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Mutagenesis studies indicated that the function of the promoter was dependent upon synergistic interactions between transcription factors bound to these sites.
Mutagenesis studies indicated that ORF1 is required for L1 retrotransposition [21], [22].
Site-directed mutagenesis studies indicated for His221 and Glu282 a prominent role in substrate recognition, but not in catalysis [34], [36] [39].
Mutagenesis studies indicated a requirement for serine five residues from the amino terminus, reminiscent of myristoyl transferase, but not of ghrelin acylation.
Mutagenesis studies indicated that the preferred position for octanoylation occurs on a serine which must represent the fifth residue from the amino terminus (Ser6 was not acylated).
Early mutagenesis studies indicated that residues 438 (Pro) and 441 (Gly) in the C4 region are important for CCR5 binding.
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Mutagenesis studies indicate that FIPI binds at S757 of PLD2, which is within the HKD2 catalytic site of the enzyme, whereas NFOT binds to PLD2 at two different sites, one being at S757/S648 and another to an allosteric site that is a natural site occupied by PIP2 (R210/R212).
Our mutagenesis studies indicate that spectral tuning in C. nuchalis is mediated by mechanisms similar to those of other birds.
Rats were selected for use because site directed mutagenesis studies indicate that the binding pocket where 5-HT6R antagonists bind in human and rat is similar [13].
Moreover, mutagenesis studies indicate that VU0357121 and related analogues bind to a yet uncharacterized allosteric site on mGlu5, distinct from CPPHA, yet share a functional interaction with the MPEP site.
Furthermore, in silico mutagenesis studies indicate that the K321T and A65 V mutations, which directly form the predicted binding pocket, would cause significant losses (Δaffinity = +1.41 and 0.95, respectively) in the affinity of S20 for the pocket.
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