Associated Papers
N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease.
Pasala C et al.
Biomolecules, 2024
Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity.
Yi CW et al.
Scientific Reports, 2018
Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysis.
Kedarisetti KD et al.
Bioinformatics and Biology Insights, 2008
Effect of the E200K mutation on prion protein metabolism. Comparative study of a cell model and human brain.
Capellari S et al.
The American Journal of Pathology, 2000
Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation.
Gallo M et al.
International Journal of Immunopathology and Pharmacology, 0
Select a paper to view details