Evidence map›Paper›PMID 40028997›Full record

ArticleThe FEBS journal2025

Stabilization of the catalytically active structure of a molybdenum-dependent formate dehydrogenase depends on a highly conserved lysine residue.

Feilong Li, Michael Lienemann

Abstract read
In one paragraph

Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Feilong LiDepartment of Bioproducts and Biosystems, Aalto University, Espoo, Finland.
Michael LienemannVTT Technical Research Centre of Finland Ltd., Espoo, Finland.ORCID https://orcid.org/0000-0001-8977-8887

Funding

Research Council of Finland 321723
6 · The paper itself

Abstract

Molybdenum-dependent formate dehydrogenases (Mo-FDHs) reversibly catalyze the interconversion of CO

Indexed as

Escherichia coli ProteinsFormate DehydrogenasesLysineMolybdenumAmino Acid SubstitutionCatalytic DomainCoenzymesConserved SequenceEnzyme StabilityEscherichia coliFormatesIron-Sulfur ProteinsKineticsModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedCoenzymesEscherichia coli ProteinsFormate DehydrogenasesFormatesformic acidIron-Sulfur ProteinsLysineMolybdenumCO2 utilizationlysinemolybdenum‐dependent formate dehydrogenaseredox cofactorsite‐directed mutagenesis

Identifiers

PMID40028997
PMCPMC12176258

What Socratic 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 Socratic graph.