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The BODIPY-FL-labeled derivative 10 (see Scheme S2 in the Supporting Information) was designed as a tracer molecule for direct binding assays based on fluorescence polarization, and was found to bind to wild-type STAT5b with high affinity (Kd=0.86±0.08 μ m; Figure 2).
The design of homologous displacement ligand binding assays based on molecularly imprinted polymers (MIP) is discussed in terms of the MIP adsorption isotherm.
Competitive binding assays based on the lectin Concanavalin A (ConA) have displayed significant potential to serve in continuous glucose monitoring applications.
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To evaluate the estrogenic activity of the aqueous extract from A. pilosa, the ability of A. pilosa to bind ERα and ERβ was assessed using a competitive binding assay based on fluorescence polarization.
The results were consistent with those determined by traditional methods, which confirmed the reliability of this competitive binding assay based on β-gal.
A new simplified binding assay based on nanoLC-linear ion trap ESI-MS for quantifying complexation of the B. mori pheromone-binding protein (BmPBP) with native (1) and prepared analogues was developed.
A novel competitive binding assay based on enzyme fragmentation complementation technology was established to screen the binding affinities of emerging chemicals for estrogen receptor (ER) α or β isoforms.
We have described a simple homogeneous binding assay based on luminescence resonance energy transfer.
To overcome these difficulties we combined a direct functional assay based on electrophysiology with a direct binding assay based on label-free tryptophan fluorescence.
Enzyme binding detection was achieved with a competitive binding assay based on fluorescence enhancement which has a simple principle, is inexpensive, and is easy to interpret.
We have developed SH2-PLA, an alternative in-solution homogenous SH2 domain binding assay based on proximity ligation and real-time PCR.
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