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In a pairwise interaction assay, these three proteins do not interact with any other Gerbera MADS domain proteins.
DOI: http://dx.doi.org/10.7554/eLife.00220.011 Next, we performed a qualitative interaction assay to determine whether agrin can interact independently with the APP ectodomain.
We assessed the ability of the R492L mutant and wild-type CDC25B to interact with the substrate using an AlphaLISA-based protein protein interaction assay.
Moreover, the interaction assay in yeast clearly indicated that APIP12 employed different domains to interact with AvrPiz-t and APIP6, providing a clue of the connection among these 3 proteins.
To further identify the domain of NO66 that interacts with the activation domain of Osx, we performed an in vitro interaction assay using recombinant polypeptides.
BiFC plasmids pRTVnVN-SPIN6, pRTVnVC-OsRac1, and control pRTVcVC-LUC were used for the interaction assay between SPIN6 and OsRac1.
Employing a fluorescence polarization-based interaction assay, we evaluated inhibitory potency of these peptides and selected potent inhibitors.
To identify molecules that might differentiate between these architectures, we employed a fluorescence-based interaction assay to screen a collection of 68 known Aβ ligands against pre-formed oligomers and fibrils.
was screened using the Heme Interaction Assay.
After screening with the yeast two-hybrid interaction assay, we had identified 14 candidates.
An ELISA-based protein-protein interaction assay was utilized for p53- and NTD125 interaction studies.
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