Evidence map›Paper›PMID 28914774›Full record

ReviewInternational journal of molecular sciences2017

Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach.

Suman Chatterjee, Timothy F Burns

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 243 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
243citing papers in PubMed, 3 pooled it
23.5field-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

243 citing papers in PubMed, 3 syntheses or guidelines pooled it, 505 citations in OpenAlex.

  1. Pooled it
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  9. METTL3-mediated N6-methyladenosine modification ofProceedings of the National Academy of Sciences of the United States of America · 2026
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  17. Targeting proteostasis pathways for cancer therapy.Journal of pharmaceutical analysis · 2025
    Review
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183 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

2 authors at 1 institution in 1 country.

Suman ChatterjeeDepartment of Medicine, Division of Hematology Oncology, UPMC Hillman Cancer Center, University of Pittsburgh, Pittsburgh, PA 15213, USA. chatterjees@upmc.edu.ORCID 0000-0002-9084-5263
Timothy F BurnsDepartment of Medicine, Division of Hematology Oncology, UPMC Hillman Cancer Center, University of Pittsburgh, Pittsburgh, PA 15213, USA. burnstf@upmc.edu.
UPMC Hillman Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock proteins (HSPs) are a large family of chaperones that are involved in protein folding and maturation of a variety of "client" proteins protecting them from degradation, oxidative stress, hypoxia, and thermal stress. Hence, they are significant regulators of cellular proliferation, differentiation and strongly implicated in the molecular orchestration of cancer development and progression as many of their clients are well established oncoproteins in multiple tumor types. Interestingly, tumor cells are more HSP chaperonage-dependent than normal cells for proliferation and survival because the oncoproteins in cancer cells are often misfolded and require augmented chaperonage activity for correction. This led to the development of several inhibitors of HSP90 and other HSPs that have shown promise both preclinically and clinically in the treatment of cancer. In this article, we comprehensively review the roles of some of the important HSPs in cancer, and how targeting them could be efficacious, especially when traditional cancer therapies fail.

Indexed as

AnimalsAntineoplastic AgentsCell Transformation, NeoplasticClinical Trials as TopicDrug DiscoveryDrug Evaluation, PreclinicalGene Expression Regulation, NeoplasticHeat-Shock ProteinsHumansMolecular ChaperonesMolecular Targeted TherapyMultigene FamilyNeoplasmsSignal TransductionStress, PhysiologicalAntineoplastic AgentsHeat-Shock ProteinsMolecular Chaperonescancerheat shock proteins (HSPs)HSP70HSP90HSP90 inhibitorsoncogenes

Identifiers

PMID28914774
PMCPMC5618627
OpenAlexW2755428803

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.