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Both rGrB-H6 and the C228F mutant were found to be highly specific and efficient processing enzymes for the cleavage of fusion proteins, as demonstrated by cleavage of fusion proteins containing the IEPD recognition sequence of GrB.
In this study, the activities toward substrates of the M57T and M57A mutants, together with M57L mutant, were found to be much lower than those of the native and recombinant wild-type forms of CgPAD.
However, later, all of the expression defects of the xpr mutant were found to be caused by an additional mutation in agrC, the gene encoding agr sensor kinase [29].
erm-sensitive clones from IDM mutant were found.
The shorter siliques in the AtrabD2b/2c double mutant were found to be primarily due to the pollen defects.
In contrast, no biochemical differences between wild-type TRIM32 and the BBS11-associated P130S mutant were found.
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After this treatment, one mutant was found which had lost its antagonistic property.
Thermal fluctuation of the mutant was found to be reduced upon PhC binding, which contributes to restoring its enzymatic activity.
The mutant was found also capable to produce MA from a guaiacol-rich true lignin hydrolysate, obtained from pine through hydrothermal conversion.
The R11E mutant was found to have activity near that of wild-type ImI, while R7L and D5N demonstrated activities reduced by at least two orders of magnitude.
The epidermal growth factor receptor (EGFR) T790M mutant is found in about 50% of clinically acquired resistance to gefitinib among patients with non-small cell lung cancer (NSCLC).
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