The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins.
NMNAT
Tau
amyloid aggregation
amyloid β
chaperone
islet amyloid polypeptide
neurodegenerative diseases
protein misfolding
α-synuclein
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
07
12
2021
revised:
31
03
2022
accepted:
01
04
2022
pubmed:
11
4
2022
medline:
7
6
2022
entrez:
10
4
2022
Statut:
ppublish
Résumé
Molecular chaperones safeguard cellular protein homeostasis and obviate proteotoxicity. In the process of aging, as chaperone networks decline, aberrant protein amyloid aggregation accumulates in a mechanism that underpins neurodegeneration, leading to pathologies such as Alzheimer's disease and Parkinson's disease. Thus, it is important to identify and characterize chaperones for preventing such protein aggregation. In this work, we identified that the NAD
Identifiants
pubmed: 35398355
pii: S0021-9258(22)00352-0
doi: 10.1016/j.jbc.2022.101912
pmc: PMC9108885
pii:
doi:
Substances chimiques
Amyloidogenic Proteins
0
Molecular Chaperones
0
Nicotinamide-Nucleotide Adenylyltransferase
EC 2.7.7.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
101912Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflict of interests with the contents of this article.
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