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Unrestrained docking of the hits discovered here into the 6PG binding site indicated that alternative interactions of the carboxylate group with the area in which the carboxylate group of the substrate binds could also be possible.
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Comparison of these proteins' in vitro binding sites with their in vivo binding sites indicates that PBM-derived specificitiesificanies caccuratelyely reflect in vivo DNA sequence specificities.
The increase in binding affinity at lower pH was greater for the Ubx optimal binding site than for other DNA binding sites, indicating that subtle sequence alterations in DNA binding sites may influence pH-dependent behavior.
The unpaired probabilities, the probabilities of not forming pairs, are significantly higher than negative controls and the flanking sequence surrounding the binding site, indicating that SRSF1 proteins tend to bind on single-stranded RNA.
Molecular modeling of these peptides into the binding site indicates that these complexes are fitting well into the site and making extensive interactions with the residues crucial for PfEMP-1 binding.
The most strongly dominant alleles alter highly conserved residues of the myosin ATP binding site, indicating that functions of the myosin ATPase are important for thick filament assembly.
However, this region does not form a part of known antibody binding site indicating that in solution, this region may acquire some conformation that is accessible only to peptide antibodies.
The fact that the 14-3-3γ 14-3-3γ 14-3-3γpromotering site indicates thas 14-3-3γ expression is regulated at the transcrip53onal level binding
RAB34 contained the putative miR-9 binding site, indicating that it might be one of the targets regulated by miR-9.
Additionally, overexpression of p65 induced activity of the wild-type MMP-9 promoter, but not the promoter reporter with a mutated NF-kappa B binding site, indicating that p65 also plays a role in regulating MMP-9 expression.
Importantly, the essential ERα coactivators AIB1 (also known as SRC3) and p300 were also present at this specific binding site, indicating that ERα is likely to be functional here [ 24].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com