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"When domains that mediate the interaction of Kv1.4 and PSD-95 were disrupted, Kv1.4 localized nonspecifically."
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"Defined substitutions within the four C-terminal residues could abolish Kv1.4 interaction with PSD-95 (as measured in the yeast two-hybrid assay), and all the mutations that abolished Kv1.4 binding to PSD-95 also completely abolished coclustering in transfected COS cells ( Table 1 )."
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"However, the yeast cell growth was slowed by halothane ( xref ) and isoflurane ( xref ) in a dose-dependent manner, indicating that these anesthetics dose-dependently inhibit PDZ domain-mediated protein-protein interactions between PSD-95 and Kv1.4."
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"The strength of this interaction in the yeast two-hybrid system was similar to the binding of the Shaker-type K + channel Kv1.4 to the PDZ1+2 domains of PSD-95."
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"Although direct interaction of E-dlg PDZ domains with Kv1.4 has yet to be demonstrated, these data are consistent with a function for E-dlg in regulating development and transmission in the synapse."
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"To determine whether inhaled anesthetics disrupt PDZ domain-mediated protein-protein interactions in a physiological setting, we used a co-immunoprecipitation assay to detect in vivo binding of PSD-95 to Kv1.4."
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"In the same assay, an H 6 -tagged fusion protein of PDZ1-2 of PSD-95 bound specifically to Kv1.4 ( Figure 1B , right)."
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