Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
About this item
Full title
Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Author / Creator
Publisher
United States
Journal title
Proceedings of the National Academy of Sciences - PNAS, 2020-11, Vol.117 (46), p.28625-28631
Language
English
Formats
Publication information
Publisher
United States
Subjects
More information
Scope and Contents
Contents
Amyloid β (Aβ) aggregation has been the therapeutic target of several Alzheimer’s disease (AD) clinical trials. Aβ exists in many different aggregated forms, making it exceedingly challenging to target. Evidence links intracellular Aβ accumulation and AD pathogenesis. We report that amino acids 1 to 30 of Aβ, Aβ (1–30), do not aggregate yet display...
Alternative Titles
Full title
Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_pubmed_primary_33139554
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_33139554
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.2009238117
