Evidence map›Paper›PMID 8657121›Full record

ArticleMolecular and cellular biology1996

Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element.

M Ubeda, X Z Wang, H Zinszner, I Wu, J F Habener, D Ron

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

132 citing papers in PubMed, 308 citations in OpenAlex.

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  9. Endoplasmic reticulum stress enhances the expression of TLR3-induced TSLP by airway epithelium.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
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  11. Review
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  16. STING controls T cell memory fitness during infection through T cell-intrinsic and IDO-dependent mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Review
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  20. Blocking CHOP-dependent TXNIP shuttling to mitochondria attenuates albuminuria and mitigates kidney injury in nephrotic syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article

72 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

6 authors at 2 institutions in 2 countries.

M UbedaLaboratory of Molecular Endocrinology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
X Z Wang
H Zinszner
I Wu
J F Habener
D Ron
Howard Hughes Medical Institute · USMassachusetts General Hospital · US

Funding

Metabolic Regulation in the Acute PhaseR37DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RON, DAVID · 2003 to 2009
$3.0M
METABOLIC REGULATION IN THE ACUTE PHASER01DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RYOO, HYUNG D · 1999 to 2010
$1.5M
METABOLIC REGULATION IN THE ACUTE-PHASE RESPONSER29DK047119 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RON, DAVID · 1993 to 1997
–
NIDDK NIH HHS DK 47119
6 · The paper itself

Abstract

CHOP (GADD153) is a mammalian nuclear protein that dimerizes with members of the C/EBP family of transcriptional factors. Absent under normal conditions, CHOP is induced by the stress encountered during nutrient deprivation, the acute-phase response, and treatment of cells with certain toxins. The basic region of CHOP deviates considerably in sequence from that of other C/EBP proteins, and CHOP-C/EBP heterodimers are incapable of binding to a common class of C/EBP sites. With respect to such sites, CHOP serves as an inhibitor of the activity of C/EBP proteins. However, recent studies indicate that certain functions of CHOP, such as the induction of growth arrest by overexpression of the wild-type protein and oncogenic transformation by the TLS-CHOP fusion protein, require an intact basic region, suggesting that DNA binding by CHOP may be implicated in these activities. In this study an in vitro PCR-based selection assay was used to identify sequences bound by CHOP-C/EBP dimers. These sequences were found to contain a unique core element PuPuPuTGCAAT(A/C)CCC. Competition in DNA-binding assays, DNase 1 footprint analysis, and methylation interference demonstrate that the binding is sequence specific. Deletions in the basic region of CHOP lead to a loss of DNA binding, suggesting that CHOP participates in this process. Stress induction in NIH 3T3 cells leads to the appearance of CHOP-containing DNA-binding activity. CHOP is found to contain a transcriptional activation domain which is inducible by cellular stress, lending further support to the notion that the protein can function as a positively acting transcription factor. We conclude that CHOP may serve a dual role both as an inhibitor of the ability of C/EBP proteins to activate some target genes and as a direct activator of others.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsCCAAT-Enhancer-Binding Protein-alphaCCAAT-Enhancer-Binding ProteinsDeoxyribonuclease IDNA-Binding ProteinsHelix-Loop-Helix MotifsMiceMolecular Sequence DataNuclear ProteinsRatsSequence DeletionTrans-ActivatorsTranscription Factor CHOPTranscription FactorsCCAAT-Enhancer-Binding Protein-alphaCCAAT-Enhancer-Binding ProteinsC-EBP nuclear protein trans-activation element IIDdit3 protein, mouseDdit3 protein, ratDeoxyribonuclease IDNA-Binding ProteinsNuclear ProteinsTrans-ActivatorsTranscription Factor CHOPTranscription Factors

Identifiers

PMID8657121
PMCPMC231132
OpenAlexW2096379342

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.