Evidence map›Paper›PMID 40363830›Full record

ArticleMolecules (Basel, Switzerland)2025

Investigating Natural Product Inhibitors of IKKα: Insights from Integrative In Silico and Experimental Validation.

Muhammad Yasir, Jinyoung Park, Eun-Taek Han, Jin-Hee Han, Won Sun Park, Jongseon Choe, Wanjoo Chun

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Muhammad YasirDepartment of Pharmacology, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.
Jinyoung ParkDepartment of Pharmacology, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.
Eun-Taek HanDepartment of Medical Environmental Biology and Tropical Medicine, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.
Jin-Hee HanDepartment of Medical Environmental Biology and Tropical Medicine, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.ORCID 0000-0003-0836-6675
Won Sun ParkDepartment of Physiology, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.
Jongseon ChoeDepartment of Microbiology and Immunology, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.ORCID 0000-0002-0424-1667
Wanjoo ChunDepartment of Pharmacology, Kangwon National University School of Medicine, Chuncheon 24341, Republic of Korea.ORCID 0000-0003-1984-3545

Funding

Korea Basic Science Institute (National Research Facilities and Equipment Center) grants funded by the Ministry of Education 2020R1A6C101A195Korea Basic Science Institute (National Research Facilities and Equipment Center) grants funded by the Ministry of Education 2022R1A6C101A739
6 · The paper itself

Abstract

Nuclear factor-κB (NF-κB) signaling plays a pivotal role in regulating immune responses and is strongly implicated in cancer progression and inflammation-related diseases. The inhibitory κB kinases (IKKs), particularly IKKα, are central to modulating NF-κB activity, with distinct roles in the canonical and non-canonical signaling pathways. This study investigates the potential of selectively targeting IKKα to develop novel therapeutic strategies. A receptor-ligand interaction pharmacophore model was generated based on the co-crystallized structure of IKKα, incorporating six key features, two hydrogen bond acceptors, two hydrogen bond donors, one hydrophobic region, and one hydrophobic aromatic region. This model was used to virtually screen a diverse natural compound library of 5540 molecules, yielding 82 candidates that matched the essential pharmacophore features. Molecular docking and molecular dynamics simulations were subsequently employed to evaluate binding conformations, stability, and dynamic behavior of the top hits. The end-state free energy calculations (gmx_MMPBSA) further validated the interaction strength and stability of selected compounds. To experimentally confirm their inhibitory potential, key compounds were tested in LPS-stimulated RAW 264.7 cells, where they significantly reduced IκBα phosphorylation. These findings validate the integrative computational-experimental approach and identify promising natural compounds as selective IKKα inhibitors for further therapeutic development in cancer and inflammatory diseases.

Indexed as

Biological ProductsI-kappa B KinaseProtein Kinase InhibitorsAnimalsComputer SimulationHumansMiceMolecular Docking SimulationMolecular Dynamics SimulationNF-kappa BPhosphorylationProtein BindingRAW 264.7 CellsSignal TransductionBiological ProductsI-kappa B KinaseNF-kappa BProtein Kinase InhibitorsIKKαinflammationIκBαmolecular dockingmolecular dynamic simulationNF-κBpharmacophore modelingRAW 264.7 cells

Identifiers

PMID40363830
PMCPMC12073143

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Registered trials

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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.