Evidence map›Paper›PMID 22798951›Full record

ArticleFrontiers in pharmacology2012

Voltage-gated sodium channels: biophysics, pharmacology, and related channelopathies.

Eleonora Savio-Galimberti, Michael H Gollob, Dawood Darbar

Open access · goldAbstract read
In one paragraph

Article in Frontiers in pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. A structural atlas of druggable sites on NaChannels (Austin, Tex.) · 2024
    Review
  10. Article
  11. Dissection of the structure-function relationship of NaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Review
  13. Characterization of NaLife science alliance · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Endogenous ion channels expressed in human embryonic kidney (HEK-293) cells.Pflugers Archiv : European journal of physiology · 2022
    Review
  18. Article
  19. Article
  20. 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 2 countries.

Eleonora Savio-GalimbertiDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Nashville, TN, USA.
Michael H Gollob
Dawood Darbar
Vanderbilt University · USUniversity of Ottawa · CA

Funding

Pharmacogenomics of Arrhythmia TherapyU19HL065962 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RODEN, DAN M · 2010 to 2014
$17.4M
Positional Cloning and Candidate Gene Approach to Familial Atrial FibrillationR01HL092217 · NHLBI · VANDERBILT UNIVERSITY · PI DARBAR, DAWOOD · 2009 to 2017
$2.9M
QT Interval Remodeling in Atrial FibrillationR01HL085690 · NHLBI · VANDERBILT UNIVERSITY · PI DARBAR, DAWOOD · 2008 to 2012
$1.9M
NHLBI NIH HHS R01 HL085690NHLBI NIH HHS R01 HL092217NHLBI NIH HHS U19 HL065962
6 · The paper itself

Abstract

Voltage-gated sodium channels (VGSC) are multi-molecular protein complexes expressed in both excitable and non-excitable cells. They are primarily formed by a pore-forming multi-spanning integral membrane glycoprotein (α-subunit) that can be associated with one or more regulatory β-subunits. The latter are single-span integral membrane proteins that modulate the sodium current (I(Na)) and can also function as cell adhesion molecules. In vitro some of the cell-adhesive functions of the β-subunits may play important physiological roles independently of the α-subunits. Other endogenous regulatory proteins named "channel partners" or "channel interacting proteins" (ChiPs) like caveolin-3 and calmodulin/calmodulin kinase II (CaMKII) can also interact and modulate the expression and/or function of VGSC. In addition to their physiological roles in cell excitability and cell adhesion, VGSC are the site of action of toxins (like tetrodotoxin and saxitoxin), and pharmacologic agents (like antiarrhythmic drugs, local anesthetics, antiepileptic drugs, and newly developed analgesics). Mutations in genes that encode α- and/or β-subunits as well as the ChiPs can affect the structure and biophysical properties of VGSC, leading to the development of diseases termed sodium "channelopathies".  This review will outline the structure, function, and biophysical properties of VGSC as well as their pharmacology and associated channelopathies and highlight some of the recent advances in this field.

Indexed as

biophysicschannelopathieselectrophysiologypharmacologysodium channelsvoltage-gated sodium channels

Identifiers

PMID22798951
PMCPMC3394224
OpenAlexW2143083742

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.