The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Protein Folding and Quality Control in the ER
Open accessAbstract
The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER quality control (ERQC) system. The ERQC facilitates folding and modification of secretory and membrane proteins and eliminates terminally misfolded polypeptides through ER-associated degradation (ERAD) or autophagic degradation. This mechanism of ER protein surveillance is closely linked to redox and calcium homeostasis in the ER, whose balance is presumed to be regulated by a specific cellular compartment. The potential to modulate proteostasis and metabolism with chemical compounds or targeted siRNAs may offer an ideal option for the treatment of disease.
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Cites
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
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Selective degradation of mitochondria by mitophagy
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Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
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Nascent transcript sequencing visualizes transcription at nucleotide resolution
Churchman, L. S., & Weissman, J. S. (2011) · Nature · doi:10.1038/nature09652 · Cited by 823
Protein quality control in the early secretory pathway
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Quality and quantity control at the endoplasmic reticulum
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An Adaptable Standard for Protein Export from the Endoplasmic Reticulum
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Cited by
Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response
Gardner, B. M., Pincus, D., Gotthardt, K., Gallagher, C. M., & Walter, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013169 · Cited by 721
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Crosstalk between Hypoxia and ER Stress Response: a Key Regulator of Macrophage Polarization
Díaz-Bulnes, P., Saiz, M. L., López-Larrea, C., & Rodríguez, R. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02951 · Cited by 175
Precision Redox: The Key for Antioxidant Pharmacology
Meng, J., Lv, Z., Zhang, Y., Wang, Y., Qiao, X., Sun, C., Chen, Y., Guo, M., Han, W., Ye, A., et al. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8212 · Cited by 122
Type I interferons and endoplasmic reticulum stress in health and disease
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.10.004 · Cited by 83
Metadata
- Authors
- Araki, K., & Nagata, K.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-08-29
- Volume
- 3
- Issue
- 11
- Pages
- a007526-a007526
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2099429838
- Cited by
- 413
- References
- 12
- Type
- posted content
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
