The DOI matches its Crossref record; 179 of the 179 references it cites were found in a registry or an index.
Quality Control and Protein Folding in the Secretory Pathway
Abstract
▪ Abstract The biosynthesis of secretory and membrane proteins in the endoplasmic reticulum (ER) yields mostly properly folded and assembled structures with full biological activity. Such fidelity is maintained by quality control (QC) mechanisms that avoid the production of nonnative structures. QC relies on chaperone systems in the ER that monitor and assist in the folding process. When folding promotion is not sufficient, proteins are retained in the ER and eventually retranslocated to the cytosol for degradation by the ubiquitin proteasome pathway. Retention of proteins that fail QC can sometimes occur beyond the ER, and degradation can take place in lysosomes. Several diseases are associated with proteins that do not pass QC, fail to be degraded efficiently, and accumulate as aggregates. In other cases, pathology arises from the downregulation of mutated but potentially functional proteins that are retained and degraded by the QC system.
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Cites
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Lamkanfi, M., & Dixit, V. M. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155745 · Cited by 935
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Lamkanfi, M. (2011) · Nature Reviews Immunology · doi:10.1038/nri2936 · Cited by 434
Maxwell, K. N., Fisher, E. A., & Breslow, J. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409736102 · Cited by 415
Unconventional Secretory Routes: Direct Protein Export Across the Plasma Membrane of Mammalian Cells
Nickel, W. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00302.x · Cited by 331
Ubiquitin and membrane protein turnover: from cradle to grave
MacGurn, J. A., Hsu, P.-C., & Emr, S. D. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060210-093619 · Cited by 287
Metadata
- Authors
- Trombetta, E. S., & Parodi, A. J.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2003-11
- Volume
- 19
- Issue
- 1
- Pages
- 649-676
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2160698849
- Cited by
- 422
- References
- 179
- FWCI
- 1.79
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
