ReviewThe Journal of biological chemistry2011
Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes.
Review in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Sandacrabins - Structurally Unique Antiviral RNA Polymerase Inhibitors from a Rare Myxobacterium.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity.The Journal of biological chemistry · 2020Review
- Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Recent advances in radical SAM enzymology: new structures and mechanisms.ACS chemical biology · 2014Review
- Radical S-adenosylmethionine enzymes.Chemical reviews · 2014Review
- C-H methylation of heteroarenes inspired by radical SAM methyl transferase.Journal of the American Chemical Society · 2014Article
- Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis.Journal of the American Chemical Society · 2013Article
- Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.Nature chemical biology · 2013Article
- Article
- Radical SAM enzymes involved in the biosynthesis of purine-based natural products.Biochimica et biophysica acta · 2012Review
- Radical-mediated enzymatic methylation: a tale of two SAMS.Accounts of chemical research · 2012Review
- Answers to the carbon-phosphorus lyase conundrum.Chembiochem : a European journal of chemical biology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The radical S-adenosylmethionine (AdoMet) superfamily currently comprises thousands of proteins that participate in numerous biochemical processes across all kingdoms of life. These proteins share a common mechanism to generate a powerful 5'-deoxyadenosyl radical, which initiates a highly diverse array of biotransformations. Recent studies are beginning to reveal the role of radical AdoMet proteins in the catalysis of highly complex and chemically unusual transformations, e.g. the ThiC-catalyzed complex rearrangement reaction. The unique features and intriguing chemistries of these proteins thus demonstrate the remarkable versatility and sophistication of radical enzymology.
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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.