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This mutation leads to the destruction of the guanosine triphosphate-binding site and results in a catalytically inactive enzyme that can nevertheless bind to downstream elements of the signalling pathway.
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The role of Lrp4 as an antagonist of canonical Wnt signaling pathway is thought to be mediated in part by a displacement of the homologous Lrp5/6 proteins in the co-receptor complex formed by frizzled proteins (fzd) with Lrp5/6, which is required to bind Wnt proteins and to transduce the Wnt signal to downstream elements of the canonical cascade.
Clearly, these genes are poor due to downstream elements or global features.
Heterogeneous nuclear ribonucleoprotein 1 (HRP1) may be a marker protein that binds to the downstream element of the nonsense mutation and interacts with NMD factors [12].
However, if HvHOX2 and VRS1 still share the same target DNA sequence and retain the same level of affinity, it is possible that VRS1 competes with HvHOX2 to bind to cis-elements of downstream genes.
Proteins that bind to these elements remain to be isolated.
Thus, RARs bind to conserved elements in the Meox1 and Pax3 genes as well as to one non-conserved element upstream of Wnt3a in a population of differentiating P19 cells, indicating that RA functions both upstream and downstream of Wnt3a signalling.
GT proteins specifically bind to GT elements, and the elements are highly degenerated.
The spacing between the cis elements determines the interactions between DBTFs that bind to those elements.
Heterodimers bind to TH response elements (or T3 responsive element; TRE) in target genes.
The active GTP-bound form of Rac proteins bind to specific downstream effectors and thereby participate in various cellular events.
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