Evidence map›Paper›PMID 11055999›Full record

ArticleThe Journal of general physiology2000

Opening and closing of KCNKO potassium leak channels is tightly regulated.

N Zilberberg, N Ilan, R Gonzalez-Colaso, S A Goldstein

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Gating the pore of potassium leak channels.European biophysics journal : EBJ · 2009
    Review
  10. Article
  11. Article
  12. Neurotoxic protein expression reveals connections between the circadian clock and mating behavior in Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  13. Intrinsic noise in cultured hippocampal neurons: experiment and modeling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  14. The carboxyl tail forms a discrete functional domain that blocks closure of the yeast K+ channel.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  15. Article
  16. 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.

N ZilberbergDepartment of Pediatrics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536, USA.
N Ilan
R Gonzalez-Colaso
S A Goldstein
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Potassium-selective leak channels control neuromuscular function through effects on membrane excitability. Nonetheless, their existence as independent molecular entities was established only recently with the cloning of KCNKO from Drosophila melanogaster. Here, the operating mechanism of these 2 P domain leak channels is delineated. Single KCNKO channels switch between two long-lived states (one open and one closed) in a tenaciously regulated fashion. Activation can increase the open probability to approximately 1, and inhibition can reduce it to approximately 0.05. Gating is dictated by a 700-residue carboxy-terminal tail that controls the closed state dwell time but does not form a channel gate; its deletion (to produce a 300-residue subunit with two P domains and four transmembrane segments) yields unregulated leak channels that enter, but do not maintain, the closed state. The tail integrates simultaneous input from multiple regulatory pathways acting via protein kinases C, A, and G.

Indexed as

AnimalsCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesElectrophysiologyIon Channel GatingMutagenesis, Site-DirectedPotassium ChannelsProtein Kinase CSignal TransductionUp-RegulationXenopus laevisCyclic AMP-Dependent Protein KinasesCyclic GMP-Dependent Protein KinasesPotassium ChannelsProtein Kinase C

Identifiers

PMID11055999
PMCPMC2229483
OpenAlexW2015595533

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.