TRPV4 is a cation channel, and functional experiments suggest mutant proteins are not localized properly to the cell surface.
Our genetic interaction studies, including analysis of double-mutant combinations and epistasis experiments, suggest HtrA2 acts downstream of PINK1 but in a pathway parallel to Parkin.
Our epistatic analyses, performed with cdc-42 lf) cdc-42 lfnd cdc-42 overexpression experimutantssuggest thandcdc-42 acts doverexpressionn parallexperimentsed-1/6/7 and in parallel to the ced-2/5/12 suggestng cascades.
Overall our binding experiments suggest that the H486R mutant is altered in its interaction with CYLD.
However, our preliminary experiments suggest that the opi10∆ mutant does not affect localization of Ssa1p or Ssa2p under normal or starvation conditions (data not shown).
Additionally, our competition experiments suggest that RydC wild type and S1 mutant share at least an overlapping binding site.
Both sets of experiments suggest that mitoxantrone is a better substrate for mutant ABCG2 than wild type.
These experiments suggest that the attenuated phenotype of the mptC mutant observed in vivo is not due to defective entry or initial persistence in macrophages.
But in people with FOP, the new experiments suggest, activin A has the opposite effect on the mutant receptor, driving bone growth.
These experiments suggest that silencing Cdk5 can prevent the aberrant NF phenotype observed in cells expressing mutant HSPB1.
