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PMID: 12123602 Published · ppublish English Journal Article Review

Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones?

Neuron ·Vol. 35 ·No. 1 ·2002-07-03 ·Pages 9-12

Muchowski PJ

Abstract

The most conspicuous feature of many neurodegenerative disorders, including Alzheimer's, Parkinson's, and Huntington's disease, is the occurrence of protein aggregates in ordered fibrillar structures known as amyloid found inside and outside of brain cells. The appearance of aggregates in diseased brains implies an underlying incapacity in the cellular machinery of molecular chaperones that normally functions to prevent the accumulation of misfolded proteins. Here we review recent studies that have revealed a critical role for molecular chaperones in several neurodegenerative disorders.

MeSH Terms
Amyloid/genetics,metabolism Animals Brain/metabolism,pathology,physiopathology Disease Models, Animal Humans Molecular Chaperones/genetics,metabolism Neurodegenerative Diseases/genetics,metabolism,pathology Neurofibrillary Tangles/genetics,metabolism,pathology Neurons/metabolism,pathology Peptides/genetics,metabolism Protein Folding
Chemicals
Amyloid Molecular Chaperones Peptides polyglutamine
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Muchowski Paul J
Department of Pharmacology, University of Washington, Seattle 98195, USA. mucho@u.washington.edu
Article Info
Journal
Neuron
Abbr.
Neuron
ISSN
0896-6273
Published
2002-07-03
Pages
9-12
Language
English
Region
United States
NLM ID
8809320
Subset
IM
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