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This suggests that: 1) PPARβ/δ may indirectly regulate some of the 612 genes, 2) the dynamic nature of PPARβ/δ binding and interacting with chromatin prevents detection of receptor occupancy by ChIP-seq, and/or 3) PPARβ/δ may directly regulate these genes by binding with chromatin at more distant sites.
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It participates in glycoprotein binding and interacts with ERp57, which collaborates in the folding maturation of glycoproteins bound to CRT [6].
PPARs have functional domains for DNA and ligand binding and interact with recognition sequences in the promoter regions of their target genes to regulate transcription [ 3].
The multiple recognition of 14-3-3 14-3-3 14-3-3is mechanism to a considepends degree, with the different peptides taking different paths throngh thisbinding cleft and interacting with binding site residues in distinct ways.
Mapping of the chemical shift perturbations onto the structure of the PDZ domain clearly demonstrates that the compound is binding in the canonical peptide binding groove and interacting with the GYGF loop.
Extra cellular matrix proteins binding integrins and interacting with the cell cytoskeleton are important in controlling many steps in cell membrane-cytoskeleton attachments and in signalling pathways [ 40].
TRIM24 acts as a transcriptional regulator, binding to chromatin and interacting with several nuclear receptors and coactivators [ 25].
The ECM provides mechanical adhesive support for the cellular constituents, directs their morphological organization, and influences physiological functions, by binding growth factors and interacting with cell-surface receptors.
Ser1073.36, which was shown to be important for agonist binding in both the drd1 30 and 5-HT2A receptors, 33 is directed toward the binding crevice and interacts with the backbone carbonyl of Asp1033.32.
This motif is present in many DNA binding proteins and interacts with the minor groove of AT rich region and enhances the interaction of the protein with chromatin and/or DNA [ 45].
When it was fully ionic cross-linked by P3O103- ions in the TPP solution, CS with positive charge (NH3+) would consume most of the binding sites and interact with the negatively charged phosphate groups of TPP.
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