IndraLab

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"Consistently, by visualizing the interaction between YFP labeled CaM and Cerulean labeled hEAG1 in mammalian cells by Forster resonance energy transfer (FRET), Goncalves et al. [XREF_BIBR] found that the high affinity BD-N binding domain and the second C-terminal binding domain BD-C2 are predominantly involved in EAG1 channel inhibition by Ca 2+."

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"In conclusion, Procyanidin B1 is a small molecule inhibitor of the Kv10.1 channel, with a potent inhibitory effect on the Kv10.1 channel in a concentration-dependent manner.Studies have shown that the[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Intracellular calcium at nanomolar concentrations inhibits eag1 currents through calmodulin binding to the eag1 C-terminus [46] , the binding is calcium dependent with an apparent K D of 480 nM."

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"HEAG1 Channels Lacking the PAS-cap Are Potentiated Rather than Inhibited by Ca 2+ i."

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"Within the channels discussed here, Ca -CaM inhibits Eag1 (Kv10) and TRPV5/6 channels, activates SK channels, and inhibits or activates Kv7 channels depending on other factors.Among ion channels, those that selectively allow the passage K ions display the largest diversity."

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"XREF_BIBR reported that the inhibition of hEAG1 by Ca 2+ was mediated by the direct binding of Ca 2+ / CaM to the C-terminus (AA 707-726) of the channel."

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"Kv10.1 channels are strongly inhibited by Ca /calmodulin , reactive oxygen species , and the phospholipid PIP , and there exists the possibility that more potent endogenous modulators remain to be discovered."

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"HEAG1 Inhibition by Ca 2+ i Is CaM mediated."

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"EAG1 is strongly inhibited by Ca 2+ -calmodulin (CaM) through a mechanism that is not understood."