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All hNGFR100 mutants, including R100W and R100E mutants, were equally effective as wild type hNGF in activating this pathway in both cell lines (Fig. 1B,D,F).

Importantly, both wild-type TSC2 and the phosphorylation-site mutants were equally efficient at restoring insulin-stimulated Akt signaling to these cells.

Because the FADD-DD and FADD-DD V108E mutants were equally effective at blocking tumor regression caused by etoposide, we conclude that signaling through TRAIL receptors alone is sufficient to cause these effects.

Also, PON2 wildtype and lactonase-deficient mutants were equally protective against intrinsic apoptosis.

However, compared to the wild-type proteins, these mutants were equally competent in the activation of Grp78 and Grp94 promoters.

Indeed, in Ptch1 −/− MEFs, these mutants were equally effective as wildtype Ptch1 or cyclopamine in suppressing 8xGliBS-luc reporter independent of the Shh ligand.

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Similar(51)

In homozygous individuals with two mutant genes at this locus, mutants are equally nasty to each other.

Thus, the signalling routes used by the Met2P and Met2S specificity-switch mutants are equally sufficient, even when sensitised by lowered receptor expression levels, to execute the mechanisms leading to Pea3 propagation.

The most compelling explanation for this phenotype is that PGN hyperdegradation (in LYS1 OE plants) or lack of PGN degradation (in LYS KD mutants) are equally disadvantageous to plant immunity and that immune activation in Arabidopsis requires oligomeric PGN fragments of a particular minimum degree of polymerization (DP).

In contrast, the wild-type PA01, and PAOC-fliC (complemented fliC mutant) were equally more resistant to SDS.

However, overexpressed WT PIAS1 and the ligase-deficient mutant were equally effective in attenuating JUN induction, suggesting that the JNK-dependent phosphorylation but not sumoylation of c-Jun determines the level of autoregulation of this gene, at least at the time point examined.

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