Evidence map›Paper›PMID 32122972›Full record

ArticleThe Journal of biological chemistry2020

Mechanical stretch increases Kv1.5 current through an interaction between the S1-S2 linker and N-terminus of the channel.

Alexandria O Milton, Tingzhong Wang, Wentao Li, Jun Guo, Shetuan Zhang

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

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 35% 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, 1 synthesis or guideline pooled it, 3 citations in OpenAlex.

  1. Pooled it
  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

5 authors at 1 institution in 1 country.

Alexandria O MiltonDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Tingzhong WangDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Wentao LiDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Jun GuoDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Shetuan ZhangDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.
Queen's University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The voltage-gated potassium channel Kv1.5 plays important roles in atrial repolarization and regulation of vascular tone. In the present study, we investigated the effects of mechanical stretch on Kv1.5 channels. We induced mechanical stretch by centrifuging or culturing Kv1.5-expressing HEK 293 cells and neonatal rat ventricular myocytes in low osmolarity (LO) medium and then recorded Kv1.5 current (I

Indexed as

Stress, MechanicalAmino Acid SequenceAnimalsBinding SitesCells, CulturedGene Expression RegulationGlycosylationHEK293 CellsHumansKv1.5 Potassium ChannelMembrane PotentialsMuscle CellsOsmotic PressureProtein DomainsPyrazolesPyrimidines4-amino-5-(4-methylphenyl)-7-(tert-butyl)pyrazolo(3,4-d)pyrimidineKv1.5 Potassium ChannelPyrazolesPyrimidinessrc-Family Kinasescell biologyelectrophysiologyion channelKv1.5mechanical stretchmechanotransductionmolecular biologypatch clamppotassium channelSrcSrc kinasestructure-functionvoltage-gated potassium channel

Identifiers

PMID32122972
PMCPMC7136002
OpenAlexW3009723171

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.