Evidence map›Paper›PMID 7807012›Full record

ArticleThe Journal of experimental medicine1995

Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules.

E Nössner, P Parham

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

26 citing papers in PubMed, 156 citations in OpenAlex.

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  10. 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
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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 1 institution in 1 country.

E NössnerDepartment of Cell Biology, Stanford University, California 94305.
P Parham
Stanford University · US

Funding

STRUCTURAL BIOLOGY OF HLA-A,B ANTIGENSR01AI017892 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1985 to 2019
$6.1M
STRUCTURAL BIOLOGY OF HLA-A/B ANTIGENSR37AI017892 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1989 to 1998
–
NIAID NIH HHS AI-17892
6 · The paper itself

Abstract

Previous studies have shown that immature mouse class I molecules transiently associate with a resident endoplasmic reticulum protein of 88 kD that has been proposed to act as a chaperone for class I assembly. Subsequently, this protein was demonstrated to be identical to calnexin and to associate with immature forms of the T cell receptor complex, immunoglobulin, and human class I HLA heavy chains. In this paper we define further the interaction of human class I HLA heavy chains with chaperone proteins and find key differences with the complexes observed in the mouse system. First, calnexin and immunoglobulin binding protein (BiP) both associate with immature HLA class I heavy chains. The two chaperones are not found within the same molecular complex, suggesting that calnexin and BiP do not interact simultaneously with the same HLA class I heavy chain. Second, only free HLA class I heavy chains, and not beta 2-microglobulin (beta 2m)-associated heavy chains are found associated with the chaperones. Indeed, addition of free beta 2m in vitro induces dissociation of chaperone-class I HLA heavy chain complexes. The kinetics for dissociation of the class I HLA heavy chain-chaperone complexes and for formation of the class I HLA heavy chain-beta 2m complex display a reciprocity that suggests the interactions with chaperone and beta 2m are mutually exclusive. Mouse class I heavy chains expressed in human cells exhibit the mouse pattern of interaction with human chaperones and human beta 2m and not the human pattern, showing the difference in behavior is purely a function of the class I heavy chain sequence.

Indexed as

Heat-Shock ProteinsAnimalsbeta 2-MicroglobulinCalcium-Binding ProteinsCalnexinCarrier ProteinsCross-Linking ReagentsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPHistocompatibility Antigens Class IHumansMacromolecular SubstancesMiceMolecular ChaperonesMolecular WeightProtein Bindingbeta 2-MicroglobulinCalcium-Binding ProteinsCalnexinCarrier ProteinsCross-Linking ReagentsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHistocompatibility Antigens Class IMacromolecular SubstancesMolecular Chaperones

Identifiers

PMID7807012
PMCPMC2191818
OpenAlexW2068523436

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.