Evidence map›Paper›PMID 23829534›Full record

ReviewInternational journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group2013

High molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapy.

Xiang-Yang Wang, John R Subjeck

Open access · greenAbstract readReview
In one paragraph

Review in International journal of hyperthermia : the official journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
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  12. Structural and functional analysis of the Hsp70/Hsp40 chaperone system.Protein science : a publication of the Protein Society · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.International journal of molecular sciences · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

Xiang-Yang WangDepartment of Human Molecular Genetics, Massey Cancer Center, Virginia Commonwealth University, Richmond, Virginia, USA.
John R Subjeck
Roswell Park Comprehensive Cancer Center · USVirginia Commonwealth University · US

Funding

Large heat shock proteins and their role in cancer therapyR01CA099326 · NCI · ROSWELL PARK CANCER INSTITUTE CORP · PI REPASKY, ELIZABETH A, WANG, XIANG-YANG SHAWN · 2003 to 2020
$5.7M
Large Stress Proteins in Biology and MedicineR01CA154708 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2011 to 2015
$1.5M
Scavenger Receptor-A and Immune RegulationR01CA129111 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI WANG, XIANG-YANG SHAWN · 2007 to 2011
$1.2M
NCI NIH HHS CA099326NCI NIH HHS CA129111NCI NIH HHS CA154708NCI NIH HHS R01 CA099326NCI NIH HHS R01 CA129111NCI NIH HHS R01 CA154708
6 · The paper itself

Abstract

Although the large stress/heat shock proteins (HSPs), i.e. Hsp110 and Grp170, were identified over 30 years ago, these abundant and highly conserved molecules have received much less attention compared to other conventional HSPs. Large stress proteins act as molecular chaperones with exceptional protein-holding capability and prevent the aggregation of proteins induced by thermal stress. The chaperoning properties of Hsp110 and Grp170 are integral to the ability of these molecules to modulate immune functions and are essential for developing large chaperone complex vaccines for cancer immunotherapy. The potent anti-tumour activity of the Hsp110/Grp170-tumour protein antigen complexes demonstrated in preclinical studies has led to a phase I clinical trial through the National Cancer Institute's rapid access to intervention development (RAID) programme that is presently underway. Here we review aspects of the structure and function of these large stress proteins, their roles as molecular chaperones in the biology of cell stress, and prospects for their use in immune regulation and cancer immunotherapy. Lastly, we will discuss the recently revealed immunosuppressive activity of scavenger receptor A that binds to Hsp110 and Grp170, as well as the feasibility of targeting this receptor to promote T-cell activation and anti-tumour immunity induced by large HSP vaccines and other immunotherapies.

Indexed as

HSP110 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsAnimalsCancer VaccinesHumansImmunotherapyMolecular WeightNeoplasmsCancer VaccinesHSP110 Heat-Shock ProteinsHSP70 Heat-Shock Proteins

Identifiers

PMID23829534
PMCPMC3845003
OpenAlexW2060011747

What OpenQuestion holds

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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.