Evidence map›Paper›PMID 18425532›Full record

ArticlePflugers Archiv : European journal of physiology2008

Four-mode gating model of fast inactivation of sodium channel Nav1.2a.

Tobias Huth, Johann Schmidtmayer, Christian Alzheimer, Ulf-Peter Hansen

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. A naturally occurring amino acid substitution in the voltage-dependent sodium channel selectivity filter affects channel gating.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2013
    Article
  6. Article
  7. Article
  8. 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 1 institution in 1 country.

Tobias HuthDepartment of Physiology, University of Kiel, Olshausenstrasse 40, 24098, Kiel, Germany. t.huth@physiologie.uni-kiel.de
Johann Schmidtmayer
Christian Alzheimer
Ulf-Peter Hansen
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Basic principles of the gating mechanisms of neuronal sodium channels, especially the fast inactivation process, were revealed by a quantitative analysis of the effects of the chemically irreversible modifying agent chloramine T. The compound is known to enhance the open probability of sodium channels by interfering with the inactivation process. The key for the deduction of structure-function relationships was obtained from the analysis of single-channel patch-clamp data, especially the finding that chloramine T-induced modification of inactivation occurred in four steps. These steps were termed modes 1-4 (four-mode gating model), and their temporal sequence was always the same. The kinetic analysis of single-channel traces with an improved two-dimensional dwell-time fit revealed the possible mechanism related to each mode. Similarities to the kinetics of the sodium channel mutant F1489Q led to the assignment of modes 1 and 2 to transient defects in the locking of the inactivation particle (hinged lid). In the third mode, the hinged lid was unable to lock permanently. Finally, in mode 4, the apparent single-channel current was reduced, which could be explained by fast gating, presumably related to the selectivity filter.

Indexed as

AlgorithmsCell LineChloraminesComputer SimulationElectrophysiologyHumansIon Channel GatingMarkov ChainsModels, BiologicalNAV1.2 Voltage-Gated Sodium ChannelNerve Tissue ProteinsNormal DistributionPatch-Clamp TechniquesSodium Channel BlockersSodium ChannelsTosyl CompoundsChloramineschloramine-TNAV1.2 Voltage-Gated Sodium ChannelNerve Tissue ProteinsSCN2A protein, humanSodium Channel BlockersSodium ChannelsTosyl Compounds

Identifiers

PMID18425532
OpenAlexW2017359841

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.