ArticleACS omega2023
Effect of Colchicine Binding Site Inhibitors on the Tubulin Intersubunit Interaction.
Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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
8 citing papers in PubMed, 18 citations in OpenAlex.
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- Design, synthesis, and biological evaluation of 6-aryl-3-(3,4,5-trimethoxyphenyl)imidazo[1,2-a]pyridine derivatives as novel tubulin inhibitors with potent anticancer efficacy.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- QW-5-70 targets the colchicine site and demonstrates antitumor activity in P-gp-overexpressing cancer models.Molecular cancer therapeutics · 2026Article
- Discovery of Peptide-Based Tubulin Inhibitors Through Structure-Guided Design.Pharmaceutics · 2026Article
- Flavonoids as colchicine binding site inhibitors: emerging scaffolds in anticancer drug design.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026Review
- New naphthalene-containing enamides: synthesis, structural insights and biological screening as potential anticancer agents against Huh-7 cancer cell line.RSC advances · 2025Article
- Synthesis, Computational Studies, and Structural Analysis of 1-(3,5-Dimethoxyphenyl)azetidin-2-ones with Antiproliferative Activity in Breast Cancer and Chemoresistant Colon Cancer.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Generation of iPSCs from a Patient with the M694V Mutation in theInternational journal of molecular sciences · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are dynamic, non-covalent polymers consisting of α- and β-tubulin subunits that are involved in a wide range of intracellular processes. The polymerization and dynamics of microtubules are regulated by many factors, including small molecules that interact with different sites on the tubulin dimer. Colchicine binding site inhibitors (CBSIs) destabilize microtubules and inhibit tubulin polymerization, leading to cell cycle arrest. Because of their therapeutic potential, the molecular mechanism of CBSI function is an area of active research. Nevertheless, important details of this mechanism have yet to be resolved. In this study, we use atomistic molecular dynamics simulations to show that the binding of CBSIs to the tubulin heterodimer leads to the weakening of tubulin intersubunit interaction. Using atomistic molecular dynamics simulations and binding free energy calculations, we show that CBSIs act as protein-protein interaction inhibitors and destabilize interlinkage between α and β subunits, which is crucial for longitudinal contacts in the microtubule lattice. Our results offer new insight into the mechanisms of microtubule polymerization inhibition by colchicine and its analogs.
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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 OpenQuestion graph.