Evidence map›Paper›PMID 27098223›Full record

ArticleThe journal of physical chemistry. B2016

PEST Control of Molecular Stripping of NFκB from DNA Transcription Sites.

Davit A Potoyan, Weihua Zheng, Diego U Ferreiro, Peter G Wolynes, Elizabeth A Komives

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Post-translational Modifications of IκBα: The State of the Art.Frontiers in cell and developmental biology · 2020
    Review
  9. Disorder Mediated Oligomerization ofThe journal of physical chemistry. B · 2019
    Article
  10. Frustration, function and folding.Current opinion in structural biology · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Functional importance of stripping in NFκB signaling revealed by a stripping-impaired IκBα mutant.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
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

5 authors at 3 institutions in 2 countries.

Davit A PotoyanCenter for Theoretical Biological Physics and Department of Chemistry, Rice University , Houston, Texas 77005, United States.
Weihua ZhengCenter for Theoretical Biological Physics and Department of Chemistry, Rice University , Houston, Texas 77005, United States.
Diego U FerreiroProtein Physiology Lab, Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, UBA-CONICET-IQUIBICEN , Buenos Aires C1430EGA, Argentina.
Peter G WolynesCenter for Theoretical Biological Physics and Department of Chemistry, Rice University , Houston, Texas 77005, United States.
Elizabeth A KomivesDepartment of Chemistry and Biochemistry, University of California, San Diego , 9500 Gilman Drive, La Jolla, California 92093-0378, United States.
Rice University · USFundación Ciencias Exactas y Naturales · ARUniversity 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

We recently proposed a model for IκBα-mediated molecular stripping of NFκB from transcription sites. IκBα was shown experimentally to form a transient ternary complex with DNA-bound NFκB, but the mechanism by which the IκBα accelerates dissociation of the NFκB from the DNA was unknown. In this paper we construct and compute free energy profiles for the wild-type IκBα-mediated molecular stripping reaction of NFκB from DNA and compare with that for a mutant of IκBα bearing a charge-neutralized PEST. The differences in the free energy profile for stripping originate from the frustrated electrostatic interactions between the negatively charged PEST and the DNA. The PEST occupies two different conformations in the NFκB-IκBα binary complex, one of which occupies the DNA-binding cavity. Specific interactions with positively charged residues in the N-terminal domains of both p50 and p65 apparently draw the domains closer together hindering reassociation of DNA. Comparison with the charge-neutralized mutant reveals that all of these functional consequences result from the negative charges in the PEST sequence of IκBα.

Indexed as

Computer SimulationDNAModels, MolecularNF-kappa BNF-KappaB Inhibitor alphaProtein DomainsTranscription, GeneticDNANF-kappa BNF-KappaB Inhibitor alpha

Identifiers

PMID27098223
PMCPMC5389414
OpenAlexW2336139920

What OpenQuestion holds

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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.