Evidence map›Paper›PMID 20044833›Full record

ArticleBiochemistry2010

Functional delivery of a membrane protein into oocyte membranes using bicelles.

Congbao Kang, Carlos G Vanoye, Richard C Welch, Wade D Van Horn, Charles R Sanders

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013
    Review
  16. Review
  17. Article
  18. Stoichiometry of the KCNQ1 - KCNE1 ion channel complex.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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.

Congbao KangDepartment of Biochemistry, Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-8725, USA.
Carlos G Vanoye
Richard C Welch
Wade D Van Horn
Charles R Sanders
Vanderbilt University · US

Funding

TRAINING PROGRAM IN ION CHANNEL AND TRANSPORTER BIOLOGYT32NS007491 · NINDS · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DENTON, JEROD S. · 2001 to 2020
$4.1M
Structural Basis for KCNE Modulation of the KCNQ1 ChannelR01DC007416 · NIDCD · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R, VANOYE, CARLOS G. · 2006 to 2014
$3.0M
NIDCD NIH HHS R01 DC007416NINDS NIH HHS T32 NS007491
6 · The paper itself

Abstract

Voltage-gated potassium channel modulatory membrane protein KCNE3 was overexpressed and purified into both micelles and bicelles. Remarkably, microinjection of KCNE3 in bicelles into Xenopus oocytes resulted in functional co-assembly with the human KCNQ1 channel expressed therein. Microinjection of LMPC micelles containing KCNE3 did not result in channel modulation, indicating that bicelles sometimes succeed at delivering a membrane protein into a cellular membrane when classical micelles fail. Backbone NMR resonance assignments were completed for KCNE3 in both bicelles and LMPC, indicating that the secondary structure distribution in KCNE3's N-terminus and transmembrane domains exhibits only modest differences from that of KCNE1, even though these KCNE family members have very different effects on KCNQ1 channel function.

Indexed as

Amino Acid SequenceAnimalsHumansKCNQ1 Potassium ChannelMembrane PotentialsMembrane ProteinsMicellesMicroinjectionsModels, BiologicalMolecular Sequence DataOocytesPotassium Channels, Voltage-GatedXenopusKCNE3 protein, humanKCNQ1 Potassium ChannelKCNQ1 protein, humanMembrane ProteinsMicellesPotassium Channels, Voltage-Gated

Identifiers

PMID20044833
PMCPMC2811756
OpenAlexW1985442151

What OpenQuestion holds

Textmetadata
LicenceTDM
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.