Evidence map›Paper›PMID 10102937›Full record

ArticleThe Journal of general physiology1999

Human ether-à-go-go-related gene K+ channel gating probed with extracellular ca2+. Evidence for two distinct voltage sensors.

J P Johnson, F M Mullins, P B Bennett

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Calcium and arrhythmogenesis.Physiological reviews · 2007
    Pooled it
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  4. Review
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  9. Modification of hERG1 channel gating by Cd2+.The Journal of general physiology · 2010
    Article
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  18. Article
  19. Saxitoxin is a gating modifier of HERG K+ channels.The Journal of general physiology · 2003
    Article
  20. 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

3 authors at 1 institution in 1 country.

J P JohnsonDepartment of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6602, USA.
F M Mullins
P B Bennett
Vanderbilt University · US

Funding

TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007628 · NIGMS · VANDERBILT UNIVERSITY · PI BARNETT, JOEY VICTOR, KAVALALI, EGE T · 1985 to 2022
$11.2M
Transcriptional remodeling in cardiac arrhythmiasP01HL046681 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L. · 1992 to 2006
$8.1M
Training In Cardiovascular ResearchT32HL007411 · NHLBI · VANDERBILT UNIVERSITY · PI BECKMAN, JOSHUA A · 1985 to 2020
$7.2M
INACTIVATION GATING OF SODIUM CHANNELSR01HL051197 · NHLBI · VANDERBILT UNIVERSITY · PI BENNETT, PAUL B. · 1994 to 1998
–
NHLBI NIH HHS HL-51197NHLBI NIH HHS P01 HL046681NHLBI NIH HHS T32 HL007411NHLBI NIH HHS T32 HL07411NIGMS NIH HHS T32 GM007628NIGMS NIH HHS T32 GM07628
6 · The paper itself

Abstract

Human ether-à-go-go-related gene (HERG) encoded K+ channels were expressed in Chinese hamster ovary (CHO-K1) cells and studied by whole-cell voltage clamp in the presence of varied extracellular Ca2+ concentrations and physiological external K+. Elevation of external Ca2+ from 1.8 to 10 mM resulted in a reduction of whole-cell K+ current amplitude, slowed activation kinetics, and an increased rate of deactivation. The midpoint of the voltage dependence of activation was also shifted +22.3 +/- 2.5 mV to more depolarized potentials. In contrast, the kinetics and voltage dependence of channel inactivation were hardly affected by increased extracellular Ca2+. Neither Ca2+ screening of diffuse membrane surface charges nor open channel block could explain these changes. However, selective changes in the voltage-dependent activation, but not inactivation gating, account for the effects of Ca2+ on Human ether-à-go-go-related gene current amplitude and kinetics. The differential effects of extracellular Ca2+ on the activation and inactivation gating indicate that these processes have distinct voltage-sensing mechanisms. Thus, Ca2+ appears to directly interact with externally accessible channel residues to alter the membrane potential detected by the activation voltage sensor, yet Ca2+ binding to this site is ineffective in modifying the inactivation gating machinery.

Indexed as

CalciumCation Transport ProteinsDNA-Binding ProteinsPotassium Channels, Voltage-GatedTrans-ActivatorsAlgorithmsAnimalsCHO CellsCricetinaeDNAElectrophysiologyERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsExtracellular SpaceHumansIon Channel GatingCalciumCation Transport ProteinsDNADNA-Binding ProteinsERG1 Potassium ChannelERG protein, humanEther-A-Go-Go Potassium ChannelsKCNH2 protein, humanKCNH6 protein, humanPotassium ChannelsPotassium Channels, Voltage-GatedTrans-ActivatorsTranscriptional Regulator ERG

Identifiers

PMID10102937
PMCPMC2217168
OpenAlexW1991690011

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
measurements read1
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.