PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30111632-6	2018	Lack of structural restraint by disulfides, present in other related cytokines, is most likely reason for the low stability of IL-24.	Disulfides	32-42	interleukin 24	Homo sapiens	127-132	
24174213-2	2014	Human IL24 possesses three N glycosylation sites and a disulfide bridge.	Disulfides	55-64	interleukin 24	Homo sapiens	6-10	
19734147-0	2009	Structural mapping of post-translational modifications in human interleukin-24: role of N-linked glycosylation and disulfide bonds in secretion and activity.	Disulfides	115-124	interleukin 24	Homo sapiens	64-78	
19734147-2	2009	The primary sequence of human IL-24 differs from homologous cytokines, because it possesses three consensus N-linked glycosylation sites and the potential for a single disulfide bond.	Disulfides	168-177	interleukin 24	Homo sapiens	30-35	
19734147-8	2009	These structure-function relationships show that, although IL-24 is a member of the IL-19 subfamily of IL-10-like cytokines by sequence similarity, its surface properties and its distinctive disulfide arrangement make it unique.	Disulfides	191-200	interleukin 24	Homo sapiens	59-64	
17238830-5	2006	Cation exchange purification results in the isolation of at least two N-linked glycosylated IL-24 dimers covalently associated via intermolecular disulfide bonds.	Disulfides	146-155	interleukin 24	Homo sapiens	92-97