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Cited by 5,924

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

Walter, Peter, Ron, David·2011·Science

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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Crossref · 10.1126/science.1209038

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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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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