2017年10月11日 · It is widely recognised that the KCNQ1/KCNE1 (Q1/E1) channel requires phosphatidylinositol-4,5-bisphosphate (PIP2) binding for function. We previously identified a …

2006年10月19日 · As illustrated in figure 4C, the WT VSV-tagged KCNE1-KCNQ1 fusion protein, but not the fusion-proteins containing Y111C, L114P and P117L mutations, was readily …

To better discriminate differences in cellular localization of KCNQ1 between S and AS subjects, we transfected the iPSC-CMs with a plasmid over-expressing wild-type (WT) or mutant …

2021年7月20日 · Using recent structures of KCNQ1 and KCNE beta subunits in different states, we present a mechanism by which KCNE1 rotates the VSD relative to the PD and affects the …

2018年3月7日 · We investigated the impact of 51 KCNQ1 variants with mutations located within the voltage sensor domain (VSD), with an emphasis on elucidating effects on cell surface …

2008年8月1日 · KCNQ1 (alias KvLQT1 or Kv7.1) and KCNE1 (alias IsK or minK) co-assemble to form the voltage-activated K + channel responsible for IKs —a major repolarizing current in the …

VSV-positive staining of WT KCNQ1 was present in S-, AS-, and CTR-iPSC-CMs but the signal intensity was lower in S-iPSC-CMs compared with AS-and CTR-iPSC-CMs ( Figure 3 A).

2020年2月25日 · KCNQ1 adopts the canonical structural organization of the K V superfamily in which the central homotetrameric pore domain is flanked by four VSDs, each with four …

2020年5月1日 · KCNQ1 presents a unique functional feature when compared to other VGLs, where it can switch from the voltage dependent state to the constitutively active state. The …

2020年1月23日 · KCNQ1, also known as Kv7.1, is a voltage-dependent K + channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional …