Evidence map›Paper›PMID 19244238›Full record

ArticleThe Journal of biological chemistry2009

Bimane fluorescence scanning suggests secondary structure near the S3-S4 linker of BK channels.

Nina P Semenova, Karin Abarca-Heidemann, Eva Loranc, Brad S Rothberg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Andrology · 2025
    Review
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  11. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors at 1 institution in 1 country.

Nina P SemenovaDepartment of Physiology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, USA.
Karin Abarca-Heidemann
Eva Loranc
Brad S Rothberg
The University of Texas Health Science Center at San Antonio · US

Funding

Structure and Function of Potassium ChannelsR01GM068523 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI ROTHBERG, BRAD S. · 2004 to 2010
$1.9M
NIGMS NIH HHS GM68523NIGMS NIH HHS R01 GM068523
6 · The paper itself

Abstract

Gating of large conductance Ca(2+)-activated K(+) channels (BK or maxi-K channels) is controlled by a Ca(2+)-sensor, formed by the channel cytoplasmic C-terminal domain, and a voltage sensor, formed by its S0-S4 transmembrane helices. Here we analyze structural properties of a portion of the BK channel voltage sensing domain, the S3-S4 linker, using fluorescence lifetime spectroscopy. Single residues in the S3-S4 linker region were substituted with cysteine, and the cysteine-substituted mutants were expressed in CHO cells and covalently labeled with the sulfhydryl-reactive fluorophore monobromo-trimethylammonio-bimane (qBBr). qBBr fluorescence is quenched by tryptophan and, to a lesser extent, tyrosine side chains. We found that qBBr fluorescence in several of the labeled cysteine-substituted channels shows position-specific quenching, as indicated by increase of the brief lifetime component of the qBBr fluorescence decay. Quenching was reduced with the mutation W203F (in the S4 segment), suggesting that Trp-203 acts as a quenching group. Our results suggest a working hypothesis for the secondary structure of the BK channel S3-S4 region, and places residues Leu-204, Gly-205, and Leu-206 within the extracellular end of the S4 helix.

Indexed as

Protein Structure, SecondaryAmino Acid SequenceAnimalsBridged Bicyclo Compounds, HeterocyclicCHO CellsCricetinaeCricetulusFluorescent DyesLarge-Conductance Calcium-Activated Potassium ChannelsMiceModels, MolecularMolecular Sequence DataMolecular StructureMutagenesis, Site-DirectedSequence AlignmentSpectrometry, FluorescencebimanesBridged Bicyclo Compounds, HeterocyclicFluorescent DyesLarge-Conductance Calcium-Activated Potassium ChannelsTryptophanTyrosine

Identifiers

PMID19244238
PMCPMC2667755
OpenAlexW2019333745

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.