Sentence examples for binding of the heterodimer from inspiring English sources

With this technique, the dissociation constant for the Ubc13-Uev1 interaction was 1.0×10−9 M, indicating a high-affinity binding of the heterodimer, with values close to those reported by isothermal titration calorimetry [40] that are expected to require high affinity binding by any potential competitor.

This, in turn, inhibits binding of the heterodimer to DNA.

Polycyclic aromatic hydrocarbons activate Nrf2 transcription through binding of the heterodimer formed by the aryl hydrocarbon receptor (AhR) and the AhR nuclear translocator to xenobiotic response element-like sequences in the Nrf2 promoter [ 41].

In this situation, the subunit that does not bind DNA alone could be annotated to appropriate 'sequence-specific DNA binding' terms using the qualifier 'contributes_to' to indicate that it contributes to the DNA binding of the heterodimer.

In addition, we hypothesized that LG268, as a ligand for RXR, may also induce increased binding of the heterodimer to the DR-1 site and that combination treatment with both ligands would further increase binding to the DR-1 site since both NHRs would be liganded.

While we clearly observed binding of the hPPARα hLXRα heterodimer to DNA, previous experiments have suggested that the heterodimer of mouse PPARα (mPPARα) and hLXRα is incapable of binding DNA.

This binding of the PPARα LXRα heterodimer was compared to the binding of the respective RXRα heterodimer to the same sequences in the presence of LCFA.

Because binding of the hPPARα hLXRα heterodimer to this PPRE sequence was weak, the effect of the hPPARα hLXRα heterodimer on PPARα transactivation may not be as significant as the effect of the hPPARα hRXRα heterodimer.

Because previous studies examined the binding of the mPPARα hLXRα heterodimer to a rat PPRE and this work examined binding of the hPPARα hLXRα heterodimer to a human PPRE, this may explain some of the observed differences.

In contrast, the presence of LCFA or T0901317, a known LXRα agonist, decreased the level of binding of the PPARα LXRα heterodimer to the LXRE from the SREBP-1c promoter, possibly because of weakened heterodimer interactions.

EPA and DHA have been shown to regulate SREBP1c expression by inhibiting binding of the LXR/RXR heterodimer to the LXREs in the SREBP-1c promoter.