Thus, both ChIP-chip analysis and chromatin binding assay suggest that Pcs1 and Mde4 bind tightly to centromeres but not to nucleolar chromatin.
The results of the acyl-CoA profiling and binding assay suggest that AtACBP6 plays a major role in maintaining the cytosolic acyl-CoA pool during seed and seedling development; this is supported by its strong expression in the embryo and seedling as demonstrated using AtACBP6pro:: GUS transformants.
These data, together with the DNA binding assays, suggest that USF-1 regulates both basal and AICAR-induced PGC-1α promoter activity.
Taken together, these protein:protein binding assays suggest that TAF7L can physically associate with both PPARγ and TBP/TFIID either directly or indirectly via presently unidentified protein factors.
The combined results of potassium efflux and sequential binding assays suggest that the biological role of Halα involves binding to its target, resulting in a complex that serves as a docking site for Halβ to bind and form pores.
Importantly, unlike brain homogenates from mice injected with PBS, brain homogenates from mice injected with MSA and iLBD patient brain extracts were able to seed alpha-synuclein aggregation in vitro as determined by ThT binding assays, suggesting that these mouse brains contained abnormal misfolded alpha-synuclein that was seeding competent.
In addition, studies on the effect of phosphorylation on the autoinhibitory conformation of NHERF-1 by solution SAXS and binding assays suggest that this conformation could be disrupted by protein kinase C (PKC) phosphorylation at Ser-339 and Ser-340 in the C-terminal domain of NHERF-1.
Among the top APE1-active compounds identified in the initial HTS, WB 64 and mitoxantrone (representative plot shown in Figure 4B, right) were positive in the DNA-binding assay, suggesting that they likely act as non-competitive inhibitors (summarized in Figure 3).
