PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19497853-7	2009	Salt dependence of binding affinity indicates that the antithrombin-sulfated DHP interaction involves a massive 80-87% non-ionic component to the free energy of binding.	Salts	0-4	serpin family C member 1	Homo sapiens	55-67	
16078853-7	2005	The salt-dependence of the K(D) of the PAA-antithrombin interaction shows the formation of five ionic interactions.	Salts	4-8	serpin family C member 1	Homo sapiens	43-55	
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	Salts	4-8	serpin family C member 1	Homo sapiens	78-90	
2749614-0	1989	Dissociation of the thrombin/antithrombin III reaction from amidolytic activity of the enzyme at high salt concentration.	Salts	102-106	serpin family C member 1	Homo sapiens	29-45	
3730427-4	1986	In contrast, the limiting salt concentration values for complexes formed between antithrombin III and heparin did not change with either the degree of sulphation or the biological potency of the heparin samples.	Salts	26-30	serpin family C member 1	Homo sapiens	81-97	
6747440-7	1984	This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence.	Salts	116-120	serpin family C member 1	Homo sapiens	141-157	
872292-7	1977	In the high salt system the relative contributions of antithrombin III  to Xa neutralization in human and rabbit plasma are different.	Salts	12-16	serpin family C member 1	Homo sapiens	54-70	
26186963-7	2015	RESULTS: High salt concentrations specifically restricted the pentassacharide-induced activation of antithrombin to the beta glycoform.	Salts	14-18	serpin family C member 1	Homo sapiens	100-112	
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	86-98	
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	151-163	
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	151-163	
21751805-1	2011	The observed salt dependence of charged ligand binding to polyelectrolytes, such as proteins to DNA or antithrombin to heparin, is often interpreted by means of the "oligolysine model."	Salts	13-17	serpin family C member 1	Homo sapiens	103-115