Cited by 1,086Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchIon Channels and Receptors

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ER stress and diseases

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Yoshida, Hiderou·2007·The FEBS Journal

DOI 10.1111/j.1742-4658.2007.05639.x

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Abstract

Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein degradation (ERAD). When the amount of unfolded protein exceeds the folding capacity of the ER, human cells activate a defense mechanism called the ER stress response, which induces expression of ER chaperones and ERAD components and transiently attenuates protein synthesis to decrease the burden on the ER. It has been revealed that three independent response pathways separately regulate induction of the expression of chaperones, ERAD components, and translational attenuation. A malfunction of the ER stress response caused by aging, genetic mutations, or environmental factors can result in various diseases such as diabetes, inflammation, and neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and bipolar disorder, which are collectively known as ‘conformational diseases’. In this review, I will summarize recent progress in this field. Molecules that regulate the ER stress response would be potential candidates for drug targets in various conformational diseases.

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1 retracted

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Research works printed but not linked: 2

10.1172/JCI200521848 · DOI
10.1021/bi015967 · DOI

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See all 1,086

Authors: Yoshida, H.
Affiliations: Kyoto University (JP)
Corresponding author: Yoshida, Hiderou
ORCID: Yoshida, Hiderou
Venue: The FEBS Journal
Publisher: Wiley
Published: 2007-01-08
Volume: 274
Issue: 3
Pages: 630-658
ISSN: 1742-464X (ISSN-L)
1742-4658
DOI: 10.1111/j.1742-4658.2007.05639.x
OpenAlex: W1765185969
Cited by: 1,086
References: 293
Citations by year: 2026: 14 · 2025: 33 · 2024: 43 · 2023: 43 · 2022: 57 · 2021: 58 · 2020: 50 · 2019: 56 · 2018: 58 · 2017: 49 · 2016: 49 · 2015: 44 · 2014: 84 · 2013: 71 · 2012: 68
FWCI: 5.67
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Journal (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: ER stress response, endoplasmic reticulum, ER-associated degradation, ER chaperones, protein folding, translational attenuation, conformational diseases, neurodegenerative diseases, diabetes mellitus, inflammation, Alzheimer's disease, Parkinson's disease, bipolar disorder, aging, therapeutic target
MeSH terms: Animals, Endoplasmic Reticulum, Humans, Models, Biological, Mutation, Signal Transduction, Protein Folding, Molecular Chaperones, Neurodegenerative Diseases

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