Evidence map›Paper›PMID 22451904›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structural and mechanistic insights into the activation of Stromal interaction molecule 1 (STIM1).

Xue Yang, Hao Jin, Xiangyu Cai, Siwei Li, Yuequan Shen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
9.8field-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

129 citing papers in PubMed, 206 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Article
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  6. Review
  7. Article
  8. Article
  9. 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
  10. Article
  11. Article
  12. Exosomal microRNA as a key regulator of PI3K/AKT pathways in human tumors.Medical oncology (Northwood, London, England) · 2024
    Review
  13. 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
  14. Article
  15. Article
  16. Review
  17. The CaBiomolecules · 2023
    Review
  18. Article
  19. Review
  20. Review

69 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 2 countries.

Xue YangState Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Hao Jin
Xiangyu Cai
Siwei Li
Yuequan Shen
Life University · USState Key Laboratory of Chemical Engineering · CNNankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium influx through the Ca(2+) release-activated Ca(2+) (CRAC) channel is an essential process in many types of cells. Upon store depletion, the calcium sensor in the endoplasmic reticulum, STIM1, activates Orai1, a CRAC channel in the plasma membrane. We have determined the structures of SOAR from Homo sapiens (hSOAR), which is part of STIM1 and is capable of constitutively activating Orai1, and the entire coiled coil region of STIM1 from Caenorhabditis elegans (ceSTIM1-CCR) in an inactive state. Our studies reveal that the formation of a SOAR dimer is necessary to activate the Orai1 channel. Mutations that disrupt SOAR dimerization or remove the cluster of positive residues abolish STIM1 activation of Orai1. We identified a possible inhibitory helix within the structure of ceSTIM1-CCR that tightly interacts with SOAR. Functional studies suggest that the inhibitory helix may keep the C-terminus of STIM1 in an inactive state. Our data allowed us to propose a model for STIM1 activation.

Indexed as

Amino AcidsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCluster AnalysisHEK293 CellsHeLa CellsHumansMembrane ProteinsModels, BiologicalModels, MolecularNeoplasm ProteinsProtein ConformationProtein MultimerizationProtein Structure, TertiaryStromal Interaction Molecule 1Amino AcidsCaenorhabditis elegans ProteinsMembrane ProteinsNeoplasm Proteinsstim-1 protein, C elegansSTIM1 protein, humanStromal Interaction Molecule 1

Identifiers

PMID22451904
PMCPMC3326449
OpenAlexW1981840225

What OpenQuestion holds

Textmetadata
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.