@article { ISI:000373935600005,
	title = {Structural insight of NICD-MAML interactions: virtual screening, docking and molecular dynamics study for the identification of potential inhibitor},
	journal = {Letters in Drug Design \& Discovery},
	volume = {13},
	number = {4},
	year = {2016},
	month = {JAN},
	pages = {301-313},
	publisher = {BENTHAM SCIENCE PUBL LTD},
	address = {EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES},
	abstract = {<p>Activation of Notch signalling pathway is triggered by binding of NICD to transcription factor CSL and transcriptional co-activator MAML, which involves in various biological functions as well as progression of diseases. Recent prediction shows suppression of cancer causing genes of this pathway through inhibition of NICD-MAML interaction. Through virtual screening against {\textquoteleft}{\textquoteleft}NCI Diversity 3{\textquoteright}{\textquoteright} of Zinc database, we identified a potential inhibitor {\textquoteleft}{\textquoteleft}ZINC01690699{\textquoteright}{\textquoteright} (1-N,4-N-bis[3-(1H-benzimidazol-2-yl)phenyl]benzene-1,4-dicarboxamide; 1-N, 4-dicarboxamide) possessing highest binding affinity to block the two distinct Binding Sites of NICD to inhibit NICD-MAML interaction and also found the most imperative and essential Binding Site (Site I). Inhibition of this interaction caused by binding of ZINC01690699 is validated by protein-protein docking and the prolonged binding as well as stability of NICD-Inhibitor complex is supported by molecular dynamics simulation. The study not only identifies the best inhibitor but also proposes a potential drug for the treatment of cancers.</p>},
	keywords = {free energy of binding, MAML, NICD, Notch signalling, potential inhibitor, ZINC01690699},
	issn = {1570-1808},
	doi = {10.2174/1570180812666150819003634},
	author = {Sinha, Noopur and Chowdhury, Saikat and Sarkar, Ram Rup}
}
