Prion diseases or transmissible spongiform encephalopathies are a unique category of
infectious protein-misfolding neurodegenerative disorders. Hypothesized to be caused by …

Prion diseases are rare transmissible neurodegenerative disorders caused by the
accumulation of a misfolded isoform (PrPSc) of the cellular prion protein (PrPC) in the …

Prnp−/− mice lack the prion protein PrPC and are resistant to prion infections, but variable
phenotypes have been reported in Prnp−/− mice and the physiological function of PrPC …

Breast cancer (BRCA) is one of the most common cancers in women. Copper (Cu) is an
essential trace element implicated in many physiological processes and human diseases …

Abstract Herpes simplex virus 1 (HSV-1) can promote beta-amyloid deposition and tau
phosphorylation, demyelination or cognitive deficits relevant to Alzheimer's disease or …

The PrPC is expressed in many types of immune cells including monocytes and
macrophages, however, its function in immune regulation remains to be elucidated. In the …

The cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored
glycoprotein on the cell surface. Previous studies have demonstrated contradictory roles for …

Elucidation of prion protein (PrP) functions is crucial to fully understand prion diseases. A
major approach to studying PrP functions is the use of PrP gene-knockout (Prnp−/−) mice …

Macrophages, especially follicular dendritic cells, contribute to the pathogenesis of prion
diseases by accumulating an abnormal isoform of prion protein (PrPSc), which is converted …

Prion protein (PrPC) was originally known as the causative agent of transmissible
spongiform encephalopathy (TSE) but with recent research, its true function in cells is …