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These interactions can result in stabilization of general transcription machinery and activation of gene expression, or in transcriptional repression, depending on E2F interactions with other proteins, or on the particular E2F member bound to the DNA [6].
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Here, we present an approach for the prediction of binding preferences of members of a large protein family for which structural information for a number of family members bound to a substrate is available.
Given the extent to which different STAT members bound to identical genomic sites, the most conserved of these CRMs were of particular interest since they might constitute key cis-regulatory modules targeted primarily by any of the STATs.
The interface suggests that EphA family members bind to SHIP2 SAM, whereas EphB members may not; correspondingly, we demonstrate binding of EphA1, but not of EphB2, to SHIP2.
The TGF-β family members bind to the type I and type II serine/threonine kinase receptors on the cell surface.
HDAC family members bind to Runx2 and act as transcription co-repressors in skeletal development [6], [32], [33].
The TFs of the RUNX sub-family, are binding partners of heterodimeric transcriptional regulators denoted as CBFs (core-binding factors) of which the CBFa (RUNX) members bind directly to DNA and the two alternatively-spliced CBFb (also known as PEBP) members bind to the CBFa subunit and enhance its DNA binding [10].
These results highlight the similar binding properties of Lrig1 and Lrig3 and underscore the need to determine how these two family members bind to and regulate different receptors to affect diverse aspects of cell behavior in vivo.
DKK family members bind to LRP5/6 and antagonize canonical Wnt signaling by competitive inhibition [ 26].
In contrast, the relaxin-like members bind to G protein-coupled receptors with seven transmembrane domains (reviewed in ref (5)).
The remarkable sequence divergence and subfamily expansion suggests that silkworm OBP family members bind to diverse sets of odorants.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com