id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-102151-26lumewy	Cox, Robert M.	Therapeutic Targeting of Measles Virus Polymerase with ERDRP-0519 Suppresses All RNA Synthesis Activity	2020-09-24		.txt	text/plain	1797	92	43	Results demonstrate that unlike all other mononegavirus small molecule inhibitors identified to date, ERDRP-0519 inhibits all phosphodiester bond formation in both de novo initiation of RNA synthesis at the promoter and RNA elongation by a committed polymerase complex. Photocrosslinking and resistance profiling-informed ligand docking revealed that this unprecedented mechanism of action of ERDRP-0519 is due to simultaneous engagement of the L protein polyribonucleotidyl transferase (PRNTase)-like domain and the flexible intrusion loop by the compound, pharmacologically locking the polymerase in pre-initiation conformation. Photocrosslinking-based target site 27 mapping demonstrated that this class-defining prototype inhibitor stabilizes a pre-initiation conformation 28 of the viral polymerase complex that sterically cannot accommodate template RNA. Photocrosslinking-based target site 27 mapping demonstrated that this class-defining prototype inhibitor stabilizes a pre-initiation conformation 28 of the viral polymerase complex that sterically cannot accommodate template RNA.	./cache/cord-102151-26lumewy.txt	./txt/cord-102151-26lumewy.txt