Evidence map›Paper›PMID 28360219›Full record

ArticleThe Journal of general physiology2017

A new mechanism of voltage-dependent gating exposed by K

Adam P Tomczak, Jorge Fernández-Trillo, Shashank Bharill, Ferenc Papp, Gyorgy Panyi, Walter Stühmer, Ehud Y Isacoff, Luis A Pardo

Abstract read
In one paragraph

Article in The Journal of general physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020
    Review
  13. The EAG Voltage-Dependent KFrontiers in pharmacology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
  20. An Update on the Structure of hERG.Frontiers in pharmacology · 2019
    Review
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

8 authors.

Adam P TomczakOncophysiology Group, Max Planck Institute for Experimental Medicine, 37075 Göttingen, Germany.ORCID http://orcid.org/0000-0003-4814-4532
Jorge Fernández-TrilloOncophysiology Group, Max Planck Institute for Experimental Medicine, 37075 Göttingen, Germany.
Shashank BharillDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.
Ferenc PappDepartment of Biophysics and Cell Biology, University of Debrecen, 4032 Debrecen, Hungary.ORCID http://orcid.org/0000-0002-9549-6066
Gyorgy PanyiDepartment of Biophysics and Cell Biology, University of Debrecen, 4032 Debrecen, Hungary.
Walter StühmerDepartment of Molecular Biology of Neuronal Signals, Max Planck Institute for Experimental Medicine, 37075 Göttingen, Germany.
Ehud Y IsacoffDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.
Luis A PardoOncophysiology Group, Max Planck Institute for Experimental Medicine, 37075 Göttingen, Germany Pardo@em.mpg.de.ORCID http://orcid.org/0000-0003-1375-4349

Funding

Voltage Gating MechanismsR01GM117051 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 2016 to 2019
$1.3M
NIGMS NIH HHS R01 GM117051
6 · The paper itself

Abstract

Voltage-gated ion channels couple transmembrane potential changes to ion flow. Conformational changes in the voltage-sensing domain (VSD) of the channel are thought to be transmitted to the pore domain (PD) through an α-helical linker between them (S4-S5 linker). However, our recent work on channels disrupted in the S4-S5 linker has challenged this interpretation for the KCNH family. Furthermore, a recent single-particle cryo-electron microscopy structure of K

Indexed as

Ion Channel GatingAmino Acid SubstitutionAnimalsEther-A-Go-Go Potassium ChannelsMembrane PotentialsProtein DomainsXenopusEther-A-Go-Go Potassium Channels

Identifiers

PMID28360219
PMCPMC5412533

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.