Evidence map›Paper›PMID 16308567›Full record

ArticleThe EMBO journal2005

3-D structural and functional characterization of the purified KATP channel complex Kir6.2-SUR1.

Michael V Mikhailov, Jeff D Campbell, Heidi de Wet, Kenju Shimomura, Brittany Zadek, Richard F Collins, Mark S P Sansom, Robert C Ford, Frances M Ashcroft

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

80 citing papers in PubMed, 172 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Molecular structure of an open human KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Structure based analysis of KScientific reports · 2021
    Article
  6. The Pancreatic β-Cell: The Perfect Redox System.Antioxidants (Basel, Switzerland) · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. New insights into KNature reviews. Endocrinology · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. KInternal medicine (Tokyo, Japan) · 2017
    Review
  19. Article
  20. Article

20 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

9 authors at 2 institutions in 1 country.

Michael V MikhailovLaboratory of Physiology, University of Oxford, Oxford, UK.
Jeff D Campbell
Heidi de Wet
Kenju Shimomura
Brittany Zadek
Richard F Collins
Mark S P Sansom
Robert C Ford
Frances M Ashcroft
University of Oxford · GBUniversity of Manchester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

ATP-sensitive potassium (K(ATP)) channels conduct potassium ions across cell membranes and thereby couple cellular energy metabolism to membrane electrical activity. Here, we report the heterologous expression and purification of a functionally active K(ATP) channel complex composed of pore-forming Kir6.2 and regulatory SUR1 subunits, and determination of its structure at 18 A resolution by single-particle electron microscopy. The purified channel shows ATP-ase activity similar to that of ATP-binding cassette proteins related to SUR1, and supports Rb(+) fluxes when reconstituted into liposomes. It has a compact structure, with four SUR1 subunits embracing a central Kir6.2 tetramer in both transmembrane and cytosolic domains. A cleft between adjacent SUR1s provides a route by which ATP may access its binding site on Kir6.2. The nucleotide-binding domains of adjacent SUR1 appear to interact, and form a large docking platform for cytosolic proteins. The structure, in combination with molecular modelling, suggests how SUR1 interacts with Kir6.2.

Indexed as

Amino Acid SequenceAnimalsATP-Binding Cassette TransportersCryoelectron MicroscopyKcnj11 ChannelMiceMolecular Sequence DataPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Structure, TertiaryRatsReceptors, DrugRecombinant Fusion ProteinsSulfonylurea ReceptorsAbcc8 protein, mouseAbcc8 protein, ratATP-Binding Cassette TransportersKcnj11 ChannelPotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugRecombinant Fusion ProteinsSulfonylurea Receptors

Identifiers

PMID16308567
PMCPMC1356316
OpenAlexW2139404258

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.