Evidence map›Paper›PMID 38755204›Full record

ArticleNature communications2024

Extracellular modulation of TREK-2 activity with nanobodies provides insight into the mechanisms of K2P channel regulation.

Karin E J Rödström, Alexander Cloake, Janina Sörmann, Agnese Baronina, Kathryn H M Smith, Ashley C W Pike, Jackie Ang, Peter Proks, Marcus Schewe, Ingelise Holland-Kaye and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Review
  8. Cryo-EM structure of the human THIK-1 K2P KNature structural & molecular biology · 2025
    Article
  9. Article
  10. Article
  11. 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

19 authors.

Karin E J Rödström *Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Alexander Cloake *Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Janina Sörmann *Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3288-6681
Agnese Baronina *Centre for Medicines Discovery, University of Oxford, Oxford, UK.
Kathryn H M SmithClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3008-9224
Ashley C W PikeCentre for Medicines Discovery, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-9661-2607
Jackie AngCentre for Medicines Discovery, University of Oxford, Oxford, UK.
Peter ProksClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Marcus ScheweInstitute of Physiology, Medical Faculty, Kiel University, Kiel, Germany.ORCID http://orcid.org/0000-0002-6192-5651
Ingelise Holland-KayeDepartment of Biochemistry, University of Oxford, Oxford, UK.
Simon R BushellCentre for Medicines Discovery, University of Oxford, Oxford, UK.
Jenna ElliottClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-3703-4234
Els PardonStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.ORCID http://orcid.org/0000-0002-2466-0172
Thomas BaukrowitzInstitute of Physiology, Medical Faculty, Kiel University, Kiel, Germany.ORCID http://orcid.org/0000-0003-4562-0505
Raymond J OwensThe Rosalind Franklin Institute, Harwell Campus, Didcot, UK.ORCID http://orcid.org/0000-0002-3705-2993
Simon NewsteadKavli Institute for Nanoscience Discovery, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7432-2270
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.ORCID http://orcid.org/0000-0002-3825-874X
Elisabeth P CarpenterCentre for Medicines Discovery, University of Oxford, Oxford, UK. lizcarpen1@gmail.com.
Stephen J TuckerClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK. stephen.tucker@physics.ox.ac.uk.ORCID http://orcid.org/0000-0001-8996-2000

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) BA 1793/6-2Deutsche Forschungsgemeinschaft (German Research Foundation) SCHE 2112/1-2RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/S008608/1RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/T002018/1RCUK | Medical Research Council (MRC) MR/W017741/1Wellcome TrustWellcome Trust (Wellcome) 102161/B/13/ZWellcome Trust (Wellcome) 106169/Z/14/ZWellcome Trust (Wellcome) WT084655MA
6 · The paper itself

Abstract

Potassium channels of the Two-Pore Domain (K2P) subfamily, KCNK1-KCNK18, play crucial roles in controlling the electrical activity of many different cell types and represent attractive therapeutic targets. However, the identification of highly selective small molecule drugs against these channels has been challenging due to the high degree of structural and functional conservation that exists not only between K2P channels, but across the whole K

Indexed as

Potassium Channels, Tandem Pore DomainSingle-Domain AntibodiesAnimalsCryoelectron MicroscopyCrystallography, X-RayHEK293 CellsHumansModels, MolecularKCNK10 protein, humanPotassium Channels, Tandem Pore DomainSingle-Domain Antibodies

Identifiers

PMID38755204
PMCPMC11099193

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.