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In contrast, the somatic mutations did not differ from expectation.
The mutations did not affect β-FNA affinity or efficacy.
The above mentioned mutations did not significantly affect the helical secondary structure of this domain.
Introduction of these mutations did not compromise BMP-7 in vitro bioactivity.
Selective pressure analysis showed that most of these mutations did not reflect positive selection.
However, these mutations did not abolish the binding shift of CTCF to M1 (Fig. 2C F), except M1-Mut1.
Moreover, temperature- and pH-activity profiles revealed that the designed mutations did not affect the catalytic activity of the enzyme.
In line with these observations, XP gene mutations did not markedly affect the chromosomal stability, and the basal CPD levels are comparable between XP cells and WT cells.
Significantly, the mutations did not result in 'catL-like' specificity, suggesting that substrate-based inhibitors could be rationally designed against these important parasite-specific structural determinants.
The YCPPC and WCPPC mutations did not improve the reactivity of Grx with the chloroplastic NADP-malate dehydrogenase, a well known target of thioredoxins (Trxs).
The number of T/A and A1896 stop codon mutations did not yield a statistically significant difference between ALT normal and elevated groups.
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