PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6259143-9	1981	Thrombin associated with the former was released into the media when the cells were incubated at 0-4 degrees C with hirudin or hydroxylamine, or transferred to the insensitive compartment when incubated at 22 degrees C. Finally, confluent cultures of fibroblasts bind 2-3 x 10(4) 125I-alpha-thrombin molecules/cell with an apparent binding constant, i.e. Kd, of 0.7 nM (a true Kd could not be determined because of the irreversible nature of thrombin binding).	Hydroxylamine	127-140	coagulation factor II, thrombin	Homo sapiens	0-8	
1850875-5	1991	The two active site directed fluorophores, dansyl fluoride and p-nitrophenyl anthranilate showed differences in both lambda emmax and lambda exmax of the complexes with bovine and human-alpha-thrombin, respectively, Several of the effects observed i.e., ligand binding (indole or benzamidine) and the subtle hydrophobic interactions between the nitroxide moiety and the protein active site would be difficult to assess from an x-ray structure determination alone.	Hydroxylamine	345-354	coagulation factor II, thrombin	Homo sapiens	192-200	
2831973-0	1988	Evidence for multiple conformational changes in the active center of thrombin induced by complex formation with thrombomodulin: an analysis employing nitroxide spin-labels.	Hydroxylamine	150-159	coagulation factor II, thrombin	Homo sapiens	69-77	
3886645-5	1985	Addition of hydroxylamine to ethoxyformylated prothrombin reversed the loss of fibrinogen-clotting activity.	Hydroxylamine	12-25	coagulation factor II, thrombin	Homo sapiens	46-57	
6197765-0	1983	The alpha 2 macroglobulin/thrombin interaction in the presence of hydroxylamine.	Hydroxylamine	66-79	coagulation factor II, thrombin	Homo sapiens	26-34	
6197765-1	1983	The influence of a primary amine, hydroxylamine, on the interaction between alpha 2 macroglobulin (alpha 2M) and thrombin was analyzed by electrophoretic and enzymatic methods.	Hydroxylamine	34-47	coagulation factor II, thrombin	Homo sapiens	113-121	
6197765-2	1983	Hydroxylamine (final concentrations 0.01 M and 0.1 M) was added to the alpha 2M solution 3 to 5 min before thrombin.	Hydroxylamine	0-13	coagulation factor II, thrombin	Homo sapiens	107-115	
6197765-5	1983	However the rate of inhibition of the clotting activity of thrombin was diminished in function of the hydroxylamine concentration.	Hydroxylamine	102-115	coagulation factor II, thrombin	Homo sapiens	59-67	
6193011-2	1983	The thrombin-alpha 2M binding is normally covalent, but the presence of hydroxylamine during the reaction leads to the formation of a non-covalent complex.	Hydroxylamine	72-85	coagulation factor II, thrombin	Homo sapiens	4-12	
6885787-18	1983	When thrombin-PN complexes are dissociated with 1 M hydroxylamine a smaller form of PN (approximately 46 kilodaltons) is detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that the complexed PN is proteolytically modified.	Hydroxylamine	52-65	coagulation factor II, thrombin	Homo sapiens	5-13	
10514286-6	1999	s(-1) for 4c) and thrombin (k(i)/K(I) = 7 200 M(-1).s(-1) for 3b) as demonstrated by spontaneous or hydroxylamine-accelerated reactivation, irrespective of the nature of the substituent at the 6-position.	Hydroxylamine	100-113	coagulation factor II, thrombin	Homo sapiens	18-26	
1333213-5	1992	In general, the nitroxide immobilization was greater for spin-labeled thrombin complexes with HV2-Lys 47 vs. HV1.	Hydroxylamine	16-25	coagulation factor II, thrombin	Homo sapiens	70-78	
1634535-6	1992	Subsequent mild treatment of the covalent thrombin-inhibitor complexes with NH2OH in the presence of 5-(iodoacetamido)fluorescein resulted in generation of the thiol group together with its selective modification and incorporation of 0.96 +/- 0.07 mol of probe/mol of active sites.	Hydroxylamine	76-81	coagulation factor II, thrombin	Homo sapiens	42-50	
1634536-4	1992	An array of 16 thrombin derivatives was prepared by affinity labeling of the proteinase active site with the thioester peptide chloromethyl ketones, N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2Cl or N alpha-[(acetylthio)acetyl]-D-Phe-Phe-Arg-CH2Cl, followed by selective modification of the NH2OH-generated thiol group on the covalently incorporated inhibitors with each of eight thiol-reactive fluorescence probes.	Hydroxylamine	293-298	coagulation factor II, thrombin	Homo sapiens	15-23	
10945437-0	2000	Atomic structures of two nitroxide spin labels complexed with human thrombin: comparison with solution studies.	Hydroxylamine	25-34	coagulation factor II, thrombin	Homo sapiens	68-76	
3219359-8	1988	Incubation of N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-thrombin with 5-(iodoacetamido)fluorescein in the presence of NH2OH resulted in incorporation of 0.96 mol of the fluorescence probe/mol of active sites and the appearance of fluorescein fluorescence associated with the active site containing B-chain on sodium dodecyl sulfate-polyacrylamide gels.	Hydroxylamine	119-124	coagulation factor II, thrombin	Homo sapiens	57-65	
3219359-9	1988	Fluorescence labeling of thrombin required reaction of the inhibitor at the active site as well as subsequent generation of the thiol group with NH2OH.	Hydroxylamine	145-150	coagulation factor II, thrombin	Homo sapiens	25-33	
60792-2	1976	The nature of the binding between thrombin and the inhibitor is studied by treatment of the complex with 6 M guanidinium chloride, hydroxylamine, and dilute alkali.	Hydroxylamine	131-144	coagulation factor II, thrombin	Homo sapiens	34-42	
60792-5	1976	Treatment of dodecyl sulfate-denatured complex with hydroxylamine results in dissociation of the complex to yield free thrombin and heparin cofactor.	Hydroxylamine	52-65	coagulation factor II, thrombin	Homo sapiens	119-127	
1180962-2	1975	The nature of the binding between thrombin and the inhibitor is studied by treatment of the complex with 6 M guanidinium chloride, hydroxylamine, and dilute alkali.	Hydroxylamine	131-144	coagulation factor II, thrombin	Homo sapiens	34-42	
1180962-5	1975	Treatment of dodecylsulfate-denatured complex with hydroxylamine results in dissociation of the complex to yield free thrombin and heparin cofactor.	Hydroxylamine	51-64	coagulation factor II, thrombin	Homo sapiens	118-126	
1168069-3	1975	The reaction of thrombin was perturbed by addition of hydroxylamine or a competitive inhibitor and by variation of pH and it was compared with the reactions of other proteases.	Hydroxylamine	54-67	coagulation factor II, thrombin	Homo sapiens	16-24