To develop cellular TRIM24 binding assays for drug-target engagement studies, we generated stable HeLa cell lines expressing full-length TRIM24 (TRIM24-FL) or isolated PHD-bromodomain (TRIM24-PB) as shown by Western blotting (Fig. 2a).
In this study, we generated a neutralizing monoclonal antibody, 5C4, which inhibited TT binding to its receptor and was efficiently protective at 73.7 IU/mg.
In our study, we generated random combinations of expression p-values with scrambled binding p-values, so that we could choose a cutoff threshold by comparing the ordered p-values with the ordered "scrambled" p-values.
In this study, we generated a novel anti-CXCR4 mAb, CF172, which showed a specific binding reactivity, and a neutralizing activity, against human CXCR4.
In the present study, we generated induced pluripotent stem cells (iPSCs) from bovine testicular cells by electroporation of octamer-binding transcription factor 4 (OCT4).
In the present study we generated mice in which loxP sites flank exons 12 14 of Foxp2; these exons encode the DNA-binding motif, a key functional domain.
For that study we generated two datasets.
In the present study we generated five chimeras with different 5-HT3A receptor sequences of murine and human origin to determine the structural basis for clozapine binding.
In this study, we generated a mouse line harboring a point mutation in the endogenous Nrp1 locus that selectively abolishes VEGF-NRP1 binding (Nrp1 VEGF− ).
In this study, we generated mice carrying an identical point mutation to that of the KE family, yielding the equivalent arginine-to-histidine substitution in the Foxp2 DNA-binding domain.
