Evidence map›Paper›PMID 29476081›Full record

ArticleScientific reports2018

Amyloid-β with isomerized Asp7 cytotoxicity is coupled to protein phosphorylation.

O G Zatsepina, O I Kechko, V A Mitkevich, S A Kozin, M M Yurinskaya, M G Vinokurov, M V Serebryakova, A P Rezvykh, M B Evgen'ev, A A Makarov

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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-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

15 citing papers in PubMed, 29 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

10 authors at 2 institutions in 1 country.

O G ZatsepinaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
O I KechkoEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
V A MitkevichEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.ORCID 0000-0002-1517-1983
S A KozinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
M M YurinskayaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
M G VinokurovInstitute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
M V SerebryakovaA.N. Belozersky Institute of Physico-Chemical Biology MSU, Moscow, Russia.
A P RezvykhEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
M B Evgen'evEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
A A MakarovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. aamakarov@eimb.ru.
Engelhardt Institute of Molecular Biology · RUInstitute of Cell Biophysics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuronal dysfunction and loss associated with the accumulation of amyloid-β (Aβ) in the form of extracellular amyloid plaques and hyperphosphorylated tau in the form of intraneuronal neurofibrillary tangles represent key features of Alzheimer's disease (AD). Amyloid plaques found in the brains of AD patients are predominantly composed of Aβ42 and its multiple chemically or structurally modified isoforms. Recently, we demonstrated that Aβ42 with isomerised Asp7 (isoAβ42) which is one of the most abundant Aβ isoform in plaques, exhibited high neurotoxicity in human neuronal cells. Here, we show that, in SH-SY5Y neuroblastoma cells, the administration of synthetic isoAβ42 rather than intact Aβ42 resulted in a significantly higher level of protein phosphorylation, especially the phosphorylation of tau, tubulins, and matrin 3. IsoAβ42 induced a drastic reduction of tau protein levels. Our data demonstrate, for the first time, that isoAβ42, being to date the only known synthetic Aβ species to cause AD-like amyloidogenesis in an animal AD model, induced cell death by disabling structural proteins in a manner characteristic of that observed in the neurons of AD patients. The data emphasize an important role of isoAβ42 in AD progression and provide possible neurotoxicity paths for this particular isoform.

Indexed as

Protein Processing, Post-TranslationalAlzheimer DiseaseAmyloid beta-PeptidesApoptosisAspartic AcidCell Line, TumorCell SurvivalElectrophoresis, Gel, Two-DimensionalHumansModels, BiologicalNeuronsNuclear Matrix-Associated ProteinsPeptide FragmentsPhosphorylationPhosphoserineProtein IsoformsAmyloid beta-Peptidesamyloid beta-protein (1-42)Aspartic AcidMAPT protein, humanMATR3 protein, humanNuclear Matrix-Associated ProteinsPeptide FragmentsPhosphoserineProtein IsoformsRNA-Binding Proteinstau ProteinsTubulin

Identifiers

PMID29476081
PMCPMC5824883
OpenAlexW2789794269

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.