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Binding experiments confirmed that benzo[h]-[1,6]naphthyridine ligands selected by this VS approach exert high affinity for both H3 and 5-HT4 receptors.
Our binding experiments confirmed that the ICS of DSG2 links the molecule to other desmosomal components.
Our heparin binding experiments confirmed that Norrin shows high affinity interaction with heparin, consistent with previous studies (Perez-Vilar and Hill, 1997; Xu et al., 2004; Smallwood et al., 2007; Ohlmann et al., 2010), and further demonstrated Norrin Fz4CRD complex binding to heparin.
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Independent competition binding experiments confirm that TIP47 interacts with the membrane-proximal portion of the CI-MPR cytoplasmic domain.
Receptor binding experiments confirmed binding of these ligand peptides to their receptors in vitro.
The subsequent mutagenesis and binding experiments confirmed the predicted binding pose.
While the LNA binding experiments confirmed the existence of all helices unique to the SHAPE-directed model, the formamide denaturation and in virio experiments showed that some of these helices are relatively unstable.
The bioinformatics analysis of the RIG-I sequence, as well as RNA binding experiments, confirm previous findings [1] indicating that this molecule belongs to the DExD/H RNA helicase family.
DSC and thermal melting experiments confirmed that the binding resulted in strong thermal stabilization.
In addition, ANS, UV vis and RLS experiments confirmed that GA binding causes a certain structural changes in BSA.
Immunocytochemistry experiments confirmed that VEGF binding was also inhibited by the 6a-P peptide.
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