Evidence map›Paper›PMID 39126794›Full record

ReviewEuropean journal of medicinal chemistry2024

Extracellular heat shock protein 90 alpha (eHsp90α)'s role in cancer progression and the development of therapeutic strategies.

Tyelor S Reynolds, Brian S J Blagg

Abstract readReview
In one paragraph

Review in European journal of medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. EvaluatingTranslational cancer research · 2025
    Article
  10. Article
  11. Article
  12. Drug Target Investigation ofAntioxidants (Basel, Switzerland) · 2024
    Article
  13. Article
  14. Review
  15. 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.

Tyelor S ReynoldsDepartment of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA.
Brian S J BlaggDepartment of Chemistry and Biochemistry, The University of Notre Dame, 305 McCourtney Hall, Notre Dame, IN, 46556, USA. Electronic address: bblagg@nd.edu.

Funding

Chemistry-Biochemistry-Biology Interface (CBBI) Program at Notre DameT32GM145773 · NIGMS · UNIVERSITY OF NOTRE DAME · PI Christian Corey Melander · 2022 to 2026
$1.5M
Development of Hsp90 inhibitors for the treatment of cancerR01CA167079 · NCI · UNIVERSITY OF NOTRE DAME · PI BLAGG, BRIAN S J · 2012 to 2016
$1.5M
NCI NIH HHS R01 CA167079NIGMS NIH HHS T32 GM145773
6 · The paper itself

Abstract

Heat shock protein 90 alpha (Hsp90α) is an abundantly expressed and evolutionarily conserved molecular chaperone. Hsp90α is the inducible Hsp90 isoform, and its expression and secretion extracellularly (eHsp90α) can be triggered in response to a variety of cellular stresses to protect/activate client proteins and to facilitate cellular adjustment to the stress. As a result, cancers often have high expression levels of intracellular and extracellular (plasma) Hsp90α, allowing them to support their oncogenesis and progression. In fact, (e)Hsp90α has been implicated in regulating processes such as cell signaling transduction, DNA repair, promotion of the Epithelial-to-Mesenchymal Transition (EMT), promotion of angiogenesis, immune response, and cell migration. Hsp90α levels have been correlated with cancer progression and severity in several cancers, indicating that it may be a useful biomarker or drug-target for cancer. To date, the development of intracellular Hsp90α-targeted therapies include standard N-terminal ATP-competitive inhibitors and allosteric regulators that bind to Hsp90α's middle or C-terminal domain. On-target toxicities and dosing complications as a result of Hsp90α inhibition has driven the development of eHsp90α-targeted therapies. Examples include anti-Hsp90α monoclonal antibodies and cell-impermeable Hsp90α small molecule inhibitors. This review aims to discuss the many roles Hsp90α plays in cancer progression with a focus on the current development of Hsp90α-targeted therapies.

Indexed as

Antineoplastic AgentsHSP90 Heat-Shock ProteinsNeoplasmsAnimalsDisease ProgressionHumansAntineoplastic AgentsHSP90 Heat-Shock ProteinsCancer biomarkerCancer targetDrug discoveryExtracellular heat shock protein 90 alphaSmall molecule inhibitors

Identifiers

PMID39126794
PMCPMC11374465

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.