Evidence map›Paper›PMID 32005818›Full record

ArticleNature communications2020

Structural basis of proton-coupled potassium transport in the KUP family.

Igor Tascón, Joana S Sousa, Robin A Corey, Deryck J Mills, David Griwatz, Nadine Aumüller, Vedrana Mikusevic, Phillip J Stansfeld, Janet Vonck, Inga Hänelt

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
8.4field-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

48 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  6. Advances in native cell membrane nanoparticles system.Current opinion in structural biology · 2025
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  8. Limited Diversity of Thermal Adaptation to a Critical Temperature inInternational journal of molecular sciences · 2025
    Article
  9. Article
  10. Arabidopsis HAK5 under low KNature communications · 2024
    Article
  11. Regulation of potassium uptake inJournal of bacteriology · 2024
    Article
  12. Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  13. Adaptation ofMicroorganisms · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Cyclic di-AMP traps proton-coupled KNature communications · 2023
    Article
  18. Article
  19. Article
  20. 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

10 authors at 4 institutions in 2 countries.

Igor Tascón *Institute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0003-2526-6238
Joana S Sousa *Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Robin A CoreyDepartment of Biochemistry, University of Oxford, Oxford, UK.
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
David GriwatzInstitute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.ORCID http://orcid.org/0000-0002-3564-897X
Nadine AumüllerInstitute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.
Vedrana MikusevicInstitute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-8800-7669
Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany. janet.vonck@biophys.mpg.de.
Inga HäneltInstitute of Biochemistry, Goethe University Frankfurt, Frankfurt am Main, Germany. Haenelt@biochem.uni-frankfurt.de.ORCID http://orcid.org/0000-0003-1495-3163
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DEUniversity of Oxford · GBUniversity of Warwick · GB

Funding

RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/P01948X/1, BB/R002517/1 BB/S003339/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EP/R029407/1RCUK | Medical Research Council (MRC) MR/S009213/1Wellcome Trust
6 · The paper itself

Abstract

Potassium homeostasis is vital for all organisms, but is challenging in single-celled organisms like bacteria and yeast and immobile organisms like plants that constantly need to adapt to changing external conditions. KUP transporters facilitate potassium uptake by the co-transport of protons. Here, we uncover the molecular basis for transport in this widely distributed family. We identify the potassium importer KimA from Bacillus subtilis as a member of the KUP family, demonstrate that it functions as a K

Indexed as

Bacillus subtilisBacterial ProteinsBinding SitesBiological TransportCation Transport ProteinsDimerizationIon TransportModels, MolecularMultigene FamilyPotassiumProtein DomainsBacterial ProteinsCation Transport ProteinsPotassium

Identifiers

PMID32005818
PMCPMC6994465
OpenAlexW3003423249

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.