IndraLab

Statements


| 2 6

reach
"The data in our report demonstrated that ATO treatment reduces the binding of USP10 to FLT3 protein, which might partly contribute to the enhanced ubiquitination of mutant FLT3 protein.Hsp90 is an important chaperone molecule assisting in folding and preventing client proteins from ubiquitination and degradation [44]."

sparser
"A similar interaction between USP10 and FLT3 was demonstrated in 293T cells engineered to exogenously express these proteins ( xref )."

reach
"Co-immunoprecipitation assays showed that ATO treatment led to significantly reduced binding of USP10 with FLT3 protein in TF1/ITD-Ub cells."

sparser
"Co-immunoprecipitation assays showed that ATO treatment led to significantly reduced binding of USP10 with FLT3 protein in TF1/ITD-Ub cells."

sparser
"The data in our report demonstrated that ATO treatment reduces the binding of USP10 to FLT3 protein, which might partly contribute to the enhanced ubiquitination of mutant FLT3 protein."

sparser
"Our current data also support our previous observation that FLT3 and USP10 bind to one another, xref as FLT3 and USP10 co-immunoprecipitate in Ba/F3-FLT3-ITD cells (an AKT immunoprecipitation was included as a control for nonspecific binding) (Fig.  xref , lower panel)."

sparser
"ATO facilitates poly-ubiquitination and degradation of FLT3 partly through reducing the binding of mutant FLT3 to the deubiquitinating enzyme USP10."

sparser
"We observed robust co-immunoprecipitation (co-I.P.) of USP10 with FLT3 in Ba/F3-FLT3-ITD cells; reverse co-I.P. studies confirmed the association of FLT3 with USP10 ( xref )."