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1 in precursor, an arrangement common to other knottins.
2 mice by small animal CT, and both 64Cu-DOTA-knottin 2.5F and FDG were able to differentiate lung nod
3 Collectively, these results show 64Cu-DOTA-knottin 2.5F to be a promising candidate for clinical tr
7 ial peptides (e.g., defensins, thionins, and knottins), alkaloids, nonproteogenic amino acids, and ph
12 based dimerization strategy was critical, as knottin dimers created through genetic fusion to a bival
14 o contains a region homologous to the TAXI-1 knottin domain; however, a deletion in this domain restr
15 complexity from simple to highly elaborated knottin domains, as well as double-knot toxins, that lik
19 us to natural cysteine-rich peptides such as knottins in that it is small and stable but can accommod
24 cantly higher after the administration of MB-Knottin(Integrin) than after the administration of MB(al
25 blocking of integrins, the attachment of MB-Knottin(Integrin) to alpha(v)beta(3) integrin-positive c
26 ging contrast agent was created by attaching Knottin(Integrin) to the shell of perfluorocarbon-filled
27 aging signals after the administration of MB-Knottin(Integrin) were not significantly different in th
32 ize dimers of integrin-binding cystine knot (knottin) miniproteins with low-picomolar binding affinit
33 s introduced at different locations within a knottin monomer and reacted with dialdehyde-containing c
37 e/gram (%ID/g), compared with a low-affinity knottin peptide (IC(50), approximately 0.4 mumol/L; 1.48
40 decane-N,N',N'',N'''-tetraacetic acid (DOTA)-knottin peptide that targets integrins upregulated durin
44 with a fluorescent, engineered cystine knot (knottin) peptide that binds with high affinity to alphav
45 a small, disulfide-constrained cystine knot (knottin) peptide that bound to alpha(v)beta(3) integrins
46 pared with other engineered integrin-binding knottin peptides and with c(RGDfK), a well-studied integ
50 usly, we used directed evolution to engineer knottin peptides that bind with high affinity ( approxim
51 is work expands the therapeutic relevance of knottin peptides to include targeted drug delivery, and
52 roximately 20 nmol/L) (64)Cu-DOTA-conjugated knottin peptides was 4.47% +/- 1.21% and 4.56% +/- 0.64%
57 3.0 A) and the antifungal protein Rs-Afp1 [a knottin protein from radish (Raphanus sativus), rmsd of
58 bility to inhibit binding of a biotinylated "knottin"-RGD peptide to surface-immobilized integrins an
59 ers, such as integrin-immobilization levels, knottin-RGD concentration, buffer compositions, type of
60 near GRGDS, (ii) cyclo[RGDfK], and (iii) the knottin-RGD itself for binding to three different integr
65 cysteine residues forming a disulfide-bonded knottin scaffold that creates a contiguous solvent-acces
68 The binding of MB-Knottin(Integrin) and MB-Knottin(Scrambled) to alpha(v)beta(3) integrin-positive
71 upting cell membranes; and 3) disulfide-rich knottins similar to those that dominate spider venoms.
72 h peptides, and we show that 15 of these are knottins that contribute >90% of the venom proteome.
73 nd validation of a new cystine knot peptide (knottin) that selectively recognizes human integrin alph