Sentence examples for mutation destabilizes the from inspiring English sources

Mutation destabilizes the mutated MPV17 transcript in the lymphocytes and prevents its translation in the transfected cells.

These results are consistent with the hypothesis that the mutation destabilizes the protein [35]; however, whether the mutation leads to degradation of the protein (as typically happens with temperature-sensitive proteins) or only inactivation remains to be determined.

T142S channels have a mean open time that is ∼3 fold shorter than wild type (289.7±292.2 ms, Kir2.1, 93.4±92.6 ms, T142S) but display no change in intraburst open probability (0.84±0.041, Kir2.1, 0.88±0.042, T142S) suggesting that the mutation destabilizes the conducting conformation of the selectivity filter.

This supports the observation from the FTIR and circular dichroism analysis that the W8Y mutation destabilizes the fold.

This score should be devised so that the fixation probability is low if the proposed mutation destabilizes the structure or complicates the folding process.

The G229S mutation destabilizes the binding of Ero1 to a flavin cofactor at the restrictive temperature, which likely impairs its ability to oxidize PDI (Gross et al. 2004).

In this context, any mutation destabilizing the HA appearing during vaccine construction or production can severely affect vaccine immunogenicity.

For example, the L858R mutation in EGFR is a common mutation in cancer and is classified as an activating mutation, but its effect is a result of the mutation destabilizing the inactive conformation of the enzyme and causing it to fold into an active conformation even in the absence of ligand [51].

FTDP-17 mutations +3 to +16, as well as the exonic S305N mutation, destabilize the stem loop making the 5′ splice site of intron 10 constitutively available, hence promoting E10 inclusion (14, 15, 20).

Strikingly, the C-terminal 40 kDa fragment of the KRcanyon mutants was rapidly further degraded, suggesting that the KRcanyon mutations destabilize the UCS domain, making its C-terminal part more susceptible to protease digestion.

Both mutations destabilize the coiled coil conformation at neutral pH and increase the pKa of the formerly ion-paired Glu side-chain, verifying the formation of a salt bridge even in the case where a charged side-chain is destabilizing.