Evidence map›Paper›PMID 26405037›Full record

ArticleThe Journal of biological chemistry2015

Structural Studies of IRF4 Reveal a Flexible Autoinhibitory Region and a Compact Linker Domain.

Soumya G Remesh, Vishaka Santosh, Carlos R Escalante

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
0.8field-weighted citation impact, top 27% 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, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. The dynamic functions of IRF4 in B cell malignancies.Clinical and experimental medicine · 2023
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Review
  16. Role of IRF4-Mediated Inflammation: Implication in Neurodegenerative Diseases.Neurology & neurotherapy open access journal · 2017
    Article
  17. Construction of irf4a Transgenic Zebrafish Using Tol2 System and Its Potential Application.Dose-response : a publication of International Hormesis Society
    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

3 authors at 1 institution in 1 country.

Soumya G RemeshFrom the Department of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia 23298.
Vishaka SantoshFrom the Department of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia 23298.
Carlos R EscalanteFrom the Department of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia 23298 cescalante@vcu.edu.
Virginia Commonwealth University · US

Funding

AAV Rep-DNA Complexes Underlaying Site-specific IntegrationR01GM092854 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI ESCALANTE, CARLOS R · 2010 to 2013
$1.1M
Structural Studies of epigenetic regulation of rRNA gene by TTF-IR21CA179008 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI ESCALANTE, CARLOS R · 2013 to 2014
$360k
NCI NIH HHS R21 CA179008NCI NIH HHS R21-CA179008NIGMS NIH HHS R01 GM092854NIGMS NIH HHS R01-GM092854
6 · The paper itself

Abstract

IRF4 is a unique member of the interferon regulatory factor (IRF) family playing critical regulatory roles in immune cell development, regulation of obesity-induced inflammation, and control of thermogenic gene expression. The ability of IRF4 to control diverse transcriptional programs arises from its proficiency to interact with numerous transcriptional partners. In this study, we present the structural characterization of full-length IRF4. Using a combination of x-ray and small angle x-ray scattering studies, we reveal unique features of the interferon activation domain, including a set of β-sheets and loops that serve as the binding site for PU.1, and also show that unlike other IRF members, IRF4 has a flexible autoinhibitory region. In addition, we have determined the small angle x-ray scattering solution structure of full-length IRF4, which, together with circular dichroism studies, suggests that the linker region is not extended but folds into a domain structure.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayInterferon Regulatory Factor-4Interferon Regulatory FactorsMiceModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryScattering, Small AngleX-Ray DiffractionInterferon Regulatory Factor-4Interferon Regulatory Factorsgene regulationinterferon regulatory factor (IRF)small angle x-ray scattering (SAXS)structural biologytranscription factorx-ray crystallography

Identifiers

PMID26405037
PMCPMC4646024
OpenAlexW2278197292

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.