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The ability of a transcription factor to recognize and bind to specific elements in a promoter/enhancer is an essential step in transcription regulation.
Androgen effects are classically exerted through binding of the hormone to intracellular specific receptors [ 18, 19], which consequently dimerize, translocate to the nucleus and bind to specific elements of DNA, affecting thus the transcription of androgen-responsive genes [ 14].
The Nrd1 and Nab3 proteins bind to specific elements in nascent transcripts (Creamer et al. 2011; Jamonnak et al. 2011; Wlotzka et al. 2011) and can direct termination of transcription for snoRNAs, snRNAs, some mRNAs, and numerous intergenic transcripts (Arigo et al. 2006; Thiebaut et al. 2006; Carroll et al. 2007; Rondon et al. 2009; Kim and Levin 2011).
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The heterodimer complex binds to specific elements in the DNA known as retinoic acid response elements (RARE) in the promoter region of the genes that are regulated by that specific retinoid thus regulating the transcriptional activity of that retinoid-responsive gene.
Moreover, Totary-Jain et al. reported that CRT also binds to specific element in 3′-UTR of glucose transporter-1 mRNA and destabilizes the mRNA under high-glucose conditions [ 58].
Like most other members of this family, TRs bind to specific DNA elements called T3 response elements or TREs and regulate target genes bearing such elements in a ligand-dependent manner.
BMPs belong to the TGF (transforming growth factor) superfamily which, upon binding to their cognate receptors, activate phosphorylation of Smad proteins, which in turn bind to specific promoter elements and regulate gene transcription.
Transcriptional activators bind to specific sequence elements in genes and initiate the recruitment of the molecular machines needed to decondense chromatin and activate transcription.
Gene expression is regulated at the transcriptional level by a variety of trans-acting factors that bind to specific promoter elements to elicit transcription initiation in response to intra- and extra-cellular signals.
However, DM segregation was not affected by disruption of the telosome nucleoprotein complex and DMs readily migrated from human to murine chromatin in human/mouse cell hybrids, indicating that they do not bind to specific positional elements in human chromosomes.
They either act as ligand-activated transcription factors that bind to specific response elements located on the promoters of target genes, or by tethering to transcription factor complexes that contact DNA at alternative sites [9], [10].
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