Evidence map›Paper›PMID 23144459›Full record

ArticleThe Journal of biological chemistry2012

Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism.

Omer Kabil, Ruma Banerjee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.7field-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

91 citing papers in PubMed, 156 citations in OpenAlex.

  1. A Dinuclear Iron(II) Persulfide Complex Reacts with OJournal of the American Chemical Society · 2026
    Article
  2. Self-bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Role of cystathionine-β-synthase and hydrogen sulfide in down syndrome.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  7. Article
  8. Gut sulfide metabolism modulates behavior and brain bioenergetics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Emerging roles of hydrogen sulfide-metabolizing enzymes in cancer.Redox report : communications in free radical research · 2024
    Review
  13. Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Role of Hydrogen Sulfide in Inflammatory Bowel Disease.Antioxidants (Basel, Switzerland) · 2023
    Review
  20. Article

31 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

2 authors at 1 institution in 1 country.

Omer KabilDepartment of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600, USA.
Ruma Banerjee
University of Michigan–Ann Arbor · US

Funding

Transsulfuration and HyperhomocysteinemiaR01HL058984 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1997 to 2020
$6.0M
NHLBI NIH HHS HL58984NHLBI NIH HHS R01 HL058984
6 · The paper itself

Abstract

Hydrogen sulfide (H(2)S) is a recently described endogenously produced gaseous signaling molecule that influences various cellular processes in the central nervous system, cardiovascular system, and gastrointestinal tract. The biogenesis of H(2)S involves the cytoplasmic transsulfuration enzymes, cystathionine β-synthase and γ-cystathionase, whereas its catabolism occurs in the mitochondrion and couples to the energy-yielding electron transfer chain. Low steady-state levels of H(2)S appear to be controlled primarily by efficient oxygen-dependent catabolism via sulfide quinone oxidoreductase, persulfide dioxygenase (ETHE1), rhodanese, and sulfite oxidase. Mutations in the persulfide dioxgenase, i.e. ETHE1, result in ethylmalonic encephalopathy, an inborn error of metabolism. In this study, we report the biochemical characterization and kinetic properties of human persulfide dioxygenase and describe the biochemical penalties associated with two patient mutations, T152I and D196N. Steady-state kinetic analysis reveals that the T152I mutation results in a 3-fold lower activity, which is correlated with a 3-fold lower iron content compared with the wild-type enzyme. The D196N mutation results in a 2-fold higher K(m) for the substrate, glutathione persulfide.

Indexed as

Mutation, MissenseBrain Diseases, Metabolic, InbornHumansHydrogen SulfideKineticsMitochondrial ProteinsNucleocytoplasmic Transport ProteinsPurpuraETHE1 protein, humanHydrogen SulfideMitochondrial ProteinsNucleocytoplasmic Transport Proteins

Identifiers

PMID23144459
PMCPMC3531769
OpenAlexW1990590665

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.