Evidence map›Paper›PMID 31587407›Full record

ArticleProtein science : a publication of the Protein Society2019

Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65).

Bastian Kohl, Vanessa Granitzka, Amrinder Singh, Pedro Quintas, Elli Xiromeriti, Fabian Mörtel, Peter E Wright, Gerard Kroon, H Jane Dyson, Raphael Stoll

Open access · hybridAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

10 authors at 2 institutions in 2 countries.

Bastian KohlBiomolecular NMR spectroscopy, Ruhr University of Bochum, Bochum, Germany.
Vanessa GranitzkaBiomolecular NMR spectroscopy, Ruhr University of Bochum, Bochum, Germany.
Amrinder SinghDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Pedro QuintasDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Elli XiromeritiBiomolecular NMR spectroscopy, Ruhr University of Bochum, Bochum, Germany.
Fabian MörtelBiomolecular NMR spectroscopy, Ruhr University of Bochum, Bochum, Germany.
Peter E WrightDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Gerard KroonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
H Jane DysonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.ORCID 0000-0001-6855-3398
Raphael StollBiomolecular NMR spectroscopy, Ruhr University of Bochum, Bochum, Germany.
Ruhr University Bochum · DEScripps Research Institute · 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
Structural Studies of Large Dynamic ComplexesR35GM131693 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2019 to 2023
$2.6M
Structural Dynamics of NFkappaB Signaling ComplexesR01GM127807 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2018 to 2018
$368k
NIGMS NIH HHS GM127807NIGMS NIH HHS GM131693NIGMS NIH HHS GM71862NIGMS NIH HHS R35 GM131693
6 · The paper itself

Abstract

The nuclear factor of kappa light polypeptide gene enhancer in B-cells (NFκB) transcription factors play a critical role in human immune response. The family includes homodimers and heterodimers of five component proteins, which mediate different transcriptional responses and bind preferentially to different DNA sequences. Crystal structures of DNA complexes show that the dimers of the Rel-homology regions are structurally very similar. Differing DNA sequence preference together with structural similarity suggests that the dimers may differ in their dynamics. In this study, we present the first near-complete

Indexed as

DimerizationHumansModels, MolecularNF-kappa B p50 SubunitTranscription Factor RelANF-kappa B p50 SubunitRELA protein, humanTranscription Factor RelA{1H} -15N NOENFκB1p50 dimerization domainprotein dynamicsR1/R2 relaxation

Identifiers

PMID31587407
PMCPMC6863704
OpenAlexW2979189929

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.