Evidence map›Paper›PMID 15298895›Full record

ArticleBiophysical journal2004

Effects of Kv1.2 intracellular regions on activation of Kv2.1 channels.

Annette Scholle, Thomas Zimmer, Rolf Koopmann, Birgit Engeland, Olaf Pongs, Klaus Benndorf

Abstract read
In one paragraph

Article in Biophysical journal, 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
–field-weighted citation impact
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.

  1. Kv2.1 channels play opposing roles in regulating membrane potential, CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  2. Article
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  4. Article
  5. Article
  6. Article
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  8. Intracellular regions of potassium channels: Kv2.1 and heag.European biophysics journal : EBJ · 2009
    Review
  9. Article
  10. Article
  11. Interdomain cytoplasmic interactions govern the intracellular trafficking, gating, and modulation of the Kv2.1 channel.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  12. Article
  13. The axon-dendrite targeting of Kv3 (Shaw) channels is determined by a targeting motif that associates with the T1 domain and ankyrin G.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  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

6 authors.

Annette ScholleInstitut für Physiologie II, Friedrich-Schiller-Universität, 07740 Jena, Germany.
Thomas Zimmer
Rolf Koopmann
Birgit Engeland
Olaf Pongs
Klaus Benndorf

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Depolarizing voltage steps activate voltage-dependent K(+) (Kv) channels by moving the voltage sensor, which triggers a coupling reaction leading to the opening of the pore. We constructed chimeric channels in which intracellular regions of slowly activating Kv2.1 channels were replaced by respective regions of rapidly activating Kv1.2 channels. Substitution of either the N-terminus, S4-S5 linker, or C-terminus generated chimeric Kv2.1/1.2 channels with a paradoxically slow and approximately exponential activation time course consisting of a fast and a slow component. Using combined chimeras, each of these Kv1.2 regions further slowed activation at the voltage of 0 mV, irrespective of the nature of the other two regions, whereas at the voltage of 40 mV both slowing and accelerating effects were observed. These results suggest voltage-dependent interactions of the three intracellular regions. This observation was quantified by double-mutant cycle analysis. It is concluded that interactions between N-terminus, S4-S5 linker, and/or C-terminus modulate the activation time course of Kv2.1 channels and that part of these interactions is voltage dependent.

Indexed as

AnimalsCells, CulturedIntracellular SpaceIon Channel GatingKv1.2 Potassium ChannelMutagenesis, Site-DirectedOocytesPotassium Channels, Voltage-GatedProtein Structure, TertiaryRecombinant ProteinsShab Potassium ChannelsStructure-Activity RelationshipXenopus laevisKv1.2 Potassium ChannelPotassium Channels, Voltage-GatedRecombinant ProteinsShab Potassium Channels

Identifiers

PMID15298895
PMCPMC1304496

What OpenQuestion holds

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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.