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While Nrf2 was incapable of binding to HepcARE on its own, MafG homodimers bound to this element.
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The TF-A gene incorporates a TF-RE, and when homodimers bind to this element, TF-A transcription is increased.
Lutterbach et al. found that p21 WAF1 promoter contains three putative RUNX-binding sites and the proximal element is required for the downregulation of p21 WAF1 in NIH3T3 cells, indicating that RUNX2 directly binds to this element and thereby reducing p21 WAF1 expression.
Chromatin immunoprecipitation (ChIP) analysis confirmed that HapX also binds to this promoter element in vivo, notably independent of the ambient iron concentration (Fig 6C).
This sequence, C/T TAA C/T NGCT (N168), was predicted to be a novel transcriptional element but no transcription factor has yet been identified which binds to this element.
We provide biochemical data to support the notion that ΔNp63 can bind to this element both by EMSA and ChIP experiments and that all three isoforms of ΔNp63 can induce K5 when ectopically expressed, thus confirming that K5, similar to its partner K14, is a direct transcriptional target of ΔNp63.
TTP could bind to this element as well as to the TNF-α ARE.
It is possible that estrogen receptor α can bind to this element in hTERT promoter and then activate hTERT transcription (Kyo et al. 1999; Misiti et al. 2000).
Chromatin immunoprecipitation (ChIP) assay revealed that both sublytic C5b-9-induced IRF-1 and overexpressed IRF-1 by using pEGFP-N1/XAF1 could bind to this element.
Kumari et al. identified a protein called Ybx1 that could bind to this element: this protein may help to correctly position RNAs in many other organisms, including fruit flies and mammals.
Curiously, however, chick FOXD3 does not bind to this element, at least in vitro; rather, its repressive activity comes about by a mechanism that is independent of DNA binding.
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