id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-263532-q044i7ym	Goyal, Bhupesh	Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy	2020-05-13		.txt	text/plain	6017	402	54	In this regard, we have compiled the literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV M(pro) on its dimerization and, thus, catalytic activity. The individual monomers of SARS-CoV M pro are enzymatically inactive, and two strategies have been employed to develop inhibitors against this enzyme: (i) molecules targeting the substrate binding pocket to block the catalytic activity, and (ii) dimerization inhibitors. 14, 15 In the present review, literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV M pro on its dimerization and, thus, catalytic activity are compiled. The various mutation analyses, N-terminal truncation studies, and MD simulation studies that highlighted key residues of SARS-CoV M pro involved in the stabilization of the catalytically active dimeric structure of the enzyme are listed in Table 2 and are arranged in chronological order.	./cache/cord-263532-q044i7ym.txt	./txt/cord-263532-q044i7ym.txt