Evidence map›Paper›PMID 12626667›Full record

ArticleThe Journal of physiology2003

Modulation of human ether-à-go-go-related K+ (HERG) channel inactivation by Cs+ and K+.

Shetuan Zhang, Steven J Kehl, David Fedida

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Recording ten-fold larger IFrontiers in physiology · 2024
    Article
  2. Article
  3. Bidirectional flow of the funny current (IProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. KNeuroscience · 2020
    Article
  6. Modulation of Ether-à-Go-Go Related Gene (ERG) Current Governs Intrinsic Persistent Activity in Rodent Neocortical Pyramidal Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  7. Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Na+ permeation and block of hERG potassium channels.The Journal of general physiology · 2006
    Article
  15. Modulation of HERG channel inactivation by external cations.European biophysics journal : EBJ · 2004
    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.

Shetuan ZhangDepartment of Physiology, University of British Columbia, 2146 Health Sciences Mall, Vancouver, BC, Canada V6T 1Z3.
Steven J Kehl
David Fedida
University of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Unlike many other native and cloned K+ channels, human ether-à-go-go-related K+ (HERG) channels show significant Cs+ permeability with a PCs/PK (the permeability of Cs+ relative to that of K+) of 0.36 +/- 0.03 (n = 10). Here, we find that raising the concentration of external Cs+ (Cs+o) dramatically slows HERG channel inactivation without affecting activation. Replacement of 5 mM K+o by 135 mM Cs+o increased both inactivation and recovery time constants and shifted the mid-point of the steady-state inactivation curve by 25 mV in the depolarized direction (n = 6, P < 0.01). Raising [Cs+]o also modulated the voltage sensitivity of inactivation gating. With 130 mM Cs+i and 135 mM NMDG+o, the inactivation time constant decreased e-fold per 47.5 +/- 1.1 mV (n = 5), and when 20 mM Cs+ was added to the bath solution, the inactivation time constant decreased e-fold per 20.6 +/- 1.3 mV (n = 5, P < 0.01). A quantitative analysis suggests that Cs+o binds to a site in the pore that is influenced by the transmembrane electrical field, so that Cs+o-induced slowing of HERG inactivation is less prominent at strong depolarizations. K+o has effects that are similar to Cs+o and their effects were additive, suggesting Cs+o and K+o may share a common mechanism of action. The strong effects of Cs+ on inactivation but not on activation highlight the importance of ion and channel interactions during the onset of inactivation in the HERG channel.

Indexed as

Potassium Channels, Voltage-GatedCation Transport ProteinsCell LineCesiumERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsHumansKidneyKineticsMembrane PotentialsPotassiumPotassium Channel BlockersPotassium ChannelsTransfectionCation Transport ProteinsCesiumERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsKCNH2 protein, humanKCNH6 protein, humanPotassiumPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID12626667
PMCPMC2342897
OpenAlexW2171624265

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.