id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-277400-w7mvk3x4	Nasir, Arshan	Identification of Capsid/Coat Related Protein Folds and Their Utility for Virus Classification	2017-03-10		.txt	text/plain	7527	398	47	While the member viruses within a lineage exhibit strong 3D structural similarities in capsid/coat fold architectures (or principles in constructing a functional virion) regardless of the viral replicon (i.e., DNA or RNA) and/or infected host type, the lineages however are believed to be unrelated to each other indicating the polyphyletic origin of viruses (Bamford, 2003) . The b.121 fold in the SCOP hierarchy includes 7 children FSFs (that are not necessarily related in evolution according to SCOP definitions): (i) "PHM/PNGase F" FSF (b.121.1) involved in oxidation-reduction metabolic processes (not detected in any of our sampled viral proteomes), (ii) "Group II dsDNA viruses VP" FSF (b.121.2), which is the "double β-barrel" fold signature of the PRD1/Adenovirus-like lineage (read below), (iii) "Nucleoplasmin-like core domain" FSF (b.121.3) involved in the assembly of nucleosomes in cells, and (iv-vii) FSFs b.121.4, b.121.5, b.121.6, and b.121.7 (Figure 1 ) that define the picornavirus-like lineage and are individually described below.	./cache/cord-277400-w7mvk3x4.txt	./txt/cord-277400-w7mvk3x4.txt