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Molecular docking studies and competitive binding assay indicated that 5m effectively bind at the colchicine binding site of the tubulin.
The in vitro binding assay indicated that several compounds are potent selective V2 receptor antagonists.
A Congo-Red binding assay indicated that these aggregates did not contain any fibrillar structures.
The direct binding assay indicated that full length CXCR2-CTD (residues 311 355) and the first half of the CXCR2-CTD (311 330) fused to GST had the ability to bind to LASP-1, but surprisingly the second half of the CXCR2-CTD (331 355) was devoid of any direct binding activity (Figure 3C).
The result of binding assay indicated that full-length TLS protein were likely to interact with all the fragments investigated (Fig. 1b), though it showed a slight difference in the intensity of the binding.
Prior studies with this binding assay indicated that small molecule regulators of binding needed to be present while proteins were incubated to form complexes, as well as in the nondenaturing gels and electrophoresis buffer used to resolve the complexes.
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In vitro binding assays indicate that P1 directly binds the Zmf3' h1 promoter.
The ThT fluorescence binding assay indicates that the synthetic compounds can inhibit Cu II -induced Aβ1–42 aggregation.
Furthermore, DNA retardation occurred (Figure 6b) when the promoter of the simReg1 gene was used in the binding assay, indicating that SimReg1 is an autoregulatory protein.
Peptides that inhibit this interaction in an in vitro binding assay indicate that two conserved Ile-Pro-Val regions of BAG3 are involved in the interaction with αB-crystallin, which is similar to results showing BAG3 binding to HspB8 and HspB6.
The results of the binding assay indicate that the CHASE domain is the cytokinin binding domain of CRE1/AHK4.
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