PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10427858-3	1999	In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group.	Oligosaccharides	98-114	coagulation factor II, thrombin	Homo sapiens	66-74	
14556453-3	2003	In a further step, we have designed and synthesised oligosaccharides (pentadeca--to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain.	Oligosaccharides	52-68	coagulation factor II, thrombin	Homo sapiens	122-130	
15311268-6	2004	The protein-protein and protein-oligosaccharide interactions together explain the basis for heparin activation of antithrombin as a thrombin inhibitor.	Oligosaccharides	32-47	coagulation factor II, thrombin	Homo sapiens	118-126	
1618758-6	1992	Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide.	Oligosaccharides	254-269	coagulation factor II, thrombin	Homo sapiens	36-44	
10328304-2	1999	The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III.	Oligosaccharides	40-55	coagulation factor II, thrombin	Homo sapiens	73-81	
10201371-6	1999	To obtain more potent and well-tolerated antithrombotic drugs, we wished to synthesize heparin mimetics able to inhibit thrombin, that is, longer oligosaccharides.	Oligosaccharides	146-162	coagulation factor II, thrombin	Homo sapiens	120-128	
1618758-6	1992	Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide.	Oligosaccharides	254-269	coagulation factor II, thrombin	Homo sapiens	60-68	
6207810-9	1984	An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate.	Oligosaccharides	3-18	coagulation factor II, thrombin	Homo sapiens	106-114	
3218731-7	1988	However, results obtained with heparan sulfate preparations did not indicate any clear relationship between either molecular weight or sulfate content and thrombin binding, but suggested that there may be an oligosaccharide sequence containing N-sulfate residues which confers high affinity for thrombin.	Oligosaccharides	208-223	coagulation factor II, thrombin	Homo sapiens	295-303	
3377765-2	1988	The resulting oligosaccharides were fractionated by gel filtration chromatography and tested for the ability to stimulate inhibition of thrombin by purified heparin cofactor II or antithrombin.	Oligosaccharides	14-30	coagulation factor II, thrombin	Homo sapiens	136-144	
3782075-6	1986	Moreover, similar binary complexes with 3H-labeled octadecasaccharide or larger chains, but not with smaller oligosaccharides, were capable of binding to matrix-linked inactivated thrombin.	Oligosaccharides	109-125	coagulation factor II, thrombin	Homo sapiens	180-188	
6317088-0	1984	The oligosaccharide of human thrombin: investigations of functional significance.	Oligosaccharides	4-19	coagulation factor II, thrombin	Homo sapiens	29-37	
6317088-1	1984	Functional properties of the carbohydrate chain of human thrombin were examined by quantitating the activity of the enzyme before and after partial removal of its oligosaccharide by exoglycosidases.	Oligosaccharides	163-178	coagulation factor II, thrombin	Homo sapiens	57-65	
6317088-5	1984	It is concluded, therefore, that the oligosaccharide of human thrombin is located outside the major protein and platelet-binding regions of the molecule.	Oligosaccharides	37-52	coagulation factor II, thrombin	Homo sapiens	62-70	
6870248-0	1983	The carbohydrate of human thrombin: structural analysis of glycoprotein oligosaccharides by mass spectrometry.	Oligosaccharides	72-88	coagulation factor II, thrombin	Homo sapiens	26-34	
6870248-1	1983	The carbohydrate structure of human thrombin has been determined by direct probe mass spectrometry of the oligosaccharides released by trifluoroacetolysis from the asialo glycoprotein.	Oligosaccharides	106-122	coagulation factor II, thrombin	Homo sapiens	36-44	
6847629-4	1983	An anti-thrombin III-binding oligosaccharide preparation (containing predominantly eight to ten saccharide units), prepared by degradation of heparin with HNO2 had high (800 units/mg) anti-Factor Xa, but negligible anti-thrombin, specific activity.	Oligosaccharides	29-44	coagulation factor II, thrombin	Homo sapiens	8-16	
28755259-3	2017	Accurate mass measurements revealed that the predominant form of native human alpha-thrombin contains a glycosylation mass of 2205 Da, corresponding to a sialylated symmetric biantennary oligosaccharide structure without fucosylation.	Oligosaccharides	187-202	coagulation factor II, thrombin	Homo sapiens	84-92	
6721831-8	1984	The anti-thrombin activities of the octadecasaccharide and larger oligosaccharides were more readily neutralized by platelet factor 4 than were their anti-Factor Xa activities.	Oligosaccharides	66-82	coagulation factor II, thrombin	Homo sapiens	9-17