Articles tagged with Proteasomal Degradation
A new study found that proteins with a certain type of structure are more likely to misfold and be targeted for removal, yet nearly half still evade the cellular maintenance crew. This can disrupt protein production and recycling, potentially contributing to aging and disease.
A new experimental strategy enables the forced elimination of proteins that help tumors survive chemotherapy, potentially overcoming cancer treatment resistance. The approach involves delivering proteins directly to the proteasome, bypassing the tagging step, and has shown promise in tests carried out in cancer cells.
Researchers discovered that brain enzyme OTULIN regulates tau protein accumulation and has implications for treating neurodegenerative diseases. The study revealed OTULIN's role in controlling gene expression and RNA metabolism, suggesting a potential therapeutic target.
A new study from Weizmann Institute of Science reveals an immune mechanism involving proteasome products, which can kill bacteria and offer a promising treatment for infections. The researchers discovered that certain peptides produced by the proteasome have antibacterial properties and can be used to develop personalized treatments.
Scientists at Sanford Burnham Prebys have developed a clearer picture of how crucial machinery in the human cell's recycling process for obsolete and misshapen proteins—known as proteasomes—are formed. The research team shed new light on how two protein chaperones bind on the top of the alpha subunit ring as it is constructed.
Researchers found that a plakophilin-2 mutation leads to increased desmosomal protein degradation in ACM hearts, causing structural and functional changes. Studying human heart samples and mice models confirmed the role of protein degradation in ACM development.