The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The Action of Molecular Chaperones in the Early Secretory Pathway
Abstract
▪ Abstract The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of nearly all secreted proteins, and associated with or housed within the ER are factors required to catalyze their import into the ER and facilitate their folding. To ensure that only properly folded proteins are secreted and to temper the effects of cellular stress, the ER can target aberrant proteins for degradation and/or adapt to the accumulation of misfolded proteins. Molecular chaperones play critical roles in each of these phenomena.
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Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
Hammond, C., Braakman, I., & Helenius, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.913 · Cited by 841
A regulatory link between ER-associated protein degradation and the unfolded-protein response
Friedlander, R., Jarosch, E., Urban, J., Volkwein, C., & Sommer, T. (2000) · Nature Cell Biology · doi:10.1038/35017001 · Cited by 474
Hammond, C., & Helenius, A. (1994) · The Journal of cell biology · doi:10.1083/jcb.126.1.41 · Cited by 443
Jakob, C. A., Burda, P., Roth, J., & Aebi, M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.5.1223 · Cited by 338
Cited by
Quality control in the endoplasmic reticulum protein factory
Sitia, R., & Braakman, I. (2003) · Nature · doi:10.1038/nature02262 · Cited by 688
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, D. T. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 615
ER stress and UPR in Alzheimer’s disease: mechanisms, pathogenesis, treatments
Ajoolabady, A., Lindholm, D., Ren, J., & Pratico, D. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05153-5 · Cited by 261
Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation
Quan, E. M., Kamiya, Y., Kamiya, D., Denic, V., Weibezahn, J., Kato, K., & Weissman, J. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.017 · Cited by 242
Self-citationFang, M., Shen, Z., Huang, S., Zhao, L., Chen, S., Mak, T. W., & Wang, X. (2010) · Cell · doi:10.1016/j.cell.2010.10.010 · Cited by 222
Metadata
- Authors
- Fewell, S. W., Travers, K. J., Weissman, J. S., & Brodsky, J. L.
- Venue
- Annual Review of Genetics
- Publisher
- Annual Reviews
- Published
- 2001-12
- Volume
- 35
- Issue
- 1
- Pages
- 149-191
- ISSN
- 0066-4197 (ISSN-L)
- 1545-2948
- OpenAlex
- W2139786644
- Cited by
- 287
- References
- 8
- FWCI
- 1.73
- Type
- journal article
- Language
- en
- Open access
- closed
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- Fewell, S. W., Travers, K. J., Weissman, J. S., & Brodsky, J. L. (2001). The Action of Molecular Chaperones in the Early Secretory Pathway. Annual Review of Genetics. https://doi.org/10.1146/annurev.genet.35.102401.090313
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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.
