Norrin mutants that lose binding to Fz4CRD also fail to induce the luciferase reporter activity, in agreement with the SPR results and prior genetic data (Xu et al., 2004; Smallwood et al., 2007).
The SENP3 C532A mutant that lost de-SUMOylating activity did not change the Ub conjugation of Sp1 (Fig. 4A).
If the CAMP functions through a similar mechanism as the divalent cation in inducing the conformational changes of PhoQ, why the PhoQW104C-A128C muthat that lost the response to divalent cation limitation can still respond to the CAMP.
If the CAMP functions through a similar mechanism as the divalent cation in inducing the conformational changes of PhoQ, why the PhoQ W104C-A128C muthat that lost the response to divalent cation limitation can still respond to the CAMP.
The effects were dependent on E2-CD81 interaction on the cell surface, since CD81-silenced Raji cells did not respond to both treatments; and an E2 mutant that lose the CD81 binding activity, could not trigger the responses of both Raji cells and PHB cells.
Although biological dependence upon pH has not been demonstrated thus far, it is plausible that the p.R337H mutant protein operates as a conditional mutant that loses its function only in cells undergoing a small increase in intracellular pH.
The clones that maintained detectable PCR products up to Tc or over were assumed as desired mutants and those that lost detectable products, the parental molecules.
Finally, the mutants that were lost or underrepresented in one ear were virtually always lost or underrepresented in the other ear of the same chinchilla.
In two recent studies, Shen and Lutkenhaus used the block in cell division caused by overproduction of the N- or C-terminal domains of E. coli MinC to isolate FtsZ mutants that have lost the capacity to interact with MinC [30], [31].
Conversely, telomeres retain some protection from fusions in the presence of TRF2 mutants that have lost the ability to inhibit the DDR (Okamoto et al., 2013).
We then observed that only transcriptionally inactive mutants of Ets-1 (i.e., the mutants that had lost the TAD domain and/or ETS domain) were resistant to severe hypoxia-induced degradation.
