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The chain length of the substitution at the 9-position was found to be critical in modulating the binding affinities.
In this study, we have used plasma immersion ion implantation (PIII) to modify the surface of polytetrafluoroethylene (PTFE), thereby modulating the binding mechanism of collagen.
Hydroxy substitution on ring A and/or B play a key role in modulating the binding affinity at adenosine A1 and A2A receptors.
In addition, for both enzymes we have found evidence indicating that differences in shape and accessibility exist between the substrate binding site of each monomer which could be modulating the binding affinity of non-covalent molecules.
Mechanistically, BAF170 competes with BAF155 subunit in the BAF complex, affecting euchromatin structure and thereby modulating the binding efficiency of the Pax6/REST-corepressor complex to Pax6 target genes that regulate the generation of IPs and late cortical progenitors.
However, each of the sites influences mRNA translation, either directly by modulating the binding affinity of PHAS-I and eIF4E or indirectly by affecting the phosphorylation of other sites.
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The regulatory region contains cis elements such as the promoter – where the RNA polymerase initially binds – and transcription factor-binding sites (TFBS) – where transcription factors (TFs) bind to modulate the binding of the RNA polymerase (Browning & Busby, 2004).
In addition, we show that Asf1a modulates the binding of histone H3/H4 to Importin4.
These studies demonstrate that the structure of the de novo protein modulates the binding of N-donor ligands to heme.
Here we predict that genomic background surrounding specific protein-DNA binding motifs statistically modulates the binding of sequence-specific transcription regulators to these motifs.
Here we have used plasma immersion ion implantation (PIII) treatment of polystyrene to modify the polymer surface, and so modulate the binding of the extracellular matrix protein tropoelastin.
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