Evidence map›Paper›PMID 27760355›Full record

ArticleBiophysical journal2016

Extracellular Linkers Completely Transplant the Voltage Dependence from Kv1.2 Ion Channels to Kv2.1.

Fredrik Elinder, Michael Madeja, Hugo Zeberg, Peter Århem

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. An E280K Missense Variant inInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. 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

4 authors.

Fredrik ElinderDepartment of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
Michael MadejaInstitute for Physiology, University of Münster and Hertie Research Group at Center for Physiology, University of Frankfurt, Germany.
Hugo ZebergDepartment of Neuroscience, Karolinska Institutet, Stockholm, Sweden.
Peter ÅrhemDepartment of Neuroscience, Karolinska Institutet, Stockholm, Sweden. Electronic address: peter.arhem@ki.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane voltage needed to open different voltage-gated K (Kv) channels differs by up to 50 mV from each other. In this study we test the hypothesis that the channels' voltage dependences to a large extent are set by charged amino-acid residues of the extracellular linkers of the Kv channels, which electrostatically affect the charged amino-acid residues of the voltage sensor S4. Extracellular cations shift the conductance-versus-voltage curve, G(V), by interfering with these extracellular charges. We have explored these issues by analyzing the effects of the divalent strontium ion (Sr

Indexed as

Electrophysiological PhenomenaAnimalsCell MembraneEvolution, MolecularExtracellular SpaceKv1.2 Potassium ChannelXenopusKv1.2 Potassium Channel

Identifiers

PMID27760355
PMCPMC5072986

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.