ArticleBiomolecular NMR assignments2025
Article in Biomolecular NMR assignments, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The INK4 family of proteins restricts uncontrolled cell cycle progression by inhibiting cyclin-dependent kinases 4 and 6. The family consists of small, monomeric and mainly alpha-helical proteins that are conserved across all vertebrate species. We recently discovered that the human INK4 protein p16 converts into amyloid structures upon oxidation of the single cysteine residue present. Here we investigate the Danio rerio (zebrafish) orthologue P18 protein. The 170-residue protein contains two cysteines which may similarly mediate transition into amyloids upon oxidation. We present the near complete backbone assignment of the reduced P18 protein in solution. These chemical shift data provide the foundation for studying oxidation-induced structural changes and protein interactions.
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Registered trials
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