PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33582126-10 2021 Moreover, IgG of ulcerative colitis patients blocked integrin alphavbeta6-fibronectin binding through an RGD (Arg-Gly-Asp) tripeptide motif and inhibited cell adhesion. arginyl-glycyl-aspartic acid 105-108 fibronectin 1 Homo sapiens 74-85 33582126-10 2021 Moreover, IgG of ulcerative colitis patients blocked integrin alphavbeta6-fibronectin binding through an RGD (Arg-Gly-Asp) tripeptide motif and inhibited cell adhesion. arginyl-glycyl-aspartic acid 110-121 fibronectin 1 Homo sapiens 74-85 32950474-8 2020 Further study revealed that, in cells pretreated with anti-fibronectin antibody, anti-integrin beta1 antibody or RGD (Arg-Gly-Asp), the expression levels of CCL2 induced by Tp0136 were notably decreased. arginyl-glycyl-aspartic acid 118-129 fibronectin 1 Homo sapiens 59-70 33931940-5 2021 The characterization of Fn-modified surfaces showed that Fn grating via phosphonate has led to the highest amount of Fn cell-binding site (RGD, arginine, glycine, and aspartate) available on the surface. arginyl-glycyl-aspartic acid 139-142 fibronectin 1 Homo sapiens 24-26 33931940-5 2021 The characterization of Fn-modified surfaces showed that Fn grating via phosphonate has led to the highest amount of Fn cell-binding site (RGD, arginine, glycine, and aspartate) available on the surface. arginyl-glycyl-aspartic acid 139-142 fibronectin 1 Homo sapiens 57-59 33931940-5 2021 The characterization of Fn-modified surfaces showed that Fn grating via phosphonate has led to the highest amount of Fn cell-binding site (RGD, arginine, glycine, and aspartate) available on the surface. arginyl-glycyl-aspartic acid 139-142 fibronectin 1 Homo sapiens 57-59 33395296-12 2021 One of the important results in the context of cell-material interaction is that the RGD (Arg-Gly-Asp) sequence of FN was exposed to the solvent side when the field was applied along an outward direction perpendicular to the HA (001) surface. arginyl-glycyl-aspartic acid 90-101 fibronectin 1 Homo sapiens 115-117 25475857-1 2014 Integrin alpha5beta1 binds to an Arg-Gly-Asp (RGD) motif in its ligand fibronectin. arginyl-glycyl-aspartic acid 33-44 fibronectin 1 Homo sapiens 71-82 31908483-2 2019 The binding of alpha5beta1 integrin with the tripeptide Arg-Gly-Asp (RGD) motif within the extracellular matrix protein fibronectin may be influenced by the alpha-1,6-fucose core or alpha-1,2-fucose and alpha-1,3/4-fucose peripheral N-glycan profiles. arginyl-glycyl-aspartic acid 56-67 fibronectin 1 Homo sapiens 120-131 30303437-8 2018 Added NaCl concentrations were correlated with a root mean square fluctuation increase of the fibronectin arginylglycylaspartic acid (RGD) binding domain. arginyl-glycyl-aspartic acid 106-132 fibronectin 1 Homo sapiens 94-105 22919661-5 2012 Like the human extracellular matrix protein fibronectin, CagL contains an RGD (Arg-Gly-Asp) motif and is able to trigger intracellular signaling pathways by RGD-dependent binding to integrins. arginyl-glycyl-aspartic acid 79-90 fibronectin 1 Homo sapiens 44-55 9733775-5 1998 Upon saturation with divalent cations, alpha5-(229-448) binds an Arg-Gly-Asp (RGD)-containing fibronectin ligand to form a 1:1 complex. arginyl-glycyl-aspartic acid 65-76 fibronectin 1 Homo sapiens 94-105 19857872-1 2010 The Pro-His-Ser-Arg-Asn (PHSRN) sequence in fibronectin is a second cell-binding site that synergistically affects Arg-Gly-Asp (RGD). arginyl-glycyl-aspartic acid 115-126 fibronectin 1 Homo sapiens 44-55 16441427-5 2006 FN-induced ERK, p38 and Akt activation was partly blocked by the Arg-Gly-Asp (RGD)-pseudo-peptide FC-336, anti-alphav integrin antibody RMV-7, the broad-spectrum matrix metalloprotease inhibitor GM6001 and the broad spectrum a disintegrin and metalloprotease (ADAM) inhibitor TAPI-1. arginyl-glycyl-aspartic acid 65-76 fibronectin 1 Homo sapiens 0-2 12941795-4 2003 Consistent with versican being the active inhibitory factor in the CM, the integrity of chondroitin sulfate side chains and an ability to bind the RGD (Arg-Gly-Asp) peptide sequence of fibronectin were essential for the inhibition of prostate cancer cell attachment to fibronectin. arginyl-glycyl-aspartic acid 152-163 fibronectin 1 Homo sapiens 185-196 10958798-4 2000 A synthetic peptide containing the Arg-Gly-Asp (RGD) motif of fibronectin and vitronectin was used to stimulate adult feline cardiomyocytes cultured on laminin or within a type-I collagen matrix. arginyl-glycyl-aspartic acid 35-46 fibronectin 1 Homo sapiens 62-73 9748233-7 1998 *CRRETAWAC* also acted as a direct competitive inhibitor of the binding of Arg-Gly-Asp (RGD)-containing fibronectin fragments to alpha5 beta1, suggesting that the binding site for RRETAWA is also closely overlapping with that for RGD. arginyl-glycyl-aspartic acid 75-86 fibronectin 1 Homo sapiens 104-115 10839988-6 2000 Synthetic peptides containing the cell attachment sequence [Arg-Gly-Asp ("RGD")] in fibronectin, GRGDSPK, GGRGDSPK and GGGRGDSPK, were also studied; whereas GRGDSPK was a poor methyl acceptor, the longer peptides were better methyl acceptors. arginyl-glycyl-aspartic acid 60-71 fibronectin 1 Homo sapiens 84-95 9247256-6 1997 Furthermore, the cell adhesion to fibronectin was almost completely inhibited by arginine-glycine-aspartic acid (RGD)-containing peptides, but the fibronectin-stimulated cell migration was only partially inhibited. arginyl-glycyl-aspartic acid 81-111 fibronectin 1 Homo sapiens 34-45 7751028-7 1995 FN-mediated TNF-alpha production by macrophages was inhibited by both soluble arginine-glycine-aspartic acid (RGD) peptide (71%; P < 0.0001) and anti-beta 3-integrin monoclonal antibody 7G2 (54%; P < 0.0001). arginyl-glycyl-aspartic acid 78-108 fibronectin 1 Homo sapiens 0-2 9028319-3 1997 The enhanced adhesion to fibrinogen or fibronectin was mediated by the Arg-Gly-Asp (RGD) recognition sequence of alpha IIb beta 3, as it was abolished by pretreatment of cells with saturating concentrations of RGDS peptide. arginyl-glycyl-aspartic acid 71-82 fibronectin 1 Homo sapiens 39-50 8990928-4 1996 It was striking that very short amino acid sequence Arg-Gly-Asp (RGD) in the central cell binding domain of fibronectin was determined as minimum cell adhesive sequence. arginyl-glycyl-aspartic acid 52-63 fibronectin 1 Homo sapiens 108-119 8820826-2 1996 The interaction of integrins with extracellular matrices such as fibronectin and vitronectin has been shown to be mediated through an arginine-glycine-aspartic acid (RGD) sequence within adhesive proteins. arginyl-glycyl-aspartic acid 134-164 fibronectin 1 Homo sapiens 65-76 9379137-2 1997 The extracellular domains of many integrins recognize the RGD (Arg-Gly-Asp) tripeptide found in several extracellular macromolecules such as fibronectin, vitronectin, fibrinogen and osteopontin. arginyl-glycyl-aspartic acid 63-74 fibronectin 1 Homo sapiens 141-152 7630002-3 1995 Tripeptide Arg-Gly-Asp (RGD) inhibited adhesion on PANC-1 cells to fibronectin but less effective in blocking adhesion to laminin and collagen, although anti beta 1-integrin antibody significantly inhibited adhesion of fibronectin but less inhibited to laminin, collagen. arginyl-glycyl-aspartic acid 11-22 fibronectin 1 Homo sapiens 67-78 7836460-2 1995 Cell surface receptors called integrins mediate diverse cell adhesion phenomena through recognition of the sequence arginine-glycine-aspartic acid (RGD) present in proteins such as fibronectin and fibrinogen. arginyl-glycyl-aspartic acid 116-146 fibronectin 1 Homo sapiens 181-192 7784256-1 1995 Fibronectin binds to platelet membrane glycoprotein (GP) IIb/IIIa in both an Arg-Gly-Asp (RGD)-dependent and -independent manner. arginyl-glycyl-aspartic acid 77-88 fibronectin 1 Homo sapiens 0-11 8163346-0 1994 Nonpeptidic analogues of the Arg-Gly-Asp (RGD) sequence specifically inhibit the adhesion of human tenon"s capsule fibroblasts to fibronectin. arginyl-glycyl-aspartic acid 29-40 fibronectin 1 Homo sapiens 130-141 7980521-3 1994 The effect on DAMI cell morphology may be attributed to the RGD motif (Arg-Gly-Asp) of fibronectin. arginyl-glycyl-aspartic acid 71-82 fibronectin 1 Homo sapiens 87-98 1926332-1 1991 The tripeptide Arg-Gly-Asp (RGD) was originally identified as the sequence within fibronectin that mediates cell attachment. arginyl-glycyl-aspartic acid 15-26 fibronectin 1 Homo sapiens 82-93 8096183-0 1993 Streptavidin blocks immune reactions mediated by fibronectin-VLA-5 recognition through an Arg-Gly-Asp mimicking site. arginyl-glycyl-aspartic acid 90-101 fibronectin 1 Homo sapiens 49-60 7700842-2 1994 The interaction of tumor cells with extracellular matrices such as fibronectin, vitronectin, and collagen has been shown to be mediated through a family of cell surface receptors that specifically recognize an arginine-glycine-aspartic acid (RGD) sequence within each adhesive protein. arginyl-glycyl-aspartic acid 210-240 fibronectin 1 Homo sapiens 67-78 7509429-5 1993 The active amino acid sequence in fibronectin is an arginine-glycine-aspartic acid tripeptide (Arg-Gly-Asp) and it was shown that the synthetic Arg-Gly-Asp peptide specifically inhibited the adhesive function of fibronectin in trabecular meshwork samples when incubated for 30 min at a concentration of 1-2 mg/ml. arginyl-glycyl-aspartic acid 95-106 fibronectin 1 Homo sapiens 34-45 7509429-5 1993 The active amino acid sequence in fibronectin is an arginine-glycine-aspartic acid tripeptide (Arg-Gly-Asp) and it was shown that the synthetic Arg-Gly-Asp peptide specifically inhibited the adhesive function of fibronectin in trabecular meshwork samples when incubated for 30 min at a concentration of 1-2 mg/ml. arginyl-glycyl-aspartic acid 95-106 fibronectin 1 Homo sapiens 212-223 1376652-6 1992 A significant higher proportion of SF T cells were able to bind to an 80-kD fragment of FN, containing the Arg-Gly-Asp (RGD) cell binding site, compared with PB T cells. arginyl-glycyl-aspartic acid 107-118 fibronectin 1 Homo sapiens 88-90 1720779-1 1991 The binding of fibronectin (Fn) to several integrins involves the Arg-Gly-Asp (RGD) tripeptide sequence. arginyl-glycyl-aspartic acid 66-77 fibronectin 1 Homo sapiens 15-26 1720779-1 1991 The binding of fibronectin (Fn) to several integrins involves the Arg-Gly-Asp (RGD) tripeptide sequence. arginyl-glycyl-aspartic acid 66-77 fibronectin 1 Homo sapiens 28-30 1761368-1 1991 We examined the binding capacity of anti-metastatic polypeptide containing repetitive Arg-Gly-Asp(RGD) sequence derived from cell binding site of fibronectin, poly(RGD), to the surface of tumor cells. arginyl-glycyl-aspartic acid 86-97 fibronectin 1 Homo sapiens 146-157 35476306-1 2022 Cell adhesion occurs when integrin recognizes and binds to Arg-Gly-Asp (RGD) ligands present in fibronectin. arginyl-glycyl-aspartic acid 59-70 fibronectin 1 Homo sapiens 96-107 34948276-2 2021 In blastocysts, fibronectin plays a major role in the adhesion of various types of cells by binding to extracellular matrix proteins via the Arg-Gly-Asp (RGD) motif. arginyl-glycyl-aspartic acid 141-152 fibronectin 1 Homo sapiens 16-27 34948276-2 2021 In blastocysts, fibronectin plays a major role in the adhesion of various types of cells by binding to extracellular matrix proteins via the Arg-Gly-Asp (RGD) motif. arginyl-glycyl-aspartic acid 154-157 fibronectin 1 Homo sapiens 16-27 35476306-1 2022 Cell adhesion occurs when integrin recognizes and binds to Arg-Gly-Asp (RGD) ligands present in fibronectin. arginyl-glycyl-aspartic acid 72-75 fibronectin 1 Homo sapiens 96-107 3340213-9 1988 The adhesion ligands of the integrin family are glycoproteins bearing the Arg-Gly-Asp (RGD) sequence motif, for example, fibronectin, fibrinogen, vitronectin and von Willebrand factor. arginyl-glycyl-aspartic acid 74-85 fibronectin 1 Homo sapiens 121-132 2450101-1 1988 The interaction of cells with extracellular matrix components such as fibronectin, vitronectin, and type I collagen has been shown to be mediated through a family of cell-surface receptors that specifically recognize an arginine-glycine-aspartic acid (RGD) amino acid sequence within each protein. arginyl-glycyl-aspartic acid 220-250 fibronectin 1 Homo sapiens 70-81 2469686-4 1989 Adhesion to Fn, but not to laminin or collagens, was specifically blocked in the presence of Arg-Gly-Asp (RGD)-containing peptides. arginyl-glycyl-aspartic acid 93-104 fibronectin 1 Homo sapiens 12-14