Related Experiment Video
Updated: Aug 15, 2026

Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Glycosylation and misfolding of PrP
F Wiseman1, E Cancellotti, J Manson
1Neuropathogenesis Unit, Institute for Animal Health, Ogston Building, Edinburgh EH9 3JF, UK. frances.wiseman@bbsrc.ac.uk
Abstract:
The TSEs (transmissible spongiform encephalopathies) are not only devastating neurological diseases but also provide a biochemical conundrum; how can a disease agent replicate in the apparent absence of genetic material? The prion hypothesis proposes that the TSE agent is a misfolded form of the host glycoprotein PrP (prion protein). However, a number of questions regarding the hypothesis remain to be addressed. We are using gene-targeted PrP transgenics models to investigate these issues. Here we discuss our recent results that examine the importance of PrP's N-glycans to the misfolding of the protein.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding Quality Check in the RER
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Export of Misfolded Proteins out of the ER
Oligosaccharide Assembly
Multiple sugar molecules that may or may...

