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To determine whether cells that are relatively insensitive to AprA have an observable defect in the ability of rAprA to bind to this receptor, we measured binding of rAprA to cells.
We measured binding of CquiOBP1 to a few compounds known/inferred to be mosquito attractants.
To gain further insight into the molecular basis of complex formation between these two proteins we measured binding of the human and mouse NOXA1-SH3 domains to either NOXO1-SH3AB E construct by ITC.
We measured binding of U1 snRNP to a [P]-labelled 5′SS oligonucleotide by filter-binding assay.
Thus, we measured binding of p53 to the NF-Y sites of the CyclinB2 promoter by chromatin immunoprecipitation (ChIP).
Gerton et al. (2000) measured binding of Spo11 during meiosis as a proxy the rate of production of double-strand breaks.
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Online substrate cleavage was monitored by measuring binding of mAb10F12 to a SNAP-25 neo-epitope.
Joshi et al. [5] tried to address this problem by measuring binding of phospholipidosis-inducing drugs to L-α-dipalmitoyl phosphatidylcholine vesicles.
The K472E/R473E mutant Cul1 was then used to measure binding of CAND1 by coimmunoprecipitation.
Figure 1 is a schematic representation of the production of the 32P-labeled peptides and the experimental design of assays to measure binding of peptides to cell lines.
Isothermal titration calorimetry (ITC) was used to measure binding of the individual human or mouse NOXO1 SH3andnd SH3B domains to the p22phox cytoplasmic domain.
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