Evidence map›Paper›PMID 30853698›Full record

ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2019

Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.

Yasushi Okamura, Yoshifumi Okochi

Open access · diamondAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. HInternational journal of molecular sciences · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  6. Review
  7. The EAG Voltage-Dependent KFrontiers in pharmacology · 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

2 authors at 1 institution in 1 country.

Yasushi OkamuraDepartment of Physiology, Graduate School of Medicine, Osaka University.
Yoshifumi OkochiDepartment of Physiology, Graduate School of Medicine, Osaka University.
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The voltage sensor domain (VSD) has long been studied as a unique domain intrinsic to voltage-gated ion channels (VGICs). Within VGICs, the VSD is tightly coupled to the pore-gate domain (PGD) in diverse ways suitable for its specific function in each physiological context, including action potential generation, muscle contraction and relaxation, hormone and neurotransmitter secretion, and cardiac pacemaking. However, some VSD-containing proteins lack a PGD. Voltage-sensing phosphatase contains a cytoplasmic phosphoinositide phosphatase with similarity to phosphatase and tensin homolog (PTEN). H

Indexed as

Cell MembraneHumansIon Channel GatingIon ChannelsModels, MolecularPhosphoric Monoester HydrolasesProtein BindingProtein ConformationProtein MultimerizationProtein SubunitsSignal TransductionHVCN1 protein, humanIon ChannelsPhosphoric Monoester HydrolasesProtein Subunitsgatingmembrane potentialphosphoinositideprotonvoltage sensor

Identifiers

PMID30853698
PMCPMC6541726
OpenAlexW2922293390

What OpenQuestion 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 OpenQuestion graph.