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Based on these evidences our aim was to identify small molecules able to modulate EphA2-ephrinA1 activity through an ELISA-based binding screening.
Compounds selected from Aβ-RAGE binding screening displayed inhibitory activity on Aβ transport across BBB.
In this study, we employed a two-step aptamer selection strategy, comprised of a recombinant protein-based selection from the library followed by a cell-based binding screening for the selection of a thioaptamer to E-selectin.
Taken together, the streamlined yet powerful fsPAG-EMSAs offer a promising platform for rapid binding reaction analyses and support a molecular binding screening assay in a quantitative, high-throughput, and reliable manner.
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To identify interacting partners of the Xenopus FLRT3 ectodomain, we performed a cell surface binding screen [15].
Through a cell surface binding screen for FLRT3 partners, we identified Unc5B and Unc5D as high-affinity FLRT3 interactors.
In addition, a standardized receptor binding screen conducted with LM11A-31 (Cerep panel, Table S1) failed to detect binding of p75NTR ligands to other receptors.
However, the utility of these binding screens is compromised by several technical difficulties.
After three rounds of selection followed by a binding screen by phage ELISA, four unique sAB clones were identified.
Recently, a DNA-ligand binding screen has led to the identification of three Z-box binding factors, ZBF1/MYC2, ZBF2/GBF1 and ZBF3/CAM7 [ 28- 33].
In the multi-receptor binding screen, pIC50 values for ZD4054 at ETA were 22, 27 and 13 n M (mean value 21 n M) (Table 1).
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