id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-289273-zpyz1krq	Barry, Michele	Poxvirus Exploitation of the Ubiquitin-Proteasome System	2010-10-19		.txt	text/plain	7212	404	44	Members of the poxvirus family have recently been shown to encode BTB/kelch and ankyrin/F-box proteins that interact with cullin-3 and cullin-1 based ubiquitin ligases, respectively. Recently, cellular BTB domain-containing proteins have been shown to function as substrate-specific adaptors of cullin-3 based ubiquitin ligase to target proteins for ubiquitination [54] [55] [56] [57] . Although the poxviral ankyrin repeat proteins contain no obvious structural domains at their C-termini, many of the proteins display a conserved sequence, which upon closer inspection was shown to resemble the F-box domain that functions in the recruitment of substrates to the cellular SCF (Skp-1, cullin, F-box) ubiquitin ligase complex [82] [83] [84] . The complex consists of cullin-1, which serves as the molecular scaffold, Roc1, a RING finger ubiquitin ligase, Skp1, the linker protein, and one of over 70 known cellular F-box proteins which function in substrate recruitment ( Figure 2D ) [84] [85] [86] .	./cache/cord-289273-zpyz1krq.txt	./txt/cord-289273-zpyz1krq.txt