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The impact of node mutations is assessed using as target measure the average Hamming distance between a non-mutated/wild-type network and a mutated network.
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Alternate approaches for correcting the majority of X-CGD mutations were assessed, involving TALEN- or Cas9-mediated insertion of CYBB minigenes at exon 1 or 2 of the CYBB locus.
The effect of the mutations was assessed by circular dichroism spectroscopy from urea-induced equilibrium unfolding experiments and in time-resolved mode to follow the kinetics of refolding and unfolding.
To test this hypothesis, mutations were introduced at each of the three sites, and the effect of mutations was assessed using CAT-based transient expression assay.
The correlations of the in vitro response to AZD6244 or MK2206 (IC50) and gene mutations were assessed by using Wilcoxon test and Logistic regression.
Amino acid conservation at the missense mutations was assessed using SIFT software (http://sift.jcvi.org/) and Polyphen was used to predict the effect of the variation on the protein (http://coot.embl.de/PolyPhen/).
However, some of these proteins contained multiple TRD mutations, were assessed only for a limited number of phenotypes, or were evaluated in different cell types that complicated or precluded cross-study comparisons [10], [14], [15], [28].
Differences in persistence of NVP-R mutations were assessed in a small number of infants exposed to SWEN (n = 5) or SD-NVP (n = 5) who had available plasma samples and also had NVP-R mutations detected by standard population sequencing at the time of HIV diagnosis (Table 4).
NOTCH3 mutations were assessed by restriction enzyme analysis of specific mutations or by sequence analysis.
TP53 mutations were assessed by denaturing gradient gel electrophoresis analysis and DNA sequencing.
The disease burden of all the mutations was assessed by the CMT Neuropathy Score (CMTNS) and CMT Examination Score CMTESS).
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