ArticleBioinformation2013
Interaction of active compounds from Aegle marmelos CORREA with histamine-1 receptor.
Article in Bioinformation, 2013. 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.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Aegeline mitigates isoproterenol-induced myocardial infarction: insights from biochemical, histopathological, and in silico studies.Frontiers in cardiovascular medicine · 2026Article
- Substituent Effect in Histamine and Its Impact on Interactions with the G Protein-Coupled Human Receptor HMolecules (Basel, Switzerland) · 2025Article
- Phylogenetic reconstruction of endophytic fungal isolates using internal transcribed spacer 2 (ITS2) region.Bioinformation · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledThe aim of this study is to determine the affinity of six active compounds of Aegle Marmelos Correa, they are (E, R)-Marmin, skimmianine, (S)-aegeline, aurapten, zeorin, and dustanin as antihistamines in histamine H1 receptor in comparison to cetirizin, diphenhydramine and chlorpheniramine as ligands comparison. Previously, in the in vitro study marmin obviously antagonized the histamine H1 receptor in a competitive manner.
methodsmolecular docking to determine the interaction of ligand binding to its receptor. Lower docking score indicates more stable binding to that protein.
resultsMarmin, skimmianine, aegeline, aurapten, zeorin, and dustanin were potential to develop as antihistamine agents, especially as histamine H1 receptor antagonists by interacting with amino acid residues, Asp107, Lys179, Lys191, Asn198, and Trp428 of histamine H1 receptor.
conclusionsBased on molecular docking, Amino acid residues involved in ligand protein interactions were Asp107, Lys179, Lys191, Asn198, and Trp428.
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Registered trials
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