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The molecular docking studies suggested that the binding of these mimics at the colchicine site of the tubulin is similar to that of combretastatin A-4.
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Yet, molecular mimicry is not limited to structural similarity; the binding partners of these mimics must also be fooled by conformational dynamics and overall molecular interactions.
Moreover, molecular docking studies suggested the binding of this mimic at colchcine-binding site is similar to Crolibulin, as was in conformity with the observed SARs for these compounds.
This model has recently gained prominence (Gardner and Walter, 2011; Promlek et al., 2011); a study showed direct binding of unfolded peptide mimics to yeast Ire1 luminal domain in vitro (Gardner and Walter, 2011).
Furthermore, binding of miRNA374B mimic to the 3UTR-MMP14 significantly reduced expression of luciferase in U251 cells, suggesting a strong relationship between MMP14mRNA expression and miRNA374B (Fig. 4F).
In addition, we did not detect differences in the affinity binding of mutants that mimic phosphorylation by Erk and Src, which contrast our previous binding studies in which a mutant that mimics phosphorylation by Erk was found to bind preferentially to N-WASP [ 14].
Molecularly imprinted polymers (MIPs) have been developed mostly for the specific binding of the target, mimicking the function of antibodies.
In our cyanide-bound structure presented here, binding of the substrate mimic results in a distorted tetrahedral geometry of Ni.
However, phosphate inhibited chymotrypsinolysis of 14-3-3ζm 14-3-3ζm 14-3-3ζmpothesupportinginding oursmall molecules mimicking substrate makes 14-3-3ζm more stable.
Structural characterization of enzyme-inhibitor complexes revealed the original binding mode of these novel NAD mimics.
In particular, these derivatives are promising to modulate the binding preferences of the mimics for ribosomal A- versus P-site in crystallographic studies.
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