id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-269496-tnw7sxlh	Sen Gupta, Parth Sarthi	Binding mechanism and structural insights into the identified protein target of COVID-19 and importin-α with in-vitro effective drug ivermectin	2020-10-28		.txt	text/plain	4910	246	53	Molecular dynamics of corresponding protein-drug complexes reveals that the drug bound state of RdRp with RNA has better structural stability than the Helicase NCB site and Importin-α, with MM/PBSA free energy of −187.3 kJ/mol, almost twice that of Helicase (−94.6 kJ/mol) and even lower than that of Importin-α (−156.7 kJ/mol). Together, being conserved and a necessary component for the replication of coronavirus, a multi-functional protein, Nsp13-helicase, is another vital SARS-COV-2 target (Jia et al., 2019) , which can be considered further for antiviral drug discovery provided a very small number of Nsp13 inhibitors reported to date . Molecular docking of Ivermectin with twelve SARS-COV-2's targets along with Importin-a was carried out, followed by binding mechanism exploration and structural stability analysis using molecular dynamics (MD) simulation through the root-meansquare deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration (R g ), and binding free energy of the complexes of Ivermectin with the best targets.	./cache/cord-269496-tnw7sxlh.txt	./txt/cord-269496-tnw7sxlh.txt