The role of the cellular prion protein in the uptake and toxic signaling of pathological neurodegenerative aggregates.
Neurotoxicity
Oligomers
Prion protein
Receptor
Journal
Progress in molecular biology and translational science
ISSN: 1878-0814
Titre abrégé: Prog Mol Biol Transl Sci
Pays: Netherlands
ID NLM: 101498165
Informations de publication
Date de publication:
2020
2020
Historique:
entrez:
22
9
2020
pubmed:
23
9
2020
medline:
2
7
2021
Statut:
ppublish
Résumé
Neurodegenerative disorders are invariably associated with intra- or extra-cellular deposition of aggregates composed of misfolded insoluble proteins. These deposits composed of tau, amyloid-β or α-synuclein spread from cell to cell, in a prion-like manner. Emerging evidence suggests that the circulating soluble species of these misfolded proteins (usually referred as oligomers) could play a major role in pathology, while insoluble aggregates would represent their protective less toxic counterparts. Convincing data support the hypothesis that the cellular prion protein, PrP
Identifiants
pubmed: 32958237
pii: S1877-1173(20)30123-X
doi: 10.1016/bs.pmbts.2020.08.008
pii:
doi:
Substances chimiques
Amyloid beta-Peptides
0
Prion Proteins
0
Protein Aggregates
0
alpha-Synuclein
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
297-323Informations de copyright
© 2020 Elsevier Inc. All rights reserved.