Molecular chaperones biochemistry and role in neurodegenerative diseases.
Misfolded protein
Molecular chaperones
Neurodegenerative diseases
Protein aggregation
Protein toxicity
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 Jun 2019
15 Jun 2019
Historique:
received:
21
11
2018
revised:
25
02
2019
accepted:
25
02
2019
pubmed:
12
3
2019
medline:
10
9
2019
entrez:
12
3
2019
Statut:
ppublish
Résumé
Many neurodegenerative diseases including Parkinson's disease, Alzheimer's disease, Prion's disease, polyQ and Huntington's disease share abnormal folding of potentially cytotoxic protein species associated with degeneration and death of specific neuronal populations. In order to maintain cellular protein homeostasis, neurons have developed an intrinsic protein quality control system as a strategy to counteract protein aggregation and their toxicity. Heat shock proteins are an essential component for regulating protein quality control and contribute potentially in the process of protein folding, prevent protein aggregation and in disaggregation in several neurodegenerative diseases. Therefore, molecular chaperones are considered an exciting therapeutic target. In this book chapter, we will focus on the potential importance of different heat shock proteins in neurodegenerative diseases and understand their mechanisms to protect neurons form aggregates and their toxicity.
Identifiants
pubmed: 30853582
pii: S0141-8130(18)36375-X
doi: 10.1016/j.ijbiomac.2019.02.148
pii:
doi:
Substances chimiques
Molecular Chaperones
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
396-411Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.