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Although reagents that would enable direct visualization of the O-fucosylation state of Notch in cells expressing Ofut1 R 245 A do not exist, prior characterization of this mutant isoform indicates that it is completely defective in fucosylation [ 10].
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The existence of allergenic and hypoallergenic isoforms indicates that PR-10 isoforms vary in allergenicity, and some PR-10 isoforms do not bind IgE at all.
First, we employed a mutant isoform of OFUT1, OFUT1R245A.
The wild-type isoform 2 was only slightly more active than the mutant isoform 2 and clearly less active than isoform 1 (Fig. 3B).
The superscript of mutant indicates a mutant.
For the mutant isoforms T64A, Y78A, T141A and K215A, 0.03 0.27 mg protein were used with 20 mM L-asparagine.
If the receptor internalizes as an oligomer, then the wild-type and mutant isoforms will mutually influence each others' trafficking properties, causing co-internalization of the mutant or co-retention of the wild-type at the cell surface.
Second-generation TKIs that irreversibly bind to EGFR wild-type and mutant isoforms have therefore been developed and one of these candidates, afatinib, has now reached the market.
Mutant isoforms were characterized for cell surface expression and function.
A comparison of the two isoform structures indicates the possibility of developing isoform-specific inhibitors of HCPTP.
Our analysis of isoform-specific daf-16 /FoxO mutants indicates that DAF-16A is the major FoxO isoform that controls dauer arrest, longevity, and stress resistance.
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