PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18574264-2	2008	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors.	Glycosaminoglycans	34-52	coagulation factor X	Homo sapiens	159-168	
14596625-2	2003	To characterize this heparin-binding site, the extrinsic fluorescence of fluorescein-labeled, active site-blocked factor Xa was monitored as it was titrated with glycosaminoglycans of various sulfate content and chain length.	Glycosaminoglycans	162-180	coagulation factor X	Homo sapiens	114-123	
17343367-1	2007	Although the thrombin/thrombomodulin complex is considered the physiological activator of protein C, factor Xa (f.Xa) can also activate protein C in a reaction that is potentiated by glycosaminoglycans.	Glycosaminoglycans	183-201	coagulation factor X	Homo sapiens	101-110	
15957976-2	2005	It is one of a group of glycosaminoglycan compounds that accelerate the inactivation of factor Xa by inducing a conformational change in antithrombin.	Glycosaminoglycans	24-41	coagulation factor X	Homo sapiens	88-97	
14596625-3	2003	The binding of glycosaminoglycans to factor Xa appears to be charge-dependent because affinity is correlated with degree of glycosaminoglycan sulfation.	Glycosaminoglycans	15-33	coagulation factor X	Homo sapiens	37-46	
14596625-3	2003	The binding of glycosaminoglycans to factor Xa appears to be charge-dependent because affinity is correlated with degree of glycosaminoglycan sulfation.	Glycosaminoglycans	15-32	coagulation factor X	Homo sapiens	37-46	
14596625-5	2003	In contrast, when Gla-domainless factor Xa was substituted for factor Xa, glycosaminoglycans bound with similar affinities in the absence and presence of Ca(2+).	Glycosaminoglycans	74-92	coagulation factor X	Homo sapiens	33-42	
14596625-5	2003	In contrast, when Gla-domainless factor Xa was substituted for factor Xa, glycosaminoglycans bound with similar affinities in the absence and presence of Ca(2+).	Glycosaminoglycans	74-92	coagulation factor X	Homo sapiens	63-72	
14596625-7	2003	The changes in fluorescence intensity of factor Xa when titrated with glycosaminoglycans suggest that glycosaminoglycans induce conformational changes in the active site environment of factor Xa.	Glycosaminoglycans	70-88	coagulation factor X	Homo sapiens	41-50	
14596625-7	2003	The changes in fluorescence intensity of factor Xa when titrated with glycosaminoglycans suggest that glycosaminoglycans induce conformational changes in the active site environment of factor Xa.	Glycosaminoglycans	70-88	coagulation factor X	Homo sapiens	185-194	
14596625-7	2003	The changes in fluorescence intensity of factor Xa when titrated with glycosaminoglycans suggest that glycosaminoglycans induce conformational changes in the active site environment of factor Xa.	Glycosaminoglycans	102-120	coagulation factor X	Homo sapiens	41-50	
14596625-7	2003	The changes in fluorescence intensity of factor Xa when titrated with glycosaminoglycans suggest that glycosaminoglycans induce conformational changes in the active site environment of factor Xa.	Glycosaminoglycans	102-120	coagulation factor X	Homo sapiens	185-194	
14596625-9	2003	Glycosaminoglycans influenced the ability of factor Xa to cleave chromogenic substrates and attenuated the capacity of factor Xa to activate factor VII.	Glycosaminoglycans	0-18	coagulation factor X	Homo sapiens	45-54	
14596625-9	2003	Glycosaminoglycans influenced the ability of factor Xa to cleave chromogenic substrates and attenuated the capacity of factor Xa to activate factor VII.	Glycosaminoglycans	0-18	coagulation factor X	Homo sapiens	119-128	
14596625-10	2003	The potency of glycosaminoglycans in these assays reflected their affinity for factor Xa.	Glycosaminoglycans	15-33	coagulation factor X	Homo sapiens	79-88	
14596625-11	2003	These studies suggest that glycosaminoglycan binding perturbs exosites on the surface of factor Xa, potentially modifying interactions with cofactors or substrates.	Glycosaminoglycans	27-44	coagulation factor X	Homo sapiens	89-98	
29173042-1	2018	Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate.	Glycosaminoglycans	104-122	coagulation factor X	Homo sapiens	64-67	
1962899-4	1990	The half-life of anti-Factor Xa-like activity increased after repeated administration, indicating that glycosaminoglycans or other compounds are released by LMW heparin into the bloodstream.	Glycosaminoglycans	103-121	coagulation factor X	Homo sapiens	22-31	
7112518-0	1982	Demonstration of a direct anti-factor Xa activity in certain heparin-related glycosaminoglycans.	Glycosaminoglycans	77-95	coagulation factor X	Homo sapiens	31-40	
6448846-6	1980	The second-order rate constants for the neutralization of factor Xa or plasmin by the mucopolysaccharide .	Glycosaminoglycans	86-104	coagulation factor X	Homo sapiens	58-67	
22315264-3	2012	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes.	Glycosaminoglycans	34-52	coagulation factor X	Homo sapiens	160-169