Evidence map›Paper›PMID 28265056›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Hysteresis of KcsA potassium channel's activation- deactivation gating is caused by structural changes at the channel's selectivity filter.

Cholpon Tilegenova, D Marien Cortes, Luis G Cuello

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 41 citations in OpenAlex.

  1. Hysteretic Conductance in Ion Channel Gating.Entropy (Basel, Switzerland) · 2026
    Review
  2. Molecular Determinants of Voltage-Dependent Gating in Kv11.1 Channels.Advances in experimental medicine and biology · 2026
    Review
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  16. Modulation of hERG KFrontiers in pharmacology · 2020
    Review
  17. Modulation of KFrontiers in pharmacology · 2020
    Article
  18. Hysteretic Behavior in Voltage-Gated Channels.Frontiers in pharmacology · 2020
    Review
  19. Article
  20. Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

3 authors at 2 institutions in 1 country.

Cholpon TilegenovaDepartment of Cell Physiology and Molecular Biophysics and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430.
D Marien CortesDepartment of Cell Physiology and Molecular Biophysics and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430.
Luis G CuelloDepartment of Cell Physiology and Molecular Biophysics and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430 luis.cuello@ttuhsc.edu.
Texas Tech University Health Sciences Center · USTexas Tech University · US

Funding

High-resolution crystallographic and functional studies of K+ channel gatingR01GM097159 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI CUELLO, LUIS GONZALO · 2012 to 2021
$2.7M
NIGMS NIH HHS R01 GM097159
6 · The paper itself

Abstract

Mode-shift or hysteresis has been reported in ion channels. Voltage-shift for gating currents is well documented for voltage-gated cation channels (VGCC), and it is considered a voltage-sensing domain's (VSD) intrinsic property. However, uncoupling the

Indexed as

Ion Channel GatingProtein ConformationBacterial ProteinsCesiumHeavy IonsKineticsMembrane PotentialsModels, MolecularMutationPotassium ChannelsRubidiumStructure-Activity RelationshipBacterial ProteinsCesiumPotassium Channelsprokaryotic potassium channelRubidiumC-type inactivationhysteresisKcsAmode-shiftpotassium channels

Identifiers

PMID28265056
PMCPMC5373385
OpenAlexW2594449673

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.