Evidence map›Paper›PMID 19860731›Full record

ReviewCurrent topics in medicinal chemistry2009

Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.

Gary E L Brandt, Brian S J Blagg

Open access · bronzeAbstract readReview
In one paragraph

Review in Current topics in medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Design of Disruptors of the Hsp90-Cdc37 Interface.Molecules (Basel, Switzerland) · 2020
    Article
  6. Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019
    Review
  7. Article
  8. Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Novobiocin Analogues That Inhibit the MAPK Pathway.Journal of medicinal chemistry · 2016
    Article
  13. Review
  14. Review
  15. Article
  16. Protein chaperones: a composition of matter review (2008 - 2013).Expert opinion on therapeutic patents · 2014
    Review
  17. Heat shock protein 90 controls HIV-1 reactivation from latency.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Article
  19. Article
  20. 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 at 1 institution in 1 country.

Gary E L BrandtDepartment of Medicinal Chemistry, The University of Kansas, Lawrence, Kansas, 66045-7582, USA.
Brian S J Blagg
University of Kansas · US

Funding

HSP90 InhibitorsU01CA109265 · NCI · UNIVERSITY OF KANSAS LAWRENCE · PI BLAGG, BRIAN S J · 2006 to 2014
$2.2M
NCI NIH HHS U01 CA109265
6 · The paper itself

Abstract

The 90 kDa heat shock protein (Hsp90) has become a validated target for the development of anti-cancer agents. Several Hsp90 inhibitors are currently under clinical trial investigation for the treatment of cancer. All of these agents inhibit Hsp90's protein folding activity by binding to the N-terminal ATP binding site of the Hsp90 molecular chaperone. Administration of these investigational drugs elicits induction of the heat shock response, or the overexpression of several Hsps, which exhibit antiapoptotic and pro-survival effects that may complicate the application of these inhibitors. To circumvent this issue, alternate mechanisms for Hsp90 inhibition that do not elicit the heat shock response have been identified and pursued. After providing background on the structure, function, and mechanism of the Hsp90 protein folding machinery, this review describes several mechanisms of Hsp90 modulation via small molecules that do not induce the heat shock response.

Indexed as

Adenosine TriphosphateAnimalsAntineoplastic AgentsHSP90 Heat-Shock ProteinsHumansNeoplasmsNeurodegenerative DiseasesAdenosine TriphosphateAntineoplastic AgentsHSP90 Heat-Shock Proteins

Identifiers

PMID19860731
PMCPMC2853258
OpenAlexW2063709661

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.