PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24361527-3	2014	Sulfation at the C3 position of glucosamine is a relatively rare, yet biologically significant modification, initially described as a key determinant for binding and activation of antithrombin and later for infection by type I herpes simplex virus.	Glucosamine	32-43	serpin family C member 1	Homo sapiens	180-192	
19185514-1	2009	The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection.	Glucosamine	29-40	serpin family C member 1	Homo sapiens	107-123	
34626387-3	2022	Heparin polymers carrying rare 3-O-sulfated glucosamine units have been proven to be critical for binding to antithrombin and elicit an anticoagulant response.	Glucosamine	44-55	serpin family C member 1	Homo sapiens	109-121	
15325299-10	2004	We also focused our attention on di- and tetrasaccharidic species containing the 3-O-sulfated glucosamines taken as markers of the active sites for antithrombin III.	Glucosamine	94-106	serpin family C member 1	Homo sapiens	148-164	
15060080-3	2004	This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin.	Glucosamine	118-129	serpin family C member 1	Homo sapiens	235-247	
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	Glucosamine	152-163	serpin family C member 1	Homo sapiens	60-72	
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	Glucosamine	127-138	serpin family C member 1	Homo sapiens	0-6	
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	Glucosamine	127-138	serpin family C member 1	Homo sapiens	161-167	
18669628-10	2008	These antithrombin-binding chains contain more than 6% 3-O-sulfated glucosamine residues, convey an anticoagulant activity of 2.5 IU/ml to human follicular fluid, and have an anti-Factor Xa specific activity of 167 IU/mg.	Glucosamine	68-79	serpin family C member 1	Homo sapiens	6-18	
18640975-2	2008	The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)).	Glucosamine	161-165	serpin family C member 1	Homo sapiens	100-112	
12138164-2	2002	The 3-O-sulfated glucosamine residue contributes to two important biological functions of HS: binding to antithrombin and thereby carrying anticoagulant activity, and binding to herpes simplex viral envelope glycoprotein D to serve as an entry receptor for herpes simplex virus 1.	Glucosamine	17-28	serpin family C member 1	Homo sapiens	105-117	
10215897-11	1999	All monitored NMR variables, 1H and 13C chemical shifts, 1JC-H couplings and transferred NOEs, indicated that the changes in conformation at the glycosidic linkage GlcN, 6-SO3-alpha(1-4)-GlcA were induced by the presence of antithrombin and suggested that the receptor selected a conformer different from that in the free state.	Glucosamine	164-168	serpin family C member 1	Homo sapiens	224-236	
1962908-6	1990	The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II.	Glucosamine	68-79	serpin family C member 1	Homo sapiens	13-19	
2083874-4	1990	The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine.	Glucosamine	96-109	serpin family C member 1	Homo sapiens	20-32	
29031112-1	2017	The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin.	Glucosamine	93-104	serpin family C member 1	Homo sapiens	4-20	
3427019-0	1987	Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III.	Glucosamine	38-49	serpin family C member 1	Homo sapiens	107-123	
3208245-0	1988	Binding of heparin to antithrombin III: a chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue.	Glucosamine	101-126	serpin family C member 1	Homo sapiens	22-38	
6935668-0	1980	Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin.	Glucosamine	28-41	serpin family C member 1	Homo sapiens	57-69	
118968-5	1979	Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid.	Glucosamine	99-110	serpin family C member 1	Homo sapiens	32-48	
29031112-1	2017	The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin.	Glucosamine	93-104	serpin family C member 1	Homo sapiens	22-27