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Comparisons of calmodulin and S100 proteins provide insights into the role these factors play in facilitating the variety of binding configurations necessary for recognizing a diverse set of targets.
Our efficient, rigid 3D pharmacophore superpositioning technique [1] will be applied to a number of structure-based pharmacophores selected from a diverse set of targets.
However, in our IR ATR application the topology of the identity manifold is not clear owing to a lack of understanding of the intrinsic LD structure spanning a diverse set of targets.
Further, it is known to bind a large number of proteins with high specificity implying that its intrinsic mechanism of binding is finely tuned to respond to its diverse set of targets.
An important emerging question is therefore whether FOXN1 regulates this diverse set of targets via classical transactivation, or functions either additionally or alternatively as a 'pioneer factor', as recently demonstrated for FoxA proteins (Cirillo et al., 2002; Zaret and Carroll, 2011).
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Computational experiments verify the effectiveness of the approach on a diverse set of target structures.
Here, we outline a YSD methodology to isolate Fn3 binders to a diverse set of target antigens.
For all case studies, which involved a diverse set of target metabolites, the uniformly random selection scheme resulted in the highest average maximum yield.
So far, however, a comprehensive assessment incorporating a large and diverse set of target sequences has not been conducted because of practical difficulties in providing an accurately annotated target set.
Despite the identification of a diverse set of target genes for MeCP2 [20] [21], [21], it remains unclear how MeCP2 dysfunction ultimately results in the neuronal syndrome.
Together our findings establish Spt5 as a dual regulator of transcription elongation in vivo and identify a small but diverse set of target genes critically dependent on Spt5 during development.
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