ReviewBiophysics and physicobiology2019
Gating modulation of the KCNQ1 channel by KCNE proteins studied by voltage-clamp fluorometry.
Review in Biophysics and physicobiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- A Six-Gene Mitochondrial Signature Predicts Prognosis in Dedifferentiated Thyroid Cancer.International journal of general medicine · 2025Article
- NovelFrontiers in physiology · 2024Article
- Article
- Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state.eLife · 2020Article
- Validation of Identified Susceptible Gene Variants for New-Onset Diabetes in Renal Transplant Recipients.Journal of clinical medicine · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The KCNQ1 channel is a voltage-dependent potassium channel and is ubiquitously expressed throughout the human body including the heart, lung, kidney, pancreas, intestine and inner ear. Gating properties of the KCNQ1 channel are modulated by KCNE auxiliary subunits. For example, the KCNQ1-KCNE1 channel produces a slowly-activating potassium current, while KCNE3 makes KCNQ1 a voltage-independent, constitutively open channel. Thus, physiological functions of KCNQ1 channels are greatly dependent on the type of KCNE protein that is co-expressed in that organ. It has long been debated how the similar single transmembrane KCNE proteins produce quite different gating behaviors. Recent applications of voltage-clamp fluorometry (VCF) for the KCNQ1 channel have shed light on this question. The VCF is a quite sensitive method to detect structural changes of membrane proteins and is especially suitable for tracking the voltage sensor domains of voltage-gated ion channels. In this short review, I will introduce how the VCF technique can be applied to detect structural changes and what have been revealed by the recent VCF applications to the gating modulation of KCNQ1 channels by KCNE proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.