Evidence map›Paper›PMID 21963409›Full record

ArticleBiochimica et biophysica acta2012

Probing the interaction of lipids with the non-annular binding sites of the potassium channel KcsA by magic-angle spinning NMR.

Phedra Marius, Maurits R R de Planque, Philip T F Williamson

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  9. NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021
    Article
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  16. Regulation of KCNQ/Kv7 family voltage-gated KBiochimica et biophysica acta. Biomembranes · 2017
    Review
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  19. Article
  20. Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013
    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

3 authors at 1 institution in 1 country.

Phedra MariusSchool of Biological Sciences, Highfield Campus, University of Southampton, Southampton, SO17 1BJ, UK.
Maurits R R de Planque
Philip T F Williamson
University of Southampton · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The activity of the potassium channel KcsA is tightly regulated through the interactions of anionic lipids with high-affinity non-annular lipid binding sites located at the interface between the channel's subunits. Here we present solid-state phosphorous NMR studies that resolve the negatively charged lipid phosphatidylglycerol within the non-annular lipid-binding site. Perturbations in chemical shift observed upon the binding of phosphatidylglycerol are indicative of the interaction of positively charged sidechains within the non-annular binding site and the negatively charged lipid headgroup. Site directed mutagenesis studies have attributed these charge interactions to R64 and R89. Functionally the removal of the positive charges from R64 and R89 appears to act synergistically to reduce the probability of channel opening.

Indexed as

ArginineBacterial ProteinsBinding SitesCloning, MolecularElectrophysiologyEscherichia coliIon Channel GatingLipid BilayersMembrane PotentialsModels, MolecularMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhosphatidylglycerolsPlasmidsPotassiumPotassium ChannelsArginineBacterial ProteinsLipid BilayersPhosphatidylglycerolsPotassiumPotassium Channelsprokaryotic potassium channelRecombinant Proteins

Identifiers

PMID21963409
PMCPMC3236287
OpenAlexW2109420627

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.