PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23517781-1	2013	Hypochlorous acid and its acid-base counterpart, hypochlorite ions, produced under inflammatory conditions, may produce chloramides of glycosaminoglycans, perhaps through the binding of myeloperoxidase directly to the glycosaminoglycans.	Glycosaminoglycans	135-153	myeloperoxidase	Homo sapiens	186-201	
23707661-6	2013	RESULTS: MPO binds to the ECM proteins collagen IV and fibronectin, and this association is enhanced by the pre-incubation of these proteins with glycosaminoglycans.	Glycosaminoglycans	146-164	myeloperoxidase	Homo sapiens	9-12	
23707661-7	2013	Correspondingly, an excess of glycosaminoglycans in solution during incubation inhibits the binding of MPO to collagen IV and fibronectin.	Glycosaminoglycans	30-48	myeloperoxidase	Homo sapiens	103-106	
23517781-1	2013	Hypochlorous acid and its acid-base counterpart, hypochlorite ions, produced under inflammatory conditions, may produce chloramides of glycosaminoglycans, perhaps through the binding of myeloperoxidase directly to the glycosaminoglycans.	Glycosaminoglycans	218-236	myeloperoxidase	Homo sapiens	186-201	
15078224-3	2004	Exposure of glycosaminoglycans to a MPO-H2O2-Cl- system or reagent HOCl generates long-lived chloramides [R-NCl-C(O)-R"] derived from the glycosamine N-acetyl functions.	Glycosaminoglycans	12-30	myeloperoxidase	Homo sapiens	36-39	
15932347-3	2005	As MPO binds to glycosaminoglycans, oxidation of extracellular matrix and cell surfaces by HOCl may be localized to these materials.	Glycosaminoglycans	16-34	myeloperoxidase	Homo sapiens	3-6	
11748259-3	2001	Purified MPO and MPO released by intraluminal degranulation of activated human PMNs avidly bound to aortic endothelial cell glycosaminoglycans in both cell monolayer and isolated vessel models.	Glycosaminoglycans	124-142	myeloperoxidase	Homo sapiens	9-12	
11748259-3	2001	Purified MPO and MPO released by intraluminal degranulation of activated human PMNs avidly bound to aortic endothelial cell glycosaminoglycans in both cell monolayer and isolated vessel models.	Glycosaminoglycans	124-142	myeloperoxidase	Homo sapiens	17-20	
33271281-6	2021	Moreover, interaction of MPO, which is carrying a cationic charge, with anionic glycosaminoglycans (GAGs) resulted in reduction of their relative charge.	Glycosaminoglycans	80-98	myeloperoxidase	Homo sapiens	25-28	
33271281-6	2021	Moreover, interaction of MPO, which is carrying a cationic charge, with anionic glycosaminoglycans (GAGs) resulted in reduction of their relative charge.	Glycosaminoglycans	100-104	myeloperoxidase	Homo sapiens	25-28	
33271281-7	2021	By means of micro-viscometry and atomic force microscopy, we disclosed that MPO can crosslink GAG chains.	Glycosaminoglycans	94-97	myeloperoxidase	Homo sapiens	76-79	
33271281-12	2021	Altogether, these findings provide evidence that MPO through interaction with GAGs modulates overall charge of the GLX, causing modification of its structure and thus affecting EC function.	Glycosaminoglycans	78-82	myeloperoxidase	Homo sapiens	49-52