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- W2020174051 abstract "Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterised by the progressive loss of motor neurons, leading to paralysis and death within several years of onset. Although protein misfolding is a key feature of ALS, the upstream triggers of disease remain elusive. Recently, endoplasmic reticulum (ER) stress was identified as an early and central feature in ALS disease models as well as in human patient tissues, indicating that ER stress could be an important process in disease pathogenesis. One important chaperone induced by ER stress is protein disulphide isomerase (PDI), which is both upregulated and posttranslationally inhibited by S-nitrosylation in ALS. In this paper, we present evidence from studies of genetics, model organisms, and patient tissues which indicate an active role for PDI and ER stress in ALS disease processes." @default.
- W2020174051 created "2016-06-24" @default.
- W2020174051 creator A5027978540 @default.
- W2020174051 creator A5068230802 @default.
- W2020174051 date "2011-01-01" @default.
- W2020174051 modified "2023-10-14" @default.
- W2020174051 title "Mechanisms of Neuroprotection by Protein Disulphide Isomerase in Amyotrophic Lateral Sclerosis" @default.
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- W2020174051 doi "https://doi.org/10.1155/2011/317340" @default.
- W2020174051 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3096316" @default.
- W2020174051 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21603027" @default.
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