ReviewBiochemistry2026
Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.
Review in Biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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0 citing papers in PubMed.
No citing paper in PubMed yet.
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Authors and funding
5 authors.
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Abstract
Nature has devised an array of enzymatic cofactors that enable challenging chemical transformations to occur on a time scale compatible with biological life. The glycyl radical enzyme (GRE) superfamily, for example, highlights the catalytic power of protein-based amino acid radicals. GREs utilize a persistent radical housed on the α-carbon of a C-terminally conserved glycine residue to accomplish diverse chemical reactions in anaerobic environments. This radical cofactor is post-translationally installed on the mature, folded protein by a radical
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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.