Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 75, Issue 17, Pages 3159-3180Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-018-2854-4
Keywords
Parkinson's disease; Alzheimer's disease; Huntington's disease; Polyglutamine diseases; Lou Gehrig's disease; Amyotrophic lateral sclerosis; Frontotemporal dementia; Stress granules; Protein inclusions
Categories
Funding
- DGIST R&D program and Basic Science Research Program, through the National Research Foundation of Korea (NRF) - Ministry of Science and ICT [18-BD-0402, 18-BT-02, 18-01-HRSS-02, 2018R1A2B6001607, 2017R1A2B4003351, 2016M3C7A1947307, 2016M3C7A1904148]
- Development of Platform Technology for Innovative Medical Measurements Program from the Korea Research Institute of Standards and Science [KRISS-2018-GP2018-0018]
- KBRI basic research program through Korea Brain Research Institute - Ministry of Science and ICT [18-BR-04-03]
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Protein toxicity can be defined as all the pathological changes that ensue from accumulation, mis-localization, and/or multimerization of disease-specific proteins. Most neurodegenerative diseases manifest protein toxicity as one of their key pathogenic mechanisms, the details of which remain unclear. By systematically deconstructing the nature of toxic proteins, we aim to elucidate and illuminate some of the key mechanisms of protein toxicity from which therapeutic insights may be drawn. In this review, we focus specifically on protein toxicity from the point of view of various cellular compartments such as the nucleus and the mitochondria. We also discuss the cell-to-cell propagation of toxic disease proteins that complicates the mechanistic understanding of the disease progression as well as the spatiotemporal point at which to therapeutically intervene. Finally, we discuss selective neuronal vulnerability, which still remains largely enigmatic.
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