IndraLab

Statements

KCNH2 binds BeKm-1. 6 / 6
| 6
reach
"Therefore, these aspects are where we begin to characterize BeKm-1 and HERG interaction and to deduce the mechanism of toxin action.We examine the effects of 1-1000 nM BeKm-1 on the HERG current ampli[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12719233
reach
"This result is consistent with our hypothesis that the structure of the S5-P linker is highly dynamic, and can be easily perturbed by mutations, toxin binding, or conformational changes in other parts[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17293393
reach
"To study the mechanism of BeKm-1 action, we characterize BeKm-1 and HERG interaction in terms of its sensitivity to changes in the extracellular or intracellular ionic composition and to changes in me[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12719233
reach
"Starting from the hERG and BeKm-1 structures, a considerably reasonable BeKm-1 and hERG complex structure was then screened out and identified by protein protein docking, molecular dynamics (MD) simulations, and calculation of relative binding free energies."
17269718
reach
"The models were further restrained based on mutant cycle analysis of BeKm-1 and hERG interactions."
17293393
reach
"It is important to point out that although such a strong state dependence of BeKm-1 and hERG interactions appears similar to that of " gating modifying toxins " that bind to the S3-S4 linkers of targe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17293393