Evidence map›Paper›PMID 25069659›Full record

ReviewExpert opinion on therapeutic targets2014

Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.

Laura J Blair, Jonathan J Sabbagh, Chad A Dickey

Open access · greenAbstract readReview
In one paragraph

Review in Expert opinion on therapeutic targets, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.1field-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

70 citing papers in PubMed, 111 citations in OpenAlex.

  1. Proteostasis and ageing dissidence.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
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10 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Laura J BlairUniversity of South Florida, USF Health Byrd Institute, Department of Molecular Medicine , 4001 E. Fletcher Avenue, Tampa, FL 33613 , USA.
Jonathan J Sabbagh
Chad A Dickey
USF Health Byrd Alzheimer's Institute · USUniversity of South Florida · US

Funding

The Hsp90 cochaperone FKBP51 regulates tau structure and functionR01NS073899 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI Laura J Blair · 2011 to 2026
$6.9M
NINDS NIH HHS R01 NS073899
6 · The paper itself

Abstract

introductionAlzheimer's disease, characterized by the accumulation of hyperphosphorylated tau and β amyloid (Aβ), currently lacks effective treatment. Chaperone proteins, such as the heat shock protein (Hsp) 90, form macromolecular complexes with co-chaperones, which can regulate tau metabolism and Aβ processing. Although small molecule inhibitors of Hsp90 have been successful at ameliorating tau and Aβ burden, their development into drugs to treat disease has been slow due to the off- and on-target effects of this approach as well as challenges with the pharmacology of current scaffolds. Thus, other approaches are being developed to improve these compounds and to target co-chaperones of Hsp90 in an effort to limit these liabilities. AREAS COVERED: This article discusses the most current developments in Hsp90 inhibitors including advances in blood-brain barrier permeability, decreased toxicity and homolog-specific small-molecule inhibitors. In addition, we discuss current strategies targeting Hsp90 co-chaperones rather than Hsp90 itself to reduce off-target effects. EXPERT OPINION: Although Hsp90 inhibitors have proven their efficacy at reducing tau pathology, they have yet to meet with success in the clinic. The development of Hsp90/tau complex-specific inhibitors and further development of Hsp90 co-chaperone-specific drugs should yield more potent, less toxic therapeutics.

Indexed as

Molecular Targeted TherapyAlzheimer DiseaseAnimalsBlood-Brain BarrierDrug DesignHSP90 Heat-Shock ProteinsHumansMolecular Chaperonestau ProteinsHSP90 Heat-Shock ProteinsMolecular Chaperonestau ProteinsAlzheimer’s diseasechaperoneco-chaperoneheat shock protein 90heat shock protein 90 inhibitorspeptidyl-prolyl isomerasetautetratricopeptideβ amyloid

Identifiers

PMID25069659
PMCPMC4625388
OpenAlexW2168351285

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.