Evidence map›Paper›PMID 21423620›Full record

ArticlePloS one2011

X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.

Anne Chouquet, Helena Païdassi, Wai Li Ling, Philippe Frachet, Gunnar Houen, Gérard J Arlaud, Christine Gaboriaud

Abstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Article
  2. Review
  3. Crystal structure ofFrontiers in immunology · 2024
    Article
  4. Article
  5. Article
  6. Determination of crucial epitopes in the sperm protein calsperin employing synthetic peptides and monoclonal antibodies.Journal of peptide science : an official publication of the European Peptide Society · 2023
    Article
  7. Article
  8. The many faces of parasite calreticulin.Frontiers in immunology · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

7 authors.

Anne ChouquetInstitut de Biologie Structurale Jean-Pierre Ebel, CEA, Grenoble, France.
Helena Païdassi
Wai Li Ling
Philippe Frachet
Gunnar Houen
Gérard J Arlaud
Christine Gaboriaud

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 Å resolution. Interactions of the flexible N-terminal extension with the edge of the lectin site are consistently observed, revealing a hitherto unidentified peptide-binding site. A calreticulin molecular zipper, observed in all crystal lattices, could further extend this site by creating a binding cavity lined by hydrophobic residues. These data thus provide a first structural insight into the lectin-independent binding properties of calreticulin and suggest new working hypotheses, including that of a multi-molecular mechanism.

Indexed as

Amino Acid SequenceBinding SitesCalreticulinCrystallography, X-RayHumansLectinsModels, MolecularMolecular Sequence DataPeptide FragmentsPeptidesProtein BindingProtein Structure, TertiarySurface PropertiesCalreticulinLectinsPeptide FragmentsPeptides

Identifiers

PMID21423620
PMCPMC3057994

What OpenQuestion holds

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Registered trials

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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.