id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-321957-ybtk9cp1	Carey, Brian D.	Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation	2020-03-09		.txt	text/plain	6713	384	52	title: Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation A virus with capsid phosphorylation sites mutated to alanine (VEEV CPD) displayed a lower genomic copy to pfu ratio than the parental virus; suggesting more efficient viral assembly and more infectious particles being released. These data suggest that cells infected with VEEV CPD output more functional viral particles than VEEV TC-83, potentially due to more efficient viral packaging and this phenotype is due to loss of capsid phosphorylation. Loss of PKCδ through siRNA transfection also resulted in increased capsid viral RNA binding, further solidifying the link between VEEV CPD and PKCδ (Fig 7B) . To determine the impact of VEEV capsid phosphorylation on vRNA binding, we utilized quantitative RNA-IP experiments to probe the interaction between the capsid protein and the vRNA at sites identified as highly enriched, intermediately enriched, and non-enriched by our CLIP-seq studies.	./cache/cord-321957-ybtk9cp1.txt	./txt/cord-321957-ybtk9cp1.txt