Evidence map›Paper›PMID 26899474›Full record

ArticleScientific reports2016

Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.

Craig T Armstrong, Philip E Mason, J L Ross Anderson, Christopher E Dempsey

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 169 citations in OpenAlex.

  1. Pooled it
  2. Design of Lipopeptides and dsRNA-Lipopeptide Complexes for Sprayable RNAi-Based Plant Protection.Journal of peptide science : an official publication of the European Peptide Society · 2026
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  3. Characterization of an Amphiphilic Exopolymer fromInternational journal of molecular sciences · 2026
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  4. C-terminal long-QT type 1 R562S-Kv7.1 variant, the first variant in helix C impairing β-adrenergic response of the slow delayed rectifier K+ channel.Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology · 2026
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27 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Craig T ArmstrongSchool of Biochemistry, Bristol University, Bristol BS8 1TD, UK.
Philip E MasonInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic and Center for Biomolecules and Complex Molecular Systems, 16610 Prague 6, Czech Republic.
J L Ross AndersonSchool of Biochemistry, Bristol University, Bristol BS8 1TD, UK.
Christopher E DempseySchool of Biochemistry, Bristol University, Bristol BS8 1TD, UK.
University of Bristol · GBCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZ

Funding

Biotechnology and Biological Sciences Research Council BB/I014063/1
6 · The paper itself

Abstract

Gating charges in voltage-sensing domains (VSD) of voltage-sensitive ion channels and enzymes are carried on arginine side chains rather than lysine. This arginine preference may result from the unique hydration properties of the side chain guanidinium group which facilitates its movement through a hydrophobic plug that seals the center of the VSD, as suggested by molecular dynamics simulations. To test for side chain interactions implicit in this model we inspected interactions of the side chains of arginine and lysine with each of the 19 non-glycine amino acids in proteins in the protein data bank. The arginine guanidinium interacts with non-polar aromatic and aliphatic side chains above and below the guanidinium plane while hydrogen bonding with polar side chains is restricted to in-plane positions. In contrast, non-polar side chains interact largely with the aliphatic part of the lysine side chain. The hydration properties of arginine and lysine are strongly reflected in their respective interactions with non-polar and polar side chains as observed in protein structures and in molecular dynamics simulations, and likely underlie the preference for arginine as a mobile charge carrier in VSD.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceAnimalsArginineDatabases, ProteinERG1 Potassium ChannelGuanidineHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsIon Channel GatingLysineProtein IsoformsStatic ElectricityStructural Homology, ProteinStructure-Activity RelationshipArginineERG1 Potassium ChannelGuanidineKCNH2 protein, humanLysineProtein IsoformsWater

Identifiers

PMID26899474
PMCPMC4761985
OpenAlexW2298336203

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.