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The authors suggest that CRP acts, in addition to directly regulating transcription, as a chromosome-shaping protein by binding to those multiple low affinity sites.
These NAPs are assumed to be mediators of analog control exerted by long-range nucleoprotein structures formed by binding of multiple low affinity sites in the chromosome as opposed to digital control exerted by low concentrations of dedicated transcription factors binding specific DNA sites with high affinity [ 9].
However, given the potential requirement for structural determinants and the fact that direct recruiting factors for myosin-II have yet to be found, we speculate that recruitment of myosin-II may be mediated by multiple low affinity interactions that rely on structural assembly of the CR and may not be detectable by conventional solution-based assays for protein interactions.
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This instability has been associated with the extensive crosslinking between traditionally-used fluorescent ligands (presenting multiple low-affinity moieties) and ConA (presenting multiple binding sites) in free solution.
The presence of multiple low-affinity binding sites in FRQ may result in high-affinity binding to FWD-1.
In physiological systems, multiple low-affinity interactions are used to distinguish one cell type from another and to provide selectivity.
The multiple low-affinity SUMO SIM interactions enable RNF4 to specifically recognize SUMO chains with a high avidity leading to ubiquitylation of its substrates.
Significantly, despite the existence of higher affinity sites, most of the binding of toluene and skatole is still derived from interaction with multiple low-affinity sites.
Ss-LrpB interacts with multiple low-affinity sites throughout the genome without an apparent regulatory purpose and these sites are often associated with IS elements.
Monomeric Fc-fusion proteins would not be expected to cross-link multiple low-affinity receptors on APCs, which are required for the enhanced cell signalling necessary for a well-balanced immune response (Fig 2B).
Atg19 binds its prApe1 cargo with very high affinity and selects for membrane-bound Atg8 via a high-avidity interaction mediated by multiple low-affinity Atg8 interaction sites (Sawa-Makarska et al., 2014).
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