While a large number of studies failed to identify the biological target of<unk> , it was discovered to bind and stabilize firefly luciferase, thus explaining the mechanism by which it created a false positive effect on the read through assay.<unk>  is thought to make ribosomes less sensitive to premature stop codons (an effect referred to as "read-through") by promoting insertion of certain near-cognate tRNA at the site of nonsense codons with no apparent effects on downstream transcription, mRNA processing, stability of the mRNA or the resultant protein, thereby making a functional protein similar to the non-mutated endogenous product. It seems to work particularly well for the stop codon 'UGA'. Studies have demonstrated that<unk>  treatment increases expression of full-length dystrophin protein in human and mouse primary muscle cells containing the premature stop codon mutation for Duchenne muscular dystrophy and rescues striated muscle function. Studies in mice with the premature stop codon mutation for cystic fibrosis demonstrated increased CFTR protein production and function. Extending on this work, a mechanistic study with yeast and human cells has elucidated the details of<unk> -mediated nonstandard codon-anticodon base pairings which result in specific amino acid substitutions at specific codon positions in the CFTR protein. The European Medicines Agency review on the approval of<unk>  concluded that "the non-clinical data available were considered sufficient to support the proposed mechanism of action and to alleviate earlier concerns on the selectivity of<unk>  for premature stop codons."
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