Evidence map›Paper›PMID 22483432›Full record

ReviewCurrent opinion in structural biology2012

The influence of lipids on voltage-gated ion channels.

Qiu-Xing Jiang, Tamir Gonen

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Cellular Membranes, a Versatile Adaptive Composite Material.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Voltage sensor ring in a native structure of a membrane-embedded potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Review
  20. Cholesterol-Dependent Gating Effects on Ion Channels.Advances in experimental medicine and biology
    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

2 authors at 2 institutions in 1 country.

Qiu-Xing JiangDepartment of Cell Biology, UT Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, TX 75390-9039, USA.
Tamir Gonen
Helix (United States) · USThe University of Texas Southwestern Medical Center · US

Funding

Structural study of a Kv channel in different conformations in membranesR01GM093271 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2010 to 2013
$1.2M
Obtaining 3D structures with subnanogram macromoleculesR01GM088745 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2009 to 2012
$1.0M
Howard Hughes Medical InstituteNIGMS NIH HHS 01GM088745NIGMS NIH HHS R01 GM088745NIGMS NIH HHS R01 GM093271NIGMS NIH HHS R01GM093271
6 · The paper itself

Abstract

Voltage-gated ion channels are responsible for transmitting electrochemical signals in both excitable and non-excitable cells. Structural studies of voltage-gated potassium and sodium channels by X-ray crystallography have revealed atomic details on their voltage-sensor domains (VSDs) and pore domains, and were put in context of disparate mechanistic views on the voltage-driven conformational changes in these proteins. Functional investigation of voltage-gated channels in membranes, however, showcased a mechanism of lipid-dependent gating for voltage-gated channels, suggesting that the lipids play an indispensible and critical role in the proper gating of many of these channels. Structure determination of membrane-embedded voltage-gated ion channels appears to be the next frontier in fully addressing the mechanism by which the VSDs control channel opening. Currently electron crystallography is the only structural biology method in which a membrane protein of interest is crystallized within a complete lipid-bilayer mimicking the native environment of a biological membrane. At a sufficiently high resolution, an electron crystallographic structure could reveal lipids, the channel and their mutual interactions at the atomic level. Electron crystallography is therefore a promising avenue toward understanding how lipids modulate channel activation through close association with the VSDs.

Indexed as

CrystallographyHumansMembrane LipidsMicroscopy, Electron, TransmissionModels, MolecularPotassium Channels, Voltage-GatedProtein BindingProtein ConformationVoltage-Gated Sodium ChannelsMembrane LipidsPotassium Channels, Voltage-GatedVoltage-Gated Sodium Channels

Identifiers

PMID22483432
PMCPMC3408884
OpenAlexW2165698797

What OpenQuestion holds

Textmetadata
LicenceTDM
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.