Evidence map›Paper›PMID 24180257›Full record

ReviewAntioxidants & redox signaling2014

Heme oxygenase-1: a metabolic nike.

Barbara Wegiel, Zsuzsanna Nemeth, Matheus Correa-Costa, Andrew C Bulmer, Leo E Otterbein

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

90 citing papers in PubMed, 165 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Therapeutic Gases in Biomedicine: Updates on Nitric Oxide and Beyond.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  6. Extracellular heme:DNA complexes promote oxidative stress and inflammation during lupus-associated hemolysis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Heme oxygenase-1 and malaria pathogenesis.Frontiers in immunology · 2026
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Validation of Active Compound ofJournal of microbiology and biotechnology · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Heme: The Lord of the Iron Ring.Antioxidants (Basel, Switzerland) · 2023
    Review

30 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

5 authors at 2 institutions in 3 countries.

Barbara Wegiel1 Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School , Boston, Massachusetts.
Zsuzsanna Nemeth
Matheus Correa-Costa
Andrew C Bulmer
Leo E Otterbein
Beth Israel Deaconess Medical Center · USGriffith University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

significanceHeme degradation, which was described more than 30 years ago, is still very actively explored with many novel discoveries on its role in various disease models every year. RECENT ADVANCES: The heme oxygenases (HO) are metabolic enzymes that utilize NADPH and oxygen to break apart the heme moiety liberating biliverdin (BV), carbon monoxide (CO), and iron. Heme that is derived from hemoproteins can be toxic to the cells and if not removed immediately, it causes cell apoptosis and local inflammation. Elimination of heme from the milieu enables generation of three products that influences numerous metabolic changes in the cell. CRITICAL ISSUES: CO has profound effects on mitochondria and cellular respiration and other hemoproteins to which it can bind and affect their function, while BV and bilirubin (BR), the substrate and product of BV, reductase, respectively, are potent antioxidants. Sequestration of iron into ferritin and its recycling in the tissues is a part of the homeodynamic processes that control oxidation-reduction in cellular metabolism. Further, heme is an important component of a number of metabolic enzymes, and, therefore, HO-1 plays an important role in the modulation of cellular bioenergetics. FUTURE DIRECTIONS: In this review, we describe the cross-talk between heme oxygenase-1 (HO-1) and its products with other metabolic pathways. HO-1, which we have labeled Nike, the goddess who personified victory, dictates triumph over pathophysiologic conditions, including diabetes, ischemia, and cancer.

Indexed as

AnimalsBiosynthetic PathwaysCarbon MonoxideCell RespirationDiabetes MellitusHemeHeme Oxygenase-1HemeproteinsHumansIronMitochondriaNeoplasmsCarbon MonoxideHemeHeme Oxygenase-1HemeproteinsHMOX1 protein, humanIron

Identifiers

PMID24180257
PMCPMC3961788
OpenAlexW2032048503

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.