IndraLab

Statements

CALM inhibits KCNH1. 13 / 16
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"Among them, Ca 2+ / calmodulin (CaM) potently inhibits the EAG1 channel by binding to up to three discrete intracellular areas located in its N and C termini XREF_BIBR XREF_BIBR XREF_BIBR."
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"Within the channels discussed here, Ca 2+ -CaM inhibits Eag1 (Kv10) and TRPV5/6 channels, activates SK channels, and inhibits or activates Kv7 channels depending on other factors."
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"Moreover, calmodulin (CaM) and Ca 2+ / CaM dependent protein kinase II, two Ca 2+ -binding and activated molecules widely implicated in synaptic signaling mechanisms 12, 13, serve as dynamic binding partners of mammalian Eag1 and Drosophila Eag channels, respectively 14, 15, 16, 17; for example, CaM binds to and inhibits the function of mammalian Eag1 in a Ca 2+ -dependent manner."
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"Eag1 is strongly inhibited by Ca 2+ -CaM."
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"This suggests that the integrity of the PAS-CNBh interaction is important for the mechanism of CaM mediated EAG1 channel inhibition and supports a recent electrophysiological analysis of hEAG1 inhibition by CaM."
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"Kv10.1, which is inhibited by Ca 2+ -calmodulin [ xref , xref ], would provide the negative control segment of the trio, terminating the signal."
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"However, understanding the molecular interactions that regulate hEAG1 channels could help in the design of novel therapies that mimic Ca 2+ -CaM inhibition of hEAG1 to selectively target hEAG1-expressing cancer cells."
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"This suggests that the integrity of the PAS-CNBh interaction is important for the mechanism of CaM-mediated EAG1 channel inhibition and supports a recent electrophysiological analysis of hEAG1 inhibit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Ca 2+ / CaM could then inhibit hEAG1 channels, dampening the direct stimulatory effect of PIP 2 depletion on the channels described here."
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"In addition, Eag1 is inhibited by the binding of calmodulin (CaM) only in the presence of calcium."
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"This suggests that the integrity of the PAS-CNBh interaction is important for the mechanism of CaM mediated EAG1 channel inhibition and supports a recent electrophysiological analysis of hEAG1 inhibit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
27618660
sparser
"This suggests that the integrity of the PAS-CNBh interaction is important for the mechanism of CaM-mediated EAG1 channel inhibition and supports a recent electrophysiological analysis of hEAG1 inhibition by CaM ( xref )."
27618660
sparser
"EAG1 is strongly inhibited by Ca 2+ -calmodulin (CaM) through a mechanism that is not understood."
27618660