| Literature DB >> 28971461 |
Catherine Bobori1, Georgia Theocharopoulou2, Panayiotis Vlamos3.
Abstract
Stress and misfolded proteins result to dysfunction in the cell, often leading to neurodegenerative diseases and aging. Misfolded proteins form toxic aggregates that threaten cell's stability and normal functions. In order to restore its homeostasis, the cell activates the UPR system. Leading role in the restoration play the molecular chaperones which target the misfolded proteins with the purpose of either helping them to unfold and refold to their natural state or lead them degradation. This paper aims to present some of the most known molecular chaperones and their relation with diseases associated to protein misfolding and neurodegeneration, as well as the role of chaperones in proteostasis.Entities:
Keywords: Alzheimer disease; Huntington’s disease; Misfolded proteins; Molecular chaperones; Neurodegenerative diseases; Protein folding; UPR
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Year: 2017 PMID： 28971461 DOI： 10.1007/978-3-319-57379-3_20
Source DB: PubMed Journal: Adv Exp Med Biol ISSN： 0065-2598 Impact factor: 2.622