PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15870546-0	2005	von Willebrand factor multimer composition is modified following oral methionine load in women with thrombosis, but not in healthy women.	Methionine	70-80	von Willebrand factor	Homo sapiens	0-21	
15870546-4	2005	Our purpose was to investigate VWF changes in patients with thrombosis following oral methionine load.	Methionine	86-96	von Willebrand factor	Homo sapiens	31-34	
1429668-5	1992	The type IIB vWF mutation corresponds to a duplicated ATG codon, resulting in three contiguous methionines starting at position 540-541 in the normal vWF sequence (rv-WFduplMet540-541).	Methionine	95-106	von Willebrand factor	Homo sapiens	13-16	
12858444-8	2003	RESULTS: After oral methionine loading, vWF levels increased significantly, whereas FMD remained unchanged in both groups.	Methionine	20-30	von Willebrand factor	Homo sapiens	40-43	
11943773-3	2002	GPIb binding sites have been assigned in the VWF A1 domain, which consists of a disulfide loop Cys1272(509)-Cys1458(695) where amino acid residues are numbered from the starting methionine as +1.	Methionine	178-188	von Willebrand factor	Homo sapiens	45-48	
10607704-0	2000	Threonine-145/methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbalpha express HPA-2 epitopes and show equal binding of von Willebrand factor.	Methionine	14-24	von Willebrand factor	Homo sapiens	158-179	
1429668-5	1992	The type IIB vWF mutation corresponds to a duplicated ATG codon, resulting in three contiguous methionines starting at position 540-541 in the normal vWF sequence (rv-WFduplMet540-541).	Methionine	95-106	von Willebrand factor	Homo sapiens	150-153	
1912563-0	1991	Duplication of a methionine within the glycoprotein Ib binding domain of von Willebrand factor detected by denaturing gradient gel electrophoresis in a patient with type IIB von Willebrand disease.	Methionine	17-27	von Willebrand factor	Homo sapiens	73-94	
21917758-0	2011	Shear stress-induced unfolding of VWF accelerates oxidation of key methionine residues in the A1A2A3 region.	Methionine	67-77	von Willebrand factor	Homo sapiens	34-37	
21917758-3	2011	We recently showed that the neutrophil oxidant hypochlorous acid (HOCl) inhibits VWF proteolysis by ADAMTS13 by oxidizing VWF methionine 1606 (M1606) in the A2 domain.	Methionine	126-136	von Willebrand factor	Homo sapiens	81-84	
21917758-3	2011	We recently showed that the neutrophil oxidant hypochlorous acid (HOCl) inhibits VWF proteolysis by ADAMTS13 by oxidizing VWF methionine 1606 (M1606) in the A2 domain.	Methionine	126-136	von Willebrand factor	Homo sapiens	122-125	
1729889-4	1992	The encoded substitution of a methionine for a valine at this residue is nonconservative in nature and has affected a vWf protein region which has been shown to facilitate binding to the platelet receptor glycoprotein Ib.	Methionine	30-40	von Willebrand factor	Homo sapiens	118-121	
33550613-2	2021	In particular, oxidation of methionine residues in specific domains of VWF due to the release of oxidants in inflammatory conditions has been linked to an increased platelet-binding activity.	Methionine	28-38	von Willebrand factor	Homo sapiens	71-74	
33550613-3	2021	However, the atomistic details of how methionine oxidation activates VWF have not been elucidated to date.	Methionine	38-48	von Willebrand factor	Homo sapiens	69-72	
33550613-5	2021	In this manuscript, we used a combination of a dynamic flow assay and molecular dynamics (MD) simulations to investigate how methionine oxidation removes an auto-inhibitory mechanism of VWF.	Methionine	125-135	von Willebrand factor	Homo sapiens	186-189	
30222754-3	2018	This has been linked to the oxidation of methionine residues in the A1, A2 and A3 domains of VWF.	Methionine	41-51	von Willebrand factor	Homo sapiens	93-96	
30222754-8	2018	Here, molecular dynamics simulations tested the hypothesis whether methionine oxidation induced by inflammatory conditions favors unfolding of the A2 domain contributing to the experimentally observed activation of VWF.	Methionine	67-77	von Willebrand factor	Homo sapiens	215-218	
21917758-7	2011	Seven other methionine residues in the VWF A1A2A3 region (containing the sites for platelet and collagen binding and ADAMTS13 cleavage) were variably oxidized, one completely.	Methionine	12-22	von Willebrand factor	Homo sapiens	39-42	
21917758-8	2011	Oxidized methionines accumulated preferentially in the largest VWF multimers.	Methionine	9-20	von Willebrand factor	Homo sapiens	63-66