Evidence map›Paper›PMID 34614173›Full record

ArticleNucleic acids research2021

Single-molecule conformational dynamics of a transcription factor reveals a continuum of binding modes controlling association and dissociation.

Wei Chen, Wei Lu, Peter G Wolynes, Elizabeth A Komives

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
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  6. Ligand-dependent G protein dynamics underlying opioid signaling efficacy.bioRxiv : the preprint server for biology · 2025
    Article
  7. Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025
    Review
  8. Article
  9. Quantification and potential functional relevance of binding cooperativity of adjacent transcription factors on DNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Review
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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.

Wei ChenDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093, USA.ORCID 0000-0002-0166-3311
Wei LuCenter for Theoretical Biological Physics, Departments of Chemistry, Physics, and Biosciences, Rice University, Houston, Texas 77005, USA.ORCID 0000-0002-1572-2909
Peter G WolynesCenter for Theoretical Biological Physics, Departments of Chemistry, Physics, and Biosciences, Rice University, Houston, Texas 77005, USA.ORCID 0000-0001-7975-9287
Elizabeth A KomivesDepartment of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093, USA.ORCID 0000-0001-5264-3866
Center for Theoretical Biological Physics · USUniversity of California San Diego · US

Funding

STRUCTURE AND STABILITY OF IKB/NF-KB COMPLEXESP01GM071862 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2006 to 2016
$14.9M
NIGMS NIH HHS P01 GM071862
6 · The paper itself

Abstract

Binding and unbinding of transcription factors to DNA are kinetically controlled to regulate the transcriptional outcome. Control of the release of the transcription factor NF-κB from DNA is achieved through accelerated dissociation by the inhibitor protein IκBα. Using single-molecule FRET, we observed a continuum of conformations of NF-κB in free and DNA-bound states interconverting on the subseconds to minutes timescale, comparable to in vivo binding on the seconds timescale, suggesting that structural dynamics directly control binding kinetics. Much of the DNA-bound NF-κB is partially bound, allowing IκBα invasion to facilitate DNA dissociation. IκBα induces a locked conformation where the DNA-binding domains of NF-κB are too far apart to bind DNA, whereas a loss-of-function IκBα mutant retains the NF-κB conformational ensemble. Overall, our results suggest a novel mechanism with a continuum of binding modes for controlling association and dissociation of transcription factors.

Indexed as

Transcription, GeneticAnimalsAvidinBinding SitesBiotinDNAFluorescence Resonance Energy TransferGene Expression RegulationHumansImmobilized ProteinsInterferonsInverted Repeat SequencesMiceMolecular Dynamics SimulationNF-KappaB Inhibitor alphaProtein BindingAvidinBiotinDNAImmobilized ProteinsInterferonsneutravidinNF-KappaB Inhibitor alphaRela protein, mouseTranscription Factor RelA

Identifiers

PMID34614173
PMCPMC8565325
OpenAlexW3202209048

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.