Title : Cardamonin Presents in Vivo Activity against Schistosoma mansoni and Inhibits Potato Apyrase.

Pub. Date : 2021 Nov

PMID : 34608744






6 Functional Relationships(s)
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1 Cardamonin achieved a significant inhibition of the apyrase activity and the three-dimensional structure of the potato apyrase, obtained by homology modeling, showed that cardamonin may interact mainly through hydrogen bonds. cardamonin apyrase Solanum tuberosum
2 Cardamonin achieved a significant inhibition of the apyrase activity and the three-dimensional structure of the potato apyrase, obtained by homology modeling, showed that cardamonin may interact mainly through hydrogen bonds. cardamonin apyrase Solanum tuberosum
3 Cardamonin achieved a significant inhibition of the apyrase activity and the three-dimensional structure of the potato apyrase, obtained by homology modeling, showed that cardamonin may interact mainly through hydrogen bonds. cardamonin apyrase Solanum tuberosum
4 Cardamonin achieved a significant inhibition of the apyrase activity and the three-dimensional structure of the potato apyrase, obtained by homology modeling, showed that cardamonin may interact mainly through hydrogen bonds. cardamonin apyrase Solanum tuberosum
5 Cardamonin achieved a significant inhibition of the apyrase activity and the three-dimensional structure of the potato apyrase, obtained by homology modeling, showed that cardamonin may interact mainly through hydrogen bonds. Hydrogen apyrase Solanum tuberosum
6 Molecular docking studies corroborate with the action of cardamonin in binding and inhibiting both potato apyrase and S. mansoni NTPDases. cardamonin apyrase Solanum tuberosum