Evidence map›Paper›PMID 27072700›Full record

ReviewCurrent topics in medicinal chemistry2016

Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future.

Daniel T Gewirth

Abstract readReview
In one paragraph

Review in Current topics in medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Conformational plasticity of a BiP-GRP94 chaperone complex.Nature structural & molecular biology · 2025
    Article
  3. Review
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  12. Review
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  17. Review
  18. Article
  19. Inhibitors of theCells · 2021
    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

1 author.

Daniel T GewirthHauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY, 14203, USA. gewirth@hwi.buffalo.edu.

Funding

Project 3: Structural Basis for grp94 Drug Development and Chaperone FunctionP01CA186866 · NCI · OHIO STATE UNIVERSITY · PI LI, ZIHAI · 2015 to 2019
$6.7M
Structure and Regulation of hsp90 ChaperonesR01CA095130 · NCI · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI GEWIRTH, DANIEL T · 2005 to 2015
$2.8M
NCI NIH HHS P01 CA186866NCI NIH HHS R01 CA095130
6 · The paper itself

Abstract

backgroundThe high sequence and structural homology among the hsp90 paralogs - Hsp90α, Hsp90β, Grp94, and Trap-1 - has made the development of paralog-specific inhibitors a challenging proposition.

objectiveThis review surveys the state of developments in structural analysis, compound screening, and structure-based design that have been brought to bear on this problem.

resultsFirst generation compounds that selectively bind to Hsp90, Grp94, or Trap-1 have been identified.

conclusionWith the proof of principle firmly established, the prospects for further progress are bright.

Indexed as

Amino Acid SequenceHSP90 Heat-Shock ProteinsHumansResorcinolsSequence Homology, Amino AcidHSP90 Heat-Shock ProteinsresorcinolResorcinols

Identifiers

PMID27072700
PMCPMC4995118

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.