Evidence map›Paper›PMID 26745405›Full record

ReviewBiophysical journal2016

Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.

Jianmin Cui

Open access · bronzeAbstract readReview
In one paragraph

Review in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 75 citations in OpenAlex.

  1. Trial
  2. Article
  3. PIPNature communications · 2026
    Article
  4. Article
  5. PIPResearch square · 2025
    Article
  6. Article
  7. Targeting the ICirculation research · 2024
    Article
  8. Article
  9. NovelFrontiers in physiology · 2024
    Article
  10. Article
  11. The membrane electric field regulates the PIPProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Conformational rearrangements in the second voltage sensor domain switch PIPProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Cells · 2022
    Article
  15. Article
  16. PIPCommunications biology · 2021
    Article
  17. Modulating the voltage sensor of a cardiac potassium channel shows antiarrhythmic effects.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Potassium Channels and Their Potential Roles in Substance Use Disorders.International journal of molecular sciences · 2021
    Review
  19. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  20. Insights into Cardiac IKs (KCNQ1/KCNE1) Channels Regulation.International journal of molecular sciences · 2020
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Jianmin CuiDepartment of Biomedical Engineering, Cardiac Bioelectricity and Arrhythmia Center and Center for the Investigation of Membrane Excitability Disorders, Washington University, St. Louis, Missouri. Electronic address: jcui@wustl.edu.
Texas Cardiac Arrhythmia · US

Funding

Ca2+ Dependent K+ Channels: Allosteric GatingR01HL070393 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2002 to 2015
$4.9M
KCNQ CHANNELS: GATING AND SUBUNITS MODULATIONR01NS092570 · NINDS · WASHINGTON UNIVERSITY · PI SILVA, JONATHAN R · 2015 to 2020
$1.7M
SUBUNITS INTERACTION IN THE FUNCTION OF BK CHANNELSR01NS060706 · NINDS · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2010 to 2013
$1.3M
NHLBI NIH HHS R01 HL070393NHLBI NIH HHS R01-HL70393NINDS NIH HHS R01 NS060706NINDS NIH HHS R01 NS092570NINDS NIH HHS R01-NS092570
6 · The paper itself

Abstract

Gating of voltage-dependent cation channels involves three general molecular processes: voltage sensor activation, sensor-pore coupling, and pore opening. KCNQ1 is a voltage-gated potassium (Kv) channel whose distinctive properties have provided novel insights on fundamental principles of voltage-dependent gating. 1) Similar to other Kv channels, KCNQ1 voltage sensor activation undergoes two resolvable steps; but, unique to KCNQ1, the pore opens at both the intermediate and activated state of voltage sensor activation. The voltage sensor-pore coupling differs in the intermediate-open and the activated-open states, resulting in changes of open pore properties during voltage sensor activation. 2) The voltage sensor-pore coupling and pore opening require the membrane lipid PIP2 and intracellular ATP, respectively, as cofactors, thus voltage-dependent gating is dependent on multiple stimuli, including the binding of intracellular signaling molecules. These mechanisms underlie the extraordinary KCNE1 subunit modification of the KCNQ1 channel and have significant physiological implications.

Indexed as

Electrophysiological PhenomenaIon Channel GatingAdenosine TriphosphateAmino Acid SequenceIntracellular SpaceKCNQ1 Potassium ChannelMolecular Sequence DataPorosityAdenosine TriphosphateKCNQ1 Potassium Channel

Identifiers

PMID26745405
PMCPMC4805877
OpenAlexW2225015463

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.