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In this study, the molecular dynamic simulation was used to investigate the possible mechanisms by which F1174V mutation may affect the structure and activity of ALK kinase domain.
In fact, co-immunoprecipitation studies using brain lysates suggest that the M105I mutation may affect the αSNAP/SNARE complex interaction [14].
This mutation may affect one of these fusion steps and thus modify the fusion activity of S protein and syncytia formation.
Though there are mechanisms by which synonymous mutation may affect protein function, they are more likely to be effectively neutral than non-synonymous mutations [14].
While there are no epitopes described overlapping this position, that OP428 could recognize, the mutation may affect processing of the EL9 epitope.
Although this suggests that the p.A222V mutation may affect fertility, the authors observed that the homozygous prevalence rate in subfertile and fertile men was not significantly different.
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These mutations may affect other components of the regulatory network, e.g., troponin tropomyosin signaling.
Recent progress in determining the dimer structure of the desmin-related IF-protein vimentin allows us to assess how such mutations may affect desmin filament architecture.
TLR gene mutations may affect the gene products in terms of their ligand-binding ability or their signal transduction ability after ligand binding; such changes have a great influence on pathogen monitoring and disease resistance.
Thus, these mutations may affect the binding of G6P and NADP+ units.
These mutations may affect the binding of G6P and NADP+ units.
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