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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].
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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].
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.
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.
The POMs are bound differently: TEW-5 and -8 have the most binding partners and interact with four HEWL chains.
With the aim of understanding the binding mode of OT to its receptor in the context of its three-dimensional architecture, we developed a homology model of the human OTR on the template of the mouse μ-opioid receptor crystal structure with the intention of identifying whether and which residues are oriented towards the binding pocket and interact with the ligand.
Those cofactors have ubiquitin-binding domains and interact with VCP as ubiquitin adaptors [ 120– 120].
The residues where de novo mutations are found all lie at the base of the nucleotide-binding site and interact with the terminal phosphate.
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.
Dynactin is a large protein complex necessary for cargo binding of dynein and interact with various proteins, thus linking them with dynein [18], [19].
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com