The DOI matches its Crossref record; 293 of the 293 references it cites were found in a registry or an index.
ER stress and diseases
Open accessAbstract
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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“The ER stress response plays a crucial role in numerous human diseases, for example, hypoxia, ischemia/reperfusion injury, heart disease, diabetes, and neurodegenerative diseases such as Alzheimer's and Parkinson's, in which prolonged protein misfolding is detrimental to the cell (Lindholm et al, 2006; Yoshida, 2007).”
From Differential dynamics of the mammalian mRNA and protein expression response to misfolding stress (2016) · cites this paper as Yoshida, 2007
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1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
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“The accumulation of unfolded proteins could disrupt the homeostasis of the ER, inducing ER stress (Yoshida, 2007).”
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Metadata
- 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
- 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
- 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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