Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …

Flotillins are membrane proteins that form microdomains in the plasma membrane of all
mammalian cell types studied to date. They span the evolutionary spectrum, with proteins …

Amyloid-beta (Aβ) oligomers are thought to trigger Alzheimer's disease pathophysiology.
Cellular prion protein (PrPC) selectively binds oligomeric Aβ and can mediate Alzheimer's …

The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …

Lipid rafts are sphingolipid‐and cholesterol‐rich domains of the plasma membrane which
contain a variety of signalling and transport proteins. Different subtypes of lipid rafts can be …

Prions are the causative agent of the transmissible spongiform encephalopathies, such as
Creutzfeldt-Jakob disease in humans. In these prion diseases the normal cellular form of the …

Prion proteins (PrPs) are key players in fatal neurodegenerative disorders, yet their
physiological functions remain unclear, as PrP knockout mice develop rather normally. We …

Thy-1 is a 25–37 kDa glycosylphosphatidylinositol (GPI)-anchored protein involved in T cell
activation, neurite outgrowth, apoptosis, tumor suppression, wound healing, and fibrosis. To …

Reggie-1 and-2 proteins (flotillin-2 and-1 respectively) form their own type of non-caveolar
membrane microdomains, which are involved in important cellular processes such as T-cell …

Reggie-1/flotillin-2 and reggie-2/flotillin-1 are ubiquitously expressed, well-conserved
proteins that are associated with membrane microdomains known as rafts. Studies from us …