Evidence map›Paper›PMID 9545232›Full record

ArticleThe EMBO journal1998

ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly.

J A Lindquist, O N Jensen, M Mann, G J Hämmerling

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. 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
9.5field-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

46 citing papers in PubMed, 233 citations in OpenAlex.

  1. Review
  2. Article
  3. Dual role of the peptide-loading complex as proofreader and limiter of MHC-I presentation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. The role of cellular proteostasis in antitumor immunity.The Journal of biological chemistry · 2022
    Review
  5. Article
  6. Hepatitis C virus modulates signal peptide peptidase to alter host protein processing.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Review
  8. Intake ofMicroorganisms · 2021
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. ERp57/GRP58: a protein with multiple functions.Cellular & molecular biology letters · 2011
    Review
  19. Article
  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

4 authors at 1 institution in 1 country.

J A LindquistDepartment of Molecular Immunology, German Cancer Research Center, In Neuenheimer Feld 280, 69120 Heidelberg, Germany.
O N Jensen
M Mann
G J Hämmerling
German Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly of newly synthesized MHC class I molecules within the endoplasmic reticulum and their association with the transporter associated with antigen processing (TAP) is a process involving the chaperones calnexin and calreticulin. Using peptide mapping by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry to identify a new component, we now introduce a third molecular chaperone, the thiol-dependent reductase ER-60 (ERp57/GRP58/ERp61/HIP-70/Q2), into this process. ER-60 is found in MHC class I heavy chain complexes with calnexin that are generated early during the MHC class I assembly pathway. The thiol reductase activity of ER-60 raises the possibility that ER-60 is involved in the disulfide bond formation within heavy chains. In addition, ER-60 is part of the late assembly complexes consisting of MHC class I, tapasin, TAP, calreticulin and calnexin. In a beta2-microglobulin (beta2m)-negative mouse cell line, S3, ER-60-calnexin-heavy chain complexes are shown to bind to TAP, suggesting that beta2m is not required for the association of MHC class I heavy chains with TAP.

Indexed as

alpha-GlucosidasesAmino Acid SequenceAnimalsAntiportersATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3beta 2-MicroglobulinCalcium-Binding ProteinsCalnexinCalreticulinCell LineEnzyme InhibitorsGlycoside Hydrolase InhibitorsHeat-Shock ProteinsHistocompatibility Antigens Class Ialpha-GlucosidasesAntiportersATP-Binding Cassette TransportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3beta 2-MicroglobulinCalcium-Binding ProteinsCalnexinCalreticulincastanospermineEnzyme Inhibitorsglucosidase IGlycoside Hydrolase InhibitorsHeat-Shock ProteinsHistocompatibility Antigens Class IImmunoglobulinsIndolizidinesIndolizinesIsomerasesMembrane Transport ProteinsMolecular ChaperonesPDIA3 protein, humanPdia3 protein, mouseProtein Disulfide-IsomerasesProtein Disulfide Reductase (Glutathione)RibonucleoproteinsTAP1 protein, humanTap1 protein, mouseTAP2 protein, humanTap2 protein, mousetapasin

Identifiers

PMID9545232
PMCPMC1170563
OpenAlexW2132198322

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.