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Site-directed mutagenesis of a thermophilic xylanase from Caldicellulosiruptor bescii revealed that four out of five mutations could alter the enzymatic pH optima toward acidic condition without compromising the catalytic activity and thermostability.
Within just 5 h, we successfully determined the electricity generation capacity of two known bacterial electrogens (wild-type S. oneidensis and P. aeruginosa) and another metabolically more voracious organism with 4 isogenic mutants constructed with the hypothesis that such mutations could alter their electrogenic properties.
Thus, oncogenic mutations could alter the activity of c-Myb, a transcription factor that is normally regulated during the cell cycle.
We hypothesized that CN mutations in the SELENBP1 locus could associate with the disorder and that these mutations could alter the gene product's activity in patients.
Furthermore, it is hypothesized that TRPC6 mutations could alter the intracellular milieu, which, as a consequence, would induce an irreversible cell state.
Possibly, in Cystic fibrosis different mutations could alter the functional interaction of the CFTR_HUMAN protein with the DERL1_HUMAN, RNF5_HUMAN, AHSA1_HUMAN and GOPC_HUMAN proteins, or between the CHIP_HUMAN and HSP7C_HUMAN or CLCN2_HUMAN proteins.
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How this mutation could alter the lectin site at such a distance is therefore unclear.
The mutation could alter physiological functions of tumor- and apoptosis-associated genes.
However, it is not clear how this mutation could alter the binding of ΔNp63 α in a promoter-specific manner.
The finding of a germline deleterious mutation could alter treatment decisions; for instance, women with germline mutations might opt for more radical surgery or may consider prophylactic surgery to the contralateral breast or ovaries.
Thus, we predict that the Scn8a Clth Asp981Val mutation could alter SCN8A channel kinetics or sodium current properties in Scn8a Clth neurons, which could be assessed in vitro and in vivo.
More suggestions(15)
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