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The majority of cancer mutations resulted in moderate global changes, but considerable local structural changes near the mutational site and in the activation loop.
In overexpression assays in zebrafish, prickle mutations resulted in aberrant prickle function.
Care was taken to avoid diseases in which the majority of associated mutations resulted in mislocalization or 0% activity.
Strikingly, both single M112 mutations resulted in a drastic reduction in ubiquitin ligase activity of RNF125 (Fig. 7I).
Introduction of these mutations resulted in improved glycerol utilization also in industrial strains.
Engineered factor F3 with two point directed mutations resulted in a protein with an active site identical to hAPN.
Incorporation of 35 predicted mutations resulted in an enzyme with the desired substrate specificity but low catalytic activity.
The combination of beneficial mutations resulted in an additive and superior hydrogen producing strain of R. sphaeroides.
This fact was confirmed by nucleotide sequencing which also demonstrated that most mutations resulted in amino acid substitutions.
These mutations resulted in the replacement of positive charges with negatively charged residues, allowing the development of a defined structural patch that resembles the one present in the naturally evolved highly crossreactive viral chemokine-binding proteins (vCKBPs 49,50.
Although reducing the hydrophobicity drastically decreased fibril formation, the Val70Thr and Val70Pro mutations resulted in an unstable secondary structure thereby increasing non-structural aggregation, instead of fibril formation.
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