Results 71 to 80 of about 118,443 (293)

Methods to Discover and Evaluate Proteasome Small Molecule Stimulators

open access: yesMolecules, 2019
Protein accumulation has been identified as a characteristic of many degenerative conditions, such as neurodegenerative diseases and aging. In most cases, these conditions also present with diminished protein degradation. The ubiquitin-proteasome system (
Rachel A. Coleman, Darci J. Trader
doaj   +1 more source

Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions

open access: yesMolecules, 2023
Ubiquitin, a small protein, is well known for tagging target proteins through a cascade of enzymatic reactions that lead to protein degradation. The ubiquitin tag, apart from its signaling role, is paramount in destabilizing the modified protein.
Wojciech Bialek   +2 more
doaj   +1 more source

Oncogenic DMTF1β promotes cancer cell motility by regulating autophagy through ULK1 stabilization

open access: yesMolecular Oncology, EarlyView.
In the current study, we demonstrate that the oncogene DMTF1β regulates ULK1 stability by reducing its proteasomal degradation in cancer cells. This stabilization enables ULK1 to induce autophagy, which in turn facilitates cancer cell migration. Consequently, reduced DMTF1β levels lead to decreased autophagy and impaired cancer cell migration.
Jun Xu   +13 more
wiley   +1 more source

Regulation of Arabidopsis thaliana Calcineurin B-like Interacting Protein Kinases (CIPKs) by the Ubiquitin-Proteasome System [PDF]

open access: yes, 2017
Ubiquitin Proteasome System (UPS) regulates the abundance of proteins by first attaching ubiquitin molecules and then targeting the modified protein for degradation by the 26S proteasome.
Alotaibi, Dalal
core  

Proteasomal degradation of intracellularly expressed Amblyomin‐X limits suicide gene therapy potential in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel   +4 more
wiley   +1 more source

Ubiquitin, ubiquitination and the ubiquitin-proteasome system in cancer [PDF]

open access: yes, 2010
Deep insight on Ubiquitin, ubiquitination and the ubiquitin-proteasome system in ...
Voutsadakis, IA, IA Voutsadakis
core   +1 more source

Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators [PDF]

open access: yes, 2022
The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains ...
Grey, Heather   +11 more
core   +1 more source

The ubiquitin-proteasome system in glioma cell cycle control

open access: yesCell Division, 2012
A major determinant of cell fate is regulation of cell cycle. Tight regulation of this process is lost during the course of development and progression of various tumors.
Vlachostergios Panagiotis J   +2 more
doaj   +1 more source

Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. [PDF]

open access: yesPLoS Pathogens, 2007
The specific and covalent addition of ubiquitin to proteins, known as ubiquitination, is a eukaryotic-specific modification central to many cellular processes, such as cell cycle progression, transcriptional regulation, and hormone signaling ...
Aurélie Angot   +3 more
doaj   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

open access: yesFEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane   +11 more
wiley   +1 more source

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