Evidence map›Paper›PMID 23539623›Full record

ReviewThe Journal of biological chemistry2013

The molybdenum cofactor.

Ralf R Mendel

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

116 citing papers in PubMed, 263 citations in OpenAlex.

  1. Review
  2. ROS-Balancing MXene/MoSeSmall (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  3. Review
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  13. Why cells need iron: a compendium of iron utilisation.Trends in endocrinology and metabolism: TEM · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

56 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

1 author at 1 institution in 1 country.

Ralf R MendelDepartment of Plant Biology, Braunschweig University of Technology, 38106 Braunschweig, Germany. r.mendel@tu-bs.de
Technische Universität Braunschweig · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also require iron, ATP, and copper. After its synthesis, Moco is distributed, involving Moco-binding proteins. A deficiency in the biosynthesis of Moco has lethal consequences for the respective organisms.

Indexed as

AnimalsBiosynthetic PathwaysCoenzymesHumansMetalloexopeptidasesMetalloproteinsMolybdenumMolybdenum CofactorsOrganophosphorus CompoundsPteridinesPterinsCoenzymesMetalloexopeptidasesMetalloproteinsMolybdenumMolybdenum CofactorsmolybdopterinnulibryOrganophosphorus CompoundsPteridinesPterinsIronMetalloenzymesMetalloproteinsMetalsMolybdenum

Identifiers

PMID23539623
PMCPMC3650355
OpenAlexW2002473282

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.