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The proteostasis network provides targets for neurodegeneration
Author(s) -
Newton Timothy Mark,
Duce James Alex,
Bayle Elliott David
Publication year - 2019
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.14643
Subject(s) - proteostasis , neurodegeneration , chaperone (clinical) , protein folding , biology , protein aggregation , chemical chaperone , computational biology , neuroscience , co chaperone , microbiology and biotechnology , bioinformatics , disease , biochemistry , heat shock protein , medicine , endoplasmic reticulum , unfolded protein response , hsp90 , gene , pathology
The production, quality control, and degradation of proteins are a tightly controlled process necessary for cell health. In order to regulate this process, cells rely upon a network of molecular chaperone proteins that bind misfolded proteins and help them fold correctly. In addition, some molecular chaperones can target terminally misfolded proteins for degradation. Neurons are particularly dependent upon this "proteostasis" system, failures in which lead to neurodegenerative disease. In this review, we identify opportunities for modulating molecular chaperone activity with small molecules, which could lower the burden of misfolded protein within neurons, reducing cell death and ameliorating the effects of neurodegeneration. LINKED ARTICLES: This article is part of a themed section on Therapeutics for Dementia and Alzheimer's Disease: New Directions for Precision Medicine. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.18/issuetoc.