Copper Alters Aggregation Behavior of Prion Protein and Induces Novel Interactions between Its N- and C-terminal Regions
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference73 articles.
1. Spectroscopic characterization of conformational differences between PrP C and PrP Sc : an α-helix to β-sheet transition
2. Copper Converts the Cellular Prion Protein into a Protease-resistant Species That Is Distinct from the Scrapie Isoform
3. High Affinity Binding between Copper and Full-length Prion Protein Identified by Two Different Techniques
4. The amyloidogenic region of the human prion protein contains a high affinity (Met)2(His)2 Cu(I) binding site
5. Evaluation of Copper2+ Affinities for the Prion Protein
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2. Copper drives prion protein phase separation and modulates aggregation;Science Advances;2023-11-03
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