Copper(II) Ion Binding to Cellular Prion Protein
Author:
Affiliation:
1. National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia, and Faculty of Chemistry and Chemical Technology, Aškerčeva 5, SI-1000 Ljubljana, Slovenia
Publisher
American Chemical Society (ACS)
Subject
Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ci700226c
Reference36 articles.
1. Prion diseases: pathogenesis and public health concerns
2. Nobel Lecture: Prions
3. NMR structure of the mouse prion protein domain PrP(121–231)
4. Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible
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