Evidence map›Paper›PMID 25425164›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015

The mammalian molybdenum enzymes of mARC.

Gudrun Ott, Antje Havemeyer, Bernd Clement

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Hepatocyte mARC1 promotes fatty liver disease.JHEP reports : innovation in hepatology · 2023
    Article
  13. Active Site Structures of theInorganic chemistry · 2023
    Article
  14. Association ofInternational journal of molecular sciences · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. Structural Features of CytochromeInternational journal of molecular sciences · 2021
    Review
  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.

Gudrun OttInstitute of Pharmacy, Christian-Albrechts-University of Kiel, Gutenbergstraße 76, 24118, Kiel, Germany.
Antje Havemeyer
Bernd Clement
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The "mitochondrial amidoxime reducing component" (mARC) is the most recently discovered molybdenum-containing enzyme in mammals. All mammalian genomes studied to date contain two mARC genes: MARC1 and MARC2. The proteins encoded by these genes are mARC-1 and mARC-2 and represent the simplest form of eukaryotic molybdenum enzymes, only binding the molybdenum cofactor. In the presence of NADH, mARC proteins exert N-reductive activity together with the two electron transport proteins cytochrome b5 type B and NADH cytochrome b5 reductase. This enzyme system is capable of reducing a great variety of N-hydroxylated substrates. It plays a decisive role in the activation of prodrugs containing an amidoxime structure, and in detoxification pathways, e.g., of N-hydroxylated purine and pyrimidine bases. It belongs to a group of drug metabolism enzymes, in particular as a counterpart of P450 formed N-oxygenated metabolites. Its physiological relevance, on the other hand, is largely unknown. The aim of this article is to summarize our current knowledge of these proteins with a special focus on the mammalian enzymes and their N-reductive activity.

Indexed as

AnimalsCoenzymesCytochromes b5Electron TransportHumansMammalsMembrane ProteinsMetabolic Detoxication, Phase IMetalloproteinsMitochondriaMitochondrial ProteinsMolybdenumMolybdenum CofactorsNADOxidoreductasesPteridinesamidoxime reducing component, humanCoenzymesCytochromes b5Membrane ProteinsMetalloproteinsMitochondrial ProteinsMolybdenumMolybdenum CofactorsmolybdopterinMTARC2 protein, humanNADOxidoreductasesPteridines

Identifiers

PMID25425164
OpenAlexW1987327811

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.