ArticleBMC chemistry2025
Watercress-derived glucosinolates as potential allosteric PTP1B inhibitors: a dual in silico and in vitro study on insulin signaling modulation.
Article in BMC chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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
3 citing papers in PubMed.
- UntargetedNutrients · 2026Trial
- From Functional Ingredients to Functional Foods: Focus on Brassicales Plant Species and Glucosinolates.Foods (Basel, Switzerland) · 2026Review
- Bioactive metabolites from Paeonia lactiflora protect against heat-induced male infertility in Drosophila melanogaster by modulating Vasa: integrating in vivo and computational analyses.Journal of computer-aided molecular design · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
This study investigates the inhibitory potential of four glucosinolates-glucoerucin, glucoiberin, gluconasturtiin, and glucotropaeolin-isolated from watercress (Nasturtium officinale) against Protein Tyrosine Phosphatase 1B (PTP1B), a key regulator of insulin signaling. Molecular docking, molecular dynamics (MD) simulations, and MM/PBSA free energy calculations identified glucoerucin (-17.18 ± 3.51 kcal/mol) and gluconasturtiin (-13.54 ± 1.79 kcal/mol) as the strongest binders, with stable interactions involving Phe280 and Phe196 through π-π stacking. Potential Energy Landscape (PEL) analysis further confirmed that these two compounds occupied the most stable low-energy conformational states, reinforcing their favorable binding to PTP1B. In vitro enzyme inhibition assays provided experimental validation that glucoerucin (IC₅₀ = 6.07 ± 0.69 µM) and gluconasturtiin (IC₅₀ = 7.65 ± 0.45 µM) demonstrated the strongest inhibitory effects, comparable to ursolic acid (IC₅₀ = 7.11 ± 0.95 µM). Enzyme kinetics revealed a non-competitive inhibition mechanism, with K
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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 Socratic graph.