Evidence map›Paper›PMID 37337123›Full record

ReviewNature metabolism2023

Diverse biological functions of vitamin K: from coagulation to ferroptosis.

Eikan Mishima, Adam Wahida, Tobias Seibt, Marcus Conrad

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature metabolism, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
10.0field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Menaquinone-4 protects CD8Science China. Life sciences · 2026
    Article
  3. Review
  4. Article
  5. Impact of Oxidative Stress-Driven Ferroptosis in Neurodegeneration.International journal of molecular sciences · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Decoding ferroptosis for cancer therapy.Nature reviews. Cancer · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Recommendations for robust and reproducible research on ferroptosis.Nature reviews. Molecular cell biology · 2025
    Review
  17. Review
  18. Article
  19. Review
  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

4 authors at 3 institutions in 2 countries.

Eikan Mishima *Institute of Metabolism and Cell Death, Helmholtz Zentrum München, Neuherberg, Germany. eikan@med.tohoku.ac.jp.ORCID http://orcid.org/0000-0002-3706-2745
Adam Wahida *Institute of Metabolism and Cell Death, Helmholtz Zentrum München, Neuherberg, Germany.
Tobias SeibtInstitute of Metabolism and Cell Death, Helmholtz Zentrum München, Neuherberg, Germany.
Marcus ConradInstitute of Metabolism and Cell Death, Helmholtz Zentrum München, Neuherberg, Germany. marcus.conrad@helmholtz-munich.de.ORCID http://orcid.org/0000-0003-1140-5612
Helmholtz Zentrum München · DEGerman Cancer Research Center · DETohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vitamin K is essential for several physiological processes, such as blood coagulation, in which it serves as a cofactor for the conversion of peptide-bound glutamate to γ-carboxyglutamate in vitamin K-dependent proteins. This process is driven by the vitamin K cycle facilitated by γ-carboxyglutamyl carboxylase, vitamin K epoxide reductase and ferroptosis suppressor protein-1, the latter of which was recently identified as the long-sought-after warfarin-resistant vitamin K reductase. In addition, vitamin K has carboxylation-independent functions. Akin to ubiquinone, vitamin K acts as an electron carrier for ATP production in some organisms and prevents ferroptosis, a type of cell death hallmarked by lipid peroxidation. In this Perspective, we provide an overview of the diverse functions of vitamin K in physiology and metabolism and, at the same time, offer a perspective on its role in ferroptosis together with ferroptosis suppressor protein-1. A comparison between vitamin K and ubiquinone, from an evolutionary perspective, may offer further insights into the manifold roles of vitamin K in biology.

Indexed as

FerroptosisVitamin KBlood CoagulationUbiquinoneVitamin K Epoxide ReductasesUbiquinoneVitamin KVitamin K Epoxide Reductases

Identifiers

PMID37337123
OpenAlexW4381190540

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.