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The appearance of Gag mutations was analyzed overall and within subsets of minor, transient, dominant, and complete mutations.
The evolutionary conservation of amino acid sites with mutations was analyzed using ConSurf[25], [51], [52], based on alignments shown in Fig. S2 and S3.
The effect of mutations was analyzed with SIFT [ 64].
Lignin subunit composition resulting from the novel bmr mutations was analyzed using pyrolysis-GC-MS.
The additive effect of mutations was analyzed by combining mutations through site-directed mutagenesis.
In a study that evaluated the association of PIK3CA status with clinicopathological factors in primary breast cancer, the effect of PIK3CA mutations was analyzed within molecular subtypes.
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All non-synonymous mutations are analyzed, using Uniprot identifier O95835 for LATS1 and Q9NRM7 for LATS2.
Mutations were analyzed using the program DNAsp V.4 (Rozas et al. 2003).
Higher-order interactions among identified mutations were analyzed by co-variation and cluster analyses.
Possible functional consequences of the mutations were analyzed using protein modeling and structural mobility analyses.
Structural changes resulting from the mutations were analyzed and the mechanisms responsible for the enhanced activity were discussed.
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