Publications by authors named "B Wolozin"
The pathological deposition of proteins is a hallmark of several devastating neurodegenerative diseases. These pathological deposits comprise aggregates of proteins that adopt distinct structures named strains. However, the molecular factors responsible for the formation of distinct aggregate strains are unknown.
View Article and Find Full Text PDFThe RNA binding protein TIA1 is known to regulate stress responses. Here we show that TIA1 plays a much broader role in inflammatory cells, being required for the microglial sensome. We crossed TIA1 cKO mice (using a CX3CR1 driven cre element) to PS19 MAPT P301S tauopathy mice.
View Article and Find Full Text PDFSequestosome1 (SQSTM1) is an autophagy receptor that mediates the degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network, and these interactions are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA, and KIR. Technological advances in cell biology continue to expand our knowledge of the SQSTM1 protein network and the relationship between the actions of the SQSTM1 protein network in cellular physiology and disease states.
View Article and Find Full Text PDFArticle Synopsis
- The study addresses the limitations in Alzheimer's disease research due to the absence of effective animal models that reflect key disease features such as amyloid deposition, tau aggregation, inflammation, and neurodegeneration.
- Researchers created a dual transgenic mouse model (APPNL-G-F/PS19 MAPTP301S) that exhibited significant pathologies including amyloid plaques, tau pathology, and inflammation at just 6 months of age.
- The findings indicate that amyloid presence worsens tau pathology and inflammation, with specific brain regions showing stronger microglial inflammation and an increase in N-methyladenosine (mA), a modification linked to Alzheimer's, suggesting potential implications for understanding AD's mechanisms.
Sequestosome1 (SQSTM1) is an autophagy receptor that mediates degradation of intracellular cargo, including protein aggregates, through multiple protein interactions. These interactions form the SQSTM1 protein network, and these interactions are mediated by SQSTM1 functional interaction domains, which include LIR, PB1, UBA and KIR. Technological advances in cell biology continue to expand our knowledge of the SQSTM1 protein network and of the relationship of the actions of the SQSTM1 protein network in cellular physiology and disease states.
View Article and Find Full Text PDF