Evidence map›Paper›PMID 33106661›Full record

ArticleNature chemical biology2021

Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation.

Petr Rathner, Marc Fahrner, Linda Cerofolini, Herwig Grabmayr, Ferdinand Horvath, Heinrich Krobath, Agrim Gupta, Enrico Ravera, Marco Fragai, Matthias Bechmann and 4 more

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. The CaCell reports. Medicine · 2026
    Article
  4. Article
  5. Multiple weak brakes act in concert to control STIM1 and store-operated calcium entry.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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. Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Role of STIM1 in the Regulation of Cardiac Energy Substrate Preference.International journal of molecular sciences · 2023
    Review
  13. The CaBiomolecules · 2023
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

14 authors at 2 institutions in 4 countries.

Petr RathnerInstitute of Organic Chemistry, Johannes Kepler University Linz, Linz, Austria.
Marc Fahrner *Institute of Biophysics, Johannes Kepler University Linz, Linz, Austria.ORCID http://orcid.org/0000-0002-2689-0158
Linda Cerofolini *Magnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Sesto Fiorentino, Italy.ORCID http://orcid.org/0000-0002-0795-9594
Herwig Grabmayr *Institute of Biophysics, Johannes Kepler University Linz, Linz, Austria.ORCID http://orcid.org/0000-0003-0870-5833
Ferdinand HorvathInstitute for Theoretical Physics, Johannes Kepler University Linz, Linz, Austria.
Heinrich KrobathInstitute for Theoretical Physics, Johannes Kepler University Linz, Linz, Austria.ORCID http://orcid.org/0000-0001-6473-8109
Agrim GuptaInstitute of Organic Chemistry, Johannes Kepler University Linz, Linz, Austria.
Enrico RaveraMagnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Sesto Fiorentino, Italy.ORCID http://orcid.org/0000-0001-7708-9208
Marco FragaiMagnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Sesto Fiorentino, Italy.ORCID http://orcid.org/0000-0002-8440-1690
Matthias BechmannInstitute of Organic Chemistry, Johannes Kepler University Linz, Linz, Austria.
Thomas RengerInstitute for Theoretical Physics, Johannes Kepler University Linz, Linz, Austria.
Claudio LuchinatMagnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Sesto Fiorentino, Italy.
Christoph RomaninInstitute of Biophysics, Johannes Kepler University Linz, Linz, Austria. christoph.romanin@jku.at.ORCID http://orcid.org/0000-0003-3756-4136
Norbert MüllerInstitute of Organic Chemistry, Johannes Kepler University Linz, Linz, Austria. norbert.mueller@jku.at.ORCID http://orcid.org/0000-0002-7621-3980
Johannes Kepler University of Linz · ATInteruniversity Consortium for Magnetic Resonance · IT

Funding

Austrian Science Fund FWF P 32947Austrian Science Fund FWF W 1250
6 · The paper itself

Abstract

The calcium release activated calcium channel is activated by the endoplasmic reticulum-resident calcium sensor protein STIM1. On activation, STIM1 C terminus changes from an inactive, tight to an active, extended conformation. A coiled-coil clamp involving the CC1 and CC3 domains is essential in controlling STIM1 activation, with CC1 as the key entity. The nuclear magnetic resonance-derived solution structure of the CC1 domain represents a three-helix bundle stabilized by interhelical contacts, which are absent in the Stormorken disease-related STIM1 R304W mutant. Two interhelical sites between the CC1α

Indexed as

Blood Platelet DisordersCalcium Release Activated Calcium ChannelsCloning, MolecularDyslexiaErythrocytes, AbnormalHEK293 CellsHumansIchthyosisMagnetic Resonance SpectroscopyMigraine DisordersMiosisModels, MolecularMuscle FatigueMutationNeoplasm ProteinsNucleic Acid ConformationCalcium Release Activated Calcium ChannelsNeoplasm ProteinsORAI1 ProteinORAI1 protein, humanSTIM1 protein, humanStromal Interaction Molecule 1

Identifiers

PMID33106661
PMCPMC7610458
OpenAlexW3093890133

What OpenQuestion holds

Textmetadata
LicenceTDM
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.