ライフサイエンスコーパス: arginine-glycine-aspartic acid

1 Arginine-glycine-aspartic acid affinity chromatography o

2 and alginate-graft-poly(ethylene glycol)-S-S-arginine-glycine-aspartic acid (Alg-g-RGD).

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

5 Here, an arginine-glycine-aspartic acid-based peptidomimetic libr

6 ate that the interaction of cathepsin Z with arginine-glycine-aspartic acid-binding integrins, specif

7 RGD (arginine-glycine-aspartic acid) blocking peptides induce

8 Osteopontin is an arginine-glycine-aspartic acid-containing cell adhesion

9 signaling from the previously characterized arginine-glycine-aspartic acid-containing peptide.

10 with a conformationally-constrained, cyclic arginine-glycine-aspartic acid (cRGD) to enable highly s

11 l positions are functionalized with a cyclic arginine-glycine-aspartic acid (cRGD) tripeptide for tar

12 (alphav, alpha5, beta1, beta3) that use RGD (arginine-glycine-aspartic Acid)-dependent mechanisms for

13 ntegrins alpha(v)beta3 and alpha(v)beta5 are arginine-glycine-aspartic acid-dependent adhesion recept

14 grin-binding functional peptide ligand, Fmoc-arginine-glycine-aspartic acid (Fmoc-RGD) into a nanofib

15 protein penton contains a well characterized arginine-glycine-aspartic acid integrin-binding domain t

16 ic nano-blockers proportionately disconnects arginine-glycine-aspartic acid ligand-to-ligand intercon

17 e designed to mimic the tripeptide sequence (arginine-glycine-aspartic acid) of the natural ligands;

18 grin receptors bind to adhesion ligand (e.g. arginine-glycine-aspartic acid or RGD containing peptide

19 articles, surface functionalized with cyclic arginine-glycine-aspartic acid peptide ligands and radio

20 Application of arginine-glycine-aspartic acid peptide loops prevented t

21 Preincubation with a cyclic arginine-glycine-aspartic acid peptide or fibronectin-bl

22 Pretreating kidney sections with cyclic arginine-glycine-aspartic acid peptide resulted in incre

23 ifference between adhered cells under cyclic arginine-glycine-aspartic acid peptide-treated and contr

24 ane modified with a covalently attached RGD (arginine-glycine-aspartic acid) peptide sequence.

25 ntisense oligonucleotide and a bivalent RGD (arginine-glycine-aspartic acid) peptide that is a high-a

26 n this study, we report the efficacy of RGD (arginine-glycine-aspartic acid) peptide-modified polylac

27 divalent cation independent, not blocked by arginine-glycine-aspartic acid peptides and still mediat

28 S with the high-affinity amino acid sequence arginine-glycine-aspartic acid-phenylalanine-cysteine (R

29 [acetic acid]-7-[2-glutaric acid] and RGD is arginine-glycine-aspartic acid.) RESULTS: alphavbeta3 in

30 Results with an Arginine-glycine aspartic acid (RGD) peptide and monoclo

31 Pre-coating dentin slices with short arginine-glycine aspartic acid (RGD) peptides, but not a

32 becoming cell-adhesive through exhibition of arginine-glycine-aspartic acid (RGD) adhesion peptides u

33 with these receptors via a highly conserved arginine-glycine-aspartic acid (RGD) amino acid sequence

34 mational plasticity and accessibility of the arginine-glycine-aspartic acid (RGD) binding site in FN,

35 use of GP IIb/IIIa antagonists based on the arginine-glycine-aspartic acid (RGD) cell-recognition se

36 Cyclic arginine-glycine-aspartic acid (RGD) containing peptides

37 c phthalocyanine with acetylenic bombesin or arginine-glycine-aspartic acid (RGD) derivatives, either

38 tracellular matrix protein, has a functional arginine-glycine-aspartic acid (RGD) domain for binding

39 2Y(2)R) contains the integrin-binding domain arginine-glycine-aspartic acid (RGD) in its first extrac

40 Previously, we found that an arginine-glycine-aspartic acid (RGD) integrin binding do

41 We used an array of peptidic and nonpeptidic arginine-glycine-aspartic acid (RGD) mimics that specifi

42 ptor, generally alphavbeta6, via a conserved arginine-glycine-aspartic acid (RGD) motif in the expose

43 Human parechovirus 1 (HPEV1) displays an arginine-glycine-aspartic acid (RGD) motif in the VP1 ca

44 le amino acid substitution within an encoded arginine-glycine-aspartic acid (RGD) motif of the molecu

45 eal preferential binding of ChAdOx1's penton arginine-glycine-aspartic acid (RGD) motif to the activa

46 which is demonstrated by incorporation of an arginine-glycine-aspartic acid (RGD) motif, resulting in

47 o peptides and peptidomimetics containing an arginine-glycine-aspartic acid (RGD) motif.

48 Targeting peptides of cyclic arginine-glycine-aspartic acid (RGD) motifs were install

49 se required a selective interaction of virus arginine-glycine-aspartic acid (RGD) motifs with macroph

50 The arginine-glycine-aspartic acid (RGD) peptide sequence is

51 ere introduced using a ketone-functionalized arginine-glycine-aspartic acid (RGD) peptide to modify t

52 by local administration of echistatin or an arginine-glycine-aspartic acid (RGD) peptide, agents kno

53 of anti-alpha4 and -alpha5 antibodies and an arginine-glycine-aspartic acid (RGD) peptide, while the

54 These nanoparticles are conjugated with arginine-glycine-aspartic acid (RGD) peptides (CGNP clus

55 Among these, arginine-glycine-aspartic acid (RGD) peptides have shown

56 demonstration of a renoprotective effect of arginine-glycine-aspartic acid (RGD) peptides in acute r

57 yanate (FL) and alphaVbeta3-specific, cyclic arginine-glycine-aspartic acid (RGD) peptides, will bind

58 ng commercially available PEG-coated QDs and arginine-glycine-aspartic acid (RGD) peptides.

59 Gylated surface decorated with two different arginine-glycine-aspartic acid (RGD) peptides: one is cy

60 ds to cell-surface integrin molecules via an arginine-glycine-aspartic acid (RGD) sequence in capsid

61 nt conformation beta5/beta3 integrins and an arginine-glycine-aspartic acid (RGD) sequence in the fir

62 exes react to bond the cell-adhesive peptide arginine-glycine-aspartic acid (RGD) to the polymer surf

63 he integrin alpha(v)beta3 interacts with the arginine-glycine-aspartic acid (RGD) tripeptide recognit

64 robalance (QCM) gold electrode surface using arginine-glycine-aspartic acid (RGD) tripeptide was elec

65 interface where the cell adhesion tripeptide arginine-glycine-aspartic acid (RGD) was presented to th

66 Arginine-glycine-aspartic acid (RGD)-based imaging trace

67 superfamily that mediates cell attachment on arginine-glycine-aspartic acid (RGD)-containing adhesive

68 the addition of an integrin-receptor-binding arginine-glycine-aspartic acid (RGD)-containing peptide

69 vitro compared with hydrogels modified with arginine-glycine-aspartic acid (RGD)-containing peptides

70 ted by incubation with soluble uPAR (suPAR), arginine-glycine-aspartic acid (RGD)-containing peptides

71 sults demonstrate that in the presence of an arginine-glycine-aspartic acid (RGD)-containing syntheti

72 r specificity of novel peptide-dye conjugate arginine-glycine-aspartic acid (RGD)-Cy5.5 as a contrast

73 s initiated by binding to certain species of arginine-glycine-aspartic acid (RGD)-dependent integrin

74 The majority of proapoptotic activity is arginine-glycine-aspartic acid (RGD)-independent and req

75 Arginine-glycine-aspartic acid (RGD)-mimetic platelet in

76 d three to four times more adenovectors with arginine-glycine-aspartic acid (RGD)-modified fiber prot

77 re then biochemically functionalized with an arginine-glycine-aspartic acid (RGD)-terminated thiol.

78 ls (hMSC) spheroids in alginate and alginate-arginine-glycine-aspartic acid (-RGD) microgel was demon

79 n, as well as engineered peptides containing arginine-glycine-aspartic acid sequences and the disinte

80 diacrylate bioinks containing cell adhesive Arginine-Glycine-Aspartic acid-Serene (RGDS) peptide and

81 apoptotic cells, nor the tetrapeptide RGDS (arginine-glycine-aspartic acid-serine) blocked ingestion

82 y or protein content, whereas GRGDS (glycine-arginine-glycine-aspartic acid-serine)-pentapeptide (whi

83 d emission (AIE) characteristic, with cyclic arginine-glycine-aspartic acid tripeptide (cRGD), a targ

84 s, degradable constructs containing VEGF and arginine-glycine-aspartic acid tripeptide induced a sign

85 ro by cell attachment to the high density of arginine-glycine-aspartic acid tripeptide present in DAP

86 d with polyethylene glycol chains and cyclic arginine-glycine-aspartic acid-tyrosine peptides (cRGDY-