ライフサイエンスコーパス: RGD peptide

1 the RGD-623 conjugate were blocked by excess RGD peptide.

2 l effect on integrin-binding affinity of the RGD peptide.

3 hibited by tetraiodothyroacetic acid and the RGD peptide.

4 ly 100-fold better than the positive control RGD peptide.

5 ta(3) integrin did not reverse the effect of RGD peptide.

6 rin inhibited the force similar to synthetic RGD peptide.

7 oted by refolded beta1-LAP was blocked by an RGD peptide.

8 g to TSP-1 and binding was inhibited by free RGD peptide.

9 ith phage nanofibers displaying high-density RGD peptide.

10 RI is enhanced after addition of fibronectin-RGD peptides.

11 lloproteinase activity and the production of RGD peptides.

12 ion-blocking anti-alpha v beta 3 mAb, and by RGD peptides.

13 llular signaling, which are not inhibited by RGD peptides.

14 ing to 125I-echistatin and cyclic and linear RGD peptides.

15 phaIIb beta3, which is distinct from that of RGD peptides.

16 l-glycyl-aspartyl-serine)4 than to monomeric RGD peptides.

17 be reflected by a decrease in the uptake of RGD peptides.

18 ical preference for cyclized RGD over linear RGD peptides.

19 e alphaVbeta3 binding was inhibited by small RGD peptides.

20 reas this binding was not inhibited by small RGD peptides.

21 r binding to envelope-associated gB and a gB(RGD) peptide.

22 ferromagnetic beads coated with Arg-Gly-Asp (RGD) peptide.

23 ated QDs and arginine-glycine-aspartic acid (RGD) peptides.

24 activity similar to that of the free cyclic RGD peptide 1 when assayed for its ability to both promo

25 y, pretreatment with either linear or cyclic RGD peptides (10 to 1000 micromol/L) inhibited fibroblas

26 not bind alphaIIbbeta3-specific ligands or a RGD peptide, a ligand shared in common with alphavbeta3.

27 , apoptosis was induced in NECs treated with RGD peptide, a small beta1-integrin inhibitor peptide wi

28 taining a cyclic arginine-glycine-aspartate (RGD) peptide, a tetraethylene glycol spacer, and a galla

29 The assay measures (nonlabeled) RGD-peptides' ability to inhibit binding of a biotinylat

30 cant reduction in the renal perfusion, 99mTc-RGD peptide accumulates in the postischemic kidney; (3)

31 In conclusion, these data indicate that RGD peptide, acting via alpha(5)beta(1) integrin, depres

32 eport that integrin-interacting Arg-Gly-Asp (RGD) peptides activate S6K1 as observed by band shifting

33 with RGD peptides soaked into crystals, and RGD peptide affinity measurements.

34 statin or an arginine-glycine-aspartic acid (RGD) peptide, agents known to perturb bone remodeling, a

35 of RRETAWA and RGD were apparent in that (i) RGD peptides allosterically inhibited the binding of mAb

36 ceptin (anti-Her2), Erbitux (anti-Her1), and RGD peptide, allowing for multicolor Raman imaging of ce

37 rin receptors with respect to the monovalent RGD peptide alone, from 10.40 nM to 0.18 nM IC(50).

38 The RGD peptide also reduced molar drift (p < 0.05).

39 ell to allow covalent attachment of a cyclic RGD peptide and an organic fluorophore.

40 RGD peptide and antialphav beta3 mAb were without effect

41 emical properties of a coumarin-caged cyclic RGD peptide and demonstrate that uncaging can be efficie

42 The addition of an RGD peptide and echistatin to pSMC cultures that had bee

43 fibronectin was inhibited only partially by RGD peptide and gelatin, but not by heparin.

44 D could be inhibited completely by a soluble RGD peptide and partially by a soluble PHSRN peptide.

45 RGD peptide and RGD-mimetic drugs are known to induce ep

46 ate between the dicyanocoumarin-caged cyclic RGD peptide and ruthenocene, which was selected as a met

47 ine-functionalized surface was modified with RGD peptides and 1,4,7,10-tetraazacyclodocecane-N,N',N''

48 RGD and its receptor, and 3) the affinity of RGD peptides and adsorbed Fn for their receptors is incr

49 RGD peptides and alpha 5 integrin-specific Ab abolished

50 ) antagonists, including cyclic and dicyclic RGD peptides and alpha(V)beta(3) function-blocking antib

51 ing was decreased in the presence of EDTA or RGD peptides and by mutation of the TWOW-1 RGD sequence

52 Molecular interactions between RGD peptides and integrins are known to mediate many bio

53 pha(v)beta3 and alpha5beta1 was inhibited by RGD peptides and the appropriate receptor-specific antib

54 assifies three types of interactions between RGD peptides and the extracellular domains of integrin a

55 es of beta3 ligands: Class I, represented by RGD peptides and vitronectin, react similarly with alpha

56 ce into lymphatics can be blocked in vivo by RGD peptides and VLA-4 and VLA-5 but not beta(2) blockin

57 ults with an Arginine-glycine aspartic acid (RGD) peptide and monoclonal antibodies indicated a role

58 They are competable with an RGDS peptide and are stable to reduction but not boiling

59 Results demonstrated that RGDS peptide and nHA containing 3D printed scaffolds und

60 ctivation is partially sensitive to both the RGDS peptide and tyrphostin AG1478, suggesting that both

61 ere and spread on vWF, which is inhibited by RGDS peptides and antibodies against alpha(IIb)beta(3).

62 esive Arginine-Glycine-Aspartic acid-Serene (RGDS) peptide and/or nanocrystalline hydroxyapatite (nHA

63 n with the integrin receptor (inhibited with RGD peptides) and re-entry of the virus particle into a

64 ors to fibronectin remained sensitive to the RGD peptide, and antibodies that inhibit interaction wit

65 sulfhydryl blocker, N-ethylmaleimide, by the RGD peptide, and by anti-alphaIIbbeta3 antibodies.

66 Adhesion was blocked by an RGD peptide, and cells were unable to attach to a mutant

67 ing anti-beta1 integrin monoclonal antibody, RGD peptide, and cytochalasin D inhibit IGF-I-induced ce

68 Interestingly, anti-alpha 5 antibody, RGD peptide, and function-blocking mutations in alpha 5

69 These data indicate that interaction of RGD peptides, and in particular the RGDN sequence with e

70 tion, it was allowed to react with thiolated RGD peptides, and the resulting tracers were subjected t

71 angiostatin, anti-alphavbeta(3) antibodies, RGD-peptide, and a serine protease inhibitor effectively

72 ts of cationic aminosugars, Arg-Gly-Asp-Ser (RGDS) peptide, and mAbs to phagocyte alpha(v)beta3 vitro

73 ules, and HHV-8 infectivity was inhibited by RGD peptides, antibodies against RGD-dependent alpha3 an

74 Multimeric cyclic RGD peptides are capable of improving the integrin alpha

75 Radiolabeled arginine-glycine-aspartate (RGD) peptides are increasingly used in preclinical and c

76 nt and wound healing, which was inhibited by RGD peptide as well as NF-kappaB inhibitors MG-132 and 1

77 kyne-containing fluorescently labeled cyclic RGD-peptide as the homing device for internalization stu

78 esulfonamide ligand, thereby positioning the RGD peptide at the surface, where it can mediate the adh

79 ion with a CD29 neutralizing antibody or the RGD peptide attenuated exosome-induced HSC AKT phosphory

80 )beta(3)-binding affinity/specificity of the RGD peptide-based conjugates in vitro and in vivo.

81 ned here may guide the future development of RGD peptide-based imaging and internal radiotherapeutic

82 that beta(3) phosphorylation is initiated by RGD peptide binding in a dose-dependent and saturable fa

83 ndergo conformational changes in response to RGD peptide binding, and could be induced by activating

84 rin which is a ligand for osteopontin or the RGD peptide blocked both AII and osteopontin-induced col

85 inhibition of alphav integrins using cyclic RGD peptides blocked TGF-beta activation and Th17 cell g

86 rted interaction was completely inhibited by RGD peptides but not by alphavbeta3 blocking monoclonal

87 gainst osteopontin and beta3 integrin, or by RGD peptide, but not by controls.

88 by the alphaIIbbeta3 ligands fibrinogen and RGD peptides, but not by thrombin or unrelated proteins.

89 s with short arginine-glycine aspartic acid (RGD) peptides, but not arginine-glycine-glutamic acid (R

90 ules, and HHV-8 infectivity was inhibited by RGD peptides, by antibodies against alpha3 and beta1 int

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

92 g that PAMAM dendrimers conjugated to cyclic RGD peptides can increase the odontogenic potential of t

93 diolabeled cyclic arginine-glycine-aspartic (RGD) peptides can be used for noninvasive imaging of alp

94 ese cells (mechanically, with trypsin, or by RGDS peptides) caused a significant decrease in their 3-

95 s also been used to synthesize the protected RGD peptide (Cbz(alpha)-L-(omega)NO2-Arg-Gly-L-Asp-(OH)2

96 no acid scanning was performed on the cyclic RGD-peptide Cilengitide, cyclo[R-G-D-f-N(Me)V] 1, and it

97 proteins (fibronectin, laminin, vitronectin, RGD peptide, collagen type I, and collagen type IV) adso

98 A soluble RGD peptide competitor reduced both the persistence of l

99 umvent these problems, we developed a cyclic RGD peptide-conjugated poly(ethylene glycol)-co-poly(lac

100 Recently, we have identified two small RGD peptides, containing a benzophenone moiety at either

101 We proposed that radiolabeled RGD peptides could be used to detect osteoclasts in lyti

102 geting ligands have been evaluated: a cyclic RGD peptide (cRGD) and the receptor-binding domain of ap

103 on was blocked by coincubation with a cyclic RGD peptide (cyclo[RGDfV], f is d-phenylalanine) that bi

104 The pegylated RGD peptide demonstrated rapid blood clearance (0.57 +/-

105 The presence of cyclic RGD peptides did not affect the alpha(v)beta(3) integrin

106 ive than human to inhibition by Arg-Gly-Asp (RGD) peptides due to differences in the alphaIIb sequenc

107 We labeled the dimeric RGD peptide E[c(RGDyK)](2) with (18)F and evaluated its

108 The tetrameric RGD peptide E{E[c(RGDyK)](2)}(2) was derived with amino-

109 tudy, we developed (64)Cu-labeled multimeric RGD peptides, E{E[c(RGDyK)](2)}(2) (RGD tetramer) and E(

110 lls or proteins by conjugation with a cyclic RGD peptide, fibrinogen or antibodies.

111 eport an example of (18)F-labeled tetrameric RGD peptide for PET of alpha(v)beta(3) expression in bot

112 er stability in cell cultures and a terminal RGD peptide for specific targeting of cancer cells.

113 dification of the fiber knobs with PEGylated RGD peptide for targeting integrin alpha(v)beta(3) that

114 ditions, containing, for example, the cyclic RGD peptide for the biological targeting of cancer.

115 While evaluating a small library of RGD peptides for imaging alpha(V)beta(3) integrin (ABI)-

116 coupled to cyclic arginine-glycine-aspartic (RGD) peptides for integrin alphavbeta3 targeting and mac

117 2-fl uoropropionyl labeled PEGylated dimeric RGD peptide (FPPRGD2), a marker of alpha(v)beta(3) integ

118 n by targeting integrins, using Arg-Gly-Asp (RGD) peptide-functionalized gold nanorods.

119 significantly higher rates to the polymeric RGD peptide (glycyl-arginyl-glycyl-aspartyl-serine)4 tha

120 of cells with an alphavbeta3-specific cyclic RGD peptide (GpenGRGD) led to a more profound (59%) TGFb

121 ound (59%) TGFbeta inhibition; a nonspecific RGD peptide (GRGDNP) inhibited TGFbeta by only 23%.

122 Preincubation of myocytes with an RGD peptide (GRGDSP) or with soluble fibronectin, each o

123 Among the RGD peptides, H10 cells adhered at significantly higher

124 While the linear RGD peptides had no effect, the cyclic peptide penRGD in

125 A series of 18F-labeled RGD peptides have been developed for PET of integrin exp

126 Both bombesin (BBN) analogs and cyclic RGD peptides have been suitably radiolabeled for prostat

127 decorated with an integrin-targeting cyclic-RGD peptide, however, (D)PMI-alpha exerted potent p53-de

128 ells to fibronectin (5-10 mM) in contrast to RGDS peptide (IC50 = 3 mM), inhibiting completely at 10

129 response was inhibited by treatment with an RGD peptide in cells from nondegenerated, but not degene

130 on for the potent proapoptotic properties of RGD peptides in models of angiogenesis, inflammation and

131 (ii) alpha(5)beta(1) binds preferentially to RGD peptides in which RGD is followed by Gly-Trp (GW) wh

132 ve effect of arginine-glycine-aspartic acid (RGD) peptides in acute renal failure, experiments were d

133 etition ELISA to measure integrin-binding of RGD-peptides in high-throughput without using cells, ECM

134 Adding binding factors from collagen and RGD peptides increases growth rates, and change maximum

135 tal cations and was inhibited by a synthetic RGD peptide, indicating that RGD and cation-binding sequ

136 trigger integrin activation, we suggest that RGD peptides induce apoptosis by triggering conformation

137 e with 20-fold higher affinity than a linear RGD peptide induces conformational change in the beta1-s

138 In contrast, binding of a linear RGD peptide induces no shape shifting.

139 t bound to fibronectin and vitronectin in an RGDS-peptide inhibitable manner.

140 The fibronectin competitive inhibitor RGD peptide inhibited adhesion of cells expressing all M

141 The in vitro results showed that RGD peptide inhibited cell cycle proliferation by arrest

142 fibronectin 1 binding to integrin alpha8 by RGD peptide inhibited metalloproteinases (MMP)-2/9 whils

143 /2 and HP2/1, inhibitory antibody 4B5, or an RGD peptide inhibited sickle-cell adherence induced by P

144 Both anti-integrin beta1 antibody and RGD peptides inhibited the activation of ACK-2 by cell a

145 Furthermore, RGD peptides inhibited the adhesion of both cell lines t

146 urthermore, the inhibition was additive with RGD peptide inhibition and accounted for essentially all

147 eptors in cell engraftment was analyzed with RGD peptide inhibition assays.

148 Further, RGD peptide inhibition of periostin/alpha(v)beta(3) inte

149 on site on the integrin; an integrin-binding RGD peptide inhibits induction by resveratrol of ERK1/2-

150 We introduced the biotinylated knottin-RGD peptide instead of biotinylated cyclo[RGDfK] (as rep

151 s that the combination of the specificity of RGD peptide/integrin interaction with near-infrared fluo

152 Quantitation of the RGD peptide is achieved by determining the peak intensit

153 The cell-adhesive RGD peptide is chosen as a model ligand.

154 Uptake of radiolabeled RGD peptides is not necessarily decreased by effective a

155 Potent integrin antagonists, such as cyclic RGD peptides isolated from viper venom, may prove to be

156 ayers that present the high-affinity, cyclic-RGD peptide (left) show increased expression of osteogen

157 uitability for high-throughput screening of (RGD-)peptide libraries.

158 on via anti-beta1-integrin antibodies or the RGD peptide ligand-or by genetic or pharmacological corr

159 (PEI) that is PEGylated with an Arg-Gly-Asp (RGD) peptide ligand attached at the distal end of the po

160 elet GPIIbIIIa by antibodies or Arg-Gly-Asp (RGD) peptides markedly decreased adhesion.

161 nt Ad containing fibers with an incorporated RGD peptide may be of great utility for treatment of neo

162 s overexpressing pVHL were more sensitive to RGD peptide-mediated reduction in proliferation.

163 RGD peptide-modified chitosan was synthesized and then c

164 nzenesulfonamides and that also includes the RGD peptide motif that can bind to cell-surface integrin

165 ors bind ligands containing the Arg-Gly-Asp (RGD) peptide motif.

166 A disulfide-bridged cyclic RGD peptide, named iRGD (internalizing RGD, c(CRGDK/RGPD

167 terestingly, neither a Cypate-labeled linear RGD peptide nor an (111)In-labeled DOTA-GRD conjugate wa

168 These observations suggest that the bivalent RGD peptide-oligonucleotide conjugate enters cells via a

169 l time-regulated activation of cell-adhesive RGD peptide on implanted biomaterials regulates in vivo

170 hibitor Ro-32-0432, reversed the activity of RGD peptide on papillary muscle bundles.

171 enabled site-specific attachment of a cyclic-RGD peptide onto the capsid, retargeting the virus to th

172 knobs containing either an integrin-binding RGD peptide or a polylysine peptide in the exposed HI lo

173 Treatment of cells with a competitor RGD peptide or a purified recombinant RGD-containing fib

174 rin independent, since it was insensitive to RGD peptide or antibodies against the only known integri

175 ELVAX loaded with either RGD peptide or echistatin and surgically implanted next

176 we performed a competition assay with C3 and RGD peptide or with a monoclonal antibody binding to bet

177 ectin binding to integrin by the addition of RGD peptides or by the knockdown of alpha 5 integrin pre

178 In endothelial cells, attachment to RGD peptides or fibrinogen was mediated through alphavbe

179 thermore, treatment of cells with polyvalent RGD peptides or pre-polymerized fibronectin did not stim

180 An RGDS peptide or a function-blocking antibody to integrin

181 ction-independent LIBS expression induced by RGDS peptide or disintegrin albolabrin were normal or mi

182 nterfere with apoptosis mediated by the free RGDS peptide or serum-free medium.

183 Inclusion of RGDS peptides or EGTA, during activation, led to a bipha

184 ha(V), as blockage by antagonist echistatin (RGD peptide) or alpha(V)-specific siRNA resulted in a de

185 binding fragment of soluble human Fn, cyclic RGD peptide, or Ab specific to VLA3 or VLA5.

186 selectin, but not a alpha v beta 3 antibody, RGDS peptide, or heparin, blocked the formation of ULVWF

187 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) and at 24 hours and 1 we

188 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) in participants with bre

189 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) is a safe PET radiopharm

190 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET and two whole-body s

191 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/computed tomographic

192 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/CT scans were obtain

193 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/CT.

194 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) uptake with SUVmax maxim

195 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) uptake, with SUVmax maxi

196 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) was well tolerated, with

197 There are about 90 RGD peptides per QD particle, and DOTA-QD-RGD exhibited

198 Treatment of adherent TF-1 cells with RGDS peptide plus anti-alpha 4 antibody also inhibited S

199 f stirring or pretreatment of platelets with RGDS peptide prevented platelet aggregation, but not RAF

200 Moreover, we demonstrate that the two non-RGD peptides, previously identified as the alpha(v)beta(

201 nd for capturing HaloTag fusion proteins and RGD peptides promoting cell adhesion was devised.

202 In addition, treatment of septic mice with a RGD peptide recapitulated the beneficial effects of rhAP

203 We tested the hypothesis that RGDS peptides regulate osteoblast survival in culture.

204 ubated with laminin, Matrigel, or a circular RGD peptide (RGD-C), but became exposed when cells were

205 ionalized with alphavbeta3-integrin-specific RGD peptides (rHDL-RGD).

206 layers presenting the lower-affinity, linear-RGD peptide (right) express early markers of myogenesis

207 essels can bind circulating ligands and that RGD peptides selective for these integrins may be suitab

208 The cyclic RGD peptide selectively binds to alpha(v) integrin recep

209 TGF-beta 1 also caused RGD peptide-sensitive CD8+ T cell aggregation.

210 G hydrogel structure containing the adhesive RGD peptide sequence to ligate the alpha5beta1 integrin

211 The arginine-glycine-aspartic acid (RGD) peptide sequence is a common recognition motif by i

212 ydrogels were modified using an Arg-Gly-Asp (RGD) peptide sequence, with the incorporation of RGD int

213 to extracellular matrix proteins containing RGD peptide sequences.

214 othesis that integrin binding to Arg-Gly-Asp(RGD) peptide sequences in extracellular matrix proteins

215 The pegylated RGD peptide showed higher renal accumulation at early ti

216 However, addition of soluble RGD peptide (single-letter amino-acid code) or the use o

217 lpha5beta1 headpiece fragment, alone or with RGD peptides soaked into crystals, and RGD peptide affin

218 nd Lm-mediated invasion but did not abrogate RGD-peptide-stimulated invasion.

219 ta3 interactions were partially inhibited by RGD peptides, suggesting the existence of common RGD-con

220 -kDa chymotryptic fragment of fibronectin or RGD peptides suppressed PDGF-induced expression of MMP-1

221 ells are more adherent on immobilized cyclic RGD peptide than linear RGD or adsorbed Fn, 2) increased

222 d by bitistatin, a disintegrin, and a cyclic RGD peptide that are known to block this integrin.

223 ddition of an antifibronectin antibody or an RGD peptide that blocks fibronectin binding to integrins

224 Radiolabeled RGD peptides that are integrin specific can be used for

225 Fibronectin-based RGD peptides that bind alpha 5 beta 1 integrins and alph

226 Both integrin antibodies as well as cyclic RGD peptides that bind to the vitronectin receptors alph

227 ike MC3T3-E1 cells were allowed to attach to RGDS peptides that had been tethered to a silicone surfa

228 In the presence of RGD peptide, the constrained receptor was able to fully

229 th the inhibitory prostaglandin E1, a cyclic RGD peptide, the monoclonal antibody abciximab, or the a

230 by a mechanism that was inhibited by cyclic RGD peptide, the peptide did not inhibit 70K binding to

231 D crystals modified with a photo-activatable RGD peptide, the time point of presentation of adhesive

232 adhesion was abolished by soluble endoglin, RGD peptides, the anti-integrin alpha5beta1 inhibitory a

233 A cyclic RGD peptide thioester 2 was synthesized and then site-se

234 study we introduced a new method of labeling RGD peptides through a thiol-reactive synthon, N-[2-(4-1

235 cells to PAC-1 was completely blocked by an RGD peptide, thus providing evidence that tumor cell adh

236 Finally, addition of fluorescent-labeled RGD peptide to cardiomyocytes exhibits its internalizati

237 e binding of soluble fibrinogen and a cyclic RGD peptide to purified alphaIIbbeta3.

238 inhibit binding of a biotinylated "knottin"-RGD peptide to surface-immobilized integrins and, thus,

239 Conjugation of the thiolated RGD peptide to the QDs was achieved through a heterobifu

240 followed by attachment of integrin-targeting RGD peptides to anilines on the exterior surface.

241 to confirm the successful attachment of the RGD peptides to the QD surface before in vivo imaging of

242 nctionalized arginine-glycine-aspartic acid (RGD) peptide to modify the O-hydroxylamines by oxime bon

243 The tetrameric RGD peptide tracer (18)F-FPRGD4 possessing high integrin

244 or-binding characteristics of the tetrameric RGD peptide tracer (18)F-FPRGD4 were evaluated in vitro

245 The dimeric RGD peptide tracer (18)F-FRGD2, with high integrin speci

246 In this study we developed a tetrameric RGD peptide tracer (64)Cu-DOTA-E{E[c(RGDfK)](2)}(2) (DOT

247 high tumor-to-organ ratios for the pegylated RGD peptide tracer (at 1 h after injection: tumor-to-blo

248 r uptake compared with monomeric and dimeric RGD peptide tracer analogs.

249 for improving the in vivo kinetics of a 64Cu-RGD peptide tracer without compromising the tumor-target

250 The results indicate that (1) RGD peptide undergoes a rapid clearance predominantly vi

251 It consisted of a guiding cyclic RGD peptide unit to catch cancer cells via targeting the

252 ion in flow with endothelial cells on linear RGD peptide, versus cyclic RGD, even though initial adhe

253 ication of ECO/sibeta3 nanoparticles with an RGD peptide via a PEG spacer enhanced siRNA uptake by po

254 nhibited after application of soluble cyclic RGD peptide, vitronectin (VN), fibronectin (FN), either

255 Further, an RGD peptide was able to block the prosurvival effect of

256 To accomplish this goal, in this study, RGD peptide was radiolabeled and its biodistribution and

257 Biotinylated RGD peptide was released from ELVAX into the PDL after s

258 Binding of knottin-RGD peptide was strongest for alphavbeta3 but also detec

259 e of the anti-integrin antibodies and cyclic RGD peptides was restored when intracellular CamKII acti

260 dose-dependent manner (IC50 = 4 mM), whereas RGDS peptide was not active at the same concentration.

261 -fibronectin receptor interaction 100 microM RGDS peptide was used.

262 ing knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome forma

263 nd the PET signal obtained with radiolabeled RGD peptides, we have constructed a compartmental model

264 By using neutralizing antibodies and RGD peptides, we showed that members of the integrin fam

265 Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conf

266 either single or sequential doses of H-7 or RGD peptide were added.

267 o experiments showed that the echistatin and RGD peptide were released from ELVAX in active forms at

268 Amino-terminal fibronectin fragments and RGD peptides were able to cross-compete for binding to t

269 ntegrin antibodies, disintegrins, and cyclic RGD peptides were used to identify integrins involved in

270 odies and an arginine-glycine-aspartic acid (RGD) peptide, while the antibodies or peptide used separ

271 ific, cyclic arginine-glycine-aspartic acid (RGD) peptides, will bind to dental pulp cells (DPCs) and

272 king experiments show that binding of cyclic RGD peptide with 20-fold higher affinity than a linear R

273 jugation of monomeric and dimeric sulfhydryl-RGD peptides with 18F-FBEM was achieved in high yields (

274 Two RGD peptides with different integrin-binding specificiti

275 eed and random motility coefficients on both RGD peptides, with the largest increases found on cyclic