Evidence map›Paper›PMID 24508277›Full record

ReviewJournal of inorganic biochemistry2014

F-box and leucine-rich repeat protein 5 (FBXL5): sensing intracellular iron and oxygen.

Julio C Ruiz, Richard K Bruick

Abstract readReview
In one paragraph

Review in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of mitochondrial iron homeostasis in tumor cells.Molecular medicine (Cambridge, Mass.) · 2026
    Review
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  17. Association betweenArchives animal breeding · 2019
    Article
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  19. Review
  20. Structure, function and evolution of the hemerythrin-like domain superfamily.Protein science : a publication of the Protein Society · 2018
    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

2 authors at 1 institution in 1 country.

Julio C RuizDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9038, United States.
Richard K BruickDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9038, United States. Electronic address: richard.bruick@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

Study of an iron-responsive E3 ligase regulating mammalian iron homeostasisR01HL102481 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI BRUICK, RICHARD K · 2010 to 2014
$1.5M
NHLBI NIH HHS HL102481NHLBI NIH HHS R01 HL102481
6 · The paper itself

Abstract

Though essential for many vital biological processes, excess iron results in the formation of damaging reactive oxygen species (ROS). Therefore, iron metabolism must be tightly regulated. F-box and leucine-rich repeat protein 5 (FBXL5), an E3 ubiquitin ligase subunit, regulates cellular and systemic iron homeostasis by facilitating iron regulatory protein 2 (IRP2) degradation. FBXL5 possesses an N-terminal hemerythrin (Hr)-like domain that mediates its own differential stability by switching between two different conformations to communicate cellular iron availability. In addition, the FBXL5-Hr domain also senses O2 availability, albeit by a distinct mechanism. Mice lacking FBXL5 fail to sense intracellular iron levels and die in utero due to iron overload and exposure to damaging levels of oxidative stress. By closely monitoring intracellular levels of iron and oxygen, FBLX5 prevents the formation of conditions that favor ROS formation. These findings suggest that FBXL5 is essential for the maintenance of iron homeostasis and is a key sensor of bioavailable iron. Here, we describe the iron and oxygen sensing mechanisms of the FBXL5 Hr-like domain and its role in mediating ROS biology.

Indexed as

Oxidative StressAnimalsF-Box ProteinsHemerythrinHomeostasisIronMiceOxygenProtein Structure, TertiaryProteolysisReactive Oxygen SpeciesF-Box ProteinsFBXL5 protein, mouseHemerythrinIronOxygenReactive Oxygen SpeciesFBXL5HemerythrinIronIron regulatory proteinsOxygenReactive oxygen species

Identifiers

PMID24508277
PMCPMC3959624
OpenAlexW2145074697

What OpenQuestion holds

Textmetadata
LicenceTDM
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.