ArticleMicrobiologyOpen2020
A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.
Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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.
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.
Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- A conserved aspartate residue in [4Fe-4S]-containing HypD is required for [NiFe]-cofactor biosynthesis and for efficient interaction of the HypCD scaffold complex with HypE.Metallomics : integrated biometal science · 2025Article
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024Article
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- Conformational and mechanical stability of the isolated large subunit of membrane-bound [NiFe]-hydrogenase fromFrontiers in microbiology · 2022Article
- High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase FromFrontiers in microbiology · 2022Article
- Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production fromMicroorganisms · 2021Article
- Activation of a [NiFe]-hydrogenase-4 isoenzyme by maturation proteases.Microbiology (Reading, England) · 2020Article
- A membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturation.MicrobiologyOpen · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[NiFe]-hydrogenases catalyze the reversible conversion of molecular hydrogen into protons end electrons. This reaction takes place at a NiFe(CN)
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What OpenQuestion holds
Registered trials
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.