Evidence map›Paper›PMID 25609918›Full record

ReviewDrug design, development and therapy2015

Screening strategies to identify HSP70 modulators to treat Alzheimer's disease.

Jayanthi Repalli, Daniel Meruelo

Open access · goldAbstract readReview
In one paragraph

Review in Drug design, development and therapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Heat Shock Proteins in Alzheimer's Disease: Role and Targeting.International journal of molecular sciences · 2018
    Review
  16. Article
  17. Article
  18. Review
  19. 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

2 authors at 1 institution in 1 country.

Jayanthi RepalliDepartment of Pathology, New York University, Langone Medical Center, New York, NY, USA.
Daniel MerueloDepartment of Pathology, New York University, Langone Medical Center, New York, NY, USA.
New York University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease, the most common type of dementia, is a progressive brain disease that destroys cognitive function and eventually leads to death. In patients with Alzheimer's disease, beta amyloids and tau proteins form plaques/oligomers and oligomers/tangles that affect the ability of neurons to function properly. Heat shock protein 70 (HSP70) has the ability to prevent aggregation/oligomerization of beta amyloid/tau proteins, making it a potential drug target. To determine this potential, it is essential that we have appropriate in vitro and cell-based assays that help identify specific molecules that affect this aggregation or oligomerization through HSP70. Potential drug candidates could be identified through a series of assays, starting with ATPase assays, followed by aggregation assays with enzymes/proteins and cell-based systems. ATPase assays are effective in identification of ATPase modulators but do not determine the effect of the molecule on beta amyloid and tau proteins. Molecules identified through ATPase assays are validated by thioflavin T aggregation assays in the presence of HSP70. These assays help uncover if a molecule affects beta amyloid and tau through HSP70, but are limited by their in vitro nature. Potential drug candidates are further validated through cell-based assays using mammalian, yeast, or bacterial cultures. However, while these assays are able to determine the effect of a specific molecule on beta amyloid and tau, they fail to determine whether the action is HSP70-dependent. The creation of a novel, direct assay that can demonstrate the antiaggregation effect of a molecule as well as its action through HSP70 would reduce the number of false-positive drug candidates and be more cost-effective and time-effective.

Indexed as

Adenosine TriphosphatasesAlzheimer DiseaseAmyloid beta-PeptidesAnimalsDrug DiscoveryEnzyme InhibitorsHigh-Throughput Screening AssaysHSP70 Heat-Shock ProteinsHumansMolecular StructureMolecular Targeted TherapyNeuroprotective AgentsProteasome Endopeptidase ComplexProtein AggregatesProtein FoldingStructure-Activity RelationshipAdenosine TriphosphatasesAmyloid beta-PeptidesEnzyme InhibitorsHSP70 Heat-Shock ProteinsNeuroprotective AgentsProteasome Endopeptidase ComplexProtein Aggregatestau Proteinsadenosine triphosphatase activityaggregationbeta amyloidheat shock protein 70oligomerstau

Identifiers

PMID25609918
PMCPMC4294646
OpenAlexW2097172859

What OpenQuestion holds

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LicenceCC BY-NC
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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.