Sentence examples for binding of this factor from inspiring English sources

It can be proposed that mitosis-specific modifications of either NFAT5 or the chromatin, or a repressor protein interacting with NFAT5 in mitosis might disrupt the binding of this factor to DNA.

That exclusion of NFAT5 from mitotic DNA also occurred in hypertonic conditions indicates that binding of this factor to regulatory regions of osmoprotective genes is subject to association/dissociation cycles in proliferating cells and has to be reactivated after mitosis.

A recent ChIP-on-chip study of Pax5/BSAP in B-cell development identified binding of this factor during B-cell development [66] consistent with Pax5/BSAP acting as both a transcriptional activator (56%) and a transcriptional repressor (44% of genes), respectively [67].

The upregulation of Sp-1 transcription by TNF-α appears also to lead to increased binding of this factor to the Sp-1 binding site of the VEGFR-2 promoter region [ 7, 8].

Moreover, the authors demonstrate that the binding of this transcription factor to sequences within the caspase-8 gene sensitizes cells to TNFα or drug-induced apoptosis [ 46].

Whether this effect is mediated by binding of this transcription factor to a specific Egr-1 response element in the promotor region (925 941 bps upstream of the transcription site) of the periostin gene is currently under investigation.

We show specific binding of this element to nuclear factors.

In particular, we demonstrated that migration depends on adhesion related kinase (Axl) gene expression induced by AP-2α following direct binding of this transcription factor to the canonical AP-2 binding sites present on Axl promoter.

To rule out the possibility that this ubiquitous factor is playing a significant role in driving expression in these synthetic constructs, we repeated these experiments using a basal promoter carrying a mutation known to eliminate binding of this ubiquitous factor.

Here we report that the CssB subunit of the CS6 protein confers a specific binding of this colonization factor to a glycosphingolipid present in human and rabbit small intestine.

Thus exposure of RAW264.7 to ritonavir leads to its translocation to the nucleus, an event that is associated with binding of this regulatory factor to its target genes (Figure 7E), This effect was robustly attenuated by CDCA but not by gemfibrozil, indicating that FAXR and PPARα agonists act on different steps of post-translation regulation of CD36.