 |
|
Protein Misfolding and Neurodegeneration
Claudio Soto, PhD;
Lisbell D. Estrada, BSc
Arch Neurol. 2008;65(2):184-189.
A key molecular pathway implicated in diverse neurodegenerative diseases is the misfolding, aggregation, and accumulation of proteins in the brain. Compelling evidence strongly supports the hypothesis that accumulation of misfolded proteins leads to synaptic dysfunction, neuronal apoptosis, brain damage, and disease. However, the mechanism by which protein misfolding and aggregation trigger neurodegeneration and the identity of the neurotoxic structure is still unclear. The aim of this article is to review the literature around the molecular mechanism and role of misfolded protein aggregates in neurodegeneration and the potential for the misfolding process to lead to a transmissible form of disease by a prion-based model of propagation.
Author Affiliations: Departments of Neurology, Neuroscience and Cell Biology, and Biochemistry and Molecular Biology, George and Cynthia Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston (Dr Soto and Ms Estrada); and Facultad de Ciencias, Universidad de Chile, Santiago, Chile (Ms Estrada).
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati  Twitter
What's this?
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES
Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein
Wolschner et al.
Proc. Natl. Acad. Sci. USA 2009;106:7756-7761.
ABSTRACT
| FULL TEXT
Functional Protein Delivery into Neurons Using Polymeric Nanoparticles
Hasadsri et al.
J. Biol. Chem. 2009;284:6972-6981.
ABSTRACT
| FULL TEXT
Central Role of {alpha}-Synuclein Oligomers in Neurodegeneration in Parkinson Disease
Kazantsev and Kolchinsky
Arch Neurol 2008;65:1577-1581.
ABSTRACT
| FULL TEXT
|
