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Rather, results from the EMSA experiment suggest a mechanism by which the attB sequence interferes with virus assembly and could be related to the binding of a nuclear protein to this sequence.
Genomic activation is defined as the binding of a nuclear receptor to a response element, which activates the transcription of certain genes.
The specific binding of a nuclear factor or complex (MIF) to a cis-acting sequence motif present in this region (MEE2) corroborates this hypothesis and suggests an important role for this DNA protein interaction in mutually exclusive promoter activation.
Oct-1 might activate the epithelial- specific HPV16 enhancer by stabilizing the binding of a nuclear factor to the composite element, which in turn results in higher levels of enhancer activity[ 33].
The EMSA assay was also inconclusive: one out of the three functional sites determined by luciferase assay showed no evidence of binding of a nuclear protein, which may be due to a the protein requiring a longer binding site than the probe provided, or non-physiological binding conditions.
In order to correctly report to a referring clinician whether or not an identified promoter variant is likely to be FH-causing, bioinformatics predictions may be helpful, and although evidence that the variant affects binding of a nuclear protein by an EMSA may be suggestive, an in-vitro assay of the effect on transcriptional strength provides the strongest evidence.
Similar(54)
For example, phosphorylation of β-catenin at Tyr654 results in its dissociation from E-cadherin [16] and phosphorylation at Tyr142 acts as a switch that disrupts its binding to α-catenin and promotes binding of BCL9-2, a nuclear co-factor, resulting in increased transcription of Wnt-target genes [13].
In our analysis of FXR binding to hepatic chromatin, we showed that LRH-1 could function as a partner transcription factor for FXR on a small set of target genes through binding to a nuclear receptor half-site that was co-enriched with the FXR IR-1 element on a genome-wide scale [ 14].
The AP-2 binding site (GCTGCAGGC) at -213 to -221 was originally identified as a DNase I footprinted site that was protected by nuclear extracts from ERBB2 over-expressing cells (but not those with low expression), indicating differential DNA-binding activity of a nuclear factor, which was termed OB2-1.
These included various domains of metabolic enzymes such as serine-threonine phosphatase, polysaccharide deacetylase, and oxidoreductase and domains of structural proteins such as axonemal dynein light chain, proteasome subunit A, conserved membrane protein, and ligand-binding domain of a nuclear hormone receptor.
In nuclear polyadenylation, binding of the nuclear poly(A) binding protein, PABP2, is required to limit the length of the poly(A) tail.
More suggestions(16)
binding of a multimeric
binding of a different
binding of a monomeric
binding of a molecular
binding of a basic
binding of a ferrocene
binding of a certain
binding of a second
binding of a fatty
binding of a respective
binding of a biotinylated-BH4-BCL2
binding of a PPARα-RXRα
binding of a specific
binding of a nucleotide
binding of a large
binding of a forthcoming
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