Evidence map›Paper›PMID 9545046›Full record

ArticleBiophysical journal1998

Modulation of C-type inactivation by K+ at the potassium channel selectivity filter.

L Kiss, S J Korn

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
3.8field-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

86 citing papers in PubMed, 142 citations in OpenAlex.

  1. Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023
    Article
  2. Article
  3. Article
  4. Article
  5. Calcium channel gating.Pflugers Archiv : European journal of physiology · 2018
    Review
  6. Article
  7. Kv4.2 autism and epilepsy mutation enhances inactivation of closed channels but impairs access to inactivated state after opening.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Probing the Effects of Gating on the Ion Occupancy of the KJournal of the American Chemical Society · 2017
    Article
  9. Article
  10. Ion-binding properties of a K+ channel selectivity filter in different conformations.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Inhibition of ROMK channels by low extracellular K+ and oxidative stress.American journal of physiology. Renal physiology · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

26 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

L KissDepartment of Physiology and Neurobiology, University of Connecticut, Storrs 06269, USA.
S J Korn
University of Connecticut · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

With prolonged or repetitive activation, voltage-gated K+ channels undergo a slow (C-type) inactivation mechanism, which decreases current flow through the channel. Previous observations suggest that C-type inactivation results from a localized constriction in the outer mouth of the channel pore and that the rate of inactivation is controlled by the-rate at which K+ leaves an unidentified binding site in the pore. We have functionally identified two K+ binding sites in the conduction pathway of a chimeric K+ channel that conducts Na+ in the absence of K+. One site has a high affinity for K+ and contributes to the selectivity filter mechanism for K+ over Na+. Another site, external to the high-affinity site, has a lower affinity for K+ and is not involved in channel selectivity. Binding of K+ to the high-affinity binding site slowed inactivation. Binding of cations to the external low-affinity site did not slow inactivation directly but could slow it indirectly, apparently by trapping K+ at the high-affinity site. These data support a model whereby C-type inactivation involves a constriction at the selectivity filter, and the constriction cannot proceed when the selectivity filter is occupied by K+.

Indexed as

Potassium Channel BlockersPotassium Channels, Voltage-GatedBinding SitesBiophysical PhenomenaBiophysicsCell LineDelayed Rectifier Potassium ChannelsHumansKineticsKv1.3 Potassium ChannelMembrane PotentialsPotassiumPotassium ChannelsRecombinant Fusion ProteinsSodiumDelayed Rectifier Potassium ChannelsKCNA3 protein, humanKv1.3 Potassium ChannelPotassiumPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-GatedRecombinant Fusion ProteinsSodium

Identifiers

PMID9545046
PMCPMC1299528
OpenAlexW1970525260

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.