ArticleNature2025
Structure of the ATP-driven methyl-coenzyme M reductase activation complex.
Article in Nature, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Diversity of electron-bifurcating COScience advances · 2026Article
- Molecular basis of NNature communications · 2026Article
- Discovery and characterization of a nickel enzyme family that catalyses intermolecular hydride shuttling.Nature chemistry · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.Current biology : CB · 2026Article
- Minimal ATP-Independent NAngewandte Chemie (International ed. in English) · 2026Article
- A Synthetic Iron Model of Carbon-Sulfur Bond Activation by the Nitrogenase-Family Enzyme Methylthio-Alkane Reductase.Journal of the American Chemical Society · 2026Article
- Component A2 is a redox-sensitive archaeal ATPase activated by methyl-coenzyme M reductase.bioRxiv : the preprint server for biology · 2026Article
- Coordinated plant and microbial transcriptional responses to oil-sands process-affected water.ISME communications · 2026Article
- A C39-like protein from methanogenic archaea: structural insights and functional divergence in β-galactose analogue degradation.Frontiers in microbiology · 2026Article
- Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.Nature catalysis · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methyl-coenzyme M reductase (MCR) is the enzyme responsible for nearly all biologically generated methane
Indexed as
Identifiers
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.