Evidence map›Paper›PMID 19232514›Full record

ArticleBiochimica et biophysica acta2009

Thermal and chemical unfolding and refolding of a eukaryotic sodium channel.

Kalypso Charalambous, A O O'Reilly, Per A Bullough, B A Wallace

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Review
  14. 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

4 authors at 2 institutions in 1 country.

Kalypso CharalambousDepartment of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK.
A O O'Reilly
Per A Bullough
B A Wallace
Birkbeck, University of London · GBUniversity of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C500628/1Wellcome Trust
6 · The paper itself

Abstract

Voltage-gated sodium channels are dynamic membrane proteins essential for signaling in nervous and muscular systems. They undergo substantial conformational changes associated with the closed, open and inactivated states. However, little information is available regarding their conformational stability. In this study circular dichroism spectroscopy was used to investigate the changes in secondary structure accompanying chemical and thermal denaturation of detergent-solubilised sodium channels isolated from Electrophorus electricus electroplax. The proteins appear to be remarkably resistant to either type of treatment, with "denatured" channels, retaining significant helical secondary structure even at 77 degrees C or in 10% SDS. Further retention of helical secondary structure at high temperature was observed in the presence of the channel-blocking tetrodotoxin. It was possible to refold the thermally-denatured (but not chemically-denatured) channels in vitro. The correctly refolded channels were capable of undergoing the toxin-induced conformational change indicative of ligand binding. In addition, flux measurements in liposomes showed that the thermally-denatured (but not chemically-denatured) proteins were able to re-adopt native, active conformations. These studies suggest that whilst sodium channels must be sufficiently flexible to undergo major conformational changes during their functional cycle, the proteins are highly resistant to unfolding, a feature that is important for maintaining structural integrity during dynamic processes.

Indexed as

Action PotentialsAnimalsChromatography, AffinityElectrophorusEpithelial Sodium ChannelsIon Channel GatingMicroscopy, ElectronProtein ConformationProtein DenaturationProtein FoldingProtein Structure, SecondaryProteolipidsSodium ChlorideSpectrophotometry, UltravioletTetrodotoxinThermodynamicsEpithelial Sodium ChannelsProteolipidsproteoliposomesSodium ChlorideTetrodotoxinVeratridine

Identifiers

PMID19232514
PMCPMC2688679
OpenAlexW2198982186

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.