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Curr Opin Neurobiol. 2020 Mar 18;61:125-132. doi: 10.1016/j.conb.2020.02.009. [Epub ahead of print]

Potential benefit of manipulating protein quality control systems in neurodegenerative diseases.

Author information

1
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom.
2
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom. Electronic address: aberto@mrc-lmb.cam.ac.uk.

Abstract

The deposition of proteins of abnormal conformation is one of the major hallmarks of the common neurodegenerative diseases including Alzheimer's, Parkinson's, amyotrophic lateral sclerosis, frontotemporal dementia, and prion diseases. Protein quality control systems have evolved to protect cells and organisms against the harmful consequences of abnormally folded proteins that are constantly produced in small amounts. Mutations in rare inherited forms of neurodegenerative diseases have provided compelling evidence that failure of protein quality control systems can drive neurodegeneration. With extensive knowledge of these systems, and the notion that protein quality control may decline with age, many laboratories are now focussing on manipulating these evolutionarily optimized defence mechanisms to reduce the protein misfolding burden for therapeutic benefit.

PMID:
32199101
DOI:
10.1016/j.conb.2020.02.009

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