VCP/p97 mediates nuclear targeting of non-ER-imported prion protein to maintain proteostasis.

Mistargeting of secretory proteins in the cytosol can trigger their aggregation and subsequent proteostasis decline. We have identified a VCP/p97-dependent pathway that directs non-ER-imported prion protein (PrP) into the nucleus to prevent the formation of toxic aggregates in the cytosol. Upon impaired translocation into the ER, PrP interacts with VCP/p97, which facilitates nuclear import mediated by importin-ß.

Cross-seeding by prion protein inactivates TDP-43.

A common pathological denominator of various neurodegenerative diseases is the accumulation of protein aggregates. Neurotoxic effects are caused by a loss of the physiological activity of the aggregating protein and/or a gain of toxic function of the misfolded protein conformers. In transmissible spongiform encephalopathies or prion diseases, neurodegeneration is caused by aberrantly folded isoforms of the prion protein (PrP).

COVID-19 pandemic: a health challenge for commoners during the first unlock phase in India.

Aim: COVID-19, the disease caused by the novel coronavirus, is now a worldwide pandemic. This disease has become a reason for disturbance and concern. India, as a densely populated country, took initiative after the pandemic was declared.

Statistical data analysis of risk factor associated with mortality rate by COVID-19 pandemic in India.

The coronavirus is an infection caused by severe acute respiratory syndrome (SARS) coronavirus, known as SARS-CoV-2. It was first determined in Wuhan, China in December 2019. WHO named this virus as COVID-19.