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Overall, these results indicate that PPARα and PPARγ bind to multiple PPREs in the megalin promoter, which supports our observations of activated megalin expression in the various model systems treated with PPAR agonists.
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Thus, saccharides with multi-cis-diols will bind to multiple PBA molecules.
Of these sequences, 62 contained nonamers predicted to bind to multiple HLA supertypes.
As targeting only requires partial complementarity, a single miRNA can bind multiple mRNA transcripts and each mRNA can be bound to multiple miRNAs.
Considering that PPARα-tr variant does not bind to PPREs and does not act in a dominant negative fashion on the full-length receptor, we hypothesized that PPARα-tr exerts its inhibitory functions via crosstalk to other direct regulators of these genes.
Electrophoretic mobility shift assays were used to determine whether the hPPARα hLXRα heterodimer could bind to either PPRE or LXRE sequences.
It seems that in mice fed on HFHC diet, in spite of a significant increase in the PPARγ expression levels, this nuclear receptor seems to be unable to efficiently bind to the PPRE site in the SCARB1 gene.
Thus, Gli2 binds directly to multiple sites located up- and downstream of the Ascl1 gene.
Following ligand binding, PPARs form heterodimers with retinoid X receptors (RXRs), and bind to PPAR-response elements (PPREs) of target genes to activate transcription [2].
An ad hoc host molecule is tailored to bind to glucose by multiple hydrogen bonds.
PPARγ forms heterodimers with RXRα, which specifically bind to PPAR response elements (PPREs).
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