Evidence map›Paper›PMID 9834140›Full record

ArticleThe Journal of general physiology1998

Voltage-dependent gating of single wild-type and S4 mutant KAT1 inward rectifier potassium channels.

P C Zei, R W Aldrich

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Research Progress on Plant Shaker KPlants (Basel, Switzerland) · 2024
    Review
  2. Review
  3. Article
  4. Gating control and KPlant, cell & environment · 2018
    Article
  5. Article
  6. Review
  7. Article
  8. Article
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  15. Article
  16. The search is on for the voltage sensor-to-gate coupling.The Journal of general physiology · 2002
    Review
  17. Article
  18. Article
  19. The S4-S5 linker couples voltage sensing and activation of pacemaker channels.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  20. 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

2 authors at 2 institutions in 1 country.

P C ZeiThe Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, USA.
R W Aldrich
Howard Hughes Medical Institute · USStanford University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007365 · NIGMS · STANFORD UNIVERSITY · PI CHUA, KATRIN F · 1985 to 2021
$33.8M
NIGMS NIH HHS GM07365NIGMS NIH HHS T32 GM007365
6 · The paper itself

Abstract

The voltage-dependent gating mechanism of KAT1 inward rectifier potassium channels was studied using single channel current recordings from Xenopus oocytes injected with KAT1 mRNA. The inward rectification properties of KAT1 result from an intrinsic gating mechanism in the KAT1 channel protein, not from pore block by an extrinsic cation species. KAT1 channels activate with hyperpolarizing potentials from -110 through -190 mV with a slow voltage-dependent time course. Transitions before first opening are voltage dependent and account for much of the voltage dependence of activation, while transitions after first opening are only slightly voltage dependent. Using burst analysis, transitions near the open state were analyzed in detail. A kinetic model with multiple closed states before first opening, a single open state, a single closed state after first opening, and a closed-state inactivation pathway accurately describes the single channel and macroscopic data. Two mutations neutralizing charged residues in the S4 region (R177Q and R176L) were introduced, and their effects on single channel gating properties were examined. Both mutations resulted in depolarizing shifts in the steady state conductance-voltage relationship, shortened first latencies to opening, decreased probability of terminating bursts, and increased burst durations. These effects on gating were well described by changes in the rate constants in the kinetic model describing KAT1 channel gating. All transitions before the open state were affected by the mutations, while the transitions after the open state were unaffected, implying that the S4 region contributes to the early steps in gating for KAT1 channels.

Indexed as

Point MutationPotassium Channels, Inwardly RectifyingAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsBinding SitesFemaleIn Vitro TechniquesIon Channel GatingKineticsMembrane PotentialsModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedOocytesArabidopsis ProteinsKAT1 protein, ArabidopsisPlant ProteinsPotassium ChannelsPotassium Channels, Inwardly RectifyingRecombinant Proteins

Identifiers

PMID9834140
PMCPMC2229449
OpenAlexW2040373824

What OpenQuestion holds

Textmetadata
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.