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Cited by 721

The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.

Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response

Open access
Gardner, B. M., Pincus, D., Gotthardt, K., Gallagher, C. M., Walter, P.·2013·Cold Spring Harbor Perspectives in Biology

Abstract

Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded proteins and exit as either folded proteins in transit to their target organelles or as misfolded proteins targeted for degradation. The unfolded protein response (UPR) maintains the protein-folding homeostasis within the ER, ensuring that the protein-folding capacity of the ER meets the load of client proteins. Activation of the UPR depends on three ER stress sensor proteins, Ire1, PERK, and ATF6. Although the consequences of activation are well understood, how these sensors detect ER stress remains unclear. Recent evidence suggests that yeast Ire1 directly binds to unfolded proteins, which induces its oligomerization and activation. BiP dissociation from Ire1 regulates this oligomeric equilibrium, ultimately modulating Ire1's sensitivity and duration of activation. The mechanistic principles of ER stress sensing are the focus of this review.

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Metadata

Authors
Gardner, B. M., Pincus, D., Gotthardt, K., Gallagher, C. M., & Walter, P.
Venue
Cold Spring Harbor Perspectives in Biology
Published
2013-02-06
Volume
5
Issue
3
Pages
a013169-a013169
ISSN
1943-0264 (ISSN-L)
OpenAlex
W2153074213
Cited by
721
References
75
Type
posted content
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response. https://app.cochat.ai/papers/10.1101/cshperspect.a013169
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Gardner, B. M., Pincus, D., Gotthardt, K., Gallagher, C. M., & Walter, P. (2013). Endoplasmic Reticulum Stress Sensing in the Unfolded Protein Response. Cold Spring Harbor Perspectives in Biology. https://doi.org/10.1101/cshperspect.a013169

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