Evidence map›Paper›PMID 29311706›Full record

ArticleScientific reports2018

Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids.

V Guru KrishnaKumar, Ashim Paul, Ehud Gazit, Daniel Segal

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.9field-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

18 citing papers in PubMed, 55 citations in OpenAlex.

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  8. Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022
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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

4 authors at 1 institution in 1 country.

V Guru KrishnaKumarDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Tel Aviv, 69978, Israel.
Ashim PaulDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Tel Aviv, 69978, Israel.
Ehud GazitDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Tel Aviv, 69978, Israel. ehudg@post.tau.ac.il.
Daniel SegalDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Tel Aviv, 69978, Israel. dsegal@post.tau.ac.il.
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intra-cellular tau protein tangles and extra-cellular β-amyloid plaques are hallmarks of Alzheimer's disease (AD), characterized by the conversion of natively unfolded monomeric protein/peptide into misfolded β-sheet rich aggregates. Therefore, inhibiting the aggregation cascade or disassembling the pre-formed aggregates becomes a pivotal event in disease treatment. In the present study, we show that Naphthoquinone-Tryptophan hybrids, i.e., NQTrp and Cl-NQTrp significantly disrupted the pre-formed fibrillar aggregates of Tau-derived PHF6 (VQIVYK) peptide and full-length tau protein in vitro, in a dose-dependent manner as evident from ThS assay, CD spectroscopy, and TEM. Molecular dynamics simulation of PHF6 oligomers and fibrils with the Naphthoquinone-Tryptophan hybrids provides a possible structure-function based mechanism-of-action, highlighting the role of hydrophobic interaction and hydrogen bond formation during fibril disassembly. These findings signify the effectiveness of NQTrp and Cl-NQTrp in disassembling fibrillar aggregates and may help in designing novel hybrid molecules for AD treatment.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAmyloidCircular DichroismHumansModels, MolecularMolecular StructureNaphthalenesPeptide FragmentsProtein AggregatesProtein Aggregation, PathologicalProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein Multimerizationtau ProteinsAmyloidN-(3-chloro-1,4-dihydro-1,4-dioxo-2-naphthalenyl)-L-tryptophanNaphthalenesPeptide FragmentsProtein Aggregatestau ProteinsTryptophan

Identifiers

PMID29311706
PMCPMC5758761
OpenAlexW2782299758

What OpenQuestion holds

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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.