Evidence map›Paper›PMID 17329207›Full record

ArticleNeuron2007

Structural insight into KCNQ (Kv7) channel assembly and channelopathy.

Rebecca J Howard, Kimberly A Clark, James M Holton, Daniel L Minor

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
9.1field-weighted citation impact, top 2% 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

102 citing papers in PubMed, 164 citations in OpenAlex.

  1. MultimodalCirculation · 2026
    Article
  2. KArchiv der Pharmazie · 2026
    Review
  3. Article
  4. Mapping the Functional Landscape ofmedRxiv : the preprint server for health sciences · 2025
    Article
  5. Article
  6. Integrative analysis of KCNQ1 variants reveals molecular mechanisms of type 1 long QT syndrome pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024
    Article
  8. Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024
    Review
  9. Article
  10. Review
  11. HumanJournal of neurophysiology · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Chemical modulation of Kv7 potassium channels.RSC medicinal chemistry · 2021
    Review
  16. Article
  17. Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021
    Article
  18. High-Resolution Structures of KHandbook of experimental pharmacology · 2021
    Article
  19. Neurohormonal Regulation of IJournal of the American Heart Association · 2020
    Review
  20. Article

42 more citing papers are in PubMed but not listed here.

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 1 country.

Rebecca J HowardChemistry and Chemical Biology Graduate Program, University of California, San Francisco, CA 94158-2330, USA.
Kimberly A Clark
James M Holton
Daniel L Minor
QB3 · USLawrence Berkeley National Laboratory · USUniversity of California, San Francisco · US

Funding

Structural Studies of Ion Channel Assembly and Signaling ComplexesR01DC007664 · NIDCD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DANIEL L MINOR · 2005 to 2026
$8.2M
NIDCD NIH HHS R01 DC007664
6 · The paper itself

Abstract

Kv7.x (KCNQ) voltage-gated potassium channels form the cardiac and auditory I(Ks) current and the neuronal M-current. The five Kv7 subtypes have distinct assembly preferences encoded by a C-terminal cytoplasmic assembly domain, the A-domain Tail. Here, we present the high-resolution structure of the Kv7.4 A-domain Tail together with biochemical experiments that show that the domain is a self-assembling, parallel, four-stranded coiled coil. Structural analysis and biochemical studies indicate conservation of the coiled coil in all Kv7 subtypes and that a limited set of interactions encode assembly specificity determinants. Kv7 mutations have prominent roles in arrhythmias, deafness, and epilepsy. The structure together with biochemical data indicate that A-domain Tail arrhythmia mutations cluster on the solvent-accessible surface of the subunit interface at a likely site of action for modulatory proteins. Together, the data provide a framework for understanding Kv7 assembly specificity and the molecular basis of a distinct set of Kv7 channelopathies.

Indexed as

Amino Acid SequenceCrystallographyHumansHydrophobic and Hydrophilic InteractionsKCNQ1 Potassium ChannelKCNQ Potassium ChannelsLong QT SyndromeMolecular Sequence DataMutationProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity RelationshipKCNQ1 Potassium ChannelKCNQ1 protein, humanKCNQ4 protein, humanKCNQ Potassium Channels

Identifiers

PMID17329207
PMCPMC3011230
OpenAlexW2108022643

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.