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Here, we have used a large panel of mutant BG505 Env-pseudotyped viruses to define additional sites.
This panel of mutant ITR5s demonstrates the requirement for a three nt spacer element for Rep2 function.
We went on to test a second panel of mutant PrP proteins, in which various amino acids were substituted by cysteines.
In order to explore the level of flexibility Rep5 possessed toward non-wt nicking stems, we created a panel of mutant ITR5s harboring altered nicking stems (Fig. 2C).
Co-culture experiments with a panel of mutant EPEC strains (with specific bacterial effectors knocked out) would help uncover the effector protein(s) responsible for effects on MMR.
Similar trends were noted in the binding efficiencies of the panel of mutant SU to human CXCR4 on SupT1 cells (Table 2).
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We applied this novel technology to a large panel of mutants, clinical isolates, and host-cell types to explore the host-mycobacteria interplay and its impact on the intracellular bacterial secretome, which also revealed the unexpected capacity of phagocytes from lung granuloma to present mycobacterial antigens via MHC class II.
The panel of mutants was further utilized to define residues critical for neutralizing antibodies that recognize the V3 domain.
To determine whether or not MEN1-associated missense point mutants are phosphorylated, we screened a panel of mutants for the ability to undergo Ser487, Ser543 and Ser394 phosphorylation.
This panel of mutants displays a plethora of NGL-binding properties, summarized and discussed in Supplementary Figure S8.
The site of transposon integration was also analyzed for a panel of mutants using the TMDH protocol (see below).
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