PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9176590-2	1997	Recent reports using vWF labeled with either 125I or fluorescein isothiocyanate (FITC) have demonstrated that in shear-fields, vWF binds to both GPIb and GPIIb-IIIa.	Iodine-125	45-49	von Willebrand factor	Homo sapiens	21-24	
9176590-2	1997	Recent reports using vWF labeled with either 125I or fluorescein isothiocyanate (FITC) have demonstrated that in shear-fields, vWF binds to both GPIb and GPIIb-IIIa.	Iodine-125	45-49	von Willebrand factor	Homo sapiens	127-130	
1917949-7	1991	Accordingly, 125I-labeled botrocetin bound to vWF and to the 116-kDa fragment immobilized onto nitrocellulose but not to equivalent amounts of the reduced and alkylated 52/48-kDa fragment; it also bound to the peptide 539-553, but only when the peptide was immobilized onto nitrocellulose at a much greater concentration than vWF or the proteolytic fragments.	Iodine-125	13-17	von Willebrand factor	Homo sapiens	46-49	
1583402-7	1992	Loss of vWf antigen in supernatant samples complemented the 125I-labeled vWf bound directly to tumor cells.	Iodine-125	60-64	von Willebrand factor	Homo sapiens	8-11	
1583402-7	1992	Loss of vWf antigen in supernatant samples complemented the 125I-labeled vWf bound directly to tumor cells.	Iodine-125	60-64	von Willebrand factor	Homo sapiens	73-76	
1917949-7	1991	Accordingly, 125I-labeled botrocetin bound to vWF and to the 116-kDa fragment immobilized onto nitrocellulose but not to equivalent amounts of the reduced and alkylated 52/48-kDa fragment; it also bound to the peptide 539-553, but only when the peptide was immobilized onto nitrocellulose at a much greater concentration than vWF or the proteolytic fragments.	Iodine-125	13-17	von Willebrand factor	Homo sapiens	326-329	
3284916-7	1988	Endothelial cells as well as smooth muscle cells bound 125I-labeled vWF in a ristocetin-dependent manner, with a Kd of 7.9 nM.	Iodine-125	55-59	von Willebrand factor	Homo sapiens	68-71	
3498719-6	1987	The ability of the fragments to interfere with the vWF-collagen interaction was evaluated by measuring inhibition of 125I-labeled vWF binding to fibrillar bovine collagen types I and III.	Iodine-125	117-121	von Willebrand factor	Homo sapiens	51-54	
2450575-3	1988	Specific binding of 125I-labeled vWF to the GP Ib-IX complex coated beads was strictly ristocetin dependent with maximal binding occurring at ristocetin concentrations greater than or equal to 1 mg/mL.	Iodine-125	20-24	von Willebrand factor	Homo sapiens	33-36	
2450575-4	1988	Ristocetin-dependent specific binding of 125I-labeled vWF was saturable.	Iodine-125	41-45	von Willebrand factor	Homo sapiens	54-57	
3000477-4	1986	In addition, purified GC inhibited ristocetin-dependent binding of 125I-labeled vWF to platelets.	Iodine-125	67-71	von Willebrand factor	Homo sapiens	80-83	
6087354-7	1984	Human fibrinogen inhibited in a competitive manner the ADP-induced binding of 125I-labeled vWF (9 micrograms/ml) with an IC50 of 25 micrograms/ml.	Iodine-125	78-82	von Willebrand factor	Homo sapiens	91-94	
6087354-3	1984	Binding of 125I-labeled vWF to human platelets separated from plasma proteins and treated with ADP was specific, and time and concentration dependent, reaching equilibrium at 20 min and approaching saturation at 12 micrograms/ml.	Iodine-125	11-15	von Willebrand factor	Homo sapiens	24-27	
6087354-8	1984	Conversely, unlabeled vWF inhibited ADP-induced binding of 125I-labeled fibrinogen (60 micrograms/ml) with an IC50 of 16 micrograms/ml.	Iodine-125	59-63	von Willebrand factor	Homo sapiens	22-25	
6600402-3	1983	The focused vWF is visualized by staining fixed gels with 125I-labeled affinity-purified heterologous antibody.	Iodine-125	58-62	von Willebrand factor	Homo sapiens	12-15	
6403025-3	1983	VIII/vWF multimers are then detected by 125I-labelled antibodies to VIII/vWF, and autoradiography.	Iodine-125	40-44	von Willebrand factor	Homo sapiens	5-8	
6982084-6	1982	Large multimers of 125I-labeled purified FVIII/vWF underwent divalent cation-dependent association with platelets in the presence of thrombin, indicating that the loss of FVIII/vWF from thrombin releasates was due to reassociation with the platelet.	Iodine-125	19-23	von Willebrand factor	Homo sapiens	47-50	
6982084-6	1982	Large multimers of 125I-labeled purified FVIII/vWF underwent divalent cation-dependent association with platelets in the presence of thrombin, indicating that the loss of FVIII/vWF from thrombin releasates was due to reassociation with the platelet.	Iodine-125	19-23	von Willebrand factor	Homo sapiens	177-180	
6260227-1	1981	The binding of 125I-labeled porcine von Willebrand factor to washed human platelets was examined.	Iodine-125	15-19	von Willebrand factor	Homo sapiens	36-57	
14521605-10	2003	We examined the 125I-labeled VWF binding using a series of recombinant GPIbalpha fragments with different residues at position 233 (G233S, G233A, G233K, and G233D) together with naturally occurring mutations previously reported in patients (G233V and M239V).	Iodine-125	16-20	von Willebrand factor	Homo sapiens	29-32