title: Protein misfolding and neurodegeneration.
abstract: 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.
authors.affiliation: Department of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77555, USA. clsoto@utmb.edu
authors.forename: Claudio
authors.initials: C
authors.lastname: Soto
authors.forename: Lisbell D
authors.initials: LD
authors.lastname: Estrada
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D017772:Amyloid Neuropathies / Q000378:metabolism; D006801:Humans; D009410:Nerve Degeneration / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D017096:Prion Diseases / Q000378:metabolism; D011328:Prions / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D000682:Amyloid; D011328:Prions