Evidence map›Paper›PMID 36765939›Full record

ReviewCancers2023

Heat-Shock Proteins in Leukemia and Lymphoma: Multitargets for Innovative Therapeutic Approaches.

Vincent Cabaud-Gibouin, Manon Durand, Ronan Quéré, François Girodon, Carmen Garrido, Gaëtan Jego

Abstract readReview
In one paragraph

Review in Cancers, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
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  8. Review
  9. Nidogen-1, a Player in KMT2A-Rearranged Pediatric Acute Myeloid Leukemia.International journal of molecular sciences · 2025
    Article
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  11. Review
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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

6 authors.

Vincent Cabaud-GibouinINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.ORCID 0000-0001-9750-3779
Manon DurandINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.ORCID 0000-0001-9840-2021
Ronan QuéréINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.
François GirodonINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.
Carmen GarridoINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.
Gaëtan JegoINSERM, UMR1231, Université de Bourgogne, 21078 Dijon, France.ORCID 0000-0003-0376-9299

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat-shock proteins (HSPs) are powerful chaperones that provide support for cellular functions under stress conditions but also for the homeostasis of basic cellular machinery. All cancer cells strongly rely on HSPs, as they must continuously adapt to internal but also microenvironmental stresses to survive. In solid tumors, HSPs have been described as helping to correct the folding of misfolded proteins, sustain oncogenic pathways, and prevent apoptosis. Leukemias and lymphomas also overexpress HSPs, which are frequently associated with resistance to therapy. HSPs have therefore been proposed as new therapeutic targets. Given the specific biology of hematological malignancies, it is essential to revise their role in this field, providing a more adaptable and comprehensive picture that would help design future clinical trials. To that end, this review will describe the different pathways and functions regulated by HSP27, HSP70, HSP90, and, not least, HSP110 in leukemias and lymphomas.

Indexed as

heat-shock proteinleukemialymphomatargeted therapy

Identifiers

PMID36765939
PMCPMC9913431

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.