Evidence map›Paper›PMID 41831170›Full record

ArticleNeurogenetics2026

Targeting ABC transporters in glioma: farnesiferols as potent agents against chemotherapy resistance.

Hamidreza Jamali, Mohamad Vosough Ghanbari, Fatemeh B Rassouli

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Article in Neurogenetics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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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.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Hamidreza JamaliDepartment of Biology, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran.
Mohamad Vosough GhanbariInstitute of Biotechnology, Ferdowsi University of Mashhad, Mashhad, Iran.
Fatemeh B RassouliDepartment of Biology, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran. behnam3260@um.ac.ir.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gliomas are the most prevalent primary brain tumors in the central nervous system. ABC transporters have been identified as critical therapeutic targets in oncology, particularly in the context of overcoming chemoresistance. This study aims to investigate whether natural coumarins farnesiferol A, B and C (FFA, FFB and FFC) can inhibit the activity of drug transporters in glioma. Protein targets associated with low-grade glioma (LGG) and glioblastoma multiforme (GBM) were identified, along with potential molecular targets of verapamil—the standard inhibitor of ABC transporters. Interactome mapping was performed for the overlapping targets, followed by Gene Ontology enrichment analysis to elucidate their biological implications. The pharmacokinetics of FFA, FFB and FFC were evaluated, and these coumarins were subjected to molecular docking to assess their binding affinities for ABCB1 and ABCC1. Finally, molecular dynamics simulations assessed the conformational flexibility and binding stability of the FFA-ABCC1 complex. ABCB1 and ABCC1 were among the identified hub targets, and enrichment analyses confirmed their involvement in several biological processes. Computational predictions suggest that farnesiferols exhibit favorable pharmacokinetic profile, including high absorption, favorable distribution and low toxicity risks. Molecular docking demonstrated favorable interactions between FFA, FFB and FFC and the two ABC transporters, compared to the positive control verapamil. The binding affinity scores for FFA, FFB and FFC interacting with the active site of ABCB1 were − 7.3, − 7.0 and − 8.0 kcal/mol, respectively. For ABCC1, binding affinity scores were − 8.5, − 8.1 and − 8.1 kcal/mol for FFA, FFB and FFC, respectively. Molecular dynamics simulations also confirmed the flexibility and binding stability of the FFA-ABCC1 complex. In conclusion, present findings highlight the potential of farnesiferols as reversal agents for innovative strategies against glioma.

Indexed as

Antineoplastic AgentsATP-Binding Cassette TransportersBrain NeoplasmsCoumarinsDrug Resistance, NeoplasmGliomaATP-Binding Cassette, Sub-Family C ProteinsATP Binding Cassette Transporter, Subfamily BHumansMolecular Docking SimulationMolecular Dynamics SimulationABCB1 protein, humanAntineoplastic AgentsATP-Binding Cassette, Sub-Family C ProteinsATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily BCoumarinsmultidrug resistance-associated protein 1ATP-binding cassette transportersChemoresistanceFarnesiferolsGliomaMolecular docking and dynamics simulations

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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.