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This suggests that the affinity of the mutant CLOCKΔ19 BMAL1 complex is lower for two reasons: first, it does not preferentially bind as a tandem complex, thus binding may not be cooperative; and second, its affinity, even as a tandem complex, remains lower suggesting that the Clock Δ19 mutation interferes both with cooperativity and with affinity.
We therefore propose that a DNA dye that substantially relies on electrostatic interaction for its DNA binding may not be ideal for qPCR application because such a dye may bind to ssDNA with significant affinity and is thus more likely to interfere with the chain extension step.
If XDsh is required to promote the phosphorylation of XDpr1a by CKIδ, then mutants of XDpr1a with reduced XDsh binding may not be phosphorylated by CKIδ.
Alternatively, TF binding may not be limited to the promoter region interrogated by the tiling arrays.
This suggests that problems due to integrin fibronectin RGD binding may not be the primary causal effect in the case of this mutation.
We found more HRE-containing peaks than transcriptionally activated genes, suggesting that Hif-1α binding may not be sufficient for transcriptional activation.
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No endogenous ligand is known for ESRRG and ligand-binding may not be essential for at least some aspects of transcriptional activity (8).
However, optimization of the canonical linker length for DNA-binding may not be enough to yield opposed positioning of ZF units.
Because peptide/MHCII binding represents a multistep reaction, the IC50 for a competitive binding assay may not be directly proportional to the KD.
First, a lot of the target sites reported by the CLIP-seq methods in the CDS region may be due to transient protein-binding events and, thus, the level of downregulation due to such binding sites may not be significant [ 18, 54, 55].
However, many responding genes with binding sites may not be direct targets because response may be mediated by other genes and ChIP-binding site may not be functional in terms of transcription regulation.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com