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However, the utility of these binding screens is compromised by several technical difficulties.
While these probes could be used in competitive binding screens for substrate phosphorylation site inhibitors of PKA or Pim-1, this application has not been reported.
An alternative technology that has received attention from several laboratories, including our own, is to employ simple protein binding screens and libraries of bead-displayed compounds.
While the most common technologies today employ various types of functional screens using compounds formatted in the wells of microtiter plates, an alternative and far more economical approach is to carry out binding screens with one bead one compound (OBOC) libraries created by solid-phase split and pool synthesis.
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Compounds selected from Aβ-RAGE binding screening displayed inhibitory activity on Aβ transport across BBB.
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.
Based on these evidences our aim was to identify small molecules able to modulate EphA2-ephrinA1 activity through an ELISA-based binding screening.
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.
After three rounds of selection followed by a binding screen by phage ELISA, four unique sAB clones were identified.
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