ライフサイエンスコーパス: Arg-Gly-Asp

1 egrin interacts with fibronectin is the RGD (Arg-Gly-Asp) amino acid sequence.

2 The ability of an integrin-binding Arg-Gly-Asp-Asn (RGDN)- containing peptide to influence

3 thetic integrin-binding peptide, GRGDNP (gly-arg-gly-asp-asn-pro).

4 Arg-Gly-Asp-based molecular imaging has been shown to de

5 ) with a higher affinity compared with other Arg-Gly-Asp binding integrins.

6 gars on cell surface glycoconjugates and the ARG-GLY-ASP binding sequence, which recognizes a family

7 e in the prototypical integrin-binding motif Arg-Gly-Asp binds the integrin betaA domain of the beta-

8 TB domain (TB5), which is downstream of the arg-gly-asp cell adhesion domain, which can cause Weill-

9 ly local stresses on the cell surface via an Arg-Gly-Asp-coated magnetic bead.

10 is, morphogenesis, and wound repair, and its Arg-Gly-Asp-containing central cell-binding domain (CCBD

11 to be cation dependent and to be effected by Arg-Gly-Asp-containing peptides consistent with an integ

12 tibodies to alpha(5) or beta(1) integrin and Arg-Gly-Asp-containing peptides did not inhibit FN-f-ind

13 ccomplished with a combination of the cyclic Arg-Gly-Asp (cRGD) peptide and anti-alpha(5) integrin an

14 e ligands are based on cyclo Ac-[Cys-Asn-Dmt-Arg-Gly-Asp-Cys]-OH, which displays an affinity of 50 nM

15 Intravenous administration of cyclic Arg-Gly-Asp-d-Phe-Cys (RGDfC) peptide conjugated Au-trip

16 cence microscopy probe consisted of a cyclic Arg-Gly-Asp-D-Phe-Lys(Cys) (cRGDfK(C)) peptide tethered

17 Cells were exposed to TGFbeta (1 ng/ml), Gly-Arg-Gly-Asp-D-Ser-Pro (GRGDdSP, 50 microM), Gly-Arg-AL-A

18 scribes the synthesis of two new cyclic RGD (Arg-Gly-Asp) dimers, 3 (E[G(3)-c(RGDfK)](2)) and 4 (G(3)

19 ion tomography (PET) and [(64)Cu]DOTA-cyclo-(Arg-Gly-Asp-dPhe-Lys) {[(64)Cu]DOTA-c(RGDfK)} can be use

20 P with a nine amino acid loop containing the Arg-Gly-Asp integrin recognition motif and randomized fl

21 f these antibodies were shown to contain the Arg-Gly-Asp integrin recognition motif of the natural li

22 e alpha v beta6 integrin, in addition to the Arg-Gly-Asp interaction.

23 ance actin polymerization was dependent upon Arg-Gly-Asp-ligand-induced beta3 tyrosine phosphorylatio

24 Using mobile RGD (Arg-Gly-Asp) ligands on supported lipid membranes (RGD m

25 pha(4) ligands, and orients differently from Arg-Gly-Asp mimics.

26 es-one containing an alphav integrin-binding Arg-Gly-Asp motif and the other an Asn-Gly-Arg motif-enh

27 tide), have a common structure comprising an Arg-Gly-Asp motif at the tip of a hairpin turn followed

28 side chains terminated in a doubly cyclized Arg-Gly-Asp motif KACDCRGDCFCG (RGD4C: active peptide ta

29 ll beta1-integrin inhibitor peptide with the Arg-Gly-Asp motif, but it was independent of beta1-integ

30 which normally coordinates Arg of the ligand Arg-Gly-Asp motif, formed contacts with Arg-54 of the Fa

31 module seen in EM, VWC4, which bears the VWF Arg-Gly-Asp motif.

32 with the addition of a three-amino-acid RGD (Arg-Gly-Asp) motif (R-2xAbeta1-15; T1-R-Abeta1-15).

33 Glycoprotein B has an RGD (Arg-Gly-Asp) motif at the extracellular amino terminus r

34 of GPIIb-IIIa, variabilin contains the RGD (Arg-Gly-Asp) motif.

35 ers in shape from integrin pockets that bind Arg-Gly-Asp motifs.

36 perfused with integrin-binding peptide (RGD: Arg-Gly-Asp) or sham control peptide (RGE: Arg-Gly-Glu)

37 Arg-Gly-Asp peptide and soluble fibronectin also enhance

38 bstrate to present either a linear or cyclic Arg-Gly-Asp peptide at identical densities.

39 ed to determine whether, and how, the cyclic Arg-Gly-Asp peptide Cilengitide (EMD 121974), which targ

40 eta(3) on the cell surface, a ligand-mimetic Arg-Gly-Asp peptide did not, as judged by binding of com

41 Adhesion to fibronectin, collagen, or Arg-Gly-Asp peptide down-regulated collagenase expressio

42 eek after ligation, a (99m)Tc-labeled cyclic-Arg-Gly-Asp peptide targeted at alpha(v) integrin (NC100

43 Addition of HA, but not Arg-Gly-Asp peptide, to TPBM culture inhibited bacterial

44 nt on plasma fibronectin and inhibited by an Arg-Gly-Asp peptide.

45 ranscription was effectively blocked by RGD (Arg-Gly-Asp) peptide and neutralizing alphavbeta3 antibo

46 ed Ld lipid domains increased beta1-integrin-Arg-Gly-Asp-peptide affinity and valency, thus implicati

47 dothelial cells, BA increased beta1-integrin-Arg-Gly-Asp-peptide affinity by 18% with a transition fr

48 lpha(v)beta(3) and alpha(v)beta(5) targeting Arg-Gly-Asp peptidomimetic and the reactive lysine of al

49 ly increase the circulatory half-life of the Arg-Gly-Asp peptidomimetic, and (iv) effectively reduce

50 We studied a clinical dimeric (18)F-labeled Arg-Gly-Asp positron-emission tomography (PET) agent ((1

51 No other Arg-Gly-Asp protein (fibronectin, vitronectin, type I co

52 -EM has shown that the integrin-binding RGD (Arg-Gly-Asp) protrusion of the Ad2 penton base protein i

53 he Ad penton base as well as vitronectin, an Arg Gly Asp (RGD)-containing extracellular matrix protei

54 gment enhances the integrin binding sequence Arg, Gly, Asp (RGD), which, when present, has been shown

55 Further mutations demonstrated that both Arg-Gly-Asp (RGD) and Asp-Cys-Ser-Gly (DCSG) sequences i

56 e supports the hypothesized importance of an Arg-Gly-Asp (RGD) and surrounding sequence.

57 This process depends on both the Arg-Gly-Asp (RGD) and the synergy cell-binding sites and

58 open conformation visualized in presence of Arg-Gly-Asp (RGD) antagonists.

59 gonists targeting two or more members of the Arg-Gly-Asp (RGD) binding integrins, notably alphavbeta3

60 Tat proteins containing mutations in the Arg-Gly-Asp (RGD) cell adhesion motif or a deletion of t

61 boxyl end: (a) nine Asp (D) residues; (b) an Arg-Gly-Asp (RGD) cell adhesion motif; and (c) a predict

62 VCIP/PAP2b exhibits an Arg-Gly-Asp (RGD) cell adhesion sequence.

63 that integrin-dependent cell adhesion to the Arg-Gly-Asp (RGD) containing central cell-binding domain

64 In addition, IGFBP2 has an Arg-Gly-Asp (RGD) domain, which is a known integrin bind

65 ed lunasin) contains the cell adhesion motif Arg-Gly-Asp (RGD) followed by eight aspartic acid residu

66 Peptides containing the tripeptide sequence Arg-Gly-Asp (RGD) have the ability to bind to members of

67 Peptides containing Arg-Gly-Asp (RGD) immobilized on beads bind to integrins

68 ct in its capacity to recognize the sequence Arg-Gly-Asp (RGD) in many extra-cellular matrix (ECM) co

69 and, in lieu of the disintegrins' signature Arg-Gly-Asp (RGD) integrin binding sequence, there is an

70 Although Arg-Gly-Asp (RGD) integrin ligand and matrix softening c

71 ransgenes expressing a mutant tiggrin, whose Arg-Gly-Asp (RGD) integrin recognition sequence has been

72 ions independently of IGF binding through an Arg-Gly-Asp (RGD) integrin-binding motif.

73 subunits, or treatment with cilengitide, an Arg-Gly-Asp (RGD) mimetic, impaired HSV-induced Ca2+ rel

74 Mutation of the single Arg-Gly-Asp (RGD) motif in human L1-Ig6 effectively abro

75 Integrin alpha5beta1 binds to an Arg-Gly-Asp (RGD) motif in its ligand fibronectin.

76 c activity but instead were mediated via the Arg-Gly-Asp (RGD) motif in the enzyme prodomain, which r

77 An Arg-Gly-Asp (RGD) motif in the second EGF domain (EGF2)

78 rin interactions are mediated through the Fn Arg-Gly-Asp (RGD) motif located within the tenth type II

79 only domain in fibrillin-1 that harbours an Arg-Gly-Asp (RGD) motif needed to mediate cell-matrix in

80 A synthetic peptide containing the Arg-Gly-Asp (RGD) motif of fibronectin and vitronectin w

81 Attaching a targeting peptide bearing the Arg-Gly-Asp (RGD) motif to nano-rGO afforded selective c

82 HHV-8-gB possesses the Arg-Gly-Asp (RGD) motif, the minimal peptide region of m

83 lthough Mac(5005) and Mac(8345) each have an Arg-Gly-Asp (RGD) motif, the proteins differed in their

84 C3 harbors an Arg-Gly-Asp (RGD) motif, which is the major integrin-bin

85 with the alpha(v)beta(3) receptor contain an Arg-Gly-Asp (RGD) motif.

86 th matrix proteins through recognition of an Arg-Gly-Asp (RGD) motif.

87 he location of the integrin binding sequence Arg-Gly-Asp (RGD) on human type 2 adenovirus (Ad2) was v

88 ted cells and was reversed by treatment with Arg-Gly-Asp (RGD) or PAI-1 antibody indicating that the

89 ment abciximab, cyclic peptides based on the Arg-Gly-Asp (RGD) or related amino acid motifs, and RGD-

90 thyleneimine (PEI) that is PEGylated with an Arg-Gly-Asp (RGD) peptide ligand attached at the distal

91 hesion receptors bind ligands containing the Arg-Gly-Asp (RGD) peptide motif.

92 PEG hydrogels were modified using an Arg-Gly-Asp (RGD) peptide sequence, with the incorporati

93 We previously coupled a cyclic Arg-Gly-Asp (RGD) peptide, c(RGDyK), with 1,4,7,10-tetra

94 cell migration by targeting integrins, using Arg-Gly-Asp (RGD) peptide-functionalized gold nanorods.

95 grin-coupled ferromagnetic beads coated with Arg-Gly-Asp (RGD) peptide.

96 es, here we report that integrin-interacting Arg-Gly-Asp (RGD) peptides activate S6K1 as observed by

97 e less sensitive than human to inhibition by Arg-Gly-Asp (RGD) peptides due to differences in the alp

98 ckade of platelet GPIIbIIIa by antibodies or Arg-Gly-Asp (RGD) peptides markedly decreased adhesion.

99 Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct R

100 The integrin receptor is near the Arg-Gly-Asp (RGD) recognition site on the integrin; an i

101 can associate with endothelial cells via an Arg-Gly-Asp (RGD) recognition specificity.

102 ders fibronectin (Fn) binding by alpha5beta1 Arg-Gly-Asp (RGD) resistant.

103 rved that macrophage-mesothelial adhesion is Arg-Gly-Asp (RGD) sensitive and partially mediated by ve

104 main (CCBD) of fibronectin requires both the Arg-Gly-Asp (RGD) sequence (in the 10th type III repeat)

105 ats of FN (i.e., FN7-10) containing both the arg-gly-asp (RGD) sequence and the synergy site.

106 3 integrin, to which peptides containing the Arg-Gly-Asp (RGD) sequence are known to bind.

107 tion by binding to integrin receptors via an Arg-Gly-Asp (RGD) sequence found in the G-H loop of the

108 Cyclic peptides containing the Arg-Gly-Asp (RGD) sequence have been shown to specifical

109 Peptides containing the Arg-Gly-Asp (RGD) sequence have high affinity for alphav

110 igation of the alpha5beta1 integrin with the Arg-Gly-Asp (RGD) sequence in fibronectin and binding of

111 s: (i) although both integrins recognize the Arg-Gly-Asp (RGD) sequence in fibronectin, the interacti

112 or (VNR, alpha(v)beta3), which recognizes an Arg-Gly-Asp (RGD) sequence in the C-terminus of vWF, and

113 IMZ cell attachment to FN is mediated by the Arg-Gly-Asp (RGD) sequence located in the type III-10 re

114 Proteolysis at Arg572 destroyed the Arg-Gly-Asp (RGD) sequence motif recognized by cell surf

115 The Arg-Gly-Asp (RGD) sequence serves as the primary integri

116 cule antagonists of GP IIb/IIIa based on the Arg-Gly-Asp (RGD) sequence show similar benefit, and som

117 ct with binding receptors on cells, while an Arg-Gly-Asp (RGD) sequence usually found in the penton b

118 ovirus type 2 whose vertex capsomers lack an Arg-Gly-Asp (RGD) sequence which mediates binding of wil

119 The Arg-Gly-Asp (RGD) sequence within the third complementar

120 One of these variants (mSpeB2) contains an Arg-Gly-Asp (RGD) sequence, a tripeptide motif that is c

121 he interaction of certain integrins with the Arg-Gly-Asp (RGD) sequence, displayed on specific FNIII

122 tein sequences determined to date contain an Arg-Gly-Asp (RGD) sequence, suggesting that F engages RG

123 We found that human APC possesses an Arg-Gly-Asp (RGD) sequence, which is critical for the in

124 This domain also contains one of two Arg-Gly-Asp (RGD) sequences found in SCPB.

125 at the C-terminus of the gamma chain and two Arg-Gly-Asp (RGD) sequences in the Aalpha chain.

126 The Arg-Tyr-Asp (RYD) and Arg-Gly-Asp (RGD) sequences within the third complementa

127 everal investigators have suggested that the Arg-Gly-Asp (RGD) site at position 572-574 on the alpha

128 eptide precursor protein that contains seven Arg-Gly-Asp (RGD) sites.

129 incubation of HUVEC with a synthetic peptide Arg-Gly-Asp (RGD) that prevents vWf-mediated adhesion of

130 hat integrin-binding peptides containing the Arg-Gly-Asp (RGD) tripeptide sequence cause immediate an

131 b)beta(3) and alpha(V)beta(3) by means of an Arg-Gly-Asp (RGD) tripeptide sequence.

132 idermal growth factor (EGF)-like repeats, an Arg-Gly-Asp (RGD) tripeptide, and a mucin stalk.

133 oles in host cell interactions, including an Arg-Gly-Asp (RGD) triplet that was reported to bind inte

134 rinogen and peptides containing the sequence Arg-Gly-Asp (RGD) were also found to promote bacterial i

135 fibronectin (Fn) cell-binding domain peptide Arg-Gly-Asp (RGD) were covalently immobilized to glass,

136 gment that included the recognition sequence Arg-Gly-Asp (RGD), suggesting that stem cells may expres

137 C56631) based upon the alpha(v)beta3 ligand, Arg-Gly-Asp (RGD), which recognizes the isolated integri

138 useful intermediates for the preparation of Arg-Gly-Asp (RGD)-based cyclopentapeptides (cRGD) with n

139 ith more complex derivatives of PEG, such as Arg-Gly-Asp (RGD)-based peptide-PEG-lipids.

140 ility of T cells was critically dependent on Arg-Gly-Asp (RGD)-binding integrins in the inflamed derm

141 scle cells can be blocked specifically by an Arg-Gly-Asp (RGD)-containing antagonist of integrins.

142 rect competitive inhibitor of the binding of Arg-Gly-Asp (RGD)-containing fibronectin fragments to al

143 We previously demonstrated that Arg-Gly-Asp (RGD)-containing ligand-mimetic inhibitors o

144 Polystyrene beads coated with Arg-Gly-Asp (RGD)-containing peptide adhere to the surfa

145 We have shown that incorporation of an Arg-Gly-Asp (RGD)-containing peptide in the HI loop of t

146 Phage displaying an Arg-Gly-Asp (RGD)-containing peptide with a high affinit

147 sts to TGFbeta in the presence or absence of Arg-Gly-Asp (RGD)-containing peptides and neutralizing a

148 We previously developed Arg-Gly-Asp (RGD)-containing polyethylene glycol biomate

149 the transition from a P-selectin-independent/Arg-Gly-Asp (RGD)-dependent process at 100 s(-1) to a P-

150 se of this study was to identify the role of Arg-Gly-Asp (RGD)-dependent tyrosine phosphorylation in

151 ibit multiple phagocyte functions, including Arg-Gly-Asp (RGD)-initiated activation of phagocytosis,

152 fibroblasts adhered to fibronectin- (FN) and Arg-Gly-Asp (RGD)-modified substrata of varying surface

153 bind to plasma fibrinogen and to a number of Arg-Gly-Asp (RGD)-type ligands.

154 significantly restored by pretreatment with Arg-Gly-Asp (RGD).

155 y specificity for peptide domains other than Arg-Gly-Asp (RGD); they confirm the generality of integr

156 sted the hypothesis that integrin binding to Arg-Gly-Asp(RGD) peptide sequences in extracellular matr

157 Arg517 is part of the Arg-Gly-Asp(RGD) sequence in thrombin and contributes to

158 trategy was employed where the pharmacophore-Arg-Gly-Asp-(RGD), or RGD mimetic, was constrained in a

159 These peptides were designed to integrate an Arg-Gly-Asp sequence that confers potential activity in

160 Likewise, a peptide containing the Arg-Gly-Asp sequence was strongly inhibitory, suggesting

161 n, recombinant TSP1 fragments containing the Arg-Gly-Asp sequence, and native TSP1.

162 Cyclic heptapeptide 1, which contains an Arg-Gly-Asp sequence, has good affinity for the platelet

163 heir ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown.

164 tely 65% by synthetic peptides containing an Arg-Gly-Asp sequence, supporting roles for integrins in

165 tin was inhibited by peptides containing the Arg-Gly-Asp sequence.

166 complex with a cyclic peptide presenting the Arg-Gly-Asp sequence.

167 cyclic aza-pentapeptides containing the RGD (Arg-Gly-Asp) sequence.

168 ctions of vitronectin were sensitive to RGD (Arg-Gly-Asp)-sequence-containing peptide, indicating the

169 inhibitory effects of cationic aminosugars, Arg-Gly-Asp-Ser (RGDS) peptide, and mAbs to phagocyte al

170 termine mechanisms of this adhesion, IgG and Arg-Gly-Asp-Ser (RGDS) receptor sites on PMN were satura

171 molecules, we found that this difference in Arg-Gly-Asp-Ser (RGDS) sensitivity was the result of ami

172 Further, an Fn cell binding peptide, Arg-Gly-Asp-Ser (RGDS), decreased the attachment from 44

173 the integrin-specific tetrapeptide inhibitor Arg-Gly-Asp-Ser (RGDS).

174 invasion were blocked by the peptide ligand Arg-Gly-Asp-Ser (RGDS).

175 mulated macrophages was blocked about 50% by Arg-Gly-Asp-Ser and anti-alpha(v), and up to 20% by oxid

176 ion to 4N1-1 was obtained in the presence of Arg-Gly-Asp-Ser in mouse platelets deficient in FcR gamm

177 ntibody or alphavbeta3-directed tetrapeptide arg-gly-asp-ser or inhibition of FP receptor signalling

178 ECM proteins and in the presence of 1 mg/ml Arg-Gly-Asp-Ser peptide, which blocks ECM binding to int

179 ximately 298 amino acids that contains a Gly-Arg-Gly-Asp-Ser sequence.

180 RGDS (Arg-Gly-Asp-Ser) or antibodies to alpha5beta1 or alphaII

181 i-induced apoptosis was inhibited by peptide Arg-Gly-Asp-Ser, anti-beta3 (CD61) Ab, CD36 peptide, or

182 The integrin antagonist Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) was applied by local ejecti

183 The peptide Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP, 1 mM) inhibited the total R

184 Both integrin antagonists Gly-Arg-Gly-Asp-Ser-Pro and GAVSTA eluted a major species of

185 rfused the microvessels with the peptide Gly-Arg-Gly Asp-Thr-Pro (GRGDTP; 0.3 mmol l-1), to disrupt i

186 srupted by pretreatment with the peptide Gly-Arg-Gly-Asp-Thr-Pro (GRGDTP; 0.3 mmol l-1), we measured

187 ein containing the integrin binding sequence Arg-Gly-Asp through which it interacts with several inte

188 The integrin receptor recognition sequence Arg-Gly-Asp was successfully used as a template from whi