PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26122211-0	2015	Discovery of non-competitive thrombin inhibitor derived from competitive tryptase inhibitor skeleton: Shift in molecular recognition resulted from skeletal conversion of carboxylate into phosphonate.	Organophosphonates	187-198	coagulation factor II, thrombin	Homo sapiens	29-37	
26122211-3	2015	The internal phosphonate derivative 6 showed potent thrombin inhibitory activity with an IC50 value of 1.0 muM, whereas it exhibited no or only weak tryptase and trypsin inhibition at 10 muM.	Organophosphonates	13-24	coagulation factor II, thrombin	Homo sapiens	52-60	
26122211-5	2015	Therefore, the skeletal conversion of the carboxylate into a phosphonate alters the mode of molecular recognition of these inhibitors by thrombin.	Organophosphonates	61-72	coagulation factor II, thrombin	Homo sapiens	137-145	
28867694-4	2017	In the latter half, this review summarizes the utility of difluoromethylenephosphonic acids and phosphonic acid esters in the development of enzyme inhibitors against protein tyrosine phosphatases, sphingomyelinases, purine nucleoside phosphorylases and thrombin.	Organophosphonates	96-118	coagulation factor II, thrombin	Homo sapiens	254-262	
11493008-0	2001	Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate.	Organophosphonates	40-51	coagulation factor II, thrombin	Homo sapiens	26-34	
11493008-2	2001	Crystal structures of the complex of alpha-thrombin with the phosphonate compound were determined independently using crystals of different ages.	Organophosphonates	61-72	coagulation factor II, thrombin	Homo sapiens	43-51