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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Cites
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
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The Role of the Hypoxia-Related Unfolded Protein Response (UPR) in the Tumor Microenvironment
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Implementing N-terminomics and machine learning to probe Nt-arginylation
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Structural dynamics of IRE1 and its interaction with unfolded peptides
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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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