Evidence map›Paper›PMID 30120799›Full record

SynthesisProtein science : a publication of the Protein Society2019

Molybdenum- and tungsten-containing formate dehydrogenases and formylmethanofuran dehydrogenases: Structure, mechanism, and cofactor insertion.

Dimitri Niks, Russ Hille

Abstract readSystematic Review
In one paragraph

Synthesis in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Recent Progress in Understanding the Mechanism of Formate Dehydrogenases.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Article
  4. Article
  5. Semiartificial COChemical reviews · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Structural Insights Into COAngewandte Chemie (International ed. in English) · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. All-in-One COAccounts of chemical research · 2024
    Review
  14. Article
  15. Mechanism of Action of Formate Dehydrogenases.Journal of the American Chemical Society · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Active Site Characterization of aInorganic chemistry · 2024
    Article
  20. Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2024
    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

2 authors.

Dimitri NiksDepartment of Biochemistry, University of California, Riverside.
Russ HilleDepartment of Biochemistry, University of California, Riverside.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An overview is provided of the molybdenum- and tungsten-containing enzymes that catalyze the interconversion of formate and CO

Indexed as

Aldehyde OxidoreductasesCatalysisCoenzymesFormate DehydrogenasesMolybdenumStructure-Activity RelationshipTungstenAldehyde OxidoreductasesCoenzymesFormate Dehydrogenasesformylmethanofuran dehydrogenaseMolybdenumTungstenformate dehydrogenaseformylmethanofuran dehydrogenasemolybdenumtungsten

Identifiers

PMID30120799
PMCPMC6295890

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.