Results 121 to 130 of about 381,302 (291)
Ubiquitin carboxyl-terminal peptides. Substrates for ubiquitin activating enzyme.
The carboxyl terminus of ubiquitin is activated in the presence of ATP to enter the ubiquitin cycle in cells. Peptides corresponding to the COOH-terminal region of ubiquitin were synthesized to investigate their effects on the ATP/ubiquitin-dependent proteolytic pathway.
S, Jonnalagadda +4 more
openaire +2 more sources
Pancreatic neuroendocrine tumors frequently silence MEN1 through epigenetic mechanisms. Here, SIRT7 recruits DNMT1 to the MEN1 promoter, drives hypermethylation, and enhances DNA repair. Inhibiting SIRT7 restores MEN1, reduces MRN complex abundance, impairs double‐strand break repair, and sensitizes PanNET models to radiation, supporting SIRT7 as a ...
Jianyun Jiang +11 more
wiley +1 more source
A common pathological hallmark of age-related neurodegenerative diseases is the intracellular accumulation of protein aggregates such as α-synuclein in Parkinson’s disease, TDP-43 in ALS, and tau in Alzheimer’s disease.
Daniel Ortuno +2 more
doaj +1 more source
Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation.
Energy-dependent proteolysis in rabbit reticulocyte lysates has an absolute requirement for both ATP and ubiquitin that is believed due to the ATP-dependent covalent conjugation of ubiquitin (Ub) to substrate proteins as a signal event. Recently the enzyme responsible for activation of ubiquitin has been purified to near homogeneity by covalent ...
A L, Haas +3 more
openaire +2 more sources
G3BP1 Succinylation at K413 is Critical for Cardiac Function by Modulating PI3K‐AKT‐mTOR Signal Axis
Schematic illustrating the impact of G3BP1 succinylation at K413 on cardiac function. In the healthy human heart, G3BP1 succinylation maintains homeostatic mTOR signaling. In patients with dilated cardiomyopathy (DCM) and heart failure (HF), G3BP1 de‐succinylation induces RagA expression and disrupts the binding of the TSC1/2 complex, leading to the ...
Yuan Zhang +9 more
wiley +1 more source
Background Ubiquitination is a major post-translational protein modification that regulates essentially all cellular and physiological pathways in eukaryotes.
Chunyu Zhang +7 more
doaj +1 more source
To TRIM or not to TRIM: the balance of host-virus interactions mediated by the ubiquitin system.
The innate immune system responds rapidly to protect against viral infections, but an overactive response can cause harmful damage. To avoid this, the response is tightly regulated by post-translational modifications (PTMs).
Adam Hage, Ricardo Rajsbaum
semanticscholar +1 more source
Lactate in cervical cancer induces HNRNPU K181 lactylation, opposed by NAA50‐mediated acetylation and suppressed by Pazopanib. This lactylation enhances HNRNPU binding to PHGDH pre‐mRNA exon 1, maintaining exon 1‐containing transcripts and mRNA stability, thereby activating serine metabolism.
Chang Zhang +6 more
wiley +1 more source
In this study, chemoproteomics combined with genetic and functional analyses was integrated to identify SHMT2 as a covalent and functional target of gambogic acid (GA) in triple‐negative breast cancer (TNBC). Further validation demonstrated that GA selectively modifies the Cys241 site of SHMT2, triggering mitochondrial dysfunction, activating the Nrf2 ...
Tong Yang +15 more
wiley +1 more source
A novel approach to explore metabolic diseases: Neddylation
Protein post translational modification (PTM) is the main regulatory mechanism for eukaryotic cell function, among which ubiquitination is based on the reversible degradation of proteins by the ubiquitin proteasome system to regulate cell homeostasis ...
Huiwen Ren +4 more
doaj +1 more source

