Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy
Author:
Affiliation:
1. National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, United States
Funder
Division of Chemistry
National Institute of Allergy and Infectious Diseases
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.7b02772
Reference120 articles.
1. Nobel Lecture: Prions
2. Neurotoxicity of a prion protein fragment
3. Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106‒126
4. In Vivo Cytotoxicity of the Prion Protein Fragment 106–126
5. PrP fragment 106-126 is toxic to cerebral endothelial cells expressing PrPC
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