Evidence map›Paper›PMID 29483506›Full record

ArticleNature communications2018

A dual mechanism promotes switching of the Stormorken STIM1 R304W mutant into the activated state.

Marc Fahrner, Michael Stadlbauer, Martin Muik, Petr Rathner, Peter Stathopulos, Mitsu Ikura, Norbert Müller, Christoph Romanin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Review
  3. Listening to the quiescence of single STIM1 dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. STIM1 transmembrane helix dimerization captured by AI-guided transition path sampling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Essential role of N-terminal SAM regions in STIM1 multimerization and function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. The CaBiomolecules · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. STIM Proteins: An Ever-Expanding Family.International journal of molecular sciences · 2020
    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

8 authors at 3 institutions in 3 countries.

Marc FahrnerInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, 4020, Linz, Austria. marc.fahrner@jku.at.
Michael StadlbauerInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, 4020, Linz, Austria.
Martin MuikInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, 4020, Linz, Austria.
Petr RathnerInstitute of Organic Chemistry, Johannes Kepler University Linz, Altenbergerstrasse 69, 4040, Linz, Austria.
Peter StathopulosDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON N6A 5C1, Canada.
Mitsu IkuraPrincess Margaret Cancer Center, University Health Network, Toronto, ON M5G 1L7, Canada.
Norbert MüllerInstitute of Organic Chemistry, Johannes Kepler University Linz, Altenbergerstrasse 69, 4040, Linz, Austria.ORCID http://orcid.org/0000-0002-7621-3980
Christoph RomaninInstitute of Biophysics, Johannes Kepler University Linz, Gruberstrasse 40, 4020, Linz, Austria. christoph.romanin@jku.at.ORCID http://orcid.org/0000-0003-3756-4136
Johannes Kepler University of Linz · ATUniversity Health Network · CAWestern University · CA

Funding

Austrian Science Fund FWF P 27263Austrian Science Fund FWF P 28123Austrian Science Fund FWF P 28498
6 · The paper itself

Abstract

STIM1 and Orai1 are key components of the Ca

Indexed as

Point MutationAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding SitesBlood Platelet DisordersCalciumDyslexiaErythrocytes, AbnormalGene ExpressionGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansIchthyosisBacterial ProteinsCalciumCyan Fluorescent ProteinGreen Fluorescent ProteinsLuminescent ProteinsNeoplasm ProteinsORAI1 ProteinORAI1 protein, humanRecombinant ProteinsSTIM1 protein, humanStromal Interaction Molecule 1yellow fluorescent protein, Bacteria

Identifiers

PMID29483506
PMCPMC5827659
OpenAlexW2789493474

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.