Evidence map›Paper›PMID 26842600›Full record

ArticleNeurotoxicity research2016

Intracerebral Injection of Metal-Binding Domain of Aβ Comprising the Isomerized Asp7 Increases the Amyloid Burden in Transgenic Mice.

Alexandra A Kulikova, Ivan B Cheglakov, Michail S Kukharsky, Ruslan K Ovchinnikov, Sergey A Kozin, Alexander A Makarov

Abstract read
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Article in Neurotoxicity research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-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

11 citing papers in PubMed, 39 citations in OpenAlex.

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  7. Tetrapeptide Ac-HAEE-NHInternational journal of molecular sciences · 2020
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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

6 authors at 3 institutions in 2 countries.

Alexandra A KulikovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, Moscow, Russia, 119991. kulikovaaa@gmail.com.
Ivan B CheglakovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, Moscow, Russia, 119991.
Michail S KukharskySchool of Biosciences, Cardiff University, Museum Avenue, Cardiff, UK.
Ruslan K OvchinnikovInstitute of Physiologically Active Compounds, Russian Academy of Sciences, Severniy Proezd, Chernogolovka, Moscow region, Russia, 1142432.
Sergey A KozinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, Moscow, Russia, 119991. kozinsa@gmail.com.
Alexander A MakarovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, Moscow, Russia, 119991.
Engelhardt Institute of Molecular Biology · RUCardiff University · GBInstitute of Physiologically Active Compounds · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracerebral or intraperitoneal injections of brain extracts from the Alzheimer's disease patients result in the acceleration of cerebral β-amyloidosis in transgenic mice. Earlier, we have found that intravenous injections of synthetic full-length amyloid-β (Aβ) comprising the isomerized Asp7 trigger cerebral β-amyloidosis. In vitro studies have shown that isomerization of Asp7 promotes zinc-induced oligomerization of the Aβ metal-binding domain (Aβ1-16). Here we report that single intracerebral injection of the peptide Aβ1-16 with isomerized Asp7 (isoAβ1-16) but not the injection of Aβ1-16 significantly increases amyloid burden in 5XFAD transgenic mice. Our results provide evidence for a role of isoAβ1-16 as a minimal seeding agent of Aβ aggregation in vivo.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloidosisAnalysis of VarianceAnimalsAspartic AcidDisease Models, AnimalGene Expression RegulationHumansMiceMice, Inbred C57BLMice, TransgenicMutationPeptide FragmentsPlaque, AmyloidAmyloid beta-Peptidesamyloid beta-protein (1-16)Amyloid beta-Protein PrecursorAspartic AcidPeptide FragmentsPresenilin-1PSEN1 protein, humanAggregationAlzheimer’s diseaseAmyloid-βMetal-binding domainSeedingβ-Amyloidosis

Identifiers

PMID26842600
OpenAlexW2304739987

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.