Evidence map›Paper›PMID 8943049›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes.

J E van Leeuwen, K P Kearse

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 81 citations in OpenAlex.

  1. Essential glycan-dependent interactions optimize MHC class I peptide loading.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  2. A role for UDP-glucose glycoprotein glucosyltransferase in expression and quality control of MHC class I molecules.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  3. Article
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  7. Calreticulin recognizes misfolded HLA-A2 heavy chains.Proceedings of the National Academy of Sciences of the United States of America · 2002
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  11. Review
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  15. Cloning and functional characterization of a subunit of the transporter associated with antigen processing.Proceedings of the National Academy of Sciences of the United States of America · 1997
    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

2 authors at 2 institutions in 1 country.

J E van LeeuwenExperimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-1360, USA.
K P Kearse
National Cancer Institute · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent evidence indicates that newly synthesized major histocompatibility complex (MHC) class I proteins interact with calnexin, a transmembrane endoplasmic reticulum protein specific for certain glycoproteins bearing monoglucosylated glycans. Here, we studied the association of newly synthesized class I proteins with calreticulin, a soluble calnexin-related ER protein, in murine T cells. We found that, unlike calnexin-class I interactions, calreticulin assembly with class I proteins was markedly decreased in the absence of beta 2 microglobulin expression and that calreticulin associated with a subset of class I glycoforms distinct from those assembled with calnexin but similar to those bound to TAP (transporter associated with antigen processing) proteins. Finally, these studies show that deglucosylation of N-linked glycans is important for dissociation of class I proteins from both calreticulin and TAP and that the vast majority of newly synthesized class I proteins associated with calreticulin are simultaneously assembled with TAP. The data demonstrate that calnexin and calreticulin chaperones assemble with distinct MHC class I assembly intermediates in the ER and show that glycan processing is functionally coupled to release of MHC class I proteins from peptide transport molecules.

Indexed as

AnimalsAntibodiesATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2AutoantigensCalcium-Binding ProteinsCalnexinCalreticulinEndoplasmic ReticulumGlycosylationH-2 AntigensKineticsMiceMice, Inbred C57BLProtein BindingRibonucleoproteinsAntibodiesATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2AutoantigensCalcium-Binding ProteinsCalnexinCalreticulinH-2 AntigensRibonucleoproteinsTAP1 protein, humanTap1 protein, mouse

Identifiers

PMID8943049
PMCPMC19483
OpenAlexW2169289630

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.