Evidence map›Paper›PMID 23716661›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Pirin is an iron-dependent redox regulator of NF-κB.

Fange Liu, Imran Rehmani, Shingo Esaki, Rong Fu, Lirong Chen, Vesna de Serrano, Aimin Liu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

63 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Unravelling the Role ofAntioxidants (Basel, Switzerland) · 2024
    Article
  13. Person-specific differences in ubiquitin-proteasome mediated proteostasis in human neurons.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    Article
  14. Article
  15. Pirin Inhibits FAS-Mediated Apoptosis to Support Colorectal Cancer Survival.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  16. Article
  17. Genetic Determinants ofAntibiotics (Basel, Switzerland) · 2023
    Article
  18. Article
  19. Article
  20. Review

3 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Fange LiuDepartment of Chemistry and Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Imran Rehmani
Shingo Esaki
Rong Fu
Lirong Chen
Vesna de Serrano
Aimin Liu
Georgia State University · US

Funding

NF-kappaB Regulation by Human PirinR01GM107529 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI LI, JIAN-DONG, LIU, AIMIN · 2014 to 2017
$1.0M
NIGMS NIH HHS R01 GM107529
6 · The paper itself

Abstract

Pirin is a nuclear nonheme Fe protein of unknown function present in all human tissues. Here we describe that pirin may act as a redox sensor for the nuclear factor κB (NF-κB) transcription factor, a critical mediator of intracellular signaling that has been linked to cellular responses to proinflammatory signals and controls the expression of a vast array of genes involved in immune and stress responses. Pirin's regulatory effect was tested with several metals and at different oxidations states, and our spectroscopic results show that only the ferric form of pirin substantially facilitates binding of NF-κB proteins to target κB genes, a finding that suggests that pirin performs a redox-sensing role in NF-κB regulation. The molecular mechanism of such a metal identity- and redox state-dependent regulation is revealed by our structural studies of pirin. The ferrous and ferric pirin proteins differ only by one electron, yet they have distinct conformations. The Fe center is shown to play an allosteric role on an R-shaped surface area that has two distinct conformations based on the identity and the formal redox state of the metal. We show that the R-shaped area composes the interface for pirin-NF-κB binding that is responsible for modulation of NF-κB's DNA-binding properties. The nonheme Fe protein pirin is proposed to serve as a reversible functional switch that enables NF-κB to respond to changes in the redox levels of the cell nucleus.

Indexed as

Protein Structure, TertiaryBinding SitesCarrier ProteinsCrystallography, X-RayDioxygenasesDNAHumansIronModels, MolecularMutationNF-kappa BNuclear ProteinsOxidation-ReductionProtein BindingSpectrometry, FluorescenceTranscription Factor RelACarrier ProteinsDioxygenasesDNAIronNF-kappa BNuclear ProteinsPIR protein, humanTranscription Factor RelAcoregulatormetalloproteinoxidative stressreactive oxygen species (ROS)signal transduction activation

Identifiers

PMID23716661
PMCPMC3683729
OpenAlexW2062045792

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.