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If a mutation changes a fly's response to a drug, the researchers know that gene plays a role in drug function.
The mutation changes a single amino acid and may enhance mitochondrial function, the team reports in the April issue of the American Journal of Human Genetics.
Studies in the fly Drosophila melanogaster suggest that if a mutation changes a protein produced by a gene, about 70 percent of these mutations will be harmful with the remainder being either neutral or weakly beneficial.
Based on studies in the fly Drosophila melanogaster, it has been suggested that if a mutation changes a protein produced by a gene, this will probably be harmful, with about 70% of these mutations having damaging effects, and the remainder being either neutral or weakly beneficial.
This mutation changes a basic arginine (CGG) to a non-polar tryptophan (TGG) at a position corresponding to residue R100 in mature NGF [27].
The mutation changes a T to a C in exon 5 (c.495T>C), which substitutes a Methionine to a Tryptophan (M132T) (Figure 1B).
Similar(41)
This mutation changes an arginine to a stop codon.
The mutation changes an arginine residue to a glutamine in the C-2 domain of PTEN.
The Pasha mutation changes an invariant proline in the WW domain, which is conserved among all known Pasha orthologs.
The mutation changes an existing -10 TAnnnT motif to an "extended -10" TGnTAnnnT consensus (Newton-Foot and Gey van Pittius 2012).
This mutation changes an absolutely conserved cysteine residue, which is required for receptor maturation and cell surface expression (Piao et al., 2004).
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