ArticleBiomacromolecules2024
Assessment of the Enzymatic Dephosphorylation Kinetics in the Assemblies of a Phosphopentapeptide that Forms Intranuclear Nanoribbons.
Article in Biomacromolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Enzyme-Instructed Self-Assembly for Cellular Supramolecular Chemistry.Chemistry, an Asian journal · 2025Review
- Heterochiral and Heterotypic Self-Assembly of Intrinsically Disordered Peptides Confers Peptide Supercoils with Exceptional Proteolytic Stability.Journal of the American Chemical Society · 2025Article
- Enzymatic control of intermolecular interactions for generating synthetic nanoarchitectures in cellular environment.Science and technology of advanced materials · 2024Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Although the formation of peptide assemblies catalyzed by alkaline phosphatase (ALP) has received increasing attention in inhibiting cancer cells, the detailed enzyme kinetics of the dephosphorylation of the corresponding phosphopeptide assemblies have yet to be determined. We recently discovered that assemblies from a phosphopentapeptide can form intracellular nanoribbons that kill induced pluripotent stem cells or osteosarcoma cells, but the kinetics of enzymatic dephosphorylation remain unknown. Thus, we chose to examine the enzyme kinetics of the dephosphorylation of the phosphopentapeptide [NBD-LLLLpY (
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