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Exact(6)
This study suggests first that pathological Tau mutations may change the distribution of phosphate groups.
In addition, mutations may change surface properties promoting an abnormal interaction between PrPC and other not yet identified interactors [23], [24].
Nonsynonymous mutations may change an optimal codon to nonoptimal one.
When preferred silent base differs between synonymous families, then replacement mutations may change a codon from preferred to unpreferred.
These mutations may change the net charge of the protein, which is known to improve the enzymatic efficiency of endolysins [ 21, 22].
From small to large: TFBS mutations may change which type of TF binds, or the weight of the TFBS (i.e. activating or repressing).
Similar(54)
CST1 mutation may change the conformational structure motif of substrate and interaction site of inhibitor.
Mutation may change the activity of the encoding protein and influence antigen presentation process.
Although flowering time is controlled by many genes, a single mutation may change flowering time drastically and may produce reproductive isolation.
Alternatively, the mutation may change the active site environment of CUL3, exposing more lysine residues close to the E2∼UB binding site.
Because this domain is unique to avian HEV, as predicted by Haqshenas et al. (14 ) and Guo et al. (10 ), this point mutation may change the antigenicity of the epitopes in domain II of the capsid protein.
Related(20)
variations may change
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times may change
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breakthroughs may change
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