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As a consequence of this mutation the ability of the Gα subunit to dissociate from Gβγ is inhibited causing constitutive inactivation of heterotrimeric G-protein signalling (Yu et al., 1996).
A consequence of this mutation is that the mutant enzyme is less stable thermally in vitro.
This clearly demonstrates that gain-of-function is the dominant consequence of this mutation.
However, in vitro functional studies are needed to confirm the consequence of this mutation.
The consequence of this mutation is a truncated protein without NLC2 and 3 motifs at the C-terminus.
The resulting cDNA was amplified by PCR and cloned, and several clones were sequenced to identify the consequence of this mutation.
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To explore the consequences of this mutation on binding, we carried out a 50-ns molecular dynamic simulation of the PFN1G118V: actin complex (see Methods for details).
We provide a detailed account of the consequences of this mutation on axonal and dendritic morphogenesis as well as dendritic spine development in cultured hippocampal and cortical neurons.
We are now investigating the biochemical, cell biological, and in vivo consequences of this mutation.
In the later part of the study, we evaluated the clinical consequences of this mutation.
We have also demonstrated that a V326N mutation in Als5p prevents formation of surface nanodomains [43], but have not previously shown the functional consequences of this mutation.
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