Evidence map›Paper›PMID 19675644›Full record

ReviewNature2009

Molybdenum cofactors, enzymes and pathways.

Günter Schwarz, Ralf R Mendel, Markus W Ribbe

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 272 papers.

0numbers the graph read from it
0cells of the map it votes in
272citing papers in PubMed
23.7field-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

272 citing papers in PubMed, 857 citations in OpenAlex.

  1. Article
  2. Article
  3. One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026
    Review
  4. Article
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  9. Review
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  17. Review
  18. Article
  19. Insights into the biological effects of molybdenum in an insect model (Frontiers in bioengineering and biotechnology · 2026
    Article
  20. Article

212 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

3 authors at 3 institutions in 2 countries.

Günter SchwarzInstitute of Biochemistry, Department of Chemistry & Centre for Molecular Medicine, University of Cologne, 47 Zuelpicher Street, 50674 Cologne, Germany. gschwarz@uni-koeln.de
Ralf R Mendel
Markus W Ribbe
Technische Universität Braunschweig · DEUniversity of California, Irvine · USUniversity of Cologne · DE

Funding

Nitrogenase Assembly MechanismR01GM067626 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI RIBBE, MARKUS W · 2003 to 2024
$6.3M
NIGMS NIH HHS GM-67626
6 · The paper itself

Abstract

The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron-molybdenum cofactor and pterin-based molybdenum cofactors. Despite the different structures and functions of molybdenum-dependent enzymes, there are important similarities, which we highlight here. The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.

Indexed as

AnimalsCoenzymesCopperEnzymesHumansIronMetalloproteinsMolybdenum CofactorsNucleotidesPteridinesPterinsCoenzymesCopperEnzymesIronMetalloproteinsMolybdenum CofactorsmolybdopterinNucleotidesPteridinesPterins

Identifiers

PMID19675644
OpenAlexW2088150699

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.