Evidence map›Paper›PMID 8276462›Full record

ReviewImmunogenetics1994

Heat shock proteins transfer peptides during antigen processing and CTL priming.

P K Srivastava, H Udono, N E Blachere, Z Li

Abstract readReview
PubMed Publisher
In one paragraph

Review in Immunogenetics, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
13.6field-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

125 citing papers in PubMed, 573 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Review
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  7. Review
  8. Low-Level Inhibition of Hsp90 Forces Cells to Tip Their (Antigenic) Hand.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. PMMA-FeTheranostics · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. It's Getting Hot in Here: Targeting Cancer Stem-like Cells with Hyperthermia.Journal of stem cell and transplantation biology · 2017
    Article
  18. Review
  19. Review
  20. Article

65 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

4 authors at 1 institution in 1 country.

P K SrivastavaDepartment of Pharmacology, Mount Sinai School of Medicine, New York, NY 10029.
H Udono
N E Blachere
Z Li
Icahn School of Medicine at Mount Sinai · US

Funding

HEAT SHOCK PROTEINS AS TUMOR ANTIGENSR01CA044786 · NCI · FORDHAM UNIVERSITY · PI SRIVASTAVA, PRAMOD K. · 1993 to 1995
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IMMUNE RESPONSE TO TUMORS OF RAS AND JUN TRANSGENIC MICER03CA054990 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF CUNY · PI SRIVASTAVA, PRAMOD K. · 1991 to 1992
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GENETIC DETERMINANTS OF POLYMORPHIC SARCOMA ANTIGENSR29CA044786 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SRIVASTAVA, PRAMOD K. · 1987 to 1991
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NCI NIH HHS CA 44786NCI NIH HHS CA 54990
6 · The paper itself

Abstract

Recently emerging evidence indicates that the heat shock proteins (HSPs) gp96, hsp90, and hsp70 associate with antigenic peptides derived from cellular proteins. This evidence forms the basis of the following two hypotheses: 1) that HSPs constitute a relay line in which the peptides, after generation in the cytosol by the action of proteases, are transferred from one HSP to another, until they are finally accepted by MHC class I molecules in the endoplasmic reticulum, and 2) that the binding of peptides by HSPs constitutes a key step in the priming of cytotoxic T lymphocytes (CTLs) in vivo. The following chain of events is suggested: HSPs are released from virus-infected cells or tumor cells in vivo during lysis of cells during infection or by the action of antibodies or nonspecific effectors. The HSPs, which are now complexed with antigenic peptides derived from the cognate cells, are taken up by macrophage or other specialized antigen-presenting cells, possibly by a receptor-mediated mechanism. The HSP-borne peptide is then routed to the endogenous presentation pathway in the antigen-presenting cell and is displayed in the context of that cell's MHC class I, where it is finally recognized by the precursor CTLs. Thus it is suggested that, as with antigen presentation by MHC class II molecules, presentation by MHC class I molecules is also carried out primarily by the host antigen-presenting cells. This mechanism explains the phenomenon of cross-priming and has implications for the development of immunological strategies against cancer and infectious diseases.

Indexed as

Antigen PresentationAnimalsBiological TransportHeat-Shock ProteinsHematopoietic Stem CellsHistocompatibility AntigensHumansNeoplasmsPeptidesT-Lymphocytes, CytotoxicHeat-Shock ProteinsHistocompatibility AntigensPeptides

Identifiers

PMID8276462
OpenAlexW2083155294

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.