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The primary functional effects of these CM mutants, when expressed together at the working myocyte level, are presently unknown.
The R137C and R137L mutants when expressed in COS-7 cells exhibited a significant constitutive activity when measuring the intracellular cAMP accumulation.
This is consistent with our previous data showing that normal Roc1a can partially rescue the male sterility of Roc1b mutants when expressed from the Roc1b promoter [25].
The lack of significant biochemical abnormalities in Class I mutants when expressed in cultured mammalian cells indicates that these rhodopsin mutants are properly folded and capable of forming a light-absorbing pigment [6], [7], [8], [9].
Then, we analyzed the conjugation of SUMO to PTEN mutants when expressed in cells.
To address this, we asked whether the dpb11Δ N and dpb11Δ C mutants, when expressed together, could support checkpoint activation.
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The α-galactosylation and sialylation with NeuGc are reported in cetuximab produced from Sp2/0 (Qian et al., 2007) and infliximab from NS0 (Mimura et al., 2009) and are markedly increased for an IgG1-F243A mutant when expressed in murine cells (Mimura et al., 2016).
While we currently do not know if the S303A/LZ4m double HSF1 mutant has an increased propencity to trimerize, previous studies have shown that the LZ4m mutant, when expressed in yeast is not maximally trimerized and trimerization can be further enhanced via the addition of pharmacological HSF1 activators [28].
In contrast, PpHxk1 failed to complement the hxk1 hxk2 glk1 triple mutant when expressed from the same vector.
Similarly, the monomeric IgD-BCR mutant, when expressed in S2 Schneider cells, does not give a signal in Fab-PLA.
The corresponding TEAS L407P mutant, when expressed as a full length protein, showed pronounced self-alkylation at Asp444.
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