Evidence map›Paper›PMID 32887360›Full record

ReviewCells2020

Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury.

Jong Youl Kim, Sumit Barua, Mei Ying Huang, Joohyun Park, Midori A Yenari, Jong Eun Lee

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 97 citations in OpenAlex.

  1. Pooled it
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  14. HSPBiomedicines · 2025
    Article
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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

6 authors at 2 institutions in 2 countries.

Jong Youl KimDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea.
Sumit BaruaDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea.
Mei Ying HuangDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea.
Joohyun ParkDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea.
Midori A YenariDepartment of Neurology, University of California, San Francisco & the San Francisco Veterans Affairs Medical Center, Neurology (127) VAMC 4150 Clement St., San Francisco, CA 94121, USA.
Jong Eun LeeDepartment of Anatomy, Yonsei University College of Medicine, Seoul 03722, Korea.ORCID 0000-0001-6203-7413
Yonsei University · KRSan Francisco VA Medical Center · US

Funding

Inflammatory mechanisms in cerebral ischemiaR01NS106441 · NINDS · NORTHERN CALIFORNIA INSTITUTE/RES/EDU · PI YENARI, MIDORI A · 2019 to 2023
$1.7M
Heat shock proteins in brain ischemia and strokeI01BX000589 · VA · VETERANS AFFAIRS MED CTR SAN FRANCISCO · PI YENARI, MIDORI A · 2011 to 2019
–
BLRD VA I01 BX000589NINDS NIH HHS R01 NS106441
6 · The paper itself

Abstract

The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions. Its chaperone properties can assist in protein folding and prevent protein aggregation following several of these insults. Although its neuroprotective properties have been largely attributed to its chaperone functions, HSP70 may interact directly with proteins involved in cell death and inflammatory pathways following injury. Through the use of mutant animal models, gene transfer, or heat stress, a number of studies have now reported positive outcomes of HSP70 induction. However, these approaches are not practical for clinical translation. Thus, pharmaceutical compounds that can induce HSP70, mostly by inhibiting HSP90, have been investigated as potential therapies to mitigate neurological disease and lead to neuroprotection. This review summarizes the neuroprotective mechanisms of HSP70 and discusses potential ways in which this endogenous therapeutic molecule could be practically induced by pharmacological means to ultimately improve neurological outcomes in acute neurological disease.

Indexed as

AdenineAnimalsBenzoquinonesBrainBrain Injuries, TraumaticCell DeathDisease Models, AnimalGene Expression RegulationHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicNeuronsNeuroprotective AgentsProtein AggregatesProtein Folding17-(dimethylaminoethylamino)-17-demethoxygeldanamycin6-chloro-9-(4-methoxy-3,5-dimethylpyridin-2-ylmethyl)-9H-purin-2-ylamineAdenineBenzoquinonesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLactams, MacrocyclicNeuroprotective AgentsProtein AggregatesPyridinestanespimycinbrain injurychaperone neuroprotectionheat shock protein 70pharmacological induction

Identifiers

PMID32887360
PMCPMC7563654
OpenAlexW3081839279

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.