Evidence map›Paper›PMID 1326756›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.

K Galvin, S Krishna, F Ponchel, M Frohlich, D E Cummings, R Carlson, J R Wands, K J Isselbacher, S Pillai, M Ozturk

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.6field-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

22 citing papers in PubMed, 74 citations in OpenAlex.

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  8. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  9. Article
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  14. Calreticulin: not just another calcium-binding protein.Molecular and cellular biochemistry · 1994
    Review
  15. Article
  16. Review
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  18. Article
  19. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.Proceedings of the National Academy of Sciences of the United States of America · 1994
    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

10 authors at 1 institution in 1 country.

K GalvinMassachusetts General Hospital Cancer Center, Charlestown 02129.
S Krishna
F Ponchel
M Frohlich
D E Cummings
R Carlson
J R Wands
K J Isselbacher
S Pillai
M Ozturk
Massachusetts General Hospital · US

Funding

PATHOGENESIS, IMMUNODIAGNOSIS AND THERAPY OF HCCR37CA035711 · NCI · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 2000 to 2008
$2.9M
PATHOGENESIS, IMMUNODIAGNOSIS, AND THERAPY OF HCCR01CA035711 · NCI · RHODE ISLAND HOSPITAL (PROVIDENCE, RI) · PI WANDS, JACK R · 1985 to 1999
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TUMOR SUPPRESSOR P53 GENE IN VIRAL HEPATOCARCINOMAR01CA054567 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI ISSELBACHER, KURT J · 1991 to 1994
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STUDIES ON HUMAN HEPATOMA CELL SURFACE PROTEIN P50R29CA049832 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI OZTURK, MEHMET · 1989 to 1992
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NCI NIH HHS CA35711NCI NIH HHS CA49832NCI NIH HHS CA54567
6 · The paper itself

Abstract

A 90-kDa phosphoprotein (p90) of the endoplasmic reticulum was identified by a monoclonal antibody generated against human hepatoma cells. Pulse-chase experiments with [32P]phosphate and [35S]methionine demonstrated that p90 formed both stable and transient complexes with other cellular proteins, suggesting its role as a molecular chaperone. This protein associates with heavy chains of major histocompatibility complex class I proteins, suggesting that it is the human homolog of the recently described 88-kDa protein that transiently associates with murine class I molecules in the endoplasmic reticulum. The p90 protein also associates in B lymphocytes with membrane immunoglobulin mu heavy chains and may serve as a chaperone for many membrane-bound polypeptides. A partial human p90 cDNA was cloned from a lambda gt11 expression library and identified as the human homolog of calnexin, a major canine calcium-binding protein found to be associated with the signal-sequence receptor in endoplasmic reticulum membranes.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalBase SequenceBlotting, WesternCalcium-Binding ProteinsCalnexinCarcinoma, HepatocellularCloning, MolecularEndoplasmic ReticulumHistocompatibility Antigens Class IHumansImmunoenzyme TechniquesImmunoglobulin mu-ChainsIn Vitro TechniquesMacromolecular SubstancesMolecular Sequence DataAntibodies, MonoclonalCalcium-Binding ProteinsCalnexinHistocompatibility Antigens Class IImmunoglobulin mu-ChainsMacromolecular SubstancesPhosphoproteins

Identifiers

PMID1326756
PMCPMC49938
OpenAlexW2011341391

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.