Evidence map›Paper›PMID 15138750›Full record

ArticleThe Journal of membrane biology2004

Rate-limiting reactions determining different activation kinetics of Kv1.2 and Kv2.1 channels.

A Scholle, S Dugarmaa, T Zimmer, M Leonhardt, R Koopmann, B Engeland, O Pongs, K Benndorf

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Article in The Journal of membrane biology, 2004. 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
0.4field-weighted citation impact, top 42% 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, 24 citations in OpenAlex.

  1. Article
  2. Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022
    Article
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  7. The tarantula toxin GxTx detains KThe Journal of general physiology · 2019
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  10. Review
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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 at 3 institutions in 1 country.

A ScholleInstitut für Physiologie, Herz-Kreislauf-Physiologie, Friedrich-Schiller-Universität, 07740, Jena, Germany.
S Dugarmaa
T Zimmer
M Leonhardt
R Koopmann
B Engeland
O Pongs
K Benndorf
Friedrich Schiller University Jena · DEInstitut für Hämatopathologie Hamburg · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To identify the mechanisms underlying the faster activation kinetics in Kv1.2 channels compared to Kv2.1 channels, ionic and gating currents were studied in rat Kv1.2 and human Kv2.1 channels heterologously expressed in mammalian cells. At all voltages the time course of the ionic currents could be described by an initial sigmoidal and a subsequent exponential component and both components were faster in Kv1.2 than in Kv2.1 channels. In Kv1.2 channels, the activation time course was more sigmoid at more depolarized potentials, whereas in Kv2.1 channels it was somewhat less sigmoid at more depolarized potentials. In contrast to the ionic currents, the ON gating currents were similarly fast for both channels. The main portion of the measured ON gating charge moved before the ionic currents were activated. The equivalent gating charge of Kv1.2 ionic currents was twice that of Kv2.1 ionic currents, whereas that of Kv1.2 ON gating currents was smaller than that of Kv2.1 ON gating currents. In conclusion, the different activation kinetics of Kv1.2 and Kv2.1 channels are caused by rate-limiting reactions that follow the charge movement recorded from the gating currents. In Kv1.2 channels, the reaction coupling the voltage-sensor movement to the pore opening contributes to rate limitation in a voltage-dependent fashion, whereas in Kv2.1 channels, activation is additionally rate-limited by a slow reaction in the subunit gating.

Indexed as

Ion Channel GatingPotassium Channels, Voltage-GatedAnimalsCHO CellsCricetinaeDelayed Rectifier Potassium ChannelsElectrophysiologyHumansKineticsKv1.2 Potassium ChannelMembrane PotentialsPatch-Clamp TechniquesPotassium ChannelsShab Potassium ChannelsDelayed Rectifier Potassium ChannelsKCNA2 protein, humanKCNB1 protein, humanKv1.2 Potassium ChannelPotassium ChannelsPotassium Channels, Voltage-GatedShab Potassium Channels

Identifiers

PMID15138750
OpenAlexW2019634432

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.