Results 51 to 60 of about 17,360,329 (255)
The ubiquitin system in normal and infected germinal center B cells
The ubiquitin system plays a central role in germinal center (GC) B cells, influencing differentiation to long‐lived memory B cells. Oncogenic gammaherpesviruses gain access to memory B cells by establishing latency in GC B cells. Mapping ubiquitin mechanisms in normal and infected GC B cells will define specific molecular circuits in B cells germane ...
Destiny Davis +2 more
wiley +1 more source
Pathogenic microorganisms employ specialized virulence factors to cause disease. Biofilm formation and the production of a polysaccharide capsule are two important virulence factors in Cryptococcus neoformans, the fungal pathogen that causes ...
François L. Mayer +2 more
doaj +1 more source
The Role of Ubiquitin-Proteasome System (UPS) in Asthma Pathology. [PDF]
Shuzhou Deng,1,2 Le Ding,1,3 Yisong Qian,1 Xuan Huang1 1The National Engineering Research Center for Bioengineering Drugs and the Technologies, Jiangxi Provincial Laboratory of Bioengineering Drugs, Institute of Translational Medicine, Jiangxi Medical ...
Deng S, Ding L, Qian Y, Huang X.
europepmc +2 more sources
We identify USP29 as the only DUB mirroring CA9 expression, a marker of hypoxia and HIF pathway activation associated with PCA aggressiveness. USP29 stabilizes HIF‐1α and HIF‐2α via a noncanonical mechanism that is independent of PHD/pVHL activity yet relies on proteasomal regulation, establishing USP29 as a previously unrecognized regulator of hypoxic
Amelie S Schober +16 more
wiley +1 more source
The ubiquitin–proteasome system (UPS) participates in the degradation of proteins which play an important role in regulating the cell cycle, apoptosis, and angiogenesis, as well as in the immune system.
Anna Sankiewicz +2 more
doaj +1 more source
Oncogenic DMTF1β promotes cancer cell motility by regulating autophagy through ULK1 stabilization
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
Methods to Discover and Evaluate Proteasome Small Molecule Stimulators
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
MURF2B, a novel LC3-binding protein, participates with MURF2A in the switch between autophagy and ubiquitin proteasome system during differentiation of C2C12 muscle cells. [PDF]
The ubiquitin proteasome system and macroautophagy are proteolytic pathways essential in the maintenance of cellular homeostasis during differentiation and remodelling of skeletal muscle.
Véronique Pizon +6 more
doaj +1 more source
Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions
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
ADP‐ribosylation: An emerging regulator of the epigenome
ADP‐ribosylation has emerged as a dynamic epigenetic signaling mechanism that modifies histones and chromatin‐associated proteins. Through coordinated PARylation and MARylation, it integrates with other histone modifications to regulate chromatin structure, transcription factor activity, and gene expression, influencing genome function and disease ...
Cristel V. Camacho +2 more
wiley +1 more source

