Evidence map›Paper›PMID 9755153›Full record

ArticleThe EMBO journal1998

Potassium channel openers require ATP to bind to and act through sulfonylurea receptors.

M Schwanstecher, C Sieverding, H Dörschner, I Gross, L Aguilar-Bryan, C Schwanstecher, J Bryan

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
15.4field-weighted citation impact, top 1% 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

68 citing papers in PubMed, 218 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Pharmacological Profiling of KPharmaceuticals (Basel, Switzerland) · 2023
    Article
  6. Personalized Therapeutics for KAnnual review of pharmacology and toxicology · 2023
    Review
  7. Article
  8. Article
  9. Mitochondrial outer membrane permeabilization at the single molecule level.Cellular and molecular life sciences : CMLS · 2021
    Review
  10. Article
  11. Genetic Discovery of ATP-Sensitive KCirculation. Arrhythmia and electrophysiology · 2019
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. KATP Channels in the Cardiovascular System.Physiological reviews · 2016
    Review
  17. Article
  18. Article
  19. Article
  20. Reinterpreting the action of ATP analogs on K(ATP) channels.The Journal of biological chemistry · 2013
    Article

8 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

M SchwanstecherInstitut für Pharmakologie und Toxikologie, Universität Braunschweig, Mendelssohnstrasse 1, 38106 Braunschweig, Germany. M.Schwanstecher@tu-bs.de
C Sieverding
H Dörschner
I Gross
L Aguilar-Bryan
C Schwanstecher
J Bryan
Technische Universität Braunschweig · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

KATP channels are composed of a small inwardly rectifying K+ channel subunit, either KIR6.1 or KIR6.2, plus a sulfonylurea receptor, SUR1 or SUR2 (A or B), which belong to the ATP-binding cassette superfamily. SUR1/KIR6.2 reconstitute the neuronal/pancreatic beta-cell channel, whereas SUR2A/KIR6.2 and SUR2B/KIR6.1 (or KIR6.2) are proposed to reconstitute the cardiac and the vascular-smooth-muscle-type KATP channels, respectively. We report that potassium channel openers (KCOs) bind to and act through SURs and that binding to SUR1, SUR2A and SUR2B requires ATP. Non-hydrolysable ATP-analogues do not support binding, and Mg2+ or Mn2+ are required. Point mutations in the Walker A motifs or linker regions of both nucleotide-binding folds (NBFs) abolish or weaken [3H]P1075 binding to SUR2B, rendering reconstituted SUR2B/KIR6.2 channels insensitive towards KCOs. The C-terminus of SUR affects KCO affinity with SUR2B approximately SUR1 > SUR2A. KCOs belonging to different structural classes inhibited specific [3H]P1075 binding to SUR2B in a monophasic manner, with the exception of minoxidil sulfate, which induced a biphasic displacement. The affinities of KCO binding to SUR2B were 3.5-8-fold higher than their potencies for activation of SUR2B/KIR6.2 channels. The results establish that SURs are the KCO receptors of KATP channels and suggest that KCO binding requires a conformational change induced by ATP hydrolysis in both NBFs.

Indexed as

ATP-Binding Cassette TransportersPotassium Channels, Inwardly RectifyingAdenosine TriphosphateAnimalsBinding, CompetitiveBinding SitesCricetinaeDiazoxideGlyburideGuanidinesHumansMutationPeptide FragmentsPinacidilPotassium ChannelsProtein IsoformsABCC8 protein, humanABCC9 protein, humanAdenosine TriphosphateATP-Binding Cassette TransportersDiazoxideGlyburideGuanidinesN-cyano-N'-(1,1-dimethylpropyl)-N''-(3-pyridinyl)guanidinePeptide FragmentsPinacidilPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein IsoformsPyridinesReceptors, DrugRecombinant ProteinsSulfonylurea Receptors

Identifiers

PMID9755153
PMCPMC1170881
OpenAlexW2147706045

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.