N-Terminal Hypothesis for Alzheimer’s Disease
Author:
Affiliation:
1. Howard P. Isermann Department of Chemical and Biological Engineering and the Center for Biotechnology & Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180-3590, United States
Publisher
American Chemical Society (ACS)
Subject
Cell Biology,Cognitive Neuroscience,Physiology,Biochemistry,General Medicine
Link
https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.7b00037
Reference6 articles.
1. A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
2. A2T and A2V Aβ peptides exhibit different aggregation kinetics, primary nucleation, morphology, structure, and LTP inhibition
3. Alzheimer’s Protective A2T Mutation Changes the Conformational Landscape of the Aβ1–42 Monomer Differently Than Does the A2V Mutation
4. Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
5. η-Secretase processing of APP inhibits neuronal activity in the hippocampus
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