Evidence map›Paper›PMID 30498243›Full record

ArticleNature communications2018

Main-chain mutagenesis reveals intrahelical coupling in an ion channel voltage-sensor.

Daniel T Infield, Kimberly Matulef, Jason D Galpin, Kin Lam, Emad Tajkhorshid, Christopher A Ahern, Francis I Valiyaveetil

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Voltage sensors.Molecular pharmacology · 2025
    Review
  6. Review
  7. Review
  8. 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 3 institutions in 1 country.

Daniel T InfieldDepartment of Molecular Physiology and Biophysics, Iowa Neuroscience Institute, University of Iowa, Iowa City, IA, 52242, USA.
Kimberly MatulefProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health Sciences University, Portland, 97239, OR, USA.
Jason D GalpinDepartment of Molecular Physiology and Biophysics, Iowa Neuroscience Institute, University of Iowa, Iowa City, IA, 52242, USA.
Kin LamDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
Emad TajkhorshidDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.ORCID http://orcid.org/0000-0001-8434-1010
Christopher A AhernDepartment of Molecular Physiology and Biophysics, Iowa Neuroscience Institute, University of Iowa, Iowa City, IA, 52242, USA. christopher-ahern@uiowa.edu.ORCID http://orcid.org/0000-0002-7975-2744
Francis I ValiyaveetilProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health Sciences University, Portland, 97239, OR, USA. valiyave@ohsu.edu.
University of Iowa · USOregon Health & Science University · USUniversity of Illinois Urbana-Champaign · US

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHOU, MING · 2010 to 2017
$31.9M
WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Probing functional mechanisms in K+ channels using unnatural mutagenesisR01GM087546 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI VALIYAVEETIL, FRANCIS · 2009 to 2022
$4.0M
Chemical Biology of Voltage-Gated Sodium and Potassium ChannelsR01GM106569 · NIGMS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2013 to 2022
$2.7M
Photochemical determination of sodium channel voltage-dependent gating and compositionR01GM122420 · NIGMS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2017 to 2020
$1.5M
The Facility for Atomic MutagenesisR24NS104617 · NINDS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2018 to 2021
$1.0M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM087546NIGMS NIH HHS R01 GM106569NIGMS NIH HHS R01 GM122420NIGMS NIH HHS U54 GM087519NINDS NIH HHS R24 NS104617
6 · The paper itself

Abstract

Membrane proteins are universal signal decoders. The helical transmembrane segments of these proteins play central roles in sensory transduction, yet the mechanistic contributions of secondary structure remain unresolved. To investigate the role of main-chain hydrogen bonding on transmembrane function, we encoded amide-to-ester substitutions at sites throughout the S4 voltage-sensing segment of Shaker potassium channels, a region that undergoes rapid, voltage-driven movement during channel gating. Functional measurements of ester-harboring channels highlight a transitional region between α-helical and 3

Indexed as

Molecular Dynamics SimulationHydrogen BondingMutagenesisPotassium ChannelsPotassium Channels, Voltage-GatedProtein Structure, SecondaryShaker Superfamily of Potassium ChannelsPotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium Channels

Identifiers

PMID30498243
PMCPMC6265297
OpenAlexW2901334537

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.