IndraLab

Statements


14 7 | 3 9

sparser
"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."

sparser
"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."

sparser
"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[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"The interaction between Kv1.4 and PSD-95 was proposed to be critical for the axonal targeting of Kv1.4 channels (Arnold and Clapham, 1999)."

sparser
"In the same assay, an H 6 -tagged fusion protein of PDZ1-2 of PSD-95 bound specifically to Kv1.4 ( Figure 1B , right)."

sparser
"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."

sparser
"When domains that mediate the interaction of Kv1.4 and PSD-95 were disrupted, Kv1.4 localized nonspecifically."

sparser
"This co-clustering activity is specific for ADAM23, as N-cadherin was not recruited to the PSD-95-Kv1.4 clusters ( xref F)."

reach
"However, the yeast cell growth was slowed by halothane (Fig. 1, A and B) and isoflurane (Fig. 1, C–E) in a dose-dependent manner, indicating that these anesthetics dose-dependently inhibit PDZ domain-mediated protein-protein interactions between PSD-95 and Kv1.4."

reach
"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."

sparser
"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."

sparser
"In this scenario, PSD-95 interacts with Kv1.4, causing the aggregation of both proteins at the cell surface."