Evidence map›Paper›PMID 21044583›Full record

ArticleBiophysical journal2010

Voltage profile along the permeation pathway of an open channel.

Jorge E Contreras, Jin Chen, Albert Y Lau, Vishwanath Jogini, Benoît Roux, Miguel Holmgren

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

17 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Asymmetric Interplay Between KFrontiers in physiology · 2021
    Article
  3. Selectivity filter ion binding affinity determines inactivation in a potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. Article
  6. Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019
    Article
  7. Article
  8. Ion-triggered selectivity in bacterial sodium channels.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Pore size matters for potassium channel conductance.The Journal of general physiology · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

6 authors at 2 institutions in 1 country.

Jorge E ContrerasMolecular Neurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, USA. contrerjo@ninds.nih.gov
Jin Chen
Albert Y Lau
Vishwanath Jogini
Benoît Roux
Miguel Holmgren
National Institutes of Health · USUniversity of Chicago · US

Funding

Structure and Function of Membrane ProteinsZIANS002993 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2009 to 2025
$24.0M
Computational Studies of Ion Channels - Resubmission 01R01GM062342 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ROUX, BENOIT · 2001 to 2022
$8.7M
Intramural NIH HHS ZIA NS002993NIGMS NIH HHS GM-62342NIGMS NIH HHS R01 GM062342
6 · The paper itself

Abstract

For ion channels, the transmembrane potential plays a critical role by acting as a driving force for permeant ions. At the microscopic level, the transmembrane potential is thought to decay nonlinearly across the ion permeation pathway because of the irregular three-dimensional shape of the channel's pore. By taking advantage of the current structural and functional understanding of cyclic nucleotide-gated channels, in this study we experimentally explore the transmembrane potential's distribution across the open pore. As a readout for the voltage drop, we engineered cysteine residues along the selectivity filter and scanned the sensitivity of their modification rates by Ag(+) to the transmembrane potential. The experimental data, which indicate that the majority of the electric field drops across the selectivity filter, are in good agreement with continuum electrostatic calculations using a homology model of an open CNG channel. By focusing the transmembrane potential across the selectivity filter, the electromotive driving force is coupled with the movement of permeant ions in the filter, maximizing the efficiency of this process.

Indexed as

Amino Acid SubstitutionAnimalsBiophysical PhenomenaCyclic Nucleotide-Gated Cation ChannelsCysteineFemaleIn Vitro TechniquesKineticsMembrane PotentialsModels, MolecularMutagenesis, Site-DirectedMutant ProteinsOocytesRecombinant ProteinsStatic ElectricityXenopusCyclic Nucleotide-Gated Cation ChannelsCysteineMutant ProteinsRecombinant Proteins

Identifiers

PMID21044583
PMCPMC2965955
OpenAlexW2044094305

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.