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To elucidate its molecular mechanism, in vitro kinase binding assays were carried out, which demonstrated that derivative 7 inhibited aurora kinases A and B selectively.
In vitro solid-phase radiolabeling binding assays were carried out to check whether labeling altered the galectin-3 structure and to confirm the ability of IG3 to bind to ECM targets.
The binding assays were carried in a volume of 100 µL.
Competition binding assays were carried out on crude membranes at 200 pM 125I-MLT and increasing concentrations of melatonin.
125I-insulin binding assays were carried out at 12°C on cells from 16-h fasted mice to analyze cell surface binding in the absence of internalization.
DNA-protein binding assays were carried out with nuclear extract from SALL4B transfected HeLa cells prepared with Nuclear Extract kit (Active Motif) according to manufacturer's instructions.
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DNA-binding assays were carried out using nuclear extracts isolated from cells in the log phase of growth.
This discrepancy is likely due to our SPR binding assays being carried out with monomeric Fz4CRD.
Liposome-binding assays were carried out as described previously [45].
RNA-binding assays were carried out as described previously (Hautbergue et al., 2008, 2009).
RNA-binding assays were carried out as described previously [ 12, 13].
More suggestions(16)
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binding assays were substituted
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