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