Evidence map›Paper›PMID 31816334›Full record

ReviewNeuroscience letters2020

HSP70 and HSP90 in neurodegenerative diseases.

Abha Gupta, Ankush Bansal, Kazue Hashimoto-Torii

Open access · greenAbstract readReview
In one paragraph

Review in Neuroscience letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 84 citations in OpenAlex.

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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

3 authors at 2 institutions in 2 countries.

Abha GuptaUniversity Institute of Biotechnology, Chandigarh University, Gharuan, 140413, India.
Ankush BansalCenter for Neuroscience Research, Children's Research Institute, Children's National Hospital, Washington, DC 20010, USA. Electronic address: abansal2@childrensnational.org.
Kazue Hashimoto-ToriiCenter for Neuroscience Research, Children's Research Institute, Children's National Hospital, Washington, DC 20010, USA; Department of Pediatrics, School of Medicine and Health Sciences, The George Washington University, Washington, DC, 20052, USA. Electronic address: khtorii@childrensnational.org.
Children's National · USChandigarh University · IN

Funding

Research_ProjectU54HD090257 · NICHD · CHILDREN'S RESEARCH INSTITUTE · PI VITTORIO GALLO, VITTORIO GALLO VITTORIO GALLO · 2016 to 2020
$5.9M
Mechanisms and treatments of learning deficits in Fetal Alcohol Spectrum DisordersR01AA026272 · NIAAA · CHILDREN'S RESEARCH INSTITUTE · PI HASHIMOTO-TORII, KAZUE, TORII, MASAAKI · 2019 to 2023
$2.4M
The roles of alcohol-inducible RNA-operons in the fetal brainR01AA025215 · NIAAA · CHILDREN'S RESEARCH INSTITUTE · PI HASHIMOTO-TORII, KAZUE · 2016 to 2020
$2.0M
Biomarker for intellectual disability in children prenatally exposed to alcohol SupplementUH2AA026106 · NIAAA · CHILDREN'S RESEARCH INSTITUTE · PI HASHIMOTO-TORII, KAZUE, TORII, MASAAKI · 2017 to 2018
$515k
Roles of Primary Cilia in the Developing Cortex Exposed to AlcoholR21AA024882 · NIAAA · CHILDREN'S RESEARCH INSTITUTE · PI HASHIMOTO-TORII, KAZUE, TORII, MASAAKI · 2017 to 2018
$459k
NIAAA NIH HHS R01 AA025215NIAAA NIH HHS R01 AA026272NIAAA NIH HHS R21 AA024882NIAAA NIH HHS UH2 AA026106NICHD NIH HHS U54 HD090257
6 · The paper itself

Abstract

Molecular chaperones have a role to stabilize proteins or assist them in reaching their native fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins from cellular stress during the assembly of protein complexes and also prevent the proteins from aggregation and disassembly. The immediate increase of HSPs is crucial for cellular adaptation to environmental changes and protection of other proteins from denaturation, thereby maintaining the cellular homeostasis and increasing the longevity of an organism. HSP70 and HSP90 are the most studied HSPs in this very large HSP family. Notably, HSP90 also stabilizes the disease-related proteins in neurodegenerative disorders. Therefore, small molecules that inhibit the HSP90 but also increase the HSP70 has been tested as potential drugs for neurodegenerative disorders.

Indexed as

AnimalsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansNeurodegenerative DiseasesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHSP70HSP90Neurodegernative diseasesProtein foldingStress

Identifiers

PMID31816334
PMCPMC7336893
OpenAlexW2992661194

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.