ArticleDaru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences2013
Comparative amino acid decomposition analysis of potent type I p38α inhibitors.
Article in Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- miR-4486 inhibits colorectal cancer proliferation via targeting MAP2K4 to inhibit the activation of the p38MAPK/JNK signaling.Heliyon · 2024Article
- Potential Mechanisms of Quercetin Influence the ClfB Protein During Biofilm Formation ofFrontiers in pharmacology · 2022Article
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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
background and purpose of the studyp38α is a member of mitogen-activated protein kinases (MAPK) considered as a prominent target in development of anti-inflammatory agents. Any abnormality in the phosphorylation process leads to the different human diseases such as cancer, diabetes and inflammatory diseases. Several small molecule p38α inhibitors have been developed up to now. In this regard, structural elucidation of p38 inhibitors needs to be done enabling us in rational lead development strategies.
methodsVarious interactions of three potent inhibitors with p38α active site have been evaluated in terms of binding energies and bond lengths via density function theory and MD simulations.
resultsOur comparative study showed that both ab initio and MD simulation led to the relatively similar results in pharmacophore discrimination of p38α inhibitors.
conclusionThe results of the present study may find their usefulness in pharmacophore based modification of p38α inhibitors.
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