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. 2019 Nov 28;7:822. doi: 10.3389/fchem.2019.00822

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Copyright © 2019 Dorman, Close, Wingert, Camacho, Johnston and Smithgall.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Selective activation of near-full-length Hck by allosteric modulators in vitro. Recombinant, near-full-length Hck (A) and Fgr (B) were assayed for kinase activity using the Z'Lyte kinase assay over the range of input kinase protein amounts shown. Assays were performed in the absence (None) or the presence of each of hit compound (1 through 4 at a final concentration of 50 μM). Each data point was assayed in quadruplicate, and is shown as percent of maximum substrate peptide phosphorylation ± SD. The activation curves were fit by non-linear regression analysis, and the resulting EC₅₀ values ± S.E. are summarized in the tables at right.