Evidence map›Paper›PMID 39551742›Full record

ArticleCellular & molecular biology letters2024

Different amyloid β42 preparations induce different cell death pathways in the model of SH-SY5Y neuroblastoma cells.

Alp Yigit Özdemir, Kateřina Hofbauerová, Vladimír Kopecký, Jiří Novotný, Vladimír Rudajev

Abstract read
In one paragraph

Article in Cellular & molecular biology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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

5 authors.

Alp Yigit ÖzdemirDepartment of Physiology, Faculty of Sciences, Charles University, Viničná 7, 12844, Prague 2, Czech Republic.
Kateřina HofbauerováInstitute of Physics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 12116, Prague 2, Czech Republic.
Vladimír KopeckýInstitute of Physics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 12116, Prague 2, Czech Republic.
Jiří NovotnýDepartment of Physiology, Faculty of Sciences, Charles University, Viničná 7, 12844, Prague 2, Czech Republic.
Vladimír RudajevDepartment of Physiology, Faculty of Sciences, Charles University, Viničná 7, 12844, Prague 2, Czech Republic. rudajev@natur.cuni.cz.ORCID http://orcid.org/0000-0001-9113-1636

Funding

Přírodovědecká Fakulta, Univerzita Karlova SVV-260683
6 · The paper itself

Abstract

Amyloid β42 (Aβ42) plays a decisive role in the pathology of Alzheimer's disease. The Aβ42 peptide can aggregate into various supramolecular structures, with oligomers being the most toxic form. However, different Aβ species that cause different effects have been described. Many cell death pathways can be activated in connection with Aβ action, including apoptosis, necroptosis, pyroptosis, oxidative stress, ferroptosis, alterations in mitophagy, autophagy, and endo/lysosomal functions. In this study, we used a model of differentiated SH-SY5Y cells and applied two different Aβ42 preparations for 2 and 4 days. Although we found no difference in the shape and size of Aβ species prepared by two different methods (NaOH or NH

Indexed as

Amyloid beta-PeptidesApoptosisNeuroblastomaPeptide FragmentsReactive Oxygen SpeciesAlzheimer DiseaseCell DeathCell Line, TumorHumansMitochondriaNecroptosisOxidative StressAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsReactive Oxygen SpeciesAlzheimer´s diseaseAmyloid β42ApoptosisCell deathGM1NecroptosisReactive oxygen species

Identifiers

PMID39551742
PMCPMC11572474

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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.