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In vitro, the groove mutations increase the stability of CLIP-DR3 complexes to dissociation.
Most of these mutations increase the resistance of CLIP-DR3 complexes to dissociation by SDS.
Biochemical analyses indicate that these mutations increase the enzyme's affinity for ATP while decreasing its affinity for NEDD8.
In all groups, the mutations increase the risk of certain other cancers as well.
Our analyses indicate that the G118V and T109M mutations increase the rigidity of surrounding regions, impairing actin- and PLP-binding, respectively.
Specifically, we envisage that KRAS mutations increase the intensity and duration of the growth-promoting signaling network.
Both mutations increase the secretion of Z α1-antitrypsin in the native conformation, but the double mutants remain more polymerogenic than the wild-type (M) protein.
Here we demonstrate that the prM/E mutations increase the specific infectivity of chimeric virions and the NS2A/NS3 mutations independently enhance packaging.
Our data suggest that these mutations increase the stability of the conserved catalytic sirtuin domain, thereby increasing the catalytic efficiency of the mutant enzymes.
Initial findings suggest that PD-causing mutations increase the kinase activity of the LRRK2 protein.19, 19 Protein kinases are good targets for small-molecule drugs, and modulating the LRRK2 activity could become an innovative therapeutic strategy for all patients with PD.
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The Flemish and Arctic APP mutations increase the propensity for fibrillization and decrease proteolytic clearance of Aβ peptides [17], [18], [19], [20].
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