Evidence map›Paper›PMID 31032878›Full record

ArticleBritish journal of pharmacology2019

Histidine at position 462 determines the low quinine sensitivity of ether-à-go-go channel superfamily member K

Marlen Dierich, Willem B van Ham, Anna Stary-Weinzinger, Michael G Leitner

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in British journal of pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
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 at 3 institutions in 3 countries.

Marlen DierichDepartment of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps-University Marburg, Marburg, Germany.
Willem B van HamDepartment of Medical Physiology, University Medical Center Utrecht, Utrecht, The Netherlands.
Anna Stary-WeinzingerDepartment of Pharmacology and Toxicology, University of Vienna, Vienna, Austria.
Michael G LeitnerDepartment of Neurophysiology, Institute of Physiology and Pathophysiology, Philipps-University Marburg, Marburg, Germany.ORCID 0000-0002-3259-6481
University of Vienna · ATInnsbruck Medical University · ATPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

background and purposeThe ether-à-go-go (Eag) K EXPERIMENTAL APPROACH: We analysed sensitivity of recombinant K KEY

resultsQuinine inhibited K CONCLUSIONS AND IMPLICATIONS: The quinoline-binding "motif" is not conserved within the Eag superfamily, although the overall architecture of these channels is apparently similar. Our findings highlight functional and pharmacological diversity in this group of evolutionary-conserved channels.

Indexed as

AnimalsCHO CellsCricetulusERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsHistidineModels, MolecularNerve Tissue ProteinsQuinineERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsHistidineKCNH3 protein, humanNerve Tissue ProteinsQuinine

Identifiers

PMID31032878
PMCPMC6609544
OpenAlexW2943502290

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.