IndraLab

Statements


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"HERG channel blockers have been shown to inhibit the channels in a voltage dependent manner, suggesting that these drugs bind to the open or inactivated state of HERG channels."

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"This observation demonstrates that voltage sensor return is less energetically favorable than pore closure upon repolarization and demonstrates the important role for voltage sensor relaxation is stab[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"A key hERG mutation, E518C, caused the large positive shifts in the hERG activation voltage."

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"This indicates that maintenance of the consensus site for PKA phosphorylation in the amino-terminus is not necessary for the TRH induced modifications of HERG activation voltage dependence.The shifts [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"A common structural feature shared by our three inactivating rEag1 mutant constructs is the lack of the rEag1 eag domain, which implies that the rEag1 eag domain, but not the hERG1 eag domain, may somehow modulate an inherent voltage dependent inactivation of rEag1 K + channels."

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"Erg1 mediated outward currents displayed voltage dependent activation and C-type inactivation."