PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3037722-0	1987	Inhibition of von Willebrand factor binding to platelets by two recognition site peptides: the pentadecapeptide of the carboxy terminus of the fibrinogen gamma chain and the tetrapeptide arg-gly-asp-ser.	Serine	199-202	von Willebrand factor	Homo sapiens	14-35	
3500868-8	1987	Short synthetic peptides containing the sequence Arg-Gly-Asp-Ser effectively inhibited thrombin-dependent platelet adhesion to vWf substrates but had no effect on ristocetin-dependent adhesion.	Serine	61-64	von Willebrand factor	Homo sapiens	127-130	
3131331-3	1988	Evidence is presented showing that proteolytic processing of pro-vWF by COS-1 cells occurs at the peptide bond between arginine and serine in the sequence Lys762-Arg763-Ser764, identical to endothelial cell-associated proteolysis.	Serine	132-138	von Willebrand factor	Homo sapiens	65-68	
2864688-10	1985	The tetrapeptide sequence of Arg-Gly-Asp-Ser, which mediates the cell attachment and platelet binding activity of fibronectin, was also identified in the carboxyl-terminal portion of von Willebrand factor.	Serine	41-44	von Willebrand factor	Homo sapiens	183-204	
23168412-0	2013	Distinct roles of Ser-764 and Lys-773 at the N terminus of von Willebrand factor in complex assembly with coagulation factor VIII.	Serine	18-21	von Willebrand factor	Homo sapiens	59-80	
25564400-7	2015	Substitution of hydrophobic VWF A2 domain residues to serine in a region (residues 1642-1659) previously postulated to interact with the Cys-rich domain revealed the functional importance of VWF residues Ile1642, Trp1644, Ile1649, Leu1650, and Ile1651.	Serine	54-60	von Willebrand factor	Homo sapiens	191-194	
25690668-8	2015	RESULTS: Our findings demonstrate that substitutions of R1205 with histidine, cysteine or serine all result in markedly reduced survival of full-length recombinant VWF.	Serine	90-96	von Willebrand factor	Homo sapiens	164-167	
23757730-7	2013	Serine 11 of AnxA2 was identified as the target residue of this phosphorylation switch because a phosphomimicking mutation at this site prevents complex formation with S100A10 and, in contrast to wild-type or S11A-AnxA2, is unable to restore cAMP-dependent VWF secretion in AnxA2-depleted cells.	Serine	0-6	von Willebrand factor	Homo sapiens	257-260	
23168412-6	2013	In addition, peptide Ser-764-Arg-782, which comprises the first 19 amino acid residues of mature VWF, showed a differential modification of both Lys-773 and the alpha-amino group of Ser-764.	Serine	21-24	von Willebrand factor	Homo sapiens	97-100	
22754302-4	2012	In the present study, the data indicate that the S609A mutation replacing Ser(609) of GPIbalpha with alanine (S609A) significantly prevented the association of 14-3-3zeta with GPIbalpha before and after the VWF binding to GPIbalpha.	Serine	74-77	von Willebrand factor	Homo sapiens	207-210	
12855711-6	2003	Modeling of a cyclic 6-mer peptide containing the consensus sequence and superposition of its three-dimensional structure onto the VWF A3-domain demonstrated that the Ser and Arg in the peptide matched the Ser1020 and Arg1016 in the A3-domain.	Serine	167-170	von Willebrand factor	Homo sapiens	131-134	
15606553-5	2005	Utilizing a neuronal network for prediction of O-linked glycosylation of mammalian proteins, threonine (T) and serine (S) residues located in the VWF-A1-loop flanking regions - not in the loop itself - were determined to be glycosylated n-terminal at amino acids T485, S490, T492 and T493 and c-terminal at T705.	Serine	111-117	von Willebrand factor	Homo sapiens	146-149	
10845886-8	2000	Increased thrombus formation was observed when the Arg-Gly-Gly-Ser-vWF, which does not interact with alphaIIb-beta3, was added to vWD blood and perfused at 2600 s(-1).	Serine	63-66	von Willebrand factor	Homo sapiens	67-70	
11943773-4	2002	The previous numbering from the N-terminal Ser of the mature processed VWF is indicated in parentheses.	Serine	43-46	von Willebrand factor	Homo sapiens	71-74	
11372690-9	2001	To avoid confusion with previously used numbering schemes for mature VWF, which started from serine 764 of pre-pro VWF, the use of the single letter amino acid code is recommended.	Serine	93-99	von Willebrand factor	Homo sapiens	69-72	
12351392-7	2002	Alkylation of Cys974 in the C-terminal TSP-1 construct, which is a serine in TSP-2, ablated VWF reductase activity.	Serine	67-73	von Willebrand factor	Homo sapiens	92-95	
10845886-9	2000	This increase was not observed in vWD blood at lower shear rates or after addition of Arg-Gly-Gly-Ser-vWF to reconstituted normal blood.	Serine	98-101	von Willebrand factor	Homo sapiens	102-105	
7974349-4	1994	The epitope of MAb 710, which inhibits the binding of vWF to glycoprotein Ib (GPIb), was identified between Ser 593 and Ser 678 on the tryptic 52/48 kDa fragment (aa 449-728) which contains binding domains for GPIb, collagen, heparin, sulfatides and subendothelium extracellular matrices.	Serine	108-111	von Willebrand factor	Homo sapiens	54-57	
10477273-5	1999	A second vWF-A domain with improved stability and solubility was created using a Cys(267)-->Ser mutation and a four-residue C-terminal extension of the first vWF-A domain.	Serine	95-98	von Willebrand factor	Homo sapiens	9-12	
7974349-4	1994	The epitope of MAb 710, which inhibits the binding of vWF to glycoprotein Ib (GPIb), was identified between Ser 593 and Ser 678 on the tryptic 52/48 kDa fragment (aa 449-728) which contains binding domains for GPIb, collagen, heparin, sulfatides and subendothelium extracellular matrices.	Serine	120-123	von Willebrand factor	Homo sapiens	54-57	
1871720-8	1991	Both vWf binding and platelet adhesion to sulfatides can be inhibited by the sulfated polysaccharide dextran sulfate at low concentration, fucoidan at high concentrations, but not by heparin, fibrinogen, fibronectin, or the synthetic peptides Gly-Arg-Gly-Asp-Ser-Pro or Gly-Arg-Gly-Glu-Ser-Pro.	Serine	259-262	von Willebrand factor	Homo sapiens	5-8	
1409710-3	1992	A missense mutation, Gly-561-->Ser, was identified within the proposed glycoprotein Ib binding domain of vWF in the proband with von Willebrand disease type B, a unique variant characterized by no ristocetin-induced, but normal botrocetin-induced, binding to glycoprotein Ib.	Serine	34-37	von Willebrand factor	Homo sapiens	108-111