Evidence map›Paper›PMID 14695263›Full record

ArticleBiophysical journal2004

N-type inactivation features of Kv4.2 channel gating.

Manuel Gebauer, Dirk Isbrandt, Kathrin Sauter, Britta Callsen, Andreas Nolting, Olaf Pongs, Robert Bähring

Open access · bronzeAbstract readComparative StudyEvaluation Study
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 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Inactivation of Native K Channels.The Journal of membrane biology · 2022
    Article
  7. Article
  8. Review
  9. Review
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  11. Review
  12. Article
  13. Review
  14. Modulation of human Kv4.3/KChIP2 channel inactivation kinetics by cytoplasmic CaPflugers Archiv : European journal of physiology · 2017
    Article
  15. Enhanced Sensitivity to Hyperpolarizing Inhibition in Mesoaccumbal Relative to Nigrostriatal Dopamine Neuron Subpopulations.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  16. Article
  17. Article
  18. 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

7 authors at 1 institution in 1 country.

Manuel GebauerInstitut für Neurale Signalverarbeitung, Zentrum für Molekulare Neurobiologie der Universität Hamburg, 20246 Hamburg, Germany.
Dirk Isbrandt
Kathrin Sauter
Britta Callsen
Andreas Nolting
Olaf Pongs
Robert Bähring
Universität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined whether the N-terminus of Kv4.2 A-type channels (4.2NT) possesses an autoinhibitory N-terminal peptide domain, which, similar to the one of Shaker, mediates inactivation of the open state. We found that chimeric Kv2.1(4.2NT) channels, where the cytoplasmic Kv2.1 N-terminus had been replaced by corresponding Kv4.2 domains, inactivated relatively fast, with a mean time constant of 120 ms as compared to 3.4 s in Kv2.1 wild-type. Notably, Kv2.1(4.2NT) showed features typically observed for Shaker N-type inactivation: fast inactivation of Kv2.1(4.2NT) channels was slowed by intracellular tetraethylammonium and removed by N-terminal truncation (Delta40). Kv2.1(4.2NT) channels reopened during recovery from inactivation, and recovery was accelerated in high external K+. Moreover, the application of synthetic N-terminal Kv4.2 and ShB peptides to inside-out patches containing slowly inactivating Kv2.1 channels mimicked N-type inactivation. Kv4.2 channels, after fractional inactivation, mediated tail currents with biphasic decay, indicative of passage through the open state during recovery from inactivation. Biphasic tail current kinetics were less prominent in Kv4.2/KChIP2.1 channel complexes and virtually absent in Kv4.2Delta40 channels. N-type inactivation features of Kv4.2 open-state inactivation, which may be suppressed by KChIP association, were also revealed by the finding that application of Kv4.2 N-terminal peptide accelerated the decay kinetics of both Kv4.2Delta40 and Kv4.2/KChIP2.1 patch currents. However, double mutant cycle analysis of N-terminal inactivating and pore domains indicated differences in the energetics and structural determinants between Kv4.2 and Shaker N-type inactivation.

Indexed as

Potassium Channels, Voltage-GatedAmino Acid SequenceAmino Acid SubstitutionAnimalsCell LineCHO CellsCricetinaeCricetulusHumansIon Channel GatingKidneyMolecular Sequence DataMutagenesis, Site-DirectedPotassium ChannelsShal Potassium ChannelsStructure-Activity RelationshipKCND2 protein, humanPotassium ChannelsPotassium Channels, Voltage-GatedShal Potassium Channels

Identifiers

PMID14695263
PMCPMC1303783
OpenAlexW1965987963

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.