Evidence map›Paper›PMID 25053742›Full record

ArticleeLife2014

Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress.

Jie Wang, Kristeen A Pareja, Chris A Kaiser, Carolyn S Sevier

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.7field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Article
  3. Functional Characterization ofInternational journal of molecular sciences · 2026
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  8. Article
  9. Review
  10. Article
  11. Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Cell signaling and epigenetic regulation of nicotine-induced carcinogenesis.Environmental pollution (Barking, Essex : 1987) · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Oxidative stress response pathways in fungi.Cellular and molecular life sciences : CMLS · 2022
    Review
  17. Review
  18. Article
  19. Article
  20. Review

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Jie WangDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Kristeen A ParejaDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Chris A KaiserDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Carolyn S SevierDepartment of Molecular Medicine, Cornell University, Ithaca, United States css224@cornell.edu.
Cornell University · USMassachusetts Institute of Technology · US

Funding

MOLECULAR GENETICS OF INTRACELLULAR PROTEIN TRANSPORTR01GM046941 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KAISER, CHRIS ALAN · 1992 to 2012
$4.9M
Molecular mechanisms to maintain ER redox balanceR01GM105958 · NIGMS · CORNELL UNIVERSITY · PI SEVIER, CAROLYN S · 2014 to 2022
$2.9M
NIGMS NIH HHS GM105858NIGMS NIH HHS GM46941NIGMS NIH HHS R01 GM046941NIGMS NIH HHS R01 GM105958
6 · The paper itself

Abstract

Oxidative protein folding in the endoplasmic reticulum (ER) has emerged as a potentially significant source of cellular reactive oxygen species (ROS). Recent studies suggest that levels of ROS generated as a byproduct of oxidative folding rival those produced by mitochondrial respiration. Mechanisms that protect cells against oxidant accumulation within the ER have begun to be elucidated yet many questions still remain regarding how cells prevent oxidant-induced damage from ER folding events. Here we report a new role for a central well-characterized player in ER homeostasis as a direct sensor of ER redox imbalance. Specifically we show that a conserved cysteine in the lumenal chaperone BiP is susceptible to oxidation by peroxide, and we demonstrate that oxidation of this conserved cysteine disrupts BiP's ATPase cycle. We propose that alteration of BiP activity upon oxidation helps cells cope with disruption to oxidative folding within the ER during oxidative stress.

Indexed as

Gene Expression Regulation, FungalAdenosine TriphosphatasesCysteineEndoplasmic ReticulumEndoplasmic Reticulum StressFungal ProteinsGenes, ReporterHomeostasisHSP70 Heat-Shock ProteinsHydrogen PeroxideLac OperonModels, MolecularOxidation-ReductionProtein FoldingReactive Oxygen SpeciesSaccharomyces cerevisiaeAdenosine TriphosphatasesCysteineFungal ProteinsHSP70 Heat-Shock ProteinsHydrogen PeroxideKAR2 protein, yeastReactive Oxygen SpeciesBiPendoplasmic reticulumEro1oxidative foldingROS

Identifiers

PMID25053742
PMCPMC4132286
OpenAlexW2119506154

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.