Protein Misfolding and Neurodegeneration

2008/02/01 by Claudio Soto, Lisbell D. Estrada · 1 citation
Biochemistry, Genetics and Molecular Biology · Neuroscience · Medicine · #Prion Diseases and Protein Misfolding #Neurological diseases and metabolism #Alzheimer's disease research and treatments #Neurodegeneration #Protein folding #Protein aggregation #Mechanism (biology) #Neuroscience #Biology #Disease #Cell biology #Medicine #Pathology

paper · doi:10.1001/archneurol.2007.56

openalex publication_date 2008/02/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/26

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.

Citations

• α-Synuclein in Lewy bodies
• Nature of the Scrapie Agent: Self-replication and Scrapie
• Novel Proteinaceous Infectious Particles Cause Scrapie
• Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104
• Does the Agent of Scrapie Replicate without Nucleic Acid ?
• Human spongiform encephalopathy: The national institutes of health series of 300 cases of experimentally transmitted disease
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Cited by

• Folding@home [wikipedia]

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