Evidence map›Paper›PMID 37267359›Full record

ArticleScience advances2023

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire.

Agnieszka Winiarska, Fidel Ramírez-Amador, Dominik Hege, Yvonne Gemmecker, Simone Prinz, Georg Hochberg, Johann Heider, Maciej Szaleniec, Jan Michael Schuller

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. An electron-bifurcating "plug" to a protein nanowire in tungsten-dependent aldehyde detoxification.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Article
  8. Catalytic Stability ofInternational journal of molecular sciences · 2024
    Article
  9. 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

9 authors at 4 institutions in 2 countries.

Agnieszka WiniarskaJerzy Haber Institute of Catalysis and Surface Chemistry Polish Academy of Sciences, Kraków, Poland.ORCID 0000-0003-4361-6852
Fidel Ramírez-AmadorSYNMIKRO Research Center and Department of Chemistry, Philipps-University of Marburg, Marburg, Germany.ORCID 0000-0002-4182-2487
Dominik HegeFaculty of Biology, Philipps-University of Marburg, Marburg, Germany.ORCID 0000-0002-2179-8037
Yvonne GemmeckerFaculty of Biology, Philipps-University of Marburg, Marburg, Germany.
Simone PrinzMax Planck Institute of Biophysics, Frankfurt am Main, Germany.ORCID 0000-0001-9534-3214
Georg HochbergMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.ORCID 0000-0002-7155-0451
Johann HeiderSYNMIKRO Research Center and Department of Chemistry, Philipps-University of Marburg, Marburg, Germany.ORCID 0000-0001-8328-9716
Maciej SzaleniecJerzy Haber Institute of Catalysis and Surface Chemistry Polish Academy of Sciences, Kraków, Poland.ORCID 0000-0002-7650-9263
Jan Michael SchullerSYNMIKRO Research Center and Department of Chemistry, Philipps-University of Marburg, Marburg, Germany.ORCID 0000-0002-9121-1764
Philipps University of Marburg · DEJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences · PLMax Planck Institute for Terrestrial Microbiology · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde oxidoreductases (AORs) are tungsten enzymes catalyzing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium

Indexed as

Aldehyde OxidoreductasesNanowiresAldehyde DehydrogenaseCryoelectron MicroscopyNADTungstenAldehyde DehydrogenaseAldehyde OxidoreductasesNADTungsten

Identifiers

PMID37267359
PMCPMC10413684
OpenAlexW4379184360

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.