4.7 Review

Molecular chaperones biochemistry and role in neurodegenerative diseases

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 131, Issue -, Pages 396-411

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2019.02.148

Keywords

Neurodegenerative diseases; Protein aggregation; Misfolded protein; Protein toxicity; Molecular chaperones

Ask authors/readers for more resources

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. (C) 2019 Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available