Evidence map›Paper›PMID 9518695›Full record

ArticleThe Journal of physiology1998

Modulation of reconstituted ATP-sensitive K(+)-channels by GTP-binding proteins in a mammalian cell line.

J A Sánchez, T Gonoi, N Inagaki, T Katada, S Seino

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

10 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Go2 G protein mediates galanin inhibitory effects on insulin release from pancreatic β cells.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  3. Article
  4. Article
  5. Ketogenic diet metabolites reduce firing in central neurons by opening K(ATP) channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  6. ABCC8 and ABCC9: ABC transporters that regulate K+ channels.Pflugers Archiv : European journal of physiology · 2007
    Review
  7. Article
  8. Review
  9. Article
  10. 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

5 authors at 2 institutions in 1 country.

J A SánchezResearch Centre for Pathogenic Fungi and Microbial Toxicoses, Chiba University, Japan.
T Gonoi
N Inagaki
T Katada
S Seino
Chiba University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. The action of GTP-binding proteins on ATP-sensitive potassium (KATP) channels was investigated. KATP channels were expressed in a mammalian cell line (COS-1 cells) by cotransfecting vectors carrying the sulphonylurea receptor (SUR1) and BIR (Kir6.2), a member of the inward rectifier K+ channel family. G proteins were also tested on KATP channels composed of an isoform of SUR1, SUR2A, in combination with Kir6.2. 2. The alpha and beta gamma subunits of the GTP binding protein G1 were tested separately in inside-out patches under continuous recording. G alpha-11 increases the activity of SUR1-Kir6.2 and SUR2A-Kir6.2 channels by 200 and by 30%, respectively. 3. G alpha-12 does not increase the activity of SUR1-Kir6.2 channels, but increase the activity of SUR2A-Kir6.2 channels by 30%. 4. Control experiments showed that GTP gamma S, a specific activator of G proteins, and heat-inactivated G alpha-11 do not increase the single channel activity. 5. No effects of the other subunits (beta gamma) from either G11 or G12 on the single channel activity were observed. 6. The protein kinase C inhibitors H7 and an inhibitory peptide (FARKGALRQKNV) had no effect on the modulatory action of G alpha-11 on SUR1-Kir6.2 channels. 7. We conclude that both types of reconstituted KATP channels are modulated by G proteins.

Indexed as

Potassium Channels, Inwardly Rectifying1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAdenosine TriphosphateAlgorithmsAnimalsCattleCell LineElectrophysiologyEnzyme InhibitorsGTP-Binding ProteinsMembrane PotentialsPatch-Clamp TechniquesPotassium ChannelsProtein Kinase CRatsTransfection1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAdenosine TriphosphateEnzyme InhibitorsGTP-Binding ProteinsPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Kinase C

Identifiers

PMID9518695
PMCPMC2230792
OpenAlexW1969864732

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.