Evidence map›Paper›PMID 17347852›Full record

ReviewPflugers Archiv : European journal of physiology2007

Biodiversity of voltage sensor domain proteins.

Yasushi Okamura

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  3. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
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  5. Upward movement of IS4 and IIIS4 is a rate-limiting stage in CaPflugers Archiv : European journal of physiology · 2016
    Article
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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.

Yasushi OkamuraSection of Developmental Neurophysiology, Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Higashiyama 5-1, Myodaiji-cho, Okazaki, Aichi, 444-8787, Japan. yokamura@nips.ac.jp
National Institutes of Natural Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The six-transmembrane type voltage-gated ion channels play an essential role in neuronal excitability, muscle contraction, and secretion. The voltage sensor domain (VSD) is the key element of voltage-gated ion channels for sensing transmembrane potential, and has been studied at the levels of both biophysics and protein structure. Two recently identified proteins containing VSD without a pore domain showed unexpected biological roles: regulation of phosphatase activity and proton permeation. These proteins not only provide novel platforms to understand mechanisms of voltage sensing and ion permeation but also highlight previously unappreciated roles of membrane potential in non-neuronal cells.

Indexed as

Amino Acid SequenceAnimalsCiona intestinalisHumansIon Channel GatingIon ChannelsMembrane PotentialsModels, BiologicalModels, MolecularMolecular Sequence DataPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein Structure, TertiarySequence Homology, Amino AcidShaker Superfamily of Potassium ChannelsIon ChannelsPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesShaker Superfamily of Potassium Channelsvoltage-sensor-containing phosphatase, Ciona intestinalis

Identifiers

PMID17347852
OpenAlexW2018783096

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.