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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 cal activity of a Diels-Alder cyclized (DAC) RGD peptide.
11 RI is enhanced after addition of fibronectin-RGD peptides.
12 lloproteinase activity and the production of RGD peptides.
13 ion-blocking anti-alpha v beta 3 mAb, and by RGD peptides.
14 llular signaling, which are not inhibited by RGD peptides.
15 ing to 125I-echistatin and cyclic and linear RGD peptides.
16 phaIIb beta3, which is distinct from that of RGD peptides.
17 l-glycyl-aspartyl-serine)4 than to monomeric RGD peptides.
18 be reflected by a decrease in the uptake of RGD peptides.
19 ical preference for cyclized RGD over linear RGD peptides.
20 e alphaVbeta3 binding was inhibited by small RGD peptides.
21 reas this binding was not inhibited by small RGD peptides.
22 r binding to envelope-associated gB and a gB(RGD) peptide.
23 ferromagnetic beads coated with Arg-Gly-Asp (RGD) peptide.
24 ated QDs and arginine-glycine-aspartic acid (RGD) peptides.
25 activity similar to that of the free cyclic RGD peptide 1 when assayed for its ability to both promo
26 y, pretreatment with either linear or cyclic RGD peptides (10 to 1000 micromol/L) inhibited fibroblas
27 imaging and ex vivo measurements with cyclic-RGD peptide (68)Ga-DOTA-E[c(RGDfK)](2) After the last (6
28 not bind alphaIIbbeta3-specific ligands or a RGD peptide, a ligand shared in common with alphavbeta3.
29 , apoptosis was induced in NECs treated with RGD peptide, a small beta1-integrin inhibitor peptide wi
30 taining a cyclic arginine-glycine-aspartate (RGD) peptide, a tetraethylene glycol spacer, and a galla
32 cant reduction in the renal perfusion, 99mTc-RGD peptide accumulates in the postischemic kidney; (3)
35 eport that integrin-interacting Arg-Gly-Asp (RGD) peptides activate S6K1 as observed by band shifting
37 statin or an arginine-glycine-aspartic acid (RGD) peptide, agents known to perturb bone remodeling, a
38 of RRETAWA and RGD were apparent in that (i) RGD peptides allosterically inhibited the binding of mAb
39 ceptin (anti-Her2), Erbitux (anti-Her1), and RGD peptide, allowing for multicolor Raman imaging of ce
45 emical properties of a coumarin-caged cyclic RGD peptide and demonstrate that uncaging can be efficie
48 D could be inhibited completely by a soluble RGD peptide and partially by a soluble PHSRN peptide.
50 ate between the dicyanocoumarin-caged cyclic RGD peptide and ruthenocene, which was selected as a met
51 ine-functionalized surface was modified with RGD peptides and 1,4,7,10-tetraazacyclodocecane-N,N',N''
52 RGD and its receptor, and 3) the affinity of RGD peptides and adsorbed Fn for their receptors is incr
54 ) antagonists, including cyclic and dicyclic RGD peptides and alpha(V)beta(3) function-blocking antib
55 ing was decreased in the presence of EDTA or RGD peptides and by mutation of the TWOW-1 RGD sequence
57 pha(v)beta3 and alpha5beta1 was inhibited by RGD peptides and the appropriate receptor-specific antib
58 assifies three types of interactions between RGD peptides and the extracellular domains of integrin a
59 data for these late-stage diversified cyclic RGD peptides and to further characterize their conformat
60 es of beta3 ligands: Class I, represented by RGD peptides and vitronectin, react similarly with alpha
61 ce into lymphatics can be blocked in vivo by RGD peptides and VLA-4 and VLA-5 but not beta(2) blockin
62 ults with an Arginine-glycine aspartic acid (RGD) peptide and monoclonal antibodies indicated a role
65 ctivation is partially sensitive to both the RGDS peptide and tyrphostin AG1478, suggesting that both
66 ere and spread on vWF, which is inhibited by RGDS peptides and antibodies against alpha(IIb)beta(3).
67 esive Arginine-Glycine-Aspartic acid-Serene (RGDS) peptide and/or nanocrystalline hydroxyapatite (nHA
68 n with the integrin receptor (inhibited with RGD peptides) and re-entry of the virus particle into a
69 ors to fibronectin remained sensitive to the RGD peptide, and antibodies that inhibit interaction wit
72 ing anti-beta1 integrin monoclonal antibody, RGD peptide, and cytochalasin D inhibit IGF-I-induced ce
75 tion, it was allowed to react with thiolated RGD peptides, and the resulting tracers were subjected t
76 angiostatin, anti-alphavbeta(3) antibodies, RGD-peptide, and a serine protease inhibitor effectively
77 ts of cationic aminosugars, Arg-Gly-Asp-Ser (RGDS) peptide, and mAbs to phagocyte alpha(v)beta3 vitro
78 ules, and HHV-8 infectivity was inhibited by RGD peptides, antibodies against RGD-dependent alpha3 an
80 Radiolabeled arginine-glycine-aspartate (RGD) peptides are increasingly used in preclinical and c
81 nt and wound healing, which was inhibited by RGD peptide as well as NF-kappaB inhibitors MG-132 and 1
82 Introduction of these Trp derivatives into RGD peptides as a benchmark system was performed to inve
83 kyne-containing fluorescently labeled cyclic RGD-peptide as the homing device for internalization stu
84 esulfonamide ligand, thereby positioning the RGD peptide at the surface, where it can mediate the adh
85 ion with a CD29 neutralizing antibody or the RGD peptide attenuated exosome-induced HSC AKT phosphory
87 ned here may guide the future development of RGD peptide-based imaging and internal radiotherapeutic
88 that beta(3) phosphorylation is initiated by RGD peptide binding in a dose-dependent and saturable fa
89 ndergo conformational changes in response to RGD peptide binding, and could be induced by activating
90 rin which is a ligand for osteopontin or the RGD peptide blocked both AII and osteopontin-induced col
91 inhibition of alphav integrins using cyclic RGD peptides blocked TGF-beta activation and Th17 cell g
92 rted interaction was completely inhibited by RGD peptides but not by alphavbeta3 blocking monoclonal
94 by the alphaIIbbeta3 ligands fibrinogen and RGD peptides, but not by thrombin or unrelated proteins.
95 s with short arginine-glycine aspartic acid (RGD) peptides, but not arginine-glycine-glutamic acid (R
96 ules, and HHV-8 infectivity was inhibited by RGD peptides, by antibodies against alpha3 and beta1 int
97 We previously coupled a cyclic Arg-Gly-Asp (RGD) peptide, c(RGDyK), with 1,4,7,10-tetraazacyclododec
98 g that PAMAM dendrimers conjugated to cyclic RGD peptides can increase the odontogenic potential of t
99 diolabeled cyclic arginine-glycine-aspartic (RGD) peptides can be used for noninvasive imaging of alp
100 ese cells (mechanically, with trypsin, or by RGDS peptides) caused a significant decrease in their 3-
101 s also been used to synthesize the protected RGD peptide (Cbz(alpha)-L-(omega)NO2-Arg-Gly-L-Asp-(OH)2
102 no acid scanning was performed on the cyclic RGD-peptide Cilengitide, cyclo[R-G-D-f-N(Me)V] 1, and it
103 proteins (fibronectin, laminin, vitronectin, RGD peptide, collagen type I, and collagen type IV) adso
105 umvent these problems, we developed a cyclic RGD peptide-conjugated poly(ethylene glycol)-co-poly(lac
108 geting ligands have been evaluated: a cyclic RGD peptide (cRGD) and the receptor-binding domain of ap
109 on was blocked by coincubation with a cyclic RGD peptide (cyclo[RGDfV], f is d-phenylalanine) that bi
115 ive than human to inhibition by Arg-Gly-Asp (RGD) peptides due to differences in the alphaIIb sequenc
118 ort that display of a tumor targeting cyclic RGD peptide (e.g. c(RGDyK) and c(RGDfK) on the surface o
119 tudy, we developed (64)Cu-labeled multimeric RGD peptides, E{E[c(RGDyK)](2)}(2) (RGD tetramer) and E(
121 eport an example of (18)F-labeled tetrameric RGD peptide for PET of alpha(v)beta(3) expression in bot
122 er stability in cell cultures and a terminal RGD peptide for specific targeting of cancer cells.
123 dification of the fiber knobs with PEGylated RGD peptide for targeting integrin alpha(v)beta(3) that
124 ditions, containing, for example, the cyclic RGD peptide for the biological targeting of cancer.
126 coupled to cyclic arginine-glycine-aspartic (RGD) peptides for integrin alphavbeta3 targeting and mac
127 resin results in side chain-to-tail-cyclized RGD peptides, for example, with biaryl moieties, providi
128 2-fl uoropropionyl labeled PEGylated dimeric RGD peptide (FPPRGD2), a marker of alpha(v)beta(3) integ
129 form that could be programmed to present the RGD peptide from fibronectin, mimicking cell-ECM interac
131 significantly higher rates to the polymeric RGD peptide (glycyl-arginyl-glycyl-aspartyl-serine)4 tha
132 of cells with an alphavbeta3-specific cyclic RGD peptide (GpenGRGD) led to a more profound (59%) TGFb
133 ound (59%) TGFbeta inhibition; a nonspecific RGD peptide (GRGDNP) inhibited TGFbeta by only 23%.
139 Among these, arginine-glycine-aspartic acid (RGD) peptides have shown a potential to promote tumor ac
140 decorated with an integrin-targeting cyclic-RGD peptide, however, (D)PMI-alpha exerted potent p53-de
141 ells to fibronectin (5-10 mM) in contrast to RGDS peptide (IC50 = 3 mM), inhibiting completely at 10
142 response was inhibited by treatment with an RGD peptide in cells from nondegenerated, but not degene
143 on for the potent proapoptotic properties of RGD peptides in models of angiogenesis, inflammation and
144 (ii) alpha(5)beta(1) binds preferentially to RGD peptides in which RGD is followed by Gly-Trp (GW) wh
145 ve effect of arginine-glycine-aspartic acid (RGD) peptides in acute renal failure, experiments were d
146 etition ELISA to measure integrin-binding of RGD-peptides in high-throughput without using cells, ECM
147 Adding binding factors from collagen and RGD peptides increases growth rates, and change maximum
148 tal cations and was inhibited by a synthetic RGD peptide, indicating that RGD and cation-binding sequ
149 trigger integrin activation, we suggest that RGD peptides induce apoptosis by triggering conformation
150 e with 20-fold higher affinity than a linear RGD peptide induces conformational change in the beta1-s
155 fibronectin 1 binding to integrin alpha8 by RGD peptide inhibited metalloproteinases (MMP)-2/9 whils
156 /2 and HP2/1, inhibitory antibody 4B5, or an RGD peptide inhibited sickle-cell adherence induced by P
159 urthermore, the inhibition was additive with RGD peptide inhibition and accounted for essentially all
162 on site on the integrin; an integrin-binding RGD peptide inhibits induction by resveratrol of ERK1/2-
164 s that the combination of the specificity of RGD peptide/integrin interaction with near-infrared fluo
168 Potent integrin antagonists, such as cyclic RGD peptides isolated from viper venom, may prove to be
169 ayers that present the high-affinity, cyclic-RGD peptide (left) show increased expression of osteogen
171 on via anti-beta1-integrin antibodies or the RGD peptide ligand-or by genetic or pharmacological corr
172 (PEI) that is PEGylated with an Arg-Gly-Asp (RGD) peptide ligand attached at the distal end of the po
173 rose bengal and arginylglycylaspartic acid (RGD) peptide, making them intrinsically dual-modal targe
175 nt Ad containing fibers with an incorporated RGD peptide may be of great utility for treatment of neo
178 drogel with a photoinitiator was employed on RGD peptide-modified PSi to create micropatterns with ce
179 nzenesulfonamides and that also includes the RGD peptide motif that can bind to cell-surface integrin
182 terestingly, neither a Cypate-labeled linear RGD peptide nor an (111)In-labeled DOTA-GRD conjugate wa
183 These observations suggest that the bivalent RGD peptide-oligonucleotide conjugate enters cells via a
184 l time-regulated activation of cell-adhesive RGD peptide on implanted biomaterials regulates in vivo
186 wo different arginine-glycine-aspartic acid (RGD) peptides: one is cyclic (RGDFC) and has specific af
187 enabled site-specific attachment of a cyclic-RGD peptide onto the capsid, retargeting the virus to th
188 knobs containing either an integrin-binding RGD peptide or a polylysine peptide in the exposed HI lo
190 rin independent, since it was insensitive to RGD peptide or antibodies against the only known integri
191 was largely inhibited either by a synthetic RGD peptide or by a disrupted RGD sequence in ICOSL.
193 Disrupting target cell integrin using an RGD peptide or through CRISPR-Cas9 knockout of the alpha
194 we performed a competition assay with C3 and RGD peptide or with a monoclonal antibody binding to bet
195 ectin binding to integrin by the addition of RGD peptides or by the knockdown of alpha 5 integrin pre
197 thermore, treatment of cells with polyvalent RGD peptides or pre-polymerized fibronectin did not stim
199 ction-independent LIBS expression induced by RGDS peptide or disintegrin albolabrin were normal or mi
202 ha(V), as blockage by antagonist echistatin (RGD peptide) or alpha(V)-specific siRNA resulted in a de
204 selectin, but not a alpha v beta 3 antibody, RGDS peptide, or heparin, blocked the formation of ULVWF
205 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) and at 24 hours and 1 we
206 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) in participants with bre
207 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) is a safe PET radiopharm
208 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET and two whole-body s
209 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/computed tomographic
210 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/CT scans were obtain
212 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) uptake with SUVmax maxim
213 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) uptake, with SUVmax maxi
214 2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) was well tolerated, with
217 f stirring or pretreatment of platelets with RGDS peptide prevented platelet aggregation, but not RAF
218 Moreover, we demonstrate that the two non-RGD peptides, previously identified as the alpha(v)beta(
220 In addition, treatment of septic mice with a RGD peptide recapitulated the beneficial effects of rhAP
222 ubated with laminin, Matrigel, or a circular RGD peptide (RGD-C), but became exposed when cells were
224 layers presenting the lower-affinity, linear-RGD peptide (right) express early markers of myogenesis
225 essels can bind circulating ligands and that RGD peptides selective for these integrins may be suitab
228 G hydrogel structure containing the adhesive RGD peptide sequence to ligate the alpha5beta1 integrin
230 ydrogels were modified using an Arg-Gly-Asp (RGD) peptide sequence, with the incorporation of RGD int
232 othesis that integrin binding to Arg-Gly-Asp(RGD) peptide sequences in extracellular matrix proteins
235 lpha5beta1 headpiece fragment, alone or with RGD peptides soaked into crystals, and RGD peptide affin
237 ta3 interactions were partially inhibited by RGD peptides, suggesting the existence of common RGD-con
238 -kDa chymotryptic fragment of fibronectin or RGD peptides suppressed PDGF-induced expression of MMP-1
239 ng the multiplicity m of the coiled-coil and RGD peptide targeting regions from 1 to 2, we can increa
240 ells are more adherent on immobilized cyclic RGD peptide than linear RGD or adsorbed Fn, 2) increased
242 ddition of an antifibronectin antibody or an RGD peptide that blocks fibronectin binding to integrins
245 Both integrin antibodies as well as cyclic RGD peptides that bind to the vitronectin receptors alph
246 ike MC3T3-E1 cells were allowed to attach to RGDS peptides that had been tethered to a silicone surfa
248 th the inhibitory prostaglandin E1, a cyclic RGD peptide, the monoclonal antibody abciximab, or the a
249 by a mechanism that was inhibited by cyclic RGD peptide, the peptide did not inhibit 70K binding to
250 D crystals modified with a photo-activatable RGD peptide, the time point of presentation of adhesive
251 adhesion was abolished by soluble endoglin, RGD peptides, the anti-integrin alpha5beta1 inhibitory a
253 study we introduced a new method of labeling RGD peptides through a thiol-reactive synthon, N-[2-(4-1
254 cells to PAC-1 was completely blocked by an RGD peptide, thus providing evidence that tumor cell adh
255 Finally, addition of fluorescent-labeled RGD peptide to cardiomyocytes exhibits its internalizati
257 inhibit binding of a biotinylated "knottin"-RGD peptide to surface-immobilized integrins and, thus,
260 n our study, we investigated the efficacy of RGD peptides to improve the tumor accumulation of PEGyla
261 to confirm the successful attachment of the RGD peptides to the QD surface before in vivo imaging of
262 nctionalized arginine-glycine-aspartic acid (RGD) peptide to modify the O-hydroxylamines by oxime bon
263 catalytic halogenation was incorporated into RGD peptides together with a variety of alkyl or aryl bo
265 or-binding characteristics of the tetrameric RGD peptide tracer (18)F-FPRGD4 were evaluated in vitro
267 In this study we developed a tetrameric RGD peptide tracer (64)Cu-DOTA-E{E[c(RGDfK)](2)}(2) (DOT
268 high tumor-to-organ ratios for the pegylated RGD peptide tracer (at 1 h after injection: tumor-to-blo
270 for improving the in vivo kinetics of a 64Cu-RGD peptide tracer without compromising the tumor-target
274 ion in flow with endothelial cells on linear RGD peptide, versus cyclic RGD, even though initial adhe
275 ication of ECO/sibeta3 nanoparticles with an RGD peptide via a PEG spacer enhanced siRNA uptake by po
276 nhibited after application of soluble cyclic RGD peptide, vitronectin (VN), fibronectin (FN), either
279 To accomplish this goal, in this study, RGD peptide was radiolabeled and its biodistribution and
281 that the lethal immunotoxicity of the cyclic RGD peptide was RGD sequence and peptide cyclization dep
283 e of the anti-integrin antibodies and cyclic RGD peptides was restored when intracellular CamKII acti
285 dose-dependent manner (IC50 = 4 mM), whereas RGDS peptide was not active at the same concentration.
287 ing knockout mouse embryonic fibroblasts and RGD peptide, we demonstrate that linear invadosome forma
288 nd the PET signal obtained with radiolabeled RGD peptides, we have constructed a compartmental model
290 Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conf
292 o experiments showed that the echistatin and RGD peptide were released from ELVAX in active forms at
293 Amino-terminal fibronectin fragments and RGD peptides were able to cross-compete for binding to t
294 ntegrin antibodies, disintegrins, and cyclic RGD peptides were used to identify integrins involved in
295 odies and an arginine-glycine-aspartic acid (RGD) peptide, while the antibodies or peptide used separ
296 ific, cyclic arginine-glycine-aspartic acid (RGD) peptides, will bind to dental pulp cells (DPCs) and
297 king experiments show that binding of cyclic RGD peptide with 20-fold higher affinity than a linear R
298 jugation of monomeric and dimeric sulfhydryl-RGD peptides with 18F-FBEM was achieved in high yields (
300 eed and random motility coefficients on both RGD peptides, with the largest increases found on cyclic