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The authors found 14% 'non-specific' cases where a primer/probe set can bind to multiple regions in the genome.
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Ttk69 binds to multiple regions in the introns and upstream of duf (Fig. 3V) at the approximate site of the rP298 P-element insertion (Ruiz-Gómez et al., 2000).
Here we present a detailed examination of two divergent examples: 1) p53, which uses different disordered regions to bind to different partners and which also has several individual disordered regions that each bind to multiple partners, and 2) 14-3-3, which is a structured protein that associates with many different intrinsically disordered partners.
Chameleon behavior could be an important feature that enables one disordered region to bind to multiple partners.
What if a region used to bind to multiple partners uses different secondary structures and different amino acids?
Several groups have tested these overall ideas further via bioinformatics studies on collections of hub proteins, and these studies support the common use of disordered regions by hub proteins to bind to multiple partners [ 130- 134].
Using chromatin immunoprecipitation assays, we showed that Gli2 bound to multiple regulatory regions in the Ascl1 gene, including promoter and enhancer regions during Gli2-induced neurogenesis.
The flexible, disordered region may allow CheY6 to bind to multiple ligands.
These data support the conjecture that hub proteins often utilize intrinsic disorder to bind to multiple partners and provide detailed information about induced fit in structured regions.
In the case of p53, different regions in the disordered tails enable this protein to bind to multiple partners at the same time.
The fact that the N- and C-terminal regions of Cby are somewhat independent may be crucial for the protein to bind to multiple targets via the distinct structural modules located in these two segments.
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