Evidence map›Paper›PMID 20161407›Full record

ReviewFuture medicinal chemistry2009

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

Laura B Peterson, Brian S J Blagg

Open access · greenAbstract readReview
In one paragraph

Review in Future medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

59 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Recent advances toward the development of Hsp90 C-terminal inhibitors.Bioorganic & medicinal chemistry letters · 2023
    Review
  7. Article
  8. Review
  9. Review
  10. Hsp90 Inhibition: A Promising Therapeutic Approach for ARSACS.International journal of molecular sciences · 2021
    Article
  11. Article
  12. Neurobiological Opportunities in Diabetic Polyneuropathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Novobiocin-ferrocene conjugates possessing anticancer and antiplasmodial activity independent of HSP90 inhibition.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  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

2 authors at 1 institution in 1 country.

Laura B PetersonDepartment of Medicinal Chemistry, The University of Kansas, 1251 Wescoe Hall Drive, Malott 4070, Lawrence, KA 66045-7563, USA. bblagg@ku.edu
Brian S J Blagg
University of Kansas · US

Funding

TRAINING GRANT IN DYNAMIC ASPECTS OF CHEMICAL BIOLOGYT32GM008545 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LAMB, AUDREY L · 1994 to 2019
$4.9M
HSP90 InhibitorsU01CA109265 · NCI · UNIVERSITY OF KANSAS LAWRENCE · PI BLAGG, BRIAN S J · 2006 to 2014
$2.2M
NCI NIH HHS CA109265NCI NIH HHS U01 CA109265NIGMS NIH HHS T32 GM008545
6 · The paper itself

Abstract

backgroundThe 90-kDa heat-shock proteins (Hsp90) have rapidly evolved into promising therapeutic targets for the treatment of several diseases, including cancer and neurodegenerative diseases. Hsp90 is a molecular chaperone that aids in the conformational maturation of nascent polypeptides, as well as the rematuration of denatured proteins. DISCUSSION: Many of the Hsp90-dependent client proteins are associated with cellular growth and survival and, consequently, inhibition of Hsp90 represents a promising approach for the treatment of cancer. Conversely, stimulation of heat-shock protein levels has potential therapeutic applications for the treatment of neurodegenerative diseases that result from misfolded and aggregated proteins.

conclusionHsp90 modulation exhibits the potential to treat unrelated disease states, from cancer to neurodegenerative diseases, and, thus, to fold or not to fold, becomes a question of great value.

Indexed as

Amyloid beta-PeptidesHSP90 Heat-Shock ProteinsHumansNeoplasmsNervous System DiseasesProtein FoldingSmall Molecule Librariestau ProteinsAmyloid beta-PeptidesHSP90 Heat-Shock ProteinsSmall Molecule Librariestau Proteins

Identifiers

PMID20161407
PMCPMC2784693
OpenAlexW2018964386

What OpenQuestion holds

Textmetadata
LicenceTDM
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.