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3 with these receptors via a highly conserved arginine-glycine-aspartic acid amino acid sequence motif
4 30%) revealed that lysine, leucine, alanine, arginine, glycine, aspartic acid and glutamic acid resid
6 ate that the interaction of cathepsin Z with arginine-glycine-aspartic acid-binding integrins, specif
10 l positions are functionalized with a cyclic arginine-glycine-aspartic acid (cRGD) tripeptide for tar
11 (alphav, alpha5, beta1, beta3) that use RGD (arginine-glycine-aspartic Acid)-dependent mechanisms for
12 ntegrins alpha(v)beta3 and alpha(v)beta5 are arginine-glycine-aspartic acid-dependent adhesion recept
13 protein penton contains a well characterized arginine-glycine-aspartic acid integrin-binding domain t
14 e designed to mimic the tripeptide sequence (arginine-glycine-aspartic acid) of the natural ligands;
15 grin receptors bind to adhesion ligand (e.g. arginine-glycine-aspartic acid or RGD containing peptide
16 articles, surface functionalized with cyclic arginine-glycine-aspartic acid peptide ligands and radio
20 ifference between adhered cells under cyclic arginine-glycine-aspartic acid peptide-treated and contr
22 ntisense oligonucleotide and a bivalent RGD (arginine-glycine-aspartic acid) peptide that is a high-a
23 n this study, we report the efficacy of RGD (arginine-glycine-aspartic acid) peptide-modified polylac
24 divalent cation independent, not blocked by arginine-glycine-aspartic acid peptides and still mediat
25 [acetic acid]-7-[2-glutaric acid] and RGD is arginine-glycine-aspartic acid.) RESULTS: alphavbeta3 in
28 becoming cell-adhesive through exhibition of arginine-glycine-aspartic acid (RGD) adhesion peptides u
29 with these receptors via a highly conserved arginine-glycine-aspartic acid (RGD) amino acid sequence
30 mational plasticity and accessibility of the arginine-glycine-aspartic acid (RGD) binding site in FN,
31 use of GP IIb/IIIa antagonists based on the arginine-glycine-aspartic acid (RGD) cell-recognition se
33 c phthalocyanine with acetylenic bombesin or arginine-glycine-aspartic acid (RGD) derivatives, either
34 tracellular matrix protein, has a functional arginine-glycine-aspartic acid (RGD) domain for binding
35 2Y(2)R) contains the integrin-binding domain arginine-glycine-aspartic acid (RGD) in its first extrac
37 We used an array of peptidic and nonpeptidic arginine-glycine-aspartic acid (RGD) mimics that specifi
38 ptor, generally alphavbeta6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the expose
39 Human parechovirus 1 (HPEV1) displays an arginine-glycine-aspartic acid (RGD) motif in the VP1 ca
40 le amino acid substitution within an encoded arginine-glycine-aspartic acid (RGD) motif of the molecu
43 se required a selective interaction of virus arginine-glycine-aspartic acid (RGD) motifs with macroph
45 ere introduced using a ketone-functionalized arginine-glycine-aspartic acid (RGD) peptide to modify t
46 by local administration of echistatin or an arginine-glycine-aspartic acid (RGD) peptide, agents kno
47 of anti-alpha4 and -alpha5 antibodies and an arginine-glycine-aspartic acid (RGD) peptide, while the
48 demonstration of a renoprotective effect of arginine-glycine-aspartic acid (RGD) peptides in acute r
49 yanate (FL) and alphaVbeta3-specific, cyclic arginine-glycine-aspartic acid (RGD) peptides, will bind
51 ds to cell-surface integrin molecules via an arginine-glycine-aspartic acid (RGD) sequence in capsid
52 nt conformation beta5/beta3 integrins and an arginine-glycine-aspartic acid (RGD) sequence in the fir
53 exes react to bond the cell-adhesive peptide arginine-glycine-aspartic acid (RGD) to the polymer surf
54 he integrin alpha(v)beta3 interacts with the arginine-glycine-aspartic acid (RGD) tripeptide recognit
55 robalance (QCM) gold electrode surface using arginine-glycine-aspartic acid (RGD) tripeptide was elec
57 superfamily that mediates cell attachment on arginine-glycine-aspartic acid (RGD)-containing adhesive
58 the addition of an integrin-receptor-binding arginine-glycine-aspartic acid (RGD)-containing peptide
59 vitro compared with hydrogels modified with arginine-glycine-aspartic acid (RGD)-containing peptides
60 ted by incubation with soluble uPAR (suPAR), arginine-glycine-aspartic acid (RGD)-containing peptides
61 sults demonstrate that in the presence of an arginine-glycine-aspartic acid (RGD)-containing syntheti
62 r specificity of novel peptide-dye conjugate arginine-glycine-aspartic acid (RGD)-Cy5.5 as a contrast
63 s initiated by binding to certain species of arginine-glycine-aspartic acid (RGD)-dependent integrin
64 The majority of proapoptotic activity is arginine-glycine-aspartic acid (RGD)-independent and req
66 d three to four times more adenovectors with arginine-glycine-aspartic acid (RGD)-modified fiber prot
67 re then biochemically functionalized with an arginine-glycine-aspartic acid (RGD)-terminated thiol.
68 ls (hMSC) spheroids in alginate and alginate-arginine-glycine-aspartic acid (-RGD) microgel was demon
69 n, as well as engineered peptides containing arginine-glycine-aspartic acid sequences and the disinte
70 diacrylate bioinks containing cell adhesive Arginine-Glycine-Aspartic acid-Serene (RGDS) peptide and
71 apoptotic cells, nor the tetrapeptide RGDS (arginine-glycine-aspartic acid-serine) blocked ingestion
72 y or protein content, whereas GRGDS (glycine-arginine-glycine-aspartic acid-serine)-pentapeptide (whi
73 d emission (AIE) characteristic, with cyclic arginine-glycine-aspartic acid tripeptide (cRGD), a targ
74 s, degradable constructs containing VEGF and arginine-glycine-aspartic acid tripeptide induced a sign
75 ro by cell attachment to the high density of arginine-glycine-aspartic acid tripeptide present in DAP
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