ArticleJournal of computer-aided molecular design2025
Structure-guided discovery of microtubule affinity-regulating kinase 4 inhibitory potential of Harmane: towards therapeutic targeting of Alzheimer's disease.
Article in Journal of computer-aided molecular design, 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.
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Who cites it
1 citing paper in PubMed.
- Irilone and Lupinisoflavone C as Potential Plant-Based Modulators of S1PR1 for Neuroimmune Modulation in Multiple Sclerosis: Insights from Molecular Docking and Dynamics.Journal of molecular neuroscience : MN · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
Microtubule affinity-regulating kinase (MARK), particularly MARK4, are involved in the pathological phosphorylation of tau, contributing to neurodegenerative diseases and conditions such as cancer, inflammation, and atherosclerosis. The β-carboline family, specifically Harmane, exhibits broad biological activity, including neuroprotective effects. We investigated the inhibitory potential of Harmane against MARK4 using both computational and experimental approaches. The interaction between Harmane and MARK4 was studied using a combination of computational and experimental approaches. Molecular docking was carried out to understand the binding of Harmane to the binding pocket of MARK4, focusing on key interactions. Molecular dynamics simulations further assessed the stability of the MARK4-Harmane complex. Enzyme inhibition assays were conducted to assess Harmane's inhibitory potential on kinase, and a fluorescence quenching assay was complemented to validate the binding affinity of Harmane with MARK4. Molecular docking revealed that Harmane binds to the active site of MARK4, a finding supported by molecular dynamics simulations, demonstrating increased stability of the MARK4-Harmane complex. Structural analysis further highlighted the specificity of this interaction. Enzyme inhibition assays estimated Harmane's IC
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Registered trials
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