id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-306904-8iteddug	Uversky, Vladimir N	Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs	2014-12-12		.txt	text/plain	18422	1012	48	86 Figure 8C represents the results of the computational disorder analysis in human APC (UniProt ID: P04070) and shows that mentioned loops enriched in basic residues are predicted to be disordered or very flexible, thereby providing an interesting mechanistic plane for the molecular basis of APC recognition and binding of FVIII. 96 Figure 8E shows that although human PECAM-1 (UniProt ID: P16284) is predicted to be mostly ordered, the residues, phosphorylation of which is crucial for its function (Y 663 and Y 686 ), are located within the highly disordered C-terminal tail. 210 Figure 14C represents the results of the disorder analysis of human AMSH (UniProt ID: O95630) and shows that this protein contains a long IDPR (residues 90-250) thereby illustrating that the N-terminal part of the analyzed catalytic domain is predicted to be disordered. [222] [223] [224] Figure 14D shows that human Purb protein (UniProt ID: O35295) is predicted to possess significant amount of functionally important intrinsic disorder.	./cache/cord-306904-8iteddug.txt	./txt/cord-306904-8iteddug.txt