Evidence map›Paper›PMID 21454671›Full record

ArticleThe Journal of biological chemistry2011

Uncoupling charge movement from channel opening in voltage-gated potassium channels by ruthenium complexes.

Andrés Jara-Oseguera, Itzel G Ishida, Gisela E Rangel-Yescas, Noel Espinosa-Jalapa, José A Pérez-Guzmán, David Elías-Viñas, Ronan Le Lagadec, Tamara Rosenbaum, León D Islas

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. 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
  6. The tarantula toxin GxTx detains KThe Journal of general physiology · 2019
    Article
  7. Gas Signaling Molecules and Mitochondrial Potassium Channels.International journal of molecular sciences · 2018
    Review
  8. CO-independent modification of KEuropean journal of pharmacology · 2017
    Article
  9. Gasotransmitter Heterocellular Signaling.Antioxidants & redox signaling · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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

9 authors.

Andrés Jara-OsegueraDepartamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México, Distrito Federal, México.
Itzel G Ishida
Gisela E Rangel-Yescas
Noel Espinosa-Jalapa
José A Pérez-Guzmán
David Elías-Viñas
Ronan Le Lagadec
Tamara Rosenbaum
León D Islas

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Kv2.1 channel generates a delayed-rectifier current in neurons and is responsible for modulation of neuronal spike frequency and membrane repolarization in pancreatic β-cells and cardiomyocytes. As with other tetrameric voltage-activated K(+)-channels, it has been proposed that each of the four Kv2.1 voltage-sensing domains activates independently upon depolarization, leading to a final concerted transition that causes channel opening. The mechanism by which voltage-sensor activation is coupled to the gating of the pore is still not understood. Here we show that the carbon-monoxide releasing molecule 2 (CORM-2) is an allosteric inhibitor of the Kv2.1 channel and that its inhibitory properties derive from the CORM-2 ability to largely reduce the voltage dependence of the opening transition, uncoupling voltage-sensor activation from the concerted opening transition. We additionally demonstrate that CORM-2 modulates Shaker K(+)-channels in a similar manner. Our data suggest that the mechanism of inhibition by CORM-2 may be common to voltage-activated channels and that this compound should be a useful tool for understanding the mechanisms of electromechanical coupling.

Indexed as

Allosteric RegulationAnimalsInsulin-Secreting CellsIon Channel GatingMembrane PotentialsOrganometallic CompoundsPotassium Channel BlockersProtein Structure, TertiaryRatsShab Potassium ChannelsShaker Superfamily of Potassium ChannelsXenopus laevisKcnb1 protein, ratOrganometallic CompoundsPotassium Channel BlockersShab Potassium ChannelsShaker Superfamily of Potassium Channelstricarbonyldichlororuthenium (II) dimer

Identifiers

PMID21454671
PMCPMC3091247

What OpenQuestion holds

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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.