Evidence map›Paper›PMID 19860737›Full record

ReviewCurrent topics in medicinal chemistry2009

Pharmacological targeting of the Hsp70 chaperone.

Srikanth Patury, Yoshinari Miyata, Jason E Gestwicki

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 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 125 citations in OpenAlex.

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  10. Therapeutic Strategies for Restoring Tau Homeostasis.Cold Spring Harbor perspectives in medicine · 2018
    Review
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5 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 1 institution in 1 country.

Srikanth PaturyDepartment of Pathology and the Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA.
Yoshinari Miyata
Jason E Gestwicki
University of Michigan–Ann Arbor · US

Funding

Molecular Chaperones and Small MoleculesR01NS059690 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jason E Gestwicki · 2008 to 2026
$7.9M
NINDS NIH HHS NS059690NINDS NIH HHS R01 NS059690
6 · The paper itself

Abstract

The molecular chaperone, heat shock protein 70 (Hsp70), acts at multiple steps in a protein's life cycle, including during the processes of folding, trafficking, remodeling and degradation. To accomplish these various tasks, the activity of Hsp70 is shaped by a host of co-chaperones, which bind to the core chaperone and influence its functions. Genetic studies have strongly linked Hsp70 and its co-chaperones to numerous diseases, including cancer, neurodegeneration and microbial pathogenesis, yet the potential of this chaperone as a therapeutic target remains largely underexplored. Here, we review the current state of Hsp70 as a drug target, with a special emphasis on the important challenges and opportunities imposed by its co-chaperones, protein-protein interactions and allostery.

Indexed as

AnimalsDiterpenesFlavonoidsGlycolipidsGuanidinesHSP70 Heat-Shock ProteinsHumansProtein ConformationProtein FoldingPyrimidinesDiterpenesFlavonoidsgeranylgeranylacetoneGlycolipidsGuanidinesHSP70 Heat-Shock ProteinsPyrimidinesspergualinsulfoglycolipids

Identifiers

PMID19860737
PMCPMC2799686
OpenAlexW2106134308

What OpenQuestion holds

Textmetadata
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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.