PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2420006-3	1986	An affinity matrix made of an insolubilized heptapeptide containing the Arg-Gly-Asp sequence selectively binds the platelet membrane glycoprotein IIb/IIIa from detergent extracts of platelets.	Arginine	72-75	integrin subunit alpha 2b	Homo sapiens	115-149	
2713490-2	1989	We have examined the role of the two chains of GPIIb in the maintenance of the GPIIb-IIIa heterodimer and Arg-Gly-Asp (RGD) peptide-binding function.	Arginine	106-109	integrin subunit alpha 2b	Homo sapiens	47-52	
3422188-13	1988	These homologies further establish that GPIIb-IIIa from platelets, together with the vitronectin and the fibronectin receptors, are members of a supergene family of adhesion receptors with a recognition specificity for Arg-Gly-Asp amino acid sequences.	Arginine	219-222	integrin subunit alpha 2b	Homo sapiens	40-45	
2753902-1	1989	The platelet glycoprotein IIb-IIIa complex (GP IIb-IIIa) is a member of the integrin receptor family that recognizes adhesive proteins containing the Arg-Gly-Asp (RGD) sequence.	Arginine	150-153	integrin subunit alpha 2b	Homo sapiens	44-50	
2773809-8	1989	Clustering was also induced by the addition of the GPIIb-IIIa binding domains of fibrinogen--namely, the tetrapeptide Arg-Gly-Asp-Ser on the alpha-chain or the gamma-chain decapeptide gamma 402-411.	Arginine	118-121	integrin subunit alpha 2b	Homo sapiens	51-56	
3584243-10	1987	Clustering was also induced by the addition of the GPIIb-IIIa-binding domains of fibrinogen, namely the tetrapeptide Arg-Gly-Asp-Ser on the alpha-chain or the gamma-chain decapeptide gamma 402-411.	Arginine	117-120	integrin subunit alpha 2b	Homo sapiens	51-56	
21529934-1	2011	Platelet adhesion to adsorbed plasma proteins, such as fibrinogen (Fg), has been conventionally thought to be mediated by the GPIIb/IIIa receptor binding to Arg-Gly-Asp (RGD)-like motifs in the adsorbed protein.	Arginine	157-160	integrin subunit alpha 2b	Homo sapiens	126-131	
15134514-4	2004	The search for these compounds is based on the molecular design of structures mimicking some fragment of RGD (Arg-Gly-Asp) sequence, responsible for the binding of fibrinogen to GP IIb/IIIa.	Arginine	110-113	integrin subunit alpha 2b	Homo sapiens	178-184	
18316480-6	2008	We find arginine-methylated RUNX1 on the promoters of two bona fide RUNX1 target genes, CD41 and PU.1 and show that shRNA against PRMT1 or RUNX1 down-regulates their expression.	Arginine	8-16	integrin subunit alpha 2b	Homo sapiens	88-92	
16454727-4	2006	Thrombin, factor Xa, tissue factor/factor VIIa and platelet GPIIb/IIIa receptors display a preference for molecules containing highly basic arginine and/or acidic aspartate moieties, which are, however, associated with poor bioavailability after oral application.	Arginine	140-148	integrin subunit alpha 2b	Homo sapiens	60-65	
16326711-3	2006	GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268).	Arginine	64-67	integrin subunit alpha 2b	Homo sapiens	0-3	
11920243-9	2001	Our results also demonstrate that Arg 1715 is not essential in the function but it is necessary for maintaining the conformation recognized by MoAb 9 specific for the GPIIb/IIIa-binding domain of VWF.	Arginine	34-37	integrin subunit alpha 2b	Homo sapiens	167-172	
9950658-2	1999	Small-molecule antagonists of GP IIb/IIIa based on the Arg-Gly-Asp (RGD) sequence show similar benefit, and some of these agents are orally active.	Arginine	55-58	integrin subunit alpha 2b	Homo sapiens	30-36	
10963786-6	2000	Blocking of GPIIb-IIIa by Arg-Gly-Asp-Ser peptide prevented platelet adhesion to the polystyrene while an extensive adhesion of single platelets to extracellular matrix was observed.	Arginine	26-29	integrin subunit alpha 2b	Homo sapiens	12-17	
9468476-4	1998	Substitutions Thr178 --> Ser, Ile181 --> Phe, and Lys205 --> Arg of Gtalpha did not alter its interaction with hRGSr.	Arginine	70-73	integrin subunit alpha 2b	Homo sapiens	77-84	
9568289-1	1998	A novel hexapeptide, H-Pro-Ser-Nva-Gly-Asp-Trp-OH 6, a specific antagonist of platelet fibrinogen receptor (GpIIb/IIIa), was discovered in a structure-activity relationship (SAR) study where the role of the N-terminal Pro moiety of an RGD-containing peptide, H-Pro-Ser-Arg-Gly-Asp-Trp-OH 1, which is a potent but not specific antagonist toward GpIIb/IIIa integrin, was investigated.	Arginine	269-272	integrin subunit alpha 2b	Homo sapiens	108-113	
8747525-2	1996	8-Guanidino-octanoyl-aspartic acid-phenylalanine (SC-49992), a mimetic of the tetrapeptide arginine-glycine-aspartic acid-phelylalanine, inhibits fibrinogen and vitronectin binding to GP IIb/IIIa.	Arginine	91-99	integrin subunit alpha 2b	Homo sapiens	184-190	
8977249-4	1996	From patient ITP-1 (known to have two distinct autoantibodies), we identified anti-GPIIb/IIIa antibody-specific phage encoding the peptide sequences Arg-Glu-Lys-Ala-Lys-Trp (REKAKW) and Pro-Val-Val-Trp-Lys-Asn (PVVWKN).	Arginine	149-152	integrin subunit alpha 2b	Homo sapiens	83-88	
7524891-0	1994	Bioactive Arg-Gly-Asp conformations in anti-integrin GPIIb-IIIa antibodies.	Arginine	10-13	integrin subunit alpha 2b	Homo sapiens	53-58	
8571304-5	1995	We found in the second family a previously described nonsense mutation: 584 Arg to stop codon in exon 17 of the GPIIb gene.	Arginine	76-79	integrin subunit alpha 2b	Homo sapiens	112-117	
8025347-10	1993	The "ligand-binding pocket" of GP IIb-IIIa contains at least three sequences essential for ligand binding; fibrinogen also binds to the activated complex through identified domains, one of which, the Arg-Gly-Asp (RGD) sequence, is also found in vWF and the other adhesive proteins able to support platelet aggregation.	Arginine	200-203	integrin subunit alpha 2b	Homo sapiens	31-37	
8152339-7	1994	Similarly, when platelet GpIIb/IIIa receptors were blocked in normal platelets by the tripeptide Arg-Gly-Asp (RGD) or the tetrapeptide Arg-Gly-Asp-Ser (RGDS) at 10(-3) M, agonist-induced platelet aggregation and fibrinogen binding were blocked, but platelet PAI-1 release was not blocked.	Arginine	97-100	integrin subunit alpha 2b	Homo sapiens	25-30	
1326944-4	1992	Tetrapeptide RGDS (Arg-Gly-Asp-Ser), which blocks the interaction of ligands such as fibrinogen with platelet integrin alpha IIb beta 3 (GPIIb-IIIa), inhibited only the late-phase PtdIns(3,4)P2 accumulation that was associated with added Ca2+.	Arginine	19-22	integrin subunit alpha 2b	Homo sapiens	137-142	
8417803-0	1993	Arg-Gly-Asp-dependent occupancy of GPIIb/IIIa by applaggin: evidence for internalization and cycling of a platelet integrin.	Arginine	0-3	integrin subunit alpha 2b	Homo sapiens	35-40	
21043846-5	1993	Like some other adhesive proteins such as fibrinogen, fibronectin, and von Willebrand factor, vitronectin contains the amino-acid sequence Arg-Gly-Asp (RGD) which enables binding to the platelet membrane glycoprotein complex IIb/IIIa (GPIIb/IIIa).	Arginine	139-142	integrin subunit alpha 2b	Homo sapiens	235-240	
8485050-4	1993	Two primers for polymerase chain reaction (PCR) were then designed, and a 394 bp PCR product was generated and sequenced, indicating that a stop codon (TGA) was substituted for an Arg codon (CGA) at amino acid position 584 of GPIIb, and resulted in a premature termination of translation and production of a shortened protein.	Arginine	180-183	integrin subunit alpha 2b	Homo sapiens	226-231	
1447740-2	1992	Replacement of the N-terminal arginine by p-amidinophenylalanine or the Gly moiety by m-aminobenzoic acid led to compounds which are superior to the lead peptide with regard to activity and selectivity for GP IIb-IIIa vs the closely related vitronectin receptor alpha v beta 3.	Arginine	30-38	integrin subunit alpha 2b	Homo sapiens	206-212	
1527012-8	1992	Active GPIIb-IIIa was heavily degraded by Arg-C, whereas inactive GPIIb-IIIa was highly resistant to degradation.	Arginine	42-45	integrin subunit alpha 2b	Homo sapiens	7-12	
1323869-3	1992	The GP IIb/IIIa complex is an adhesion receptor belonging to the integrin superfamily; it can bind five adhesive proteins containing the arginine-glycine-aspartic acid (RGD) sequence in their structure: fibrinogen (Fg), von Willebrand factor (vWf), thrombospondin (Tsp), fibronectin (Fn) and vitronectin (Vn).	Arginine	137-145	integrin subunit alpha 2b	Homo sapiens	4-10	
2320569-3	1990	Each of the protein in this family, which range from 47 to 83 residues, contains an Arg-Gly-Asp amino acid sequence found in protein ligands that binds to GPIIb-IIIa, a high (17 +/- 1%) cysteine content conserved in the primary sequence, and a homologous N-terminal region absent only in the echistatin isoforms.	Arginine	84-87	integrin subunit alpha 2b	Homo sapiens	155-160	
1659747-9	1991	In the third experiment the RGDS peptide (ARG-GLY-ASP-SER), a blocker of GPIIb/IIIa platelet receptor dose dependently inhibited platelet aggregation by 93 +/- 17%.	Arginine	42-45	integrin subunit alpha 2b	Homo sapiens	73-78	
1907272-1	1991	The Arg-Gly-Asp (RGD)-binding domain of GPIIb-IIIa has been localized in a fragment of the GPIIIa subunit that includes the sequence between amino acids 109 and 171.	Arginine	4-7	integrin subunit alpha 2b	Homo sapiens	40-45	
2018974-1	1991	Integrin alpha IIb beta 3 (platelet GPIIb-IIIa) binds fibrinogen via recognition sequences such as Arg-Gly-Asp (RGD).	Arginine	99-102	integrin subunit alpha 2b	Homo sapiens	36-41	
1715119-7	1990	In spite of the cross-reactivity for binding to vWF, only the two antibodies whose epitopes included residues in the Arg-Gly-Asp sequence inhibited vWF interaction with GP IIb-IIIa.	Arginine	117-120	integrin subunit alpha 2b	Homo sapiens	169-175	
34440879-4	2021	Additionally, activated GPIIb/IIIa complex (PAC-1) expression was higher on platelets from severe COVID-19 patients compared to healthy controls and inversely correlated with L-arginine plasmatic concentration.	Arginine	175-185	integrin subunit alpha 2b	Homo sapiens	24-29