The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

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 …

Maternal immune dysregulation is a prenatal risk factor for autism spectrum disorder (ASD).
Importantly, a clinically relevant connection exists between inflammation and metabolic …

The presence of the cellular prion protein (PrP C) on the cell surface is critical for the
neurotoxicity of prions. Although several biological activities have been attributed to PrP C, a …

Mammalian pregnancy involves tremendous de novo maternal vascular construction to
adequately support conceptus development. In early mouse decidua basalis (DB), maternal …

Prion protein (PrP C) is a cell surface glycoprotein whose misfolding is responsible for prion
diseases. Although its physiological role is not completely defined, several lines of evidence …

Stress‐inducible phosphoprotein 1 (STI1) is part of the chaperone machinery, but it also
functions as an extracellular ligand for the prion protein. However, the physiological …

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a
group of fatal neurodegenerative disorders affecting humans and other mammalian species …

Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded,
self-replicating state of a sialoglycoprotein called the prion protein, or PrPC. Sialylation of …

Abstract The Hsp70/Hsp90 organising protein (Hop), also known as stress-inducible protein
1 (STI1), has received considerable attention for diverse cellular functions in both healthy …