Evidence map›Paper›PMID 14757705›Full record

ArticleBritish journal of pharmacology2004

Molecular analysis of the subtype-selective inhibition of cloned KATP channels by PNU-37883A.

H Kovalev, J M Quayle, T Kamishima, D Lodwick

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 2004. 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 21% 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, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Rapid Characterization of the Functional and Pharmacological Consequences of Cantú Syndrome KThe Journal of pharmacology and experimental therapeutics · 2023
    Article
  6. CL-705G: a novel chemical Kir6.2-specific KFrontiers in pharmacology · 2023
    Article
  7. Kir6.1 and SUR2B in Cantú syndrome.American journal of physiology. Cell physiology · 2022
    Review
  8. Article
  9. The Pharmacology of ATP-Sensitive KHandbook of experimental pharmacology · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. K(ATP) channel action in vascular tone regulation: from genetics to diseases.Sheng li xue bao : [Acta physiologica Sinica] · 2012
    Review
  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 3 institutions in 1 country.

H KovalevDepartment of Cardiovascular Sciences, University of Leicester, Robert Kilpatrick Clinical Sciences Building, Leicester Royal Infirmary, PO Box 65, Leicester LE2 7LX.
J M Quayle
T Kamishima
D Lodwick
University of Liverpool · GBLeicester Royal Infirmary · GBUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. In this study, we have used Kir6.1/Kir6.2 chimeric proteins and current recordings to investigate the molecular basis of PNU-37883A inhibition of cloned K(ATP) channels. 2. Rat Kir6.1, Kir6.2 and Kir6.1/Kir6.2 chimeras were co-expressed with either SUR2B or SUR1, following RNA injection into Xenopus oocytes, and fractional inhibition of K(ATP) currents by 10 microm PNU-37883A reported. 3. Channels containing Kir6.1/SUR2B were more sensitive to inhibition by PNU-37883A than those containing Kir6.2/SUR2B (mean fractional inhibition: 0.70, cf. 0.07). 4. On expression with SUR2B, a chimeric channel with the Kir6.1 pore and the Kir6.2 amino- and carboxy-terminal domains was PNU-37883A insensitive (0.06). A chimera with the Kir6.1 carboxy-terminus and Kir6.2 amino-terminus and pore was inhibited (0.48). These results, and those obtained with other chimeras, suggest that the C-terminus is an important determinant of PNU-37883A inhibition of Kir6.1. Similar results were seen when constructs were co-expressed with SUR1. Further chimeric constructs localised PNU-37883A sensitivity to an 81 amino-acid residue section in the Kir6.1 carboxy-terminus. 5. Our data show that structural differences between Kir6.1 and Kir6.2 are important in determining sensitivity to PNU-37883A. This compound may prove useful in probing the structural and functional differences between the two channel subtypes.

Indexed as

AdamantaneAdenosine TriphosphateAnimalsCloning, MolecularDose-Response Relationship, DrugFemaleMembrane ProteinsMorpholinesPotassium Channel BlockersPotassium ChannelsRatsXenopus laevisAdamantaneAdenosine TriphosphateMembrane Proteinsmitochondrial K(ATP) channelMorpholinesPotassium Channel BlockersPotassium ChannelsU 37883A

Identifiers

PMID14757705
PMCPMC1574259
OpenAlexW2066467948

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.