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To further map the minimal region of DIDATRX essential for DAXX interaction, we generated a series of DIDATRX truncations based on secondary structural analysis, and performed isothermal titration calorimetry (ITC) studies (Fig. 1B).

To understand the mechanism of intersectin regulation, we have used deletion analysis to map the minimal autoinhibited fragment of the protein.

Where cell numbers permitted, shorter peptides were used to map the minimal epitope, and ICS was used to determine the phenotype (CD4 vs CD8) of the response.

Since the interaction between TAF8 and TAF10 has been confirmed in several different species [13], [15], [18], [23] we wanted to fine map the minimal regions of either TAF8 or TAF10 that are sufficient for this interaction.

To begin to map the minimal 3' sequence requirements for stable MHC class I expression, we first truncated the 9 Kb genomic fragment used to generate the PD1 transgenic mouse, removing 3.7 Kb of distal intergenic sequences 3' to the PD1 gene, leaving 730 bp immediately downstream of the polyadenylation site.

To map the minimal CALM interaction domain of FHL2, yeast cells were co-transformed with several FHL2 deletion mutants fused to GAL4-DBD and with a CALM prey clone, obtained in the Y2H screening using the CALM bait.

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Similar(52)

The work by Francillon et al. [17] maps the minimal collection of hardware and software components that are needed for a secure verification, based on a precise definition of the desired verification service.

To determine whether the animals might be recognizing the same epitope, we mapped the minimal optimal epitope recognized by both animals.

Based on this result, we mapped the minimal interaction region of HCV core, both in vitro and in vivo, to include amino acids 16 to 36 (Figure 1, Figure 2).

In order to disrupt possible interactions between DDX3X and its viral or host factors responsible for DDX3X stimulation of HCV propagation, we first mapped the minimal segment of HCV core protein that is capable of interacting with DDX3X.

When mapping the minimal interaction domain of TAF10 with TAF8 in a similar GST pull-down experiment we found that amino acids 100 to 218 of TAF10, containing its evolutionary conserved region including the putative HF, are sufficient to interact with TAF8 (Fig. 2B).

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