Evidence map›Paper›PMID 16550488›Full record

ArticleThe Journal of membrane biology2005

Interactions between charged residues in the transmembrane segments of the voltage-sensing domain in the hERG channel.

M Zhang, J Liu, M Jiang, D-M Wu, K Sonawane, H R Guy, G-N Tseng

Abstract read
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In one paragraph

Article in The Journal of membrane biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Rare pathogenic mutation ofFrontiers in cardiovascular medicine · 2026
    Article
  4. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Modulation of hERG KFrontiers in pharmacology · 2020
    Review
  13. The EAG Voltage-Dependent KFrontiers in pharmacology · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Free-energy landscape of ion-channel voltage-sensor-domain activation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

7 authors.

M ZhangDepartment of Physiology, Virginia Commonwealth University, Richmond, VA 23298, USA.
J Liu
M Jiang
D-M Wu
K Sonawane
H R Guy
G-N Tseng

Funding

POST INFARCTION K CHANNEL REMODELING/MOLECULAR MECHANISMR01HL067840 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI TSENG, GEA-NY · 2001 to 2010
$2.2M
K+ CHANNELS--STRUCTURE/FUNCTION RELATION &PHARMACOLOGYR01HL046451 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI TSENG, GEA-NY · 1994 to 2006
$1.7M
NHLBI NIH HHS HL 46451NHLBI NIH HHS HL 67840
6 · The paper itself

Abstract

Studies on voltage-gated K channels such as Shaker have shown that positive charges in the voltage-sensor (S4) can form salt bridges with negative charges in the surrounding transmembrane segments in a state-dependent manner, and different charge pairings can stabilize the channels in closed or open states. The goal of this study is to identify such charge interactions in the hERG channel. This knowledge can provide constraints on the spatial relationship among transmembrane segments in the channel's voltage-sensing domain, which are necessary for modeling its structure. We first study the effects of reversing S4's positive charges on channel activation. Reversing positive charges at the outer (K525D) and inner (K538D) ends of S4 markedly accelerates hERG activation, whereas reversing the 4 positive charges in between either has no effect or slows activation. We then use the 'mutant cycle analysis' to test whether D456 (outer end of S2) and D411 (inner end of S1) can pair with K525 and K538, respectively. Other positive charges predicted to be able, or unable, to interact with D456 or D411 are also included in the analysis. The results are consistent with predictions based on the distribution of these charged residues, and confirm that there is functional coupling between D456 and K525 and between D411 and K538.

Indexed as

Amino AcidsAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCell MembraneERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsIon Channel GatingMembrane PotentialsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedOocytesProtein BindingProtein Structure, TertiaryAmino AcidsERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsMembrane Proteins

Identifiers

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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.