PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19076073-5	2009	Modelling of mouse ceruloplasmin against the known X-ray structure of human ceruloplasmin indicated subtle but potentially significant changes in the pPD- and azide-binding sites.	Azides	159-164	ceruloplasmin	Homo sapiens	76-89	
10727774-4	2000	Hydroxyl radical scavengers such as azide and mannitol inhibited the fragmentation of ceruloplasmin.	Azides	36-41	ceruloplasmin	Homo sapiens	86-99	
11832331-3	2002	Here, we show that azide-sensitive oxidase activity is enriched in the same fractions, correlating subcellular localization of enzyme activity with ceruloplasmin immunoreactivity.	Azides	19-24	ceruloplasmin	Homo sapiens	148-161	
6289706-7	1982	The "antioxidant" activity of ceruloplasmin is inhibited by azide.	Azides	60-65	ceruloplasmin	Homo sapiens	30-43	
4037797-7	1985	Chicken ceruloplasmin catalyzed the azide-sensitive oxidation of p-phenylenediamine (PPD) and N,N"-dimethyl-p-phenylenediamine (DPD), and showed ferroxidase activity similar to that of human ceruloplasmin.	Azides	36-41	ceruloplasmin	Homo sapiens	191-204	
10550686-0	1999	An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates to ceruloplasmin, a multi-copper oxidase in the plasma.	Azides	60-65	ceruloplasmin	Homo sapiens	102-115	
11945940-0	1971	Kinetic studies of ceruloplasmin-azide interaction.	Azides	33-38	ceruloplasmin	Homo sapiens	19-32	
30960224-4	2019	The cyclic backbone (c-P2) was then coupled with azide-containing polymer double-chain (l-PS-PhN3) via CuAAC reaction to construct a novel cyclic double-grafted polymer (c-P2-g-Ph-PS).	Azides	49-54	ceruloplasmin	Homo sapiens	21-25	
30960224-4	2019	The cyclic backbone (c-P2) was then coupled with azide-containing polymer double-chain (l-PS-PhN3) via CuAAC reaction to construct a novel cyclic double-grafted polymer (c-P2-g-Ph-PS).	Azides	49-54	ceruloplasmin	Homo sapiens	170-174