Evidence map›Paper›PMID 39452054›Full record

ArticleBrain sciences2024

Beta-Amyloid and Its Asp7 Isoform: Morphological and Aggregation Properties and Effects of Intracerebroventricular Administration.

Valeriya Ushakova, Yana Zorkina, Olga Abramova, Regina Kuanaeva, Evgeny Barykin, Alexander Vaneev, Roman Timoshenko, Peter Gorelkin, Alexander Erofeev, Eugene Zubkov and 5 more

Abstract read
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In one paragraph

Article in Brain sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

15 authors.

Valeriya UshakovaDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.ORCID 0000-0003-3480-910X
Yana ZorkinaDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.ORCID 0000-0003-0247-2717
Olga AbramovaDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.ORCID 0000-0001-8793-1833
Regina KuanaevaLaboratory of Biophysics, National University of Science and Technology "MISIS", 119049 Moscow, Russia.
Evgeny BarykinEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119334 Moscow, Russia.
Alexander VaneevLaboratory of Biophysics, National University of Science and Technology "MISIS", 119049 Moscow, Russia.ORCID 0000-0001-8201-8498
Roman TimoshenkoLaboratory of Biophysics, National University of Science and Technology "MISIS", 119049 Moscow, Russia.
Peter GorelkinLaboratory of Biophysics, National University of Science and Technology "MISIS", 119049 Moscow, Russia.ORCID 0000-0002-4860-9013
Alexander ErofeevLaboratory of Biophysics, National University of Science and Technology "MISIS", 119049 Moscow, Russia.
Eugene ZubkovDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.
Marat ValikhovDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.ORCID 0000-0001-8988-3417
Olga GurinaDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.
Vladimir MitkevichEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119334 Moscow, Russia.ORCID 0000-0002-1517-1983
Vladimir ChekhoninDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.
Anna MorozovaDepartment of Basic and Applied Neurobiology, V.P. Serbsky National Medical Research Center of Psychiatry and Narcology, The Ministry of Health of the Russian Federation, 119034 Moscow, Russia.

Funding

The Ministry of Education and Science of the Russian Federation 075-15-2022-264
6 · The paper itself

Abstract

BACKGROUND/

objectivesOne of the hallmarks of Alzheimer's disease (AD) is the accumulation of aggregated beta-amyloid (Aβ) protein in the form of senile plaques within brain tissue. Senile plaques contain various post-translational modifications of Aβ, including prevalent isomerization of Asp7 residue. The Asp7 isomer has been shown to exhibit increased neurotoxicity and induce amyloidogenesis in brain tissue of transgenic mice. The toxicity of Aβ peptides may be partly mediated by their structure and morphology. In this respect, in this study we analyzed the structural and aggregation characteristics of the Asp7 isoform of Aβ

methodsAtomic force microscopy (AFM) was conducted to compare the morphological and aggregation properties of Aβ

resultsAFM measurements revealed structural differences between the two peptides, most notably in their soluble toxic oligomeric forms. The i.c.v. administration of Asp7 iso-Aβ

conclusionsThe findings support the further investigation of Asp7 iso-Aβ

Indexed as

AFMAlzheimer’s diseaseamyloidintracerebroventricular injectionrat modelROS

Identifiers

PMID39452054
PMCPMC11506273

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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.