Evidence map›Paper›PMID 17892302›Full record

ArticleBiochemistry2007

Preparation, functional characterization, and NMR studies of human KCNE1, a voltage-gated potassium channel accessory subunit associated with deafness and long QT syndrome.

Changlin Tian, Carlos G Vanoye, Congbao Kang, Richard C Welch, Hak Jun Kim, Alfred L George, Charles R Sanders

Open access · greenAbstract read
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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 58 citations in OpenAlex.

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  9. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  10. Article
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  12. Structural interplay of KHeartRhythm case reports · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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 at 1 institution in 1 country.

Changlin TianDepartment of Biochemistry, Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-8725, USA.
Carlos G Vanoye
Congbao Kang
Richard C Welch
Hak Jun Kim
Alfred L George
Charles R Sanders
Vanderbilt University · US

Funding

Southeast Collaboratory for High-Field Biomolecular NMRP41GM066340 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI PRESTEGARD, JAMES H · 2002 to 2006
$5.5M
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 DC007416NIGMS NIH HHS P41 GM066340
6 · The paper itself

Abstract

KCNE1, also known as minK, is a member of the KCNE family of membrane proteins that modulate the function of KCNQ1 and certain other voltage-gated potassium channels (KV). Mutations in human KCNE1 cause congenital deafness and congenital long QT syndrome, an inherited predisposition to potentially life-threatening cardiac arrhythmias. Although its modulation of KCNQ1 function has been extensively characterized, many questions remain regarding KCNE1's structure and location within the channel complex. In this study, KCNE1 was overexpressed in Escherichia coli and purified. Micellar solutions of the protein were then microinjected into Xenopus oocytes expressing KCNQ1 channels, followed by electrophysiological recordings aimed at testing whether recombinant KCNE1 can co-assemble with the channel. Nativelike modulation of channel properties was observed following injection of KCNE1 in lyso-myristoylphosphatidylglycerol (LMPG) micelles, indicating that KCNE1 is not irreversibly misfolded and that LMPG is able to act as a vehicle for delivering membrane proteins into the membranes of viable cells. 1H-15N TROSY NMR experiments indicated that LMPG micelles are well-suited for structural studies of KCNE1, leading to assignment of its backbone resonances and to relaxation studies. The chemical shift data confirmed that KCNE1's secondary structure includes several alpha-helices and demonstrated that its distal C-terminus is disordered. Surprisingly, for KCNE1 in LMPG micelles, there appears to be a break in alpha-helicity at sites 59-61, near the middle of the transmembrane segment, a feature that is accompanied by increased local backbone mobility. Given that this segment overlaps with sites 57-59, which are known to play a critical role in modulating KCNQ1 channel activation kinetics, this unusual structural feature likely has considerable functional relevance.

Indexed as

Amino Acid SequenceAnimalsArrhythmias, CardiacCloning, MolecularDeafnessEscherichia coliFemaleHumansKCNQ1 Potassium ChannelLong QT SyndromeMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataOocytesPolymerase Chain ReactionPotassium Channels, Voltage-GatedKCNE1 protein, humanKCNQ1 Potassium ChannelKCNQ1 protein, humanPotassium Channels, Voltage-GatedRecombinant ProteinsSolutions

Identifiers

PMID17892302
PMCPMC2565491
OpenAlexW2031981850

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.