Evidence map›Paper›PMID 8534914›Full record

ArticleMolecular biology of the cell1995

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.

J R Peterson, A Ora, P N Van, A Helenius

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
9.9field-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

87 citing papers in PubMed, 280 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson's disease.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  5. Article
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Chaperoning theViruses · 2018
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. N-linked sugar-regulated protein folding and quality control in the ER.Seminars in cell & developmental biology · 2015
    Review
  19. Review
  20. Review

27 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

4 authors at 1 institution in 1 country.

J R PetersonDepartment of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
A Ora
P N Van
A Helenius
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The soluble, calcium-binding protein calreticulin shares high sequence homology with calnexin, a transmembrane chaperone of glycoprotein folding. Our experiments demonstrated that calreticulin, like calnexin, associated transiently with numerous newly synthesized proteins in the endoplasmic reticulum. The population of proteins that bound to calreticulin was partially overlapping with those that bound to calnexin. Hemagglutinin (HA) of influenza virus was shown to associate with both calreticulin and calnexin. Using HA as a model substrate, it was found that both calreticulin- and calnexin-bound HA corresponded primarily to incompletely disulfide-bonded folding intermediates and conformationally trapped forms. Binding of all substrates was oligosaccharide-dependent and required the trimming of glucose residues from asparagine-linked core glycans by glucosidases I and II. In vitro, alpha-mannosidase digestion of calreticulin-bound HA indicated that calreticulin was specific for monoglucosylated glycans. Thus, calreticulin appeared to be a lectin with similar oligosaccharide specificity as its membrane-bound homologue, calnexin. Both are therefore likely to play an important role in glycoprotein maturation and quality control in the endoplasmic reticulum.

Indexed as

Membrane GlycoproteinsProtein FoldingAnimalsCalcium-Binding ProteinsCalnexinCalreticulinCarbohydrate SequenceCHO CellsCricetinaeCystineEndoplasmic ReticulumGlycoproteinsHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralLectinsMolecular Sequence DataCalcium-Binding ProteinsCalnexinCalreticulinCystineGlycoproteinsG protein, vesicular stomatitis virusHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralLectinsMembrane GlycoproteinsOligosaccharidesPolysaccharidesRibonucleoproteinsViral Envelope ProteinsViral Proteins

Identifiers

PMID8534914
PMCPMC301275
OpenAlexW2051690692

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.