ReviewCell stress & chaperones2004
The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity.
Review in Cell stress & chaperones, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- A pilot study with a therapeutic vaccine based on hydroxyapatite ceramic particles and self-antigens in cancer patients.Cell stress & chaperones · 2007Trial
- Heat Shock Proteins 90 kDa: Immunomodulators and Adjuvants in Vaccine Design Against Infectious Diseases.Frontiers in bioengineering and biotechnology · 2020Review
- The double-edged sword: conserved functions of extracellular hsp90 in wound healing and cancer.Cancers · 2014Article
- Article
- High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy.International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group · 2013Review
- Heat shock proteins, autoimmunity, and cancer treatment.Autoimmune diseases · 2012Article
- Heat shock proteins: conditional mediators of inflammation in tumor immunity.Frontiers in immunology · 2012Article
- Heat shock proteins and cancer vaccines: developments in the past decade and chaperoning in the decade to come.Expert review of vaccines · 2011Review
- Comparison of adjuvant activity of N- and C-terminal domain of gp96 in a Her2-positive breast cancer model.Cell stress & chaperones · 2011Article
- Re-examination of CD91 function in GRP94 (glycoprotein 96) surface binding, uptake, and peptide cross-presentation.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Caught with their PAMPs down? The extracellular signalling actions of molecular chaperones are not due to microbial contaminants.Cell stress & chaperones · 2010Review
- Heat-shock protein vaccines as active immunotherapy against human gliomas.Expert review of anticancer therapy · 2009Article
- Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- The exception that reinforces the rule: crosspriming by cytosolic peptides that escape degradation.Immunity · 2008Article
- Heat shock proteins HSP70 and GP96: structural insights.Cancer immunology, immunotherapy : CII · 2006Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vaccination of mice with tumor-derived stress proteins, such as Hsp70 and gp96 (GRP94), can elicit antitumor immune responses, yielding a marked suppression of tumor growth and metastasis. The molecular basis for this response is proposed to reflect a peptide-binding function for these proteins. In this view, stress proteins bind the antigenic peptide repertoire of their parent cell, and when provided to the immune system, tumor-derived stress protein-peptide complexes are processed by antigen-presenting cells (APCs) to yield the subsequent activation of tumor-directed cytotoxic T lymphocyte activity. This model predicts that stress proteins, whose primary intracellular function concerns the proper folding and assembly of nascent polypeptides, intersect with the cellular pathways responsible for the generation, processing, or assembly (or all) of peptide antigens onto nascent major histocompatability class I molecules. Recent insights into the pathways for peptide generation now allow this hypothesis to be critically examined, which is the subject of this review.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.