Evidence map›Paper›PMID 28981703›Full record

ArticleNucleic acids research2017

Activator Protein-1: redox switch controlling structure and DNA-binding.

Zhou Yin, Mischa Machius, Eric J Nestler, Gabby Rudenko

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  6. Assessing the validity of leucine zipper constructs predicted by AlphaFold.Protein science : a publication of the Protein Society · 2026
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  16. Anti-Inflammatory Activities of Constituents fromPlants (Basel, Switzerland) · 2022
    Article
  17. Review
  18. Review
  19. Review
  20. Antioxidants (Basel, Switzerland) · 2022
    Review
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.

Zhou YinDepartment of Pharmacology and Toxicology, and the Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Mischa MachiusDepartment of Pharmacology and Toxicology, and the Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Eric J NestlerFishberg Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, 1 Gustave L Levy Place, New York, NY 10029, USA.
Gabby RudenkoDepartment of Pharmacology and Toxicology, and the Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
The University of Texas Medical Branch at Galveston · USAllen Institute for Brain Science · US

Funding

Small molecule modulators of ΔFosB FunctionR01DA040621 · NIDA · UNIVERSITY OF TEXAS MED BR GALVESTON · PI NESTLER, ERIC J., ROBISON, ALFRED J · 2016 to 2025
$7.1M
MOLECULAR STUDIES OF COCAINE ACTION IN BRAINR37DA007359 · NIDA · YALE UNIVERSITY · PI NESTLER, ERIC J. · 1996 to 2020
$6.9M
NIDA NIH HHS R01 DA040621NIDA NIH HHS R37 DA007359
6 · The paper itself

Abstract

The transcription factor, activator protein-1 (AP-1), binds to cognate DNA under redox control; yet, the underlying mechanism has remained enigmatic. A series of crystal structures of the AP-1 FosB/JunD bZIP domains reveal ordered DNA-binding regions in both FosB and JunD even in absence DNA. However, while JunD is competent to bind DNA, the FosB bZIP domain must undergo a large conformational rearrangement that is controlled by a 'redox switch' centered on an inter-molecular disulfide bond. Solution studies confirm that FosB/JunD cannot undergo structural transition and bind DNA when the redox-switch is in the 'OFF' state, and show that the mid-point redox potential of the redox switch affords it sensitivity to cellular redox homeostasis. The molecular and structural studies presented here thus reveal the mechanism underlying redox-regulation of AP-1 Fos/Jun transcription factors and provide structural insight for therapeutic interventions targeting AP-1 proteins.

Indexed as

Protein DomainsAmino Acid SequenceAnimalsCrystallography, X-RayDNADNA-Binding ProteinsHumansModels, MolecularOxidation-ReductionProtein BindingProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junSequence Homology, Amino AcidTranscription Factor AP-1DNADNA-Binding ProteinsFOSB protein, humanJunD protein, humanProto-Oncogene Proteins c-fosProto-Oncogene Proteins c-junTranscription Factor AP-1

Identifiers

PMID28981703
PMCPMC5737521
OpenAlexW2753385537

What OpenQuestion holds

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LicenceCC BY-NC
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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.