IndraLab

Statements

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"Furthermore, HCN4 has the most hyperpolarized midpoint of activation (V ≈ −100 mV) and HCN1 the most depolarized (V ≈ −70 mV).1, 42 Additionally, the activation curve of HCN4 can be strongly shifted toward more depolarized potentials by direct binding of cAMP and by Src kinase phosphorylation, whereas HCN1 activation is only slightly modulated by cAMP and not affected by Src kinase."
30585408
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"HCN2-related I (but not HCN1-related I ) is highly modulated by cAMP which: a) increases I magnitude by increasing HCN2 open probability [54], [55]; b) depolarises V (by ∼15 mV) and c) accelerates I activation [1]."
23236374
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"In contrast to HCN2 and HCN4, PEX5R failed to exert any obvious effect on gating and cAMP modulation of HCN1 channels in excised patches."
19555650
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"By contrast, the C-linker and CNBD inhibit HCN1 channel opening to a lesser extent and this lesser tonic inhibition is relieved by cAMP."
34237319
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"It is known that heteromeric channels of HCN1/HCN2 have voltage and cAMP dependency similar to HCN2 rather than HCN1 (Chen et al., 2001; Ulens and Tytgat, 2001), while HCN1 and HCN2 are modulated mostly by PKC (Reetz and Strauss, 2013) and cAMP (Wainger et al., 2001; Kusch et al., 2011), respectively."
35558874
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"First, cAMP activates homomers of intact bCNG1 with low efficacy, so low efficacy is not in itself an absolute indicator of BD misfolding."
11696610
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"This mutation did not change the cAMP-induced effect in HCN1, supporting the structural evidence that the tetrad is not formed in this isoform."
34166608
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"It has been shown that binding of TRIP8b impairs cAMP effects on HCN2 and HCN4 but does not affect cAMP modulation of HCN1."
30585408
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"Thus, cAMP might produce little or no net shift in the activation range of I h due solely to HCN1 and HCN3."
21456027
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"However, the I h fast time course of activation and cAMP-induced shift in activation are consistent neither with HCN1 nor HCN2 homomeric channels expressed in a heterologous system."
34197835