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Obvious candidates are the KDM2A and CFP1 proteins since genome-wide binding data reveals that they bind also to some extent outside of CGIs (66% of KDM2A and 7.4% of Cfp1 clusters do not overlap with a CGI [ 11, 12]).
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[H]palonosetron binding data revealed that binding affinities and functional responses were unaltered in these modified 5-HT3AB receptors.
Comparison of the CD spectra in Figure 4 to the thermostability binding data revealed that the change in the CD spectrum observed between 25°C and 65°C reflected the structural changes underlying the complete loss of [H]ZM241385 binding by the A2AR.
Five out of the seven selected amino acids for p260 and p263, respectively, displayed binding to Aq and the SAR analysis of the Aq glycopeptide binding data revealed structural elements within the modified amino acids that were important for binding.
Cell binding data revealed significant better binding properties of the dimer (IC50 = 3.9 ± 1.8 nM; IC50 (monomer) = 12.1 ± 2.1 nM).
Bioinformatic analysis of the data reveals that clustered binding sites, spanning a broad range of affinities, best predict occupancy in cells.
Collectively, this data reveals that cyclin binding to PTP1B facilitates its direct phosphorylation by Cdk1 on serine 386.
Complex 2 exhibits moderate G-quadruplex binding and stabilizing ability, while CD titration data reveals that complex 2 could promote the formation of parallel G-quadruplex structure.
The data reveals that helix D stabilizes CaM binding, promoting trans-binding (CaM embracing neighboring subunits), and they suggest that the ABCD domain can be exchanged between subunits of the tetramer.
Our analysis of proteomic data reveals that fibronectin is heavily phosphorylated in cancer tissues particularly within its growth factor binding sites and on domains that regulate fibrillogenesis.
This data reveals that regulatory regions within the human β-globin DNA contain preferred nucleosome-binding sites as reflected by the in vitro binding profile.
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