The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Abstract
The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from the ER to the cell surface. To ascertain fidelity in protein folding, cells regulate the protein-folding capacity in the ER according to need. The ER responds to the burden of unfolded proteins in its lumen (ER stress) by activating intracellular signal transduction pathways, collectively termed the unfolded protein response (UPR). Together, at least three mechanistically distinct branches of the UPR regulate the expression of numerous genes that maintain homeostasis in the ER or induce apoptosis if ER stress remains unmitigated. Recent advances shed light on mechanistic complexities and on the role of the UPR in numerous diseases.
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Citations
Cites
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
The unfolded protein response signals through high-order assembly of Ire1
Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., Stroud, R. M., & Walter, P. (2009) · Nature · doi:10.1038/nature07661 · Cited by 656
Self-citationThe differentiation and stress response factor XBP-1 drives multiple myeloma pathogenesis
Carrasco, D. R., Sukhdeo, K., Protopopova, M., Sinha, R., Enos, M., Carrasco, D. E., Zheng, M., Mani, M., Henderson, J., Pinkus, G. S., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.02.015 · Cited by 414
Endoplasmic reticulum stress and pancreatic β-cell death
Fonseca, S. G., Gromada, J., & Urano, F. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.02.008 · Cited by 384
Translational Pausing Ensures Membrane Targeting and Cytoplasmic Splicing of XBP1u mRNA
Yanagitani, K., Kimata, Y., Kadokura, H., & Kohno, K. (2011) · Science · doi:10.1126/science.1197142 · Cited by 362
Harding, H. P., Zhang, Y., Scheuner, D., Chen, J.-J., Kaufman, R. J., & Ron, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809632106 · Cited by 267
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Cited by
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
Mechanisms, regulation and functions of the unfolded protein response
Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666
Dynamics and functions of lipid droplets
Olzmann, J. A., & Carvalho, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0085-z · Cited by 2,740
Disease Tolerance as a Defense Strategy
Medzhitov, R., Schneider, D. S., & Soares, M. P. (2012) · Science · doi:10.1126/science.1214935 · Cited by 1,718
ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
Han, J., Back, S. H., Hur, J., Lin, Y.-H., Gildersleeve, R., Shan, J., Yuan, C. L., Krokowski, D., Wang, S., Hatzoglou, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2738 · Cited by 1,691
Metadata
- Authors
- Walter, P., & Ron, D.
- Venue
- Science
- Published
- 2011-11-25
- Volume
- 334
- Issue
- 6059
- Pages
- 1081-1086
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1977603207
- Cited by
- 5,924
- References
- 6
- FWCI
- 110.42
- Type
- journal article
- Language
- en
- Open access
- closed
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