Evidence map›Paper›PMID 36030306›Full record

ArticleCellular and molecular life sciences : CMLS2022

Misfolded protein oligomers induce an increase of intracellular Ca

Giulia Fani, Chiara Ester La Torre, Roberta Cascella, Cristina Cecchi, Michele Vendruscolo, Fabrizio Chiti

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Amyloid β-Oligomers Inhibit the Nuclear CaAntioxidants (Basel, Switzerland) · 2023
    Article
  16. Review
  17. Article
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  19. Structural polymorphism and cytotoxicity of brain-derived β-amyloid extracts.Protein science : a publication of the Protein Society · 2023
    Review
  20. Review
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 2 institutions in 2 countries.

Giulia FaniDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134, Florence, Italy.
Chiara Ester La TorreDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134, Florence, Italy.
Roberta CascellaDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134, Florence, Italy.
Cristina CecchiDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134, Florence, Italy.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. mv245@cam.ac.uk.
Fabrizio ChitiDepartment of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134, Florence, Italy. fabrizio.chiti@unifi.it.ORCID http://orcid.org/0000-0002-1330-1289
University of Florence · ITUniversity of Cambridge · GB

Funding

Ministero dell'Istruzione, dell'Università e della Ricerca Dipartimento di eccellenzaRegione Toscana FAS-Salute 2018-PRAMAUniversità degli studi di Firenze Fondi di ateneo
6 · The paper itself

Abstract

Alzheimer's disease is characterized by the accumulation in the brain of the amyloid β (Aβ) peptide in the form of senile plaques. According to the amyloid hypothesis, the aggregation process of Aβ also generates smaller soluble misfolded oligomers that contribute to disease progression. One of the mechanisms of Aβ oligomer cytotoxicity is the aberrant interaction of these species with the phospholipid bilayer of cell membranes, with a consequent increase in cytosolic Ca

Indexed as

Alzheimer DiseaseNeuroblastomaAmyloid beta-PeptidesAnimalsHumansOxidative StressRatsReactive Oxygen SpeciesAmyloid beta-PeptidesReactive Oxygen SpeciesAMPA receptorsCalcium homeostasisMembrane destabilizationNeurodegenerative diseasesNMDA receptorsOxidative stressProtein misfolding

Identifiers

PMID36030306
PMCPMC9420098
OpenAlexW4293340584

What OpenQuestion holds

Textmetadata
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.