Evidence map›Paper›PMID 8302866›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

C Hammond, I Braakman, A Helenius

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 295 papers.

0numbers the graph read from it
0cells of the map it votes in
295citing papers in PubMed
21.6field-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

295 citing papers in PubMed, 835 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. ER-resident proteins are key players in cartilage and bone homeostasis.Frontiers in cell and developmental biology · 2025
    Review
  15. Article
  16. Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Review
  18. Review
  19. Article
  20. Unraveling the Connection: Pain and Endoplasmic Reticulum Stress.International journal of molecular sciences · 2024
    Review

235 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

3 authors at 1 institution in 1 country.

C HammondDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06510.
I Braakman
A Helenius
Yale University · US

Funding

ROLE OF YPT5 INTERACTING COMPONENTS IN ENDOCYTOSISP01CA046128 · NCI · YALE UNIVERSITY · PI NOVICK, PETER JAY · 1988 to 2007
$9.5M
PROTEIN FOLDING IN THE ENDOPLASMIC RETICULUMR01GM038346 · NIGMS · YALE UNIVERSITY · PI HELENIUS, ARI H · 1987 to 1997
–
NCI NIH HHS P01 CA46128NIGMS NIH HHS 5 RO1 GM38346-13
6 · The paper itself

Abstract

Using a pulse-chase approach combined with immunoprecipitation, we showed that newly synthesized influenza virus hemagglutinin (HA) and vesicular stomatitis virus G protein associate transiently during their folding with calnexin, a membrane-bound endoplasmic reticulum (ER) chaperone. Inhibitors of N-linked glycosylation (tunicamycin) and glucosidases I and II (castanospermine and 1-deoxynojirimycin) prevented the association, whereas inhibitors of ER alpha-mannosidases did not. Our results indicated that binding of these viral glycoproteins to calnexin correlated closely with the composition of their N-linked oligosaccharide side chains. Proteins with monoglucosylated oligosaccharides were the most likely binding species. On the basis of our data and existing information concerning the role of monoglucosylated oligosaccharides on glycoproteins, we propose that the ER contains a unique folding and quality control machinery in which calnexin acts as a chaperone that binds proteins with partially glucose-trimmed carbohydrate side chains. In this model glucosidases I and II serve as signal modifiers and UDP-glucose:glycoprotein glucosyltransferase, as a folding sensor.

Indexed as

Membrane GlycoproteinsAnimalsCalcium-Binding ProteinsCalnexinCHO CellsCricetinaeEndoplasmic ReticulumGlucoseGlycoproteinsHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralModels, BiologicalOligosaccharidesOrthomyxoviridaeProtein BindingProtein FoldingCalcium-Binding ProteinsCalnexinGlucoseGlycoproteinsG protein, vesicular stomatitis virusHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralMembrane GlycoproteinsOligosaccharidesViral Envelope Proteins

Identifiers

PMID8302866
PMCPMC521423
OpenAlexW2121217914

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.