Inhibitory Effects of Isobavachalcone on Tau Protein Aggregation, Tau Phosphorylation, and Oligomeric Tau-Induced Apoptosis.
Tau protein
apoptosis
compound−protein interaction
isobavachalcone
protein aggregation
Journal
ACS chemical neuroscience
ISSN: 1948-7193
Titre abrégé: ACS Chem Neurosci
Pays: United States
ID NLM: 101525337
Informations de publication
Date de publication:
06 01 2021
06 01 2021
Historique:
pubmed:
16
12
2020
medline:
22
6
2021
entrez:
15
12
2020
Statut:
ppublish
Résumé
Alzheimer's disease (AD) is one of the most common neurodegenerative diseases without any effective medicine treatments. The neurofibrillary tangles containing hyperphosphorylated tau protein are one important pathological characteristic. Thus, one practicable strategy for AD drug design is to discover compounds that could inhibit tau protein aggregation and/or phosphorylation. In this study, isobavachalcone, a natural plant-derived compound, has been shown to inhibit tau protein aggregation and disaggregate tau fibrils
Identifiants
pubmed: 33320518
doi: 10.1021/acschemneuro.0c00617
doi:
Substances chimiques
Chalcones
0
Protein Aggregates
0
tau Proteins
0
isobavachalcone
20784-50-3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM