PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3949798-5	1986	An octasaccharide with characteristic marked ability to accelerate the inactivation of Factor Xa by antithrombin retained greater than 50% of its activity even at a histidine-rich glycoprotein/oligosaccharide molar ratio of 500:1.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	100-112	
3427019-2	1987	The octasaccharide produced a maximum 48% increase in intrinsic fluorescence at 37 degrees C and a rate of factor Xa inhibition of 6 X 10(5) M-1 s-1 as measured by stopped-flow fluorometry at 25 degrees C. The basal rate of the antithrombin-factor Xa interaction observed in the absence of oligosaccharide was 2 X 10(3) M-1 s-1.	Octasaccharide	4-18	serpin family C member 1	Homo sapiens	228-240	
2732232-10	1989	A size dependence was observed for the heparin effect since an anticoagulantly active octasaccharide fragment of heparin, with avid antithrombin binding activity, was without effect on the inactivation of antithrombin by neutrophil elastase.	Octasaccharide	86-100	serpin family C member 1	Homo sapiens	132-144	
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	Octasaccharide	169-183	serpin family C member 1	Homo sapiens	79-95	
6525337-1	1984	We have isolated from nitrous acid cleavage products of heparin two major octasaccharide fragments which bind with high affinity to human antithrombin.	Octasaccharide	74-88	serpin family C member 1	Homo sapiens	138-150	
6525337-4	1984	This suggests that the conformation of antithrombin in the region of the factor Xa binding site is similar when the protease inhibitor is complexed with either octasaccharide.	Octasaccharide	160-174	serpin family C member 1	Homo sapiens	39-51	
6698980-14	1984	A model of the antithrombin III-binding octasaccharide (Lindahl, U., Backstrom, G., Thunberg, L., and Leder, I. G. (1980) Proc.	Octasaccharide	40-54	serpin family C member 1	Homo sapiens	15-31	
6698980-19	1984	These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III.	Octasaccharide	166-180	serpin family C member 1	Homo sapiens	219-235	
6583694-1	1984	We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin.	Octasaccharide	86-100	serpin family C member 1	Homo sapiens	183-195	
6583694-2	1984	Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis.	Octasaccharide	27-41	serpin family C member 1	Homo sapiens	127-139	
6486808-3	1984	Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor.	Octasaccharide	39-53	serpin family C member 1	Homo sapiens	17-29	
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	Octasaccharide	169-183	serpin family C member 1	Homo sapiens	149-165	
6885772-2	1983	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53	
6885772-3	1983	After digestion of this octasaccharide with alpha-L-iduronidase and N-acetylglucosamine-6-sulfate sulfatase, two fractions, with high and low affinity for antithrombin, respectively, were isolated by affinity chromatography on antithrombin-Sepharose.	Octasaccharide	24-38	serpin family C member 1	Homo sapiens	155-167	
6935668-1	1980	An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53	
7083257-1	1982	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin and previously found to have the following predominant structure (see formula in text) has been studied further.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53	
7083257-11	1982	It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied.	Octasaccharide	148-162	serpin family C member 1	Homo sapiens	25-37	
7338523-1	1981	Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III.	Octasaccharide	84-98	serpin family C member 1	Homo sapiens	122-138	
7338523-1	1981	Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III.	Octasaccharide	84-98	serpin family C member 1	Homo sapiens	264-280	
7338523-3	1981	Fifty percent inactivation activities of the octasaccharide for thrombin and factor Xa in the presence of antithrombin III were 2 and 6.5 times, respectively, higher than those of the initial heparin.	Octasaccharide	45-59	serpin family C member 1	Homo sapiens	106-122	
28340300-7	2017	We identified a novel octasaccharide that interacts with antithrombin and displays anti factor Xa activity.	Octasaccharide	22-36	serpin family C member 1	Homo sapiens	57-69	
23083208-4	2013	The molecular conformation of the octasaccharide-antithrombin complex has been determined by NMR experiments and docking/energy minimization.	Octasaccharide	34-48	serpin family C member 1	Homo sapiens	49-61	
23083208-5	2013	The presence of the second 3-O-sulfated glucosamine in the octasaccharide induced more than one order of magnitude increase in affinity to antithrombin compared to the pentasaccharide AGA*IA.	Octasaccharide	59-73	serpin family C member 1	Homo sapiens	139-151