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Vogel et al. developed a time-resolved fluorescence resonance energy transfer (TR-FRET) based binding assay that allows the detection of both active or inactive conformation kinase inhibitors and has been exploited in several studies.
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To reduce undesirable effects on other SORT1 ligands, we concentrated our efforts on a compound library screen and biochemical binding assay that allowed us to identify a small molecule, BVFP, that targets the C-terminal PGRN588 593 motif.
Now, we have studied binding affinity using cantilever assay that allows for measuring the total mass of AuNPs attached to the surface of the microcantilever.
In order to investigate the effects of ATP-binding site occupancy on this inhibitory modification, an assay that allows uninhibited Csk to act upon an inhibitor-bound SFK as a substrate was needed.
The occupancy of colchicine-binding site by pertinent antimitotics inhibits the formation of the EBI: β-tubulin adduct, resulting in an assay that allows the screening of new molecules targeting this binding site.
The experiments described above demonstrate the development of an assay that allows asking whether a given actin-binding protein can recruit proteins or protein machineries driving actin filament assembly.
This was determined by using a novel in vitro activity assay that allows us to discretely occupy the two H3 binding sites in KDM5A.
One important requirement for studying photounbinding is an assay that allows us to distinguish between the loss of a binding partner (photounbinding) from the loss of fluorescence by photobleaching.
ChIP followed by MPS (ChIP-seq [ 94]) is the genome-wide assay that allows us to map chromatin components such as post-translational histone modifications, DNA-binding proteins and chromatin structure.
We also developed a gp120 overlay assay that allowed the identification of gp120 binding cells in lymphoid organ sections.
Here we developed a single-molecule fluorescence resonance energy transfer (smFRET) assay that allowed us to observe SRP binding to actively translating RNCs at physiologically relevant SRP concentrations.
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