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Pyraclofos activates KCNQ1. 24 / 24
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"Four residues in the transmembrane domain of the KCNE5 protein were found to be important for the control of the voltage dependent activation of the KCNQ1 current."
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"These results suggest that CP1 facilitates voltage-dependent activation of KCNQ1 by favoring pore opening at various voltages."
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"In addition, it has been shown that voltage sensor activation in KCNQ1 proceeds through an intermediate step before reaching full activation XREF_BIBR."
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"During a depolarizing voltage pulse that activates KCNQ1 channels, a fast decaying current following a brief hyperpolarization has been typically viewed as evidence of KCNQ1 channel inactivation."
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"Phe applications strongly facilitated voltage dependent activation of KCNQ1 and KCNE1 channels (= ~ -20 mV in V 1/2) and increased the maximal conductance over 2-fold compared to the current with no Phe application (XREF_FIG)."
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"CP1 modifies voltage-dependent activation of KCNQ1 channels by shifting the voltage dependence of channel opening, measured as the voltage dependence of the conductance ( G – V ) relationship, to more negative voltages (Fig.  xref ) among other characteristics (see below)."
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"However, after application of CP1 via injection into the oocyte, the KCNQ1 currents increased with consecutive voltage pulses, and current kinetics showed no declination during each pulse (10 µM CP1, Fig.  xref ), indicating that CP1 permits voltage-dependent activation of KCNQ1 channels, despite the depletion of PIP 2 ."
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"KCNE3 acts by promoting voltage sensor activation in KCNQ1."
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"Together our findings suggest that altered charge-pair interactions within the voltage sensor module of KCNQ1 subunits may account for slowed I (Ks) deactivation induced by S140 or V141."
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"Additionally, to test the second hypothesis that all four voltage sensors need to activate to open KCNQ1 and KCNE1 channels, we used the mutation R231C that is assumed to lock the voltage sensor in the activated state [XREF_BIBR]."
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"These results suggest the idea that CP1 interacts with the channel, such that pore opening is enhanced even in the absence of VSD activation, and that it mediates VSD-pore coupling during voltage-dependent activation in KCNQ1 channels."
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"We analyzed ML277-induced changes in the voltage-dependent activation of KCNQ1 channels."
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"In this brief review we will discuss the current evidence regarding the mechanism by which KCNE1 regulates the voltage dependent activation of KCNQ1 as the best understood example of KCNE regulation of K V channel gating."
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"Determination and validation of the KCNQ1 VSD structures in the intermediate and activated states furnishes critical information for understanding the voltage-dependent activation of KCNQ1 and interactions with KCNE accessory subunits."
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"A subsequent voltage pulse elicited much smaller KCNQ1 currents (Rundown trace, Fig. 2a) as a result of PIP depletion that had insufficient time to be replenished by endogenous enzymes between the pulses."
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"The voltage-activated K + channel Kv7.1, previously called KvLQT1, is expressed in several tissues, including the heart, kidney and cells in the inner ear lateral wall."
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"However, after application of CP1 via injection into the oocyte, the KCNQ1 currents increased with consecutive voltage pulses, and current kinetics showed no declination during each pulse (10 µM CP1, Fig. 2a, b), indicating that CP1 permits voltage-dependent activation of KCNQ1 channels, despite the depletion of PIP ."
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"KCNQ1 and KCNE1 Channel Activation by Voltage."
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"These structural models do not identify the likely mechanism for how KCNE1 modulates the voltage dependent activation of KCNQ1 as the interactions with the VSD, PGD, and S4/S5 linker suggest that regulation of VSD movement, PGD opening, and electromechanical coupling are all plausible."
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"In summary, our study demonstrates that KCNE1 alters the kinetics and voltage dependence of voltage sensor activation and channel opening of KCNQ1 channels."
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"CP1 modifies voltage-dependent activation of KCNQ1 channels by shifting the voltage dependence of channel opening, measured as the voltage dependence of the conductance (G–V) relationship, to more negative voltages (Fig. 1c) among other characteristics (see below)."
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"Here we show that KCNE5 induces both a time- and voltage dependent modulation of the KCNQ1 current."
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"XREF_BIBR The KCNQ1 gene codifies KVLQT1 (Kv7.1), a voltage activated potassium channel alpha-subunit expressed in various cell types, including cardiac myocytes."
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"KCNE5 induces time- and voltage dependent modulation of the KCNQ1 current."
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