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The capacity of PIK-75 to bind to a panel of 451 human kinases was determined by analyzing the binding interaction compared with DMSO (=100%).
The TCR specificity was then examined by analyzing the binding of peptide HLA-A2/tetramer in an ELISA assay.
A series of L-shaped ortho-quinone analogs were designed by analyzing the binding mode with NQO1.
A series of JMJD2A inhibitors had been designed by analyzing the binding mode of 5-carboxy-8-hydroxyquinoline (5-carboxy-8-HQ) with JMJD2A.
Based on the scaffold of 3,7,8-trimethylnaphtho[1,2-b]furan-4,5-dione, a series of L-shaped derivatives with substituted side chains at the position of C2 were designed by analyzing the binding mode with NQO1.
We validated this inhibitor design by comparing its structure-activity relationship (SAR) with that of corresponding indole derivatives, by analyzing the binding mode with X-ray crystallography and by evaluating its thermodynamic binding parameters.
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Pico- to nanomolar affinities were measured by analyzing the resultant binding curves with BiaEvaluation software.
We validated the ChIP findings by analyzing the p53-binding sites at the canonical p53 target CDKN1A (p21waf).
We then addressed the molecular mechanisms underlying the scFvs anti-proliferative activity by analyzing the scFvs-binding epitopes of E7.
The overall quality of the model is given by ERRAT score 24 of 98.519 by analyzing the non-binding interaction between different atom types.
We investigated the evolutionary processes underlying the relationship between each TF and its target gene by analyzing the TF-binding sequences at a genome-wide level.
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