The DOI matches its Crossref record; 54 of the 55 references it cites were found in a registry or an index.
Endoplasmic Reticulum Stress and Diabetes Mellitus.
Open accessAbstract
Pancreatic beta-cells are strongly engaged in protein secretion and have highly developed endoplasmic reticulum (ER). Proper folding of polypeptide into a three-dimensional structure is essential for cellular function and protein malfolding can threaten cell survival. Various conditions can perturb the protein folding in the ER, which is collectively called ER stress. In order to adapt ER stress conditions, the cells respond in three distinct ways such as transcriptional induction of ER chaperones, translational attenuation, and ER-associated degradation (ERAD). However, when ER functions are severely impaired, the cell is eliminated by apoptosis via transcriptional induction of CHOP/GADD153, the activation of cJUN NH2-terminal kinase, and/or the activation of caspase-12. Recent studies have revealed that beta-cell is one of the most susceptible cells for ER stress, and ER stress-mediated apoptosis in beta-cells can be a cause of diabetes. A comprehensive understanding of the impact of the ER stress pathway in beta-cells and how it relates to the development of diabetes may contribute to provide new targets for the prevention and treatment of this disease.
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“To support high-level insulin secretion, β-cells undergo highly developed ER stress [305].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [305]
Citations
Cites
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942
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Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis
Scheuner, D. L., Song, B., McEwen, E. L., Liu, C., Laybutt, D. R., Gillespie, P. J., Saunders, T. L., Bonner‐Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355
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Cited by
Sorted by citations
Type 2 diabetes as an inflammatory disease
Donath, M. Y., & Shoelson, S. E. (2011) · Nature Reviews Immunology · doi:10.1038/nri2925 · Cited by 3,737
Roles of CHOP/GADD153 in endoplasmic reticulum stress
Oyadomari, S., & Mori, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401373 · Cited by 2,879
“infant diabetes due to pancreatic hypoplasia and a reduced number of b-cells.(77,78) eIF2a knockin mice have more severe b-cell deficiency as seen in 16.”
BackgroundSelf-citationEndoplasmic reticulum stress: cell life and death decisions
Xu, C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26373 · Cited by 2,291
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
Kim, I., Xu, W., & Reed, J. C. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2755 · Cited by 1,840
“Moreover, PERK gene mutations in association with infant-onset diabetes have been described in humans with the autosomal recessive disorder Wolcott–Rallison syndrom”
BackgroundYoshida, H. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05639.x · Cited by 1,086
Metadata
- Authors
- ARAKI, E., OYADOMARI, S., & MORI, M.
- Affiliations
- Kumamoto University (JP)
- Venue
- Internal Medicine
- Published
- 2003
- Volume
- 42
- Issue
- 1
- Pages
- 7-14
- ISSN
- 0918-2918 (ISSN-L)
- 1349-7235
- OpenAlex
- W2056689556
- Cited by
- 151
- References
- 55
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 8 · 2017: 7 · 2016: 4 · 2015: 10 · 2014: 8 · 2013: 8 · 2012: 10
- FWCI
- 0.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Internal Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Japan Society for the Promotion of Science (14370339)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum stress, diabetes mellitus, pancreatic beta cells, protein folding, ER-associated degradation, CHOP/GADD153, c-Jun N-terminal kinase, caspase-12, beta-cell apoptosis, ER chaperones, translational attenuation
- MeSH terms
- Amyloid, Animals, Diabetes Mellitus, Endoplasmic Reticulum, Humans, Islets of Langerhans, Mice, Mutant Strains, Models, Biological, Nitric Oxide, Eukaryotic Initiation Factor-2, Apoptosis, Protein Folding, eIF-2 Kinase, Mice
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