The DOI matches its Crossref record; 107 of the 107 references it cites were found in a registry or an index.
ER-associated degradation: Protein quality control and beyond
Open accessAbstract
Even with the assistance of many cellular factors, a significant fraction of newly synthesized proteins ends up misfolded. Cells evolved protein quality control systems to ensure that these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose biogenesis takes place in the endoplasmic reticulum (ER). There is also increasing evidence that ERAD controls other ER-related functions through regulated degradation of certain folded ER proteins, further highlighting the role of ERAD in cellular homeostasis.
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Cites
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Metadata
- Authors
- Ruggiano, A., Foresti, O., & Carvalho, P.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-03-17
- Volume
- 204
- Issue
- 6
- Pages
- 869-879
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1932475171
- Cited by
- 607
- References
- 107
- FWCI
- 25.68
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ruggiano, A., Foresti, O., & Carvalho, P. (2014). ER-associated degradation: Protein quality control and beyond. Journal of Cell Biology. https://doi.org/10.1083/jcb.201312042
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
