PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2708912-8 1989 It is shown in addition that the tripeptide Arg-Gly-Asp, identical to the region of iC3b recognized by CR3 and by several adhesion-promoting receptors that are structurally similar to CR3, such as fibronectin or vitronectin, is a significant inhibitor of the binding to and the phagocytosis of S-RBC by monocytic-macrophagic cells. Glycine 48-51 vitronectin Homo sapiens 212-223 3693352-1 1987 Peptides containing the tripeptide sequence Arg-Gly-Asp can duplicate or inhibit the cell attachment-promoting effects of fibronectin and vitronectin. Glycine 48-51 vitronectin Homo sapiens 138-149 3238653-5 1988 These studies suggest that the glycoprotein IIb-IIIa complex on activated platelets may interact with vitronectin substrate through the Arg-Gly-Asp mechanism. Glycine 140-143 vitronectin Homo sapiens 102-113 2449435-2 1988 Liposomes containing platelet glycoproteins IIb-IIIa complex have been shown to bind vitronectin-coated surfaces through an Arg-Gly-Asp cell attachment mechanism. Glycine 128-131 vitronectin Homo sapiens 85-96 2449435-7 1988 A synthetic hexapeptide containing the Arg-Gly-Asp sequence inhibited vitronectin binding to platelets. Glycine 43-46 vitronectin Homo sapiens 70-81 2470110-1 1989 The disialogangliosides GD2 and GD3 play a major role in the ability of human melanoma cells to attach to Arg-Gly-Asp-containing substrates such as fibronectin and vitronectin, since pretreatment of these cells with monoclonal antibodies to the oligosaccharide of GD2 and GD3 can inhibit their attachment and spreading on such adhesive proteins. Glycine 110-113 vitronectin Homo sapiens 164-175 2470110-2 1989 This report demonstrates that human melanoma cells (M21) synthesize and express a glycoprotein receptor that shares antigenic epitopes with the vitronectin receptor on human fibroblasts and is capable of specifically recognizing the Gly-Arg-Gly-Asp-Ser-Pro sequence. Glycine 233-236 vitronectin Homo sapiens 144-155 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. Glycine 223-226 vitronectin Homo sapiens 85-96 2466737-6 1988 The vitronectin receptor is involved in the adhesion of endothelial cells to Arg-Gly-Asp-containing immobilized proteins such as vitronectin, fibrinogen, and von Willebrand factor. Glycine 81-84 vitronectin Homo sapiens 4-15 2466737-6 1988 The vitronectin receptor is involved in the adhesion of endothelial cells to Arg-Gly-Asp-containing immobilized proteins such as vitronectin, fibrinogen, and von Willebrand factor. Glycine 81-84 vitronectin Homo sapiens 129-140 2443507-1 1987 The disialogangliosides GD2 and GD3 play a major role in the ability of human melanoma cells to attach to Arg-Gly-Asp-containing substrates such as fibronectin and vitronectin, since pretreatment of these cells with monoclonal antibodies to the oligosaccharide of GD2 and GD3 can inhibit their attachment and spreading on such adhesive proteins. Glycine 110-113 vitronectin Homo sapiens 164-175 2443507-2 1987 This report demonstrates that human melanoma cells (M21) synthesize and express a glycoprotein receptor that shares antigenic epitopes with the vitronectin receptor on human fibroblasts and is capable of specifically recognizing the Gly-Arg-Gly-Asp-Ser-Pro sequence. Glycine 233-236 vitronectin Homo sapiens 144-155 2440809-11 1987 The binding to group G streptococci, S. aureus, and E. coli is mediated in part through a domain in the S protein containing the sequence Arg-Gly-Asp, whereas a different site is responsible for the binding to group A and C streptococci. Glycine 142-145 vitronectin Homo sapiens 104-113 2414098-9 1985 The Arg-Gly-Asp sequence appears to constitute the cell attachment site of vitronectin, since it is in the region where we have previously localized the cell attachment site, its presence correlate with cell attachment activity among the insert-coded polypeptides, and because previous results have shown that synthetic peptides containing the Arg-Gly-Asp sequence inhibit the cell attachment function of vitronectin. Glycine 348-351 vitronectin Homo sapiens 75-86 2420006-5 1986 This platelet receptor is related to the previously identified fibronectin and vitronectin receptors in that it recognizes an Arg-Gly-Asp sequence but differs from the other receptors in its wider specificity toward various adhesive proteins. Glycine 130-133 vitronectin Homo sapiens 79-90 3469204-2 1987 The peptide was designed to be triple helical and to contain the sequence Arg-Gly-Asp, which has been implicated as the cell attachment site of fibronectin, vitronectin, fibrinogen, and von Willebrand factor, and is also present in type I collagen. Glycine 78-81 vitronectin Homo sapiens 157-168 2430295-1 1986 Cells adhere to vitronectin substrates through a cell surface receptor that recognizes an Arg-Gly-Asp sequence in vitronectin. Glycine 94-97 vitronectin Homo sapiens 16-27 2430295-1 1986 Cells adhere to vitronectin substrates through a cell surface receptor that recognizes an Arg-Gly-Asp sequence in vitronectin. Glycine 94-97 vitronectin Homo sapiens 114-125 2414098-7 1985 An Arg-Gly-Asp sequence, which has previously been shown to be the cell attachment site in fibronectin, was found in vitronectin immediately after the NH2-terminal somatomedin B sequence. Glycine 7-10 vitronectin Homo sapiens 117-128 2414098-9 1985 The Arg-Gly-Asp sequence appears to constitute the cell attachment site of vitronectin, since it is in the region where we have previously localized the cell attachment site, its presence correlate with cell attachment activity among the insert-coded polypeptides, and because previous results have shown that synthetic peptides containing the Arg-Gly-Asp sequence inhibit the cell attachment function of vitronectin. Glycine 8-11 vitronectin Homo sapiens 75-86 2414098-9 1985 The Arg-Gly-Asp sequence appears to constitute the cell attachment site of vitronectin, since it is in the region where we have previously localized the cell attachment site, its presence correlate with cell attachment activity among the insert-coded polypeptides, and because previous results have shown that synthetic peptides containing the Arg-Gly-Asp sequence inhibit the cell attachment function of vitronectin. Glycine 8-11 vitronectin Homo sapiens 405-416 2412224-0 1985 A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Glycine 89-96 vitronectin Homo sapiens 49-60 30152697-3 2018 The peptide sequence Arg-Gly-Asp (RGD), which is present in a number of endogenous integrin ligands like fibronectin, vitronectin, and related proteins of the extracellular matrix (ECM), has been extensively used as a targeting vector for therapeutic as well as diagnostic purposes, and cilengitide, a cyclic RGD peptide, has entered clinical trials for the treatment of various cancers. Glycine 25-28 vitronectin Homo sapiens 118-129 23285494-13 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 24154564-3 2013 Indeed, it is well established that alphavbeta3 integrin plays a key role in tumor angiogenesis acting like a receptor for the extracellular matrix proteins like vitronectin, fibronectin through the arginine-glycine-aspartic acid (RGD) sequence. Glycine 208-215 vitronectin Homo sapiens 162-173 26956095-5 2016 These integrins are known to specifically interact with vitronectin and collagen-IV, respectively, through binding to an Arg-Gly-Asp (RGD) sequence. Glycine 125-128 vitronectin Homo sapiens 56-67 23720861-16 2004 Extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) contain a tripeptide sequence consisting of Arg-Gly-Asp (RGD), which binds to a variety of integrins, including alphavbeta3. Glycine 127-130 vitronectin Homo sapiens 31-42 22649803-19 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 23115806-4 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 22649804-19 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 20641959-20 2004 A tripeptide sequence consisting of Arg-Gly-Asp (RGD) is identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins including alphavbeta3. Glycine 40-43 vitronectin Homo sapiens 130-141 20641584-4 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3 and alphavbeta5. Glycine 25-28 vitronectin Homo sapiens 121-132 20641300-6 2004 A tripeptide sequence consisting of Arg-Gly-Asp (RGD) was identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins including alphavbeta3. Glycine 40-43 vitronectin Homo sapiens 131-142 20642000-4 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 20641531-7 2004 A tripeptide sequence consisting of Arg-Gly-Asp (RGD) is identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins including alphavbeta3. Glycine 40-43 vitronectin Homo sapiens 130-141 21249762-5 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 21204315-13 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (e.g., vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 127-138 21061495-2 2004 Ligands such as vitronectin, fibronectin, etc., which interact with integrins, are known to bind these receptors through an Arg-Gly-Asp (RGD) epitope. Glycine 128-131 vitronectin Homo sapiens 16-27 19882657-0 2010 Site-specific inhibition of integrin alpha v beta 3-vitronectin association by a ser-asp-val sequence through an Arg-Gly-Asp-binding site of the integrin. Glycine 117-120 vitronectin Homo sapiens 52-63 20641649-0 2004 Gly-Ser-Ser-Lys-(FITC)-Gly-Gly-Gly-Cys-Arg-Gly-Asp-Cys-CLIO-Cy5.5 The alphaupsilonbeta3 integrin, also known as the vitronectin receptor, is a heterodimeric transmembrane glycoprotein found on most cells originating from mesenchyme (1). Glycine 0-3 vitronectin Homo sapiens 116-127 20641262-5 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 20641458-5 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 20641917-5 2004 The peptide sequence Arg-Gly-Asp (RGD) has been identified as a recognition motif used by extracellular matrix proteins (vitronectin, fibrinogen, laminin, and collagen) to bind to a variety of integrins, including alphavbeta3. Glycine 25-28 vitronectin Homo sapiens 121-132 20641649-0 2004 Gly-Ser-Ser-Lys-(FITC)-Gly-Gly-Gly-Cys-Arg-Gly-Asp-Cys-CLIO-Cy5.5 The alphaupsilonbeta3 integrin, also known as the vitronectin receptor, is a heterodimeric transmembrane glycoprotein found on most cells originating from mesenchyme (1). Glycine 23-26 vitronectin Homo sapiens 116-127 20641649-0 2004 Gly-Ser-Ser-Lys-(FITC)-Gly-Gly-Gly-Cys-Arg-Gly-Asp-Cys-CLIO-Cy5.5 The alphaupsilonbeta3 integrin, also known as the vitronectin receptor, is a heterodimeric transmembrane glycoprotein found on most cells originating from mesenchyme (1). Glycine 23-26 vitronectin Homo sapiens 116-127 15722127-1 2005 A non-peptide mimic of the Arg-Gly Asp (RGD) active sequence of adhesive proteins (such as vitronectin) has been equipped with two different spacer-arms for surface anchorage. Glycine 31-34 vitronectin Homo sapiens 91-102 17886558-9 2007 Antibodies against integrin alphav or alphavbeta5 or arginine-glycine-aspartic acid-containing peptides, both of which block the vitronectin-glioma cell interactions, significantly reduced serum-induced cell migration, whereas blocking the interaction of glioma cells with fibronectin had no effect. Glycine 62-69 vitronectin Homo sapiens 129-140 12082110-2 2002 VN also interacts with two-chain high molecular weight kininogen (HKa), particularly its His-Gly-Lys-rich domain 5, and both HKa and PAI-1 are antiadhesive factors that have been shown to compete for binding to VN. Glycine 93-96 vitronectin Homo sapiens 0-2 12082110-6 2002 Although having no direct effect on PAI-1 activity itself, HKa domain 5 or the peptide Gly(486)-Lys(502) markedly destabilized the VN.PAI-1 complex interaction, resulting in a significant reduction of PAI-1 inhibitory function on plasminogen activators, resembling the effect of VN antibodies that prevent stabilization of PAI-1. Glycine 87-90 vitronectin Homo sapiens 131-133 9120775-9 1997 These studies suggest that the glycoprotein IIb/IIIa complex, present on activated-platelets, may interact with fibronectin and vitronectin substrates through the Arg-Gly-Asp-dependent mechanism. Glycine 167-170 vitronectin Homo sapiens 128-139 9765407-2 1998 We report here the expression of soluble integrin alphav beta5, which retains the ability to recognize the Ad penton base as well as vitronectin, an Arg Gly Asp (RGD)-containing extracellular matrix protein. Glycine 153-156 vitronectin Homo sapiens 133-144 11970955-2 2002 HKa and particularly its His-Gly-Lys-rich domain 5 have been previously reported to exert anti-adhesive properties by binding to the extracellular matrix protein vitronectin (VN). Glycine 29-32 vitronectin Homo sapiens 162-173 11970955-2 2002 HKa and particularly its His-Gly-Lys-rich domain 5 have been previously reported to exert anti-adhesive properties by binding to the extracellular matrix protein vitronectin (VN). Glycine 29-32 vitronectin Homo sapiens 175-177 12009947-1 2002 Three amino acids residues, Arg-Gly-Asp (RGD), in vitronectin and fibronectin show affinity for alpha(V)beta(3) integrins expressed in vascular endothelial cells. Glycine 32-35 vitronectin Homo sapiens 50-61 8648190-7 1996 Adhesion to fibronectin and vitronectin was found to be divalent cation- and arginine-glycine-aspartic acid-dependent, and could be blocked by antibodies to beta 1 or alpha 5, and alpha v or alpha v beta 5, respectively. Glycine 86-93 vitronectin Homo sapiens 28-39 8550313-13 1996 Cell adhesion to fibronectin and vitronectin was inhibited by peptides containing the Arg-Gly-Asp sequence. Glycine 90-93 vitronectin Homo sapiens 33-44 7680229-3 1993 The amino acid sequence of the fragment corresponded to residues Gly-115-Glu-121 of VN. Glycine 65-68 vitronectin Homo sapiens 84-86 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. Glycine 100-107 vitronectin Homo sapiens 161-172 7683462-0 1993 The cell attachment and spreading activity of vitronectin is dependent on the Arg-Gly-Asp sequence. Glycine 82-85 vitronectin Homo sapiens 46-57 7683462-2 1993 The cell attachment activity of vitronectin has been ascribed to an Arg-Gly-Asp (RGD) sequence near the amino terminus. Glycine 72-75 vitronectin Homo sapiens 32-43 8036014-2 1994 It contains a functional gly-arg-gly-asp-ser (GRGDS) integrin binding domain (Oldberg et al., 1986), promotes the adhesion of a variety of cell types (Somerman et al., 1989; Brown et al., 1992) and is a ligand for the vitronectin binding integrin alpha v beta 3 (Miyauchi et al., 1991). Glycine 25-28 vitronectin Homo sapiens 218-229 8036014-2 1994 It contains a functional gly-arg-gly-asp-ser (GRGDS) integrin binding domain (Oldberg et al., 1986), promotes the adhesion of a variety of cell types (Somerman et al., 1989; Brown et al., 1992) and is a ligand for the vitronectin binding integrin alpha v beta 3 (Miyauchi et al., 1991). Glycine 33-36 vitronectin Homo sapiens 218-229 7513610-6 1994 In cell adhesion assays, the 69-6-5 mAb was able to inhibit strongly in a dose-dependent manner arginine-glycine-aspartic acid-mediated adhesion of HT29-D4 cells to vitronectin, fibronectin, or ProNectin F but not to laminin or collagen. Glycine 105-112 vitronectin Homo sapiens 165-176 7683657-0 1993 Site-directed mutagenesis of the arginine-glycine-aspartic acid in vitronectin abolishes cell adhesion. Glycine 42-49 vitronectin Homo sapiens 67-78 7683657-3 1993 Many cell adhesion ligands, including vitronectin, contain an Arg-Gly-Asp (RGD) sequence mediating, in part, the ligand-receptor interaction. Glycine 66-69 vitronectin Homo sapiens 38-49 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). Glycine 146-153 vitronectin Homo sapiens 292-303 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). Glycine 146-153 vitronectin Homo sapiens 305-307 1698787-6 1990 In contrast to PAI-1, ECM-associated VN was resistant toward glycine (pH 2.3), guanidine or urokinase treatment, suggesting that VN was tightly associated with the ECM network. Glycine 61-68 vitronectin Homo sapiens 37-39 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). Glycine 143-146 vitronectin Homo sapiens 94-105 1718779-2 1991 Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. Glycine 11-14 vitronectin Homo sapiens 141-152 1718779-2 1991 Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. Glycine 217-220 vitronectin Homo sapiens 141-152 1708943-0 1991 Novel effect of cyclicization of the Arg-Gly-Asp-containing peptide on vitronectin binding to platelets. Glycine 41-44 vitronectin Homo sapiens 71-82 1693626-1 1990 Association of a novel beta 1-related subunit with alpha v. We report the isolation from two human neuroblastoma cell lines of an Arg-Gly-Asp-dependent integrin complex capable of binding to vitronectin, fibronectin, and type I collagen. Glycine 134-137 vitronectin Homo sapiens 191-202 1692034-3 1990 Recent cDNA cloning reveals that like other adhesive proteins, Vn contains the sequence Arg-Gly-Asp and binds to some members of the integrin class of adhesive membrane receptors. Glycine 92-95 vitronectin Homo sapiens 63-65 34342855-3 2022 Integrins recognize oligopeptides present on ECM proteins and are involved in three main types of interaction, namely with collagen, laminin, and the oligopeptide RGD (Arg-Gly-Asp) present on vitronectin and fibronectin proteins. Glycine 172-175 vitronectin Homo sapiens 192-203