis of the lysine succinylome in the model medicinal mushroom Ganoderma lucidum

open access: yesBMC Genomics, 2019
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]

open access: yesPLoS ONE, 2018
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

The Cancer Cell Metabolic Reprogramming Remodels the Tumor Microenvironment: Molecular Mechanisms and Therapeutic Strategies

open access: yesAdvanced Science, EarlyView.
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

open access: yesHaematologica
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

Succinylation: A Functional Nexus Between Metabolic Reprogramming and Epigenetic Modifications in Cancer

open access: yesMolecules
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

open access: yesAdvanced Science, EarlyView.
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

Chromatin Succinylation Correlates with Active Gene Expression and Is Perturbed by Defective TCA Cycle Metabolism

open access: yesiScience, 2018
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

open access: yesAdvanced Science, EarlyView.
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

Quantitative Succinyl-Proteome Profiling of Turnip (Brassica rapa var. rapa) in Response to Cadmium Stress

open access: yesCells, 2022
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

open access: yesAdvanced Science, EarlyView.
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

Home - About - Disclaimer - Privacy