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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.
Some of these abnormalities or mutations may affect mRNA- and protein-expression levels.
We suspect that these two mutations may affect the association between Usa1 and other ERAD-L ubiquitylation components.
This finding supports the notion that mutations may affect GCK function, which is intimately related to intermotion domain [7].
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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.
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].
In fact, co-immunoprecipitation studies using brain lysates suggest that the M105I mutation may affect the αSNAP/SNARE complex interaction [14].
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