Evidence map›Paper›PMID 36060252›Full record

ReviewFrontiers in molecular biosciences2022

Targeting extracellular Hsp90: A unique frontier against cancer.

Rebecca A Sager, Farzana Khan, Lorenzo Toneatto, SarahBeth D Votra, Sarah J Backe, Mark R Woodford, Mehdi Mollapour, Dimitra Bourboulia

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Hsp90: Bringing it all together.Cell stress & chaperones · 2025
    Review
  13. The role of heat shock protein 90 in idiopathic pulmonary fibrosis: state of the art.European respiratory review : an official journal of the European Respiratory Society · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

8 authors at 1 institution in 2 countries.

Rebecca A SagerDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Farzana KhanDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Lorenzo ToneattoDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
SarahBeth D VotraDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Sarah J BackeDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Mark R WoodfordDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Mehdi MollapourDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
Dimitra BourbouliaDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY, United States.
SUNY Upstate Medical University · US

Funding

Regulatory mechanisms of the Hsp90 chaperone machinery.R35GM139584 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI MOLLAPOUR, MEHDI · 2021 to 2025
$2.2M
Regulation of the extracellular HSP90 chaperone machineryR01GM139932 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI BOURBOULIA, DIMITRA · 2021 to 2024
$1.3M
NIGMS NIH HHS R01 GM139932NIGMS NIH HHS R35 GM139584
6 · The paper itself

Abstract

The molecular chaperone Heat Shock Protein-90 (Hsp90) is known to interact with over 300 client proteins as well as regulatory factors (eg. nucleotide and proteins) that facilitate execution of its role as a chaperone and, ultimately, client protein activation. Hsp90 associates transiently with these molecular modulators during an eventful chaperone cycle, resulting in acquisition of flexible structural conformations, perfectly customized to the needs of each one of its client proteins. Due to the plethora and diverse nature of proteins it supports, the Hsp90 chaperone machinery is critical for normal cellular function particularly in response to stress. In diseases such as cancer, the Hsp90 chaperone machinery is hijacked for processes which encompass many of the hallmarks of cancer, including cell growth, survival, immune response evasion, migration, invasion, and angiogenesis. Elevated levels of extracellular Hsp90 (eHsp90) enhance tumorigenesis and the potential for metastasis. eHsp90 has been considered one of the new targets in the development of anti-cancer drugs as there are various stages of cancer progression where eHsp90 function could be targeted. Our limited understanding of the regulation of the eHsp90 chaperone machinery is a major drawback for designing successful Hsp90-targeted therapies, and more research is still warranted.

Indexed as

ATPcancer therapyco-chaperonesextracellularHsp90MMP2TIMP2

Identifiers

PMID36060252
PMCPMC9428293
OpenAlexW4292299524

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.