Evidence map›Paper›PMID 31562564›Full record

ArticleCellular and molecular life sciences : CMLS2020

Purpurin modulates Tau-derived VQIVYK fibrillization and ameliorates Alzheimer's disease-like symptoms in animal model.

Guru Krishnakumar Viswanathan, Dana Shwartz, Yelena Losev, Elad Arad, Chen Shemesh, Edward Pichinuk, Hamutal Engel, Avi Raveh, Raz Jelinek, Itzik Cooper and 3 more

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.6field-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

21 citing papers in PubMed, 62 citations in OpenAlex.

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  6. Quinones as Neuroprotective Agents.Antioxidants (Basel, Switzerland) · 2023
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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

13 authors at 4 institutions in 2 countries.

Guru Krishnakumar ViswanathanDepartment of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.
Dana ShwartzDepartment of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.
Yelena LosevDepartment of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.
Elad AradIlse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.
Chen ShemeshThe Joseph Sagol Neuroscience Center, Sheba Medical Center, Tel Hashomer, 52621, Ramat Gan, Israel.
Edward PichinukBlavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.
Hamutal EngelBlavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.
Avi RavehBlavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.
Raz JelinekIlse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.
Itzik CooperThe Joseph Sagol Neuroscience Center, Sheba Medical Center, Tel Hashomer, 52621, Ramat Gan, Israel.
Fabien GosseletBlood-Brain Barrier Laboratory (LBHE), Université d'Artois, Lens, France.
Ehud GazitDepartment of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.
Daniel SegalDepartment of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel. dsegal@post.tau.ac.il.
Tel Aviv University · ILBen-Gurion University of the Negev · ILSheba Medical Center · ILUniversité d'Artois · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurofibrillary tangles of the Tau protein and plaques of the amyloid β peptide are hallmarks of Alzheimer's disease (AD), which is characterized by the conversion of monomeric proteins/peptides into misfolded β-sheet rich fibrils. Halting the fibrillation process and disrupting the existing aggregates are key challenges for AD drug development. Previously, we performed in vitro high-throughput screening for the identification of potent inhibitors of Tau aggregation using a proxy model, a highly aggregation-prone hexapeptide fragment

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAnimals, Genetically ModifiedAnthraquinonesBlood-Brain BarrierDisease Models, AnimalDrosophila melanogasterHumansHydrophobic and Hydrophilic InteractionsOligopeptidesPeptide FragmentsPhosphorylationProtein AggregatesProtein Conformation, beta-StrandRepressor ProteinsAmyloid beta-PeptidesAnthraquinonesOligopeptidesPeptide FragmentsProtein Aggregatespurpurin anthraquinoneRepressor Proteinstau hexapeptide PHF6tau ProteinsAggregationAmyloidInhibitorPHF6 peptidePurpurinTau protein

Identifiers

PMID31562564
PMCPMC11104911
OpenAlexW2977177779

What OpenQuestion holds

Textmetadata
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.