To assay the effect of these mutations on splicing we opted to introduce the mutated intron sequences at their endogenous locus, instead of within the CUP1 gene as was previously done [ 8, 9].
Moreover, the effect of these mutations was investigated for the full-length protein.
To verify the effect of these mutations on the transport activity of hENT1, a structural model for hENT1 was generated (Fig. S4).
The effect of these mutations on membrane binding was determined by a quantitative phospholipid ELISA assay and compared to wild-type α-Syn and to the Parkinson's disease-causing mutations, A30P, E46K and A53T.
The effect of these mutations on the direct electron transfer (ET) between Au and the enzyme was studied in the reaction of the bioelectrocatalytic reduction of H2O2, at –50 mV versus Ag|AgCl, on rHRP-modified Au electrodes placed in a wall-jet flow-through electrochemical cell.
The effect of these mutations on nuclear localization was easily discernible.
The effect of these mutations on the 21OH activity is unknown.
The effect of these mutations on biotinyl-lysine cleavage was not determined.
We assessed the effect of these mutations on antiviral activity and DNA editing, both individually and in combination.
To define the effect of these mutations on the Rad60 protein, we determined the stability of SLD2 using a chemical denaturation assay at 298K.
The effect of these mutations on the ability of streptococci to form a hydrophobic surface and to generate biofilms was also investigated.
