ArticleNature communications2018
Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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
35 citing papers in PubMed, 65 citations in OpenAlex.
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- Diel transcriptional dynamics of a marine sponge and its microbiome in a natural environment.Animal microbiome · 2026Article
- Structural insights into the catalytic mechanism of ammonia monooxygenase.Nature communications · 2025Article
- ER stress tolerance is regulated by copper-dependent PERK kinase activity.Cell reports · 2025Article
- Targeted assembly recovers high ammonia monooxygenase diversity in mudflat intertides.mSystems · 2025Article
- Vertical distribution characteristics and influencing factors of bacterial communities in a sediment profile of Bohai Sea.Die Naturwissenschaften · 2025Article
- Cysteine rich intestinal protein 2 links copper homeostasis to translational regulation in primary myoblasts.microPublication biology · 2025Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis.PLoS genetics · 2024Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation.bioRxiv : the preprint server for biology · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Understanding ATP Binding to DosS Catalytic Domain with a Short ATP-Lid.Biochemistry · 2023Article
- Unexpected complexity of the ammonia monooxygenase in archaea.The ISME journal · 2023Article
- Direct Activation of the C(spJournal of the American Chemical Society · 2023Article
- Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Boosting the acetol production in methanotrophic biocatalyst Methylomonas sp. DH-1 by the coupling activity of heteroexpressed novel protein PmoD with endogenous particulate methane monooxygenase.Biotechnology for biofuels and bioproducts · 2022Article
- Verrucomicrobial methanotrophs grow on diverse C3 compounds and use a homolog of particulate methane monooxygenase to oxidize acetone.The ISME journal · 2021Article
- Article
- Biochemistry of aerobic biological methane oxidation.Chemical Society reviews · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Methane-oxidizing microbes catalyze the oxidation of the greenhouse gas methane using the copper-dependent enzyme particulate methane monooxygenase (pMMO). Isolated pMMO exhibits lower activity than whole cells, however, suggesting that additional components may be required. A pMMO homolog, ammonia monooxygenase (AMO), converts ammonia to hydroxylamine in ammonia-oxidizing bacteria (AOB) which produce another potent greenhouse gas, nitrous oxide. Here we show that PmoD, a protein encoded within many pmo operons that is homologous to the AmoD proteins encoded within AOB amo operons, forms a copper center that exhibits the features of a well-defined Cu
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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.