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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
31              The assay measures (nonlabeled) RGD-peptides' ability to inhibit binding of a biotinylat
32 cant reduction in the renal perfusion, 99mTc-RGD peptide accumulates in the postischemic kidney; (3)
33                                              RGD peptides act as the efficient tailoring ligand with
34      In conclusion, these data indicate that RGD peptide, acting via alpha(5)beta(1) integrin, depres
35 eport that integrin-interacting Arg-Gly-Asp (RGD) peptides activate S6K1 as observed by band shifting
36  with RGD peptides soaked into crystals, and RGD peptide affinity measurements.
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
40 rin receptors with respect to the monovalent RGD peptide alone, from 10.40 nM to 0.18 nM IC(50).
41                                          The RGD peptide also reduced molar drift (p < 0.05).
42 ell to allow covalent attachment of a cyclic RGD peptide and an organic fluorophore.
43                                              RGD peptide and antialphav beta3 mAb were without effect
44 lop improved implants, such as cell adhesion RGD peptide and antimicrobial peptide (AMP).
45 emical properties of a coumarin-caged cyclic RGD peptide and demonstrate that uncaging can be efficie
46                           The addition of an RGD peptide and echistatin to pSMC cultures that had bee
47  fibronectin was inhibited only partially by RGD peptide and gelatin, but not by heparin.
48 D could be inhibited completely by a soluble RGD peptide and partially by a soluble PHSRN peptide.
49                                              RGD peptide and RGD-mimetic drugs are known to induce ep
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
53                                              RGD peptides and alpha 5 integrin-specific Ab abolished
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
56               Molecular interactions between RGD peptides and integrins are known to mediate many bio
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
63                  They are competable with an RGDS peptide and are stable to reduction but not boiling
64                    Results demonstrated that RGDS peptide and nHA containing 3D printed scaffolds und
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
70 sulfhydryl blocker, N-ethylmaleimide, by the RGD peptide, and by anti-alphaIIbbeta3 antibodies.
71                   Adhesion was blocked by an RGD peptide, and cells were unable to attach to a mutant
72 ing anti-beta1 integrin monoclonal antibody, RGD peptide, and cytochalasin D inhibit IGF-I-induced ce
73        Interestingly, anti-alpha 5 antibody, RGD peptide, and function-blocking mutations in alpha 5
74      These data indicate that interaction of RGD peptides, and in particular the RGDN sequence with e
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
79                            Multimeric cyclic RGD peptides are capable of improving the integrin alpha
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
86 )beta(3)-binding affinity/specificity of the RGD peptide-based conjugates in vitro and in vivo.
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
93 gainst osteopontin and beta3 integrin, or by RGD peptide, but not by controls.
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
104                                    A soluble RGD peptide competitor reduced both the persistence of l
105 umvent these problems, we developed a cyclic RGD peptide-conjugated poly(ethylene glycol)-co-poly(lac
106       Recently, we have identified two small RGD peptides, containing a benzophenone moiety at either
107                We proposed that radiolabeled RGD peptides could be used to detect osteoclasts in lyti
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
110                                The pegylated RGD peptide demonstrated rapid blood clearance (0.57 +/-
111                       The presence of cyclic RGD peptides did not affect the alpha(v)beta(3) integrin
112                                  An array of RGD peptides differing in macrocycle size, the presence
113                    Halotryptophan-containing RGD peptides display increased affinity toward integrin
114                    Halotryptophan-containing RGD peptides display increased affinity toward integrin
115 ive than human to inhibition by Arg-Gly-Asp (RGD) peptides due to differences in the alphaIIb sequenc
116                       We labeled the dimeric RGD peptide E[c(RGDyK)](2) with (18)F and evaluated its
117                               The tetrameric RGD peptide E{E[c(RGDyK)](2)}(2) was derived with amino-
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(
120 lls or proteins by conjugation with a cyclic RGD peptide, fibrinogen or antibodies.
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.
125          While evaluating a small library of RGD peptides for imaging alpha(V)beta(3) integrin (ABI)-
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
130 n by targeting integrins, using Arg-Gly-Asp (RGD) peptide-functionalized gold nanorods.
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%.
134            Preincubation of myocytes with an RGD peptide (GRGDSP) or with soluble fibronectin, each o
135                                    Among the RGD peptides, H10 cells adhered at significantly higher
136                             While the linear RGD peptides had no effect, the cyclic peptide penRGD in
137                      A series of 18F-labeled RGD peptides have been developed for PET of integrin exp
138       Both bombesin (BBN) analogs and cyclic RGD peptides have been suitably radiolabeled for prostat
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
151             In contrast, binding of a linear RGD peptide induces no shape shifting.
152 t bound to fibronectin and vitronectin in an RGDS-peptide inhibitable manner.
153        The fibronectin competitive inhibitor RGD peptide inhibited adhesion of cells expressing all M
154             The in vitro results showed that RGD peptide inhibited cell cycle proliferation by arrest
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
157        Both anti-integrin beta1 antibody and RGD peptides inhibited the activation of ACK-2 by cell a
158                                 Furthermore, RGD peptides inhibited the adhesion of both cell lines t
159 urthermore, the inhibition was additive with RGD peptide inhibition and accounted for essentially all
160 eptors in cell engraftment was analyzed with RGD peptide inhibition assays.
161                                     Further, RGD peptide inhibition of periostin/alpha(v)beta(3) inte
162 on site on the integrin; an integrin-binding RGD peptide inhibits induction by resveratrol of ERK1/2-
163       We introduced the biotinylated knottin-RGD peptide instead of biotinylated cyclo[RGDfK] (as rep
164 s that the combination of the specificity of RGD peptide/integrin interaction with near-infrared fluo
165                          Quantitation of the RGD peptide is achieved by determining the peak intensit
166                            The cell-adhesive RGD peptide is chosen as a model ligand.
167                       Uptake of radiolabeled RGD peptides is not necessarily decreased by effective a
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
170 uitability for high-throughput screening of (RGD-)peptide libraries.
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
174 elet GPIIbIIIa by antibodies or Arg-Gly-Asp (RGD) peptides markedly decreased adhesion.
175 nt Ad containing fibers with an incorporated RGD peptide may be of great utility for treatment of neo
176 s overexpressing pVHL were more sensitive to RGD peptide-mediated reduction in proliferation.
177                                              RGD peptide-modified chitosan was synthesized and then c
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
180 ors bind ligands containing the Arg-Gly-Asp (RGD) peptide motif.
181                   A disulfide-bridged cyclic RGD peptide, named iRGD (internalizing RGD, c(CRGDK/RGPD
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
185 hibitor Ro-32-0432, reversed the activity of RGD peptide on papillary muscle bundles.
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
189         Treatment of cells with a competitor RGD peptide or a purified recombinant RGD-containing fib
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.
192                     ELVAX loaded with either RGD peptide or echistatin and surgically implanted next
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
196          In endothelial cells, attachment to RGD peptides or fibrinogen was mediated through alphavbe
197 thermore, treatment of cells with polyvalent RGD peptides or pre-polymerized fibronectin did not stim
198                                           An RGDS peptide or a function-blocking antibody to integrin
199 ction-independent LIBS expression induced by RGDS peptide or disintegrin albolabrin were normal or mi
200 nterfere with apoptosis mediated by the free RGDS peptide or serum-free medium.
201                                 Inclusion of RGDS peptides or EGTA, during activation, led to a bipha
202 ha(V), as blockage by antagonist echistatin (RGD peptide) or alpha(V)-specific siRNA resulted in a de
203 binding fragment of soluble human Fn, cyclic RGD peptide, or Ab specific to VLA3 or VLA5.
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
211  2-fluoropropionyl labeled PEGylated dimeric RGD peptide (PEG3-E[c{RGDyk}]2) PET/CT.
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
215                           There are about 90 RGD peptides per QD particle, and DOTA-QD-RGD exhibited
216        Treatment of adherent TF-1 cells with RGDS peptide plus anti-alpha 4 antibody also inhibited S
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(
219 nd for capturing HaloTag fusion proteins and RGD peptides promoting cell adhesion was devised.
220 In addition, treatment of septic mice with a RGD peptide recapitulated the beneficial effects of rhAP
221                We tested the hypothesis that RGDS peptides regulate osteoblast survival in culture.
222 ubated with laminin, Matrigel, or a circular RGD peptide (RGD-C), but became exposed when cells were
223 ionalized with alphavbeta3-integrin-specific RGD peptides (rHDL-RGD).
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
226                                   The cyclic RGD peptide selectively binds to alpha(v) integrin recep
227                       TGF-beta 1 also caused RGD peptide-sensitive CD8+ T cell aggregation.
228 G hydrogel structure containing the adhesive RGD peptide sequence to ligate the alpha5beta1 integrin
229          The arginine-glycine-aspartic acid (RGD) peptide sequence is a common recognition motif by i
230 ydrogels were modified using an Arg-Gly-Asp (RGD) peptide sequence, with the incorporation of RGD int
231  to extracellular matrix proteins containing RGD peptide sequences.
232 othesis that integrin binding to Arg-Gly-Asp(RGD) peptide sequences in extracellular matrix proteins
233                                The pegylated RGD peptide showed higher renal accumulation at early ti
234                 However, addition of soluble RGD peptide (single-letter amino-acid code) or the use o
235 lpha5beta1 headpiece fragment, alone or with RGD peptides soaked into crystals, and RGD peptide affin
236 nd Lm-mediated invasion but did not abrogate RGD-peptide-stimulated invasion.
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
241 d by bitistatin, a disintegrin, and a cyclic RGD peptide that are known to block this integrin.
242 ddition of an antifibronectin antibody or an RGD peptide that blocks fibronectin binding to integrins
243                                 Radiolabeled RGD peptides that are integrin specific can be used for
244                            Fibronectin-based RGD peptides that bind alpha 5 beta 1 integrins and alph
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
247                           In the presence of RGD peptide, the constrained receptor was able to fully
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
252                                     A cyclic RGD peptide thioester 2 was synthesized and then site-se
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
256 e binding of soluble fibrinogen and a cyclic RGD peptide to purified alphaIIbbeta3.
257  inhibit binding of a biotinylated "knottin"-RGD peptide to surface-immobilized integrins and, thus,
258                 Conjugation of the thiolated RGD peptide to the QDs was achieved through a heterobifu
259 followed by attachment of integrin-targeting RGD peptides to anilines on the exterior surface.
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
264                               The tetrameric RGD peptide tracer (18)F-FPRGD4 possessing high integrin
265 or-binding characteristics of the tetrameric RGD peptide tracer (18)F-FPRGD4 were evaluated in vitro
266                                  The dimeric RGD peptide tracer (18)F-FRGD2, with high integrin speci
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
269 r uptake compared with monomeric and dimeric RGD peptide tracer analogs.
270 for improving the in vivo kinetics of a 64Cu-RGD peptide tracer without compromising the tumor-target
271 te binucleation, which could be inhibited by RGD peptide treatment.
272                The results indicate that (1) RGD peptide undergoes a rapid clearance predominantly vi
273             It consisted of a guiding cyclic RGD peptide unit to catch cancer cells via targeting the
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
277                                  Further, an RGD peptide was able to block the prosurvival effect of
278                     In addition, a thiolated RGD peptide was conjugated to the side chain of polymer
279      To accomplish this goal, in this study, RGD peptide was radiolabeled and its biodistribution and
280                                 Biotinylated RGD peptide was released from ELVAX into the PDL after s
281 that the lethal immunotoxicity of the cyclic RGD peptide was RGD sequence and peptide cyclization dep
282                           Binding of knottin-RGD peptide was strongest for alphavbeta3 but also detec
283 e of the anti-integrin antibodies and cyclic RGD peptides was restored when intracellular CamKII acti
284                Cyclic Arg-Gly-Asp-d-Phe-Lys (RGD) peptide was introduced to the surface of self-assem
285 dose-dependent manner (IC50 = 4 mM), whereas RGDS peptide was not active at the same concentration.
286 -fibronectin receptor interaction 100 microM RGDS peptide was used.
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
289         By using neutralizing antibodies and RGD peptides, we showed that members of the integrin fam
290 Carefully soaking crystals with Arg-Gly-Asp (RGD) peptides, we captured eight distinct RGD-bound conf
291  either single or sequential doses of H-7 or RGD peptide were added.
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 (
299                                          Two RGD peptides with different integrin-binding specificiti
300 eed and random motility coefficients on both RGD peptides, with the largest increases found on cyclic

 
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