Evidence map›Paper›PMID 24702237›Full record

ReviewAntioxidants & redox signaling2014

Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.

Stewart Siyan Cao, Randal J Kaufman

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 730 papers.

0numbers the graph read from it
0cells of the map it votes in
730citing papers in PubMed
26.1field-weighted citation impact, top 1% 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

730 citing papers in PubMed, 1,334 citations in OpenAlex.

  1. Article
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  9. Ferroptosis as a target mechanism in heart and kidney disease.The Journal of clinical investigation · 2026
    Review
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670 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

2 authors at 1 institution in 1 country.

Stewart Siyan Cao1 Degenerative Diseases Program, Sanford Burnham Medical Research Institute , La Jolla, California.
Randal J Kaufman
University of Michigan–Ann Arbor · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
TRANSGENIC MODELS FOR THE STUDY OF FACTOR V FUNCTIONP01HL057346 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 1997 to 2013
$19.9M
Regulation of Factor VIII SecretionR01HL052173 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 1995 to 2014
$6.5M
Role of the Unfolded Protein Response in Beta CellR37DK042394 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2007 to 2016
$4.9M
Regulation of ER stress-induced cell deathR01DK088227 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2010 to 2014
$3.1M
Unfolded Protein Response in Glucose HomeostasisR01DK042394 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KAUFMAN, RANDAL J. · 2003 to 2006
$1.2M
NCI NIH HHS P30 CA030199NHLBI NIH HHS HL052173NHLBI NIH HHS HL057346NIDDK NIH HHS DK042394NIDDK NIH HHS DK088227
6 · The paper itself

Abstract

significanceThe endoplasmic reticulum (ER) is a specialized organelle for the folding and trafficking of proteins, which is highly sensitive to changes in intracellular homeostasis and extracellular stimuli. Alterations in the protein-folding environment cause accumulation of misfolded proteins in the ER that profoundly affect a variety of cellular signaling processes, including reduction-oxidation (redox) homeostasis, energy production, inflammation, differentiation, and apoptosis. The unfolded protein response (UPR) is a collection of adaptive signaling pathways that evolved to resolve protein misfolding and restore an efficient protein-folding environment. RECENT ADVANCES: Production of reactive oxygen species (ROS) has been linked to ER stress and the UPR. ROS play a critical role in many cellular processes and can be produced in the cytosol and several organelles, including the ER and mitochondria. Studies suggest that altered redox homeostasis in the ER is sufficient to cause ER stress, which could, in turn, induce the production of ROS in the ER and mitochondria. CRITICAL ISSUES: Although ER stress and oxidative stress coexist in many pathologic states, whether and how these stresses interact is unknown. It is also unclear how changes in the protein-folding environment in the ER cause oxidative stress. In addition, how ROS production and protein misfolding commit the cell to an apoptotic death and contribute to various degenerative diseases is unknown. FUTURE DIRECTIONS: A greater fundamental understanding of the mechanisms that preserve protein folding homeostasis and redox status will provide new information toward the development of novel therapeutics for many human diseases.

Indexed as

Oxidative StressProtein FoldingCell DifferentiationEndoplasmic Reticulum StressHomeostasisHumansInflammationMitochondriaOxidation-ReductionReactive Oxygen SpeciesSignal TransductionReactive Oxygen Species

Identifiers

PMID24702237
PMCPMC4076992
OpenAlexW2317877264

What OpenQuestion holds

Textmetadata
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.