ReviewEssays in biochemistry2025
Versatile roles of inositol hexakisphosphate in the ubiquitin-proteasome system.
Review in Essays in biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed.
- Article
- A special issue of Essays in Biochemistry on proteasome and protein degradation.Essays in biochemistry · 2026Article
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Authors and funding
3 authors.
Funding
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Abstract
Inositol hexakisphosphate (IP6) is an endogenous organic molecule present in eukaryotes. First characterized as a phosphorus-storage metabolite, it has been subsequently discovered to play a role in modulating a multitude of different biological pathways. Here, we provide a concise overview of the involvement of IP6 in the ubiquitin-proteasome system (UPS). As an allosteric regulator, a molecular glue, and a potential prosthetic group, IP6 directly impacts the activities of multiple major UPS components. We specifically highlight the structural mechanisms through which IP6 binds to individual proteins or multi-protein complexes to control their functions. The serendipitous discovery of IP6 in various protein structures raises questions about the prevalence, identity, and regulation of soluble inositol polyphosphates in the UPS, which have potential translational implications.
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Registered trials
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