Evidence map›Paper›PMID 17999538›Full record

ArticleBiochemistry2007

Structural models for the KCNQ1 voltage-gated potassium channel.

Jarrod A Smith, Carlos G Vanoye, Alfred L George, Jens Meiler, Charles R Sanders

Open access · greenAbstract readValidation Study
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Article
  3. Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Compound HeterozygousFrontiers in cardiovascular medicine · 2021
    Article
  9. Review
  10. Article
  11. Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.American journal of physiology. Heart and circulatory physiology · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Late-onset severe long QT syndrome.Annals of noninvasive electrocardiology : the official journal of the International Society for Holter and Noninvasive Electrocardiology, Inc · 2018
    Article
  18. Article
  19. 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

5 authors at 1 institution in 1 country.

Jarrod A SmithDepartment of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232-8725, USA.
Carlos G Vanoye
Alfred L George
Jens Meiler
Charles R Sanders
Vanderbilt University · US

Funding

Structural Basis for KCNE Modulation of the KCNQ1 ChannelR01DC007416 · NIDCD · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R, VANOYE, CARLOS G. · 2006 to 2014
$3.0M
Molecular Physiology of KCNE Potassium Channel SubunitsR01HL077188 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L. · 2005 to 2008
$1.5M
NHLBI NIH HHS HL077188NHLBI NIH HHS R01 HL077188NIDCD NIH HHS R01 DC007416
6 · The paper itself

Abstract

Mutations in the human voltage-gated potassium channel KCNQ1 are associated with predisposition to deafness and various cardiac arrhythmia syndromes including congenital long QT syndrome, familial atrial fibrillation, and sudden infant death syndrome. In this work 3-D structural models were developed for both the open and closed states of human KCNQ1 to facilitate structurally based hypotheses regarding mutation-phenotype relationships. The KCNQ1 open state was modeled using Rosetta in conjunction with Molecular Operating Environment software, and is based primarily on the recently determined open state structure of rat Kv1.2 (Long, S. B., et al. (2005) Science 309, 897-903). The closed state model for KCNQ1 was developed based on the crystal structures of bacterial potassium channels and the closed state model for Kv1.2 of Yarov-Yarovoy et al. ((2006) Proc. Natl. Acad. Sci. U.S.A. 103, 7292-7207). Using the new models for KCNQ1, we generated a database for the location and predicted residue-residue interactions for more than 85 disease-linked sites in both open and closed states. These data can be used to generate structure-based hypotheses for disease phenotypes associated with each mutation. The potential utility of these models and the database is exemplified by the surprising observation that four of the five known mutations in KCNQ1 that are associated with gain-of-function KCNQ1 defects are predicted to share a common interface in the open state structure between the S1 segment of the voltage sensor in one subunit and both the S5 segment and top of the pore helix from another subunit. This interface evidently plays an important role in channel gating.

Indexed as

Models, MolecularAmino Acid SequenceHumansKCNQ1 Potassium ChannelMolecular Sequence DataKCNQ1 Potassium ChannelKCNQ1 protein, human

Identifiers

PMID17999538
PMCPMC2565492
OpenAlexW2066125672

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.