PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1158898-18	1975	These observations, particularly those made in the course of characterizine P"2, have led to the conclusion that cleavage of the peptide bond connecting the TA and TB portions of the prothrombin molecule (or its derivatives) produces a serine active center and, hence, a molecule possessing thrombin activity.	Terbium	164-166	coagulation factor II, thrombin	Homo sapiens	183-194	
1158898-18	1975	These observations, particularly those made in the course of characterizine P"2, have led to the conclusion that cleavage of the peptide bond connecting the TA and TB portions of the prothrombin molecule (or its derivatives) produces a serine active center and, hence, a molecule possessing thrombin activity.	Terbium	164-166	coagulation factor II, thrombin	Homo sapiens	186-194	
23074705-0	2012	A sensitive strategy for label-free and time-resolved fluorescence assay of thrombin using Tb-complex and unmodified gold nanoparticles.	Terbium	91-93	coagulation factor II, thrombin	Homo sapiens	76-84	
23074705-4	2012	The fluorescence intensity of Tb-complexes increases as the concentration of thrombin increases.	Terbium	30-32	coagulation factor II, thrombin	Homo sapiens	77-85	
23074705-5	2012	Due to the highly specific recognition ability of the aptamer for thrombin and the strong quenching property of GNPs for Tb-complexes, the proposed protocol has good selectivity and high sensitivity for thrombin.	Terbium	121-123	coagulation factor II, thrombin	Homo sapiens	66-74	
23074705-5	2012	Due to the highly specific recognition ability of the aptamer for thrombin and the strong quenching property of GNPs for Tb-complexes, the proposed protocol has good selectivity and high sensitivity for thrombin.	Terbium	121-123	coagulation factor II, thrombin	Homo sapiens	203-211	
22939121-5	2012	In the presence of target thrombin (TB), the TBA on the multilayer could catch the thrombin onto the electrode surface, which resulted in a barrier for electro-transfer, leading to the decrease of the electrochemical signal of Tb-Gra nanocomposites.	Terbium	227-229	coagulation factor II, thrombin	Homo sapiens	26-34	
22939121-5	2012	In the presence of target thrombin (TB), the TBA on the multilayer could catch the thrombin onto the electrode surface, which resulted in a barrier for electro-transfer, leading to the decrease of the electrochemical signal of Tb-Gra nanocomposites.	Terbium	227-229	coagulation factor II, thrombin	Homo sapiens	36-38	
22939121-5	2012	In the presence of target thrombin (TB), the TBA on the multilayer could catch the thrombin onto the electrode surface, which resulted in a barrier for electro-transfer, leading to the decrease of the electrochemical signal of Tb-Gra nanocomposites.	Terbium	227-229	coagulation factor II, thrombin	Homo sapiens	83-91	
22540161-5	2012	RESULTS: In spiked samples, TB-402 inhibited FVIII:C by 30%, prolonged APTT by 4.5 s, and reduced the peak height in the thrombin generation assay to 56% +- 13% of the control value.	Terbium	28-30	coagulation factor II, thrombin	Homo sapiens	121-129	
16104640-6	2005	However, the sensitivity of detection of TB in the presence of HIV increased to 87% by concomitant detection of circulating free and CIC serine protease antigen.	Terbium	41-43	coagulation factor II, thrombin	Homo sapiens	137-152	
16104640-7	2005	CONCLUSION: Detection of free and CIC tuberculous serine protease antigen along with antibody is more useful for detecting TB in the presence of HIV co-infection.	Terbium	123-125	coagulation factor II, thrombin	Homo sapiens	50-65