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Prediction and in vitro MHC binding analyses suggest that one is restricted by Mamu-A1⁎001 Mamu-A1⁎001 by Mand-another
Additionally, in vitro GR-DNA binding analyses suggest that ligand structure modulates GR-DNA interaction dynamics rather than the receptor's ability to bind DNA.
The results from both the in silico and DNA binding analyses suggest that a transcriptional network links the Wnt and Notch pathway, implying a functional regulation of canonical Wnt signaling at several levels of the Notch pathway.
Our genome-wide binding analyses suggest that the Tip60 complex has a very broad role in regulating transcription in mESCs, which is in agreement with the observation that Tip60 and several other Tip60-complex subunits are required for mESC maintenance [ 14].
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These analyses suggest that the found binding motif for HP1α may indeed be associated with its binding to DNA.
These analyses suggest that PTMs often tune binding affinity in natural systems.
Structural analyses suggest that non-productive substrate binding at high substrate concentrations could be stabilized through stacking interactions with amino acid residues above the Y300 and W351 -2 subsite (Additional file 4: Figure S4).
Results of our kinetic analyses suggest that the order of substrate binding by ASFV Pol X differs from the bi-bi ordered mechanism suggested for other DNA polymerases.
Molecular dynamics simulations and quasi-harmonic analyses suggest that the effect of inhibitor binding is transmitted from the dimer interface to the active-site loops that are known to assume an obligatory ordered substructure during catalysis.
Structural analyses suggest that this site is near important binding regions of the cytochrome c oxidase complex (fig. 3 A), and functional analyses in TreeSAAP suggest that the substitution observed here may lead to functional changes.
The previous analyses suggest that both histone modification features and transcription factor binding features are predictive for chromatin accessibility with high accuracy in DNase I hypersensitive sites.
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