Evidence map›Paper›PMID 24468676›Full record

ReviewJournal of inorganic biochemistry2014

Oxygen sensing strategies in mammals and bacteria.

Cornelius Y Taabazuing, John A Hangasky, Michael J Knapp

Open access · greenAbstract 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 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 17% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Review
  6. Genetic variability ofRadiology and oncology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. The Redox Theory of Development.Antioxidants & redox signaling · 2020
    Review
  18. Article
  19. Article
  20. 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.

Cornelius Y TaabazuingDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003, United States.
John A HangaskyDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003, United States.
Michael J KnappDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003, United States. Electronic address: mknapp@chem.umass.edu.
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Molecular mechanisms of hypoxia sensing by the HIF-hydroxylasesR01GM077413 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI KNAPP, MICHAEL J · 2007 to 2018
$2.2M
NIGMS NIH HHS R01 GM077413NIGMS NIH HHS R01-GM077413NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32-GM008515
6 · The paper itself

Abstract

The ability to sense and adapt to changes in pO2 is crucial for basic metabolism in most organisms, leading to elaborate pathways for sensing hypoxia (low pO2). This review focuses on the mechanisms utilized by mammals and bacteria to sense hypoxia. While responses to acute hypoxia in mammalian tissues lead to altered vascular tension, the molecular mechanism of signal transduction is not well understood. In contrast, chronic hypoxia evokes cellular responses that lead to transcriptional changes mediated by the hypoxia inducible factor (HIF), which is directly controlled by post-translational hydroxylation of HIF by the non-heme Fe(II)/αKG-dependent enzymes FIH and PHD2. Research on PHD2 and FIH is focused on developing inhibitors and understanding the links between HIF binding and the O2 reaction in these enzymes. Sulfur speciation is a putative mechanism for acute O2-sensing, with special focus on the role of H2S. This sulfur-centered model is discussed, as are some of the directions for further refinement of this model. In contrast to mammals, bacterial O2-sensing relies on protein cofactors that either bind O2 or oxidatively decompose. The sensing modality for bacterial O2-sensors is either via altered DNA binding affinity of the sensory protein, or else due to the actions of a two-component signaling cascade. Emerging data suggests that proteins containing a hemerythrin-domain, such as FBXL5, may serve to connect iron sensing to O2-sensing in both bacteria and humans. As specific molecular machinery becomes identified, these hypoxia sensing pathways present therapeutic targets for diseases including ischemia, cancer, or bacterial infection.

Indexed as

AnimalsBacteriaHemeHumansHypoxiaHypoxia-Inducible Factor 1Hypoxia-Inducible Factor-Proline DioxygenasesMammalsOxygenSignal TransductionEGLN1 protein, humanHemeHypoxia-Inducible Factor 1Hypoxia-Inducible Factor-Proline DioxygenasesOxygenCysteineFixLFNRHIFHypoxiaOxygen sensing

Identifiers

PMID24468676
PMCPMC4097052
OpenAlexW2037348539

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.