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Finally, secreted gp120-sfGFP enables a sensitive and easy binding assay that can quantitatively screen potential inhibitors of gp120-CD4 binding on live cells via fluorescence imaging or laser scanning cytometry.
The use of Luminescence Resonance Energy Transfer (LRET) provides a homogeneous binding assay that can be used for the detection of protein-protein interactions.
To better quantitate the inhibition of WT and mutant 3Dpols by the inhibitors we used a filter binding assay that can be run efficiently in a 96-well format.
Rauh et al. have developed an HTS compatible acrylodan-labeled kinase binding assay that can distinguish between type I and type II binding and demonstrated its utility to identify a highly selective p38α inhibitor.
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Here we report the development of a single-molecule assay that can directly report head binding in a walking kinesin molecule, and show that only a single head is bound to the microtubule between steps at low ATP concentrations.
The FLECS assay is a simple binding assay that enables proteins tagged with fluorophors to be rapidly and quantitative screened against small-molecule libraries.
Here we performed in vitro biochemical binding assays that suggested that VP19, VP24 and VP51A can also directly self-interact to form dimers (Figures 6, 7, 8 and 9).
Taken together, these considerations suggest that assays that can unambiguously detect the binding of weaker hits to a protein surface may provide a much needed alternative or complement to spectrophotometric assays, especially at early stages of hit discovery and optimizations.
To address this potential concern of immunogenicity, validated assays that can measure low and high affinity binding and neutralizing antibodies to romiplostim or TPO were developed.
Therefore, there is a need for direct binding assays for GPCRs that can distinguish between binding and function, as function is often context dependent.
Consistent with this hypothesis, a PP1c binding assay showed that APAF-1122 131 APAF-1122 131P1cann vitro (Fig. 5bind
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