ArticleJACS Au2026
Deciphering How Clustered O‑Glycosylation Shapes Substrate-Binding Preferences in an Intrinsically Disordered Protein Region.
Article in JACS Au, 2026. 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.
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Who cites it
1 citing paper in PubMed.
- Stirring glycopeptides away from the constraints of solid-phase synthesis misconceptions.Frontiers in molecular biosciences · 2026Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications such as clustered O-glycosylation are frequently enriched in intrinsically disordered regions (IDRs), yet their roles in shaping molecular behavior and functional specificity remain poorly understood. Here, we addressed this challenge through an integrative, stepwise strategy that combines chemical synthesis, experimental characterization, and molecular dynamics (MD) simulations, employing the extensively O-mannosylated linker of
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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 Socratic graph.