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Therefore, no PEL phenotypes were expected to arise from the cooperative or competitive binding of different TRs.
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In summary, we showed the equilibrium binding of TR to different regulatory elements present in the TSHβ promoter, providing a catalogue of binding affinities of TR and GATA-Zf to several enhancer elements.
The brain has abundant nuclear T3-binding sites and contains messenger RNAs (mRNAs) encoding multiple thyroid hormone receptor (TR) isoforms; the cellular distribution of these different TR isoforms is unknown.
We also downsampled in terms of the TRs and then generated image sequences using different TRs.
Importantly, these results indicate that TR complex formation enhances DNA binding of the TR-GATA2 in a ligand-dependent manner.
Interestingly, there are multiple PDB structures for a single TR/pMHC complex, showing different TR binding angles, where we have tested the validity of our inverse relationship between calculated BE and θ. 2f54 and 2bnr (PDB code; bold in Table S1) form one such pair.
Similarly, we analyzed binding of a GST-TR fusion to the predicted binding sites of these T3 responsive genes.
We observed that the ligand T3 weakens the binding of TR to NRE present in TSHβ promoter.
Also, the 4 nucleotides between the direct repeats may have an important role for the binding affinity of TR, since they were different from the short DR4 we studied here.
This indicates that the TR-DBD is not sufficient for enhancer blocking and that other domains outside the DNA binding domain of TR are needed as well to mediate enhancer blocking of the CTCF bound module and the unliganded TR.
Other possible interactions of PCBs and TR-DBD would be masking of the PCB-binding region of TR by corepressors and/or alteration of the TR-DBD conformation by PCBs binding or recruitment of a "PCB-responsive TR-binding protein".
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