Evidence map›Paper›PMID 29581567›Full record

ArticleNature structural & molecular biology2018

Gating interaction maps reveal a noncanonical electromechanical coupling mode in the Shaker K

Ana I Fernández-Mariño, Tyler J Harpole, Kevin Oelstrom, Lucie Delemotte, Baron Chanda

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

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  11. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
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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

5 authors.

Ana I Fernández-MariñoDepartment of Neuroscience, SMPH, University of Wisconsin, Madison, WI, USA.ORCID 0000-0002-6995-4529
Tyler J HarpoleScience for Life Laboratory, Department of Applied Physics, KTH Royal Institute of Technology, Solna, Sweden.
Kevin OelstromDepartment of Neuroscience, SMPH, University of Wisconsin, Madison, WI, USA.
Lucie DelemotteScience for Life Laboratory, Department of Applied Physics, KTH Royal Institute of Technology, Solna, Sweden.
Baron ChandaDepartment of Neuroscience, SMPH, University of Wisconsin, Madison, WI, USA. chanda@wisc.edu.ORCID 0000-0003-4954-7034

Funding

Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Training Program In Molecular AND Cellular PharmacologyT32GM008688 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI AUDHYA, ANJON · 1998 to 2020
$6.0M
Structural basis of modulation of Na+ channels by local anestheticsR01GM084140 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHANDA, BARON · 2008 to 2016
$3.3M
Thermodynamics and Energetics of voltage-gated ion channelsR01NS081293 · NINDS · WASHINGTON UNIVERSITY · PI CHANDA, BARON · 2012 to 2019
$2.9M
Mechanisms of voltage- and ligand-activation in HCN channelsR01NS101723 · NINDS · WASHINGTON UNIVERSITY · PI CHANDA, BARON · 2017 to 2020
$2.0M
NHLBI NIH HHS T32 HL007936NIGMS NIH HHS R01 GM084140NIGMS NIH HHS T32 GM008688NINDS NIH HHS R01 NS081293NINDS NIH HHS R01 NS101723
6 · The paper itself

Abstract

Membrane potential regulates the activity of voltage-dependent ion channels via specialized voltage-sensing modules, but the mechanisms involved in coupling voltage-sensor movement to pore opening remain unclear owing to a lack of resting state structures and robust methods to identify allosteric pathways. Here, using a newly developed interaction-energy analysis, we probe the interfaces of the voltage-sensing and pore modules in the Drosophila Shaker K

Indexed as

Membrane PotentialsProtein Interaction MappingAllosteric SiteAnimalsDrosophila melanogasterIon Channel GatingKv1.2 Potassium ChannelMolecular ConformationMolecular Dynamics SimulationMutagenesisMutationOocytesRecombinant Fusion ProteinsShab Potassium ChannelsSignal TransductionSpectrometry, FluorescenceKv1.2 Potassium ChannelRecombinant Fusion ProteinsShab Potassium Channels

Identifiers

PMID29581567
PMCPMC6170002

What OpenQuestion holds

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Registered trials

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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.