ArticleNature2017
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Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 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
60 citing papers in PubMed, 116 citations in OpenAlex.
- Isolation and in vitro characterization of BchE, the cobalamin-dependent anaerobic magnesium protoporphyrin IX monomethylester cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- Mechanistic insight into radicalNatural product reports · 2026Review
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026Article
- Insights into the stereochemical mechanism of the BCommunications biology · 2026Article
- The cobalamin-binding domain of cobalamin-dependent radical S-adenosylmethionine enzymes: Familiarity in unfamiliar places.Journal of inorganic biochemistry · 2026Review
- Novel chemistry and structural perspectives in vitamin BChemical science · 2026Review
- Orthogonal Biosynthesis of Pyrrolamides through Dehydration by a Pathway-Specific Glycoside Hydrolase-Like Enzyme in Gram-Positive Bacteria.Journal of the American Chemical Society · 2026Article
- Structural basis for iterative methylation by a cobalamin-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026Article
- Structural Basis for Iterative Methylation by a Cobalamin-dependent Radical S-Adenosylmethionine Enzyme in Cystobactamids Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- A [2.1.0]-Fused Bicyclic Intermediate Is Produced during the Biosynthesis of Oxetane Nucleosides.Journal of the American Chemical Society · 2025Article
- Biosynthesis of Biphenomycin-like Macrocyclic Peptides by Formation and Cross-Linking ofJournal of the American Chemical Society · 2025Article
- Radical Fluoromethylation Enabled by Cobalamin-Dependent Radical SAM Enzymes.ACS bio & med chem Au · 2025Article
- Biosynthesis of Macrocyclic Peptides by Formation and Crosslinking ofbioRxiv : the preprint server for biology · 2025Article
- Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024Article
- Profile of Catherine Drennan.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Changing Fates of the Substrate Radicals Generated in the Active Sites of the BJournal of the American Chemical Society · 2023Article
- Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both the oxsA and oxsB genes are required for the production of OXT-A. Biochemical analysis of the encoded proteins, a cobalamin (Cbl)-dependent S-adenosylmethionine (AdoMet) radical enzyme, OxsB, and an HD-domain phosphohydrolase, OxsA, reveals that OXT-A is derived from a 2'-deoxyadenosine phosphate in an OxsB-catalysed ring contraction reaction initiated by hydrogen atom abstraction from C2'. Hence, OxsB represents the first biochemically characterized non-methylating Cbl-dependent AdoMet radical enzyme. X-ray analysis of OxsB reveals the fold of a Cbl-dependent AdoMet radical enzyme, a family of enzymes with an estimated 7,000 members. Overall, this work provides a framework for understanding the interplay of AdoMet and Cbl cofactors and expands the catalytic repertoire of Cbl-dependent AdoMet radical enzymes.
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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.