Associated Papers
The Pathogenic Mutation T182A Converts the Prion Protein into a Molten Globule-like Conformation Whose Misfolding to Oligomers but Not to Fibrils Is Drastically Accelerated.
Singh J et al.
Biochemistry, 2016
Early Delivery of Misfolded PrP from ER to Lysosomes by Autophagy.
Cortes CJ et al.
International Journal of Cell Biology, 2013
Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum.
Campana V et al.
Journal of Cell Science, 2006
Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.
Cancellotti E et al.
The Journal of Biological Chemistry, 2005
Loss of glycosylation associated with the T183A mutation in human prion disease.
Grasbon-Frodl E et al.
Acta Neuropathologica, 2004
Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells.
Lehmann S et al.
The Journal of Biological Chemistry, 1997
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