Evidence map›Paper›PMID 30092511›Full record

ArticleNeurobiology of aging2018

The effect of amyloid-β peptide on synaptic plasticity and memory is influenced by different isoforms, concentrations, and aggregation status.

Walter Gulisano, Marcello Melone, Domenica D Li Puma, Maria Rosaria Tropea, Agostino Palmeri, Ottavio Arancio, Claudio Grassi, Fiorenzo Conti, Daniela Puzzo

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of aging, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

37 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  3. Decoding the mechanisms of amyloid-β in synaptic toxicity.Journal of Alzheimer's disease : JAD · 2026
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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

9 authors at 4 institutions in 2 countries.

Walter GulisanoDepartment Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Marcello MeloneDepartment Experimental and Clinical Medicine, Section of Neuroscience and Cell Biology, Università Politecnica delle Marche, Ancona, Italy; Center for Neurobiology of Aging, INRCA IRCCS, Ancona, Italy.
Domenica D Li PumaInstitute of Human Physiology, Università Cattolica Medical School, Rome, Italy.
Maria Rosaria TropeaDepartment Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Agostino PalmeriDepartment Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy.
Ottavio ArancioTaub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University, New York, NY, USA.
Claudio GrassiInstitute of Human Physiology, Università Cattolica Medical School, Rome, Italy; Fondazione Policlinico Universitario A. Gemelli, Rome, Italy.
Fiorenzo ContiDepartment Experimental and Clinical Medicine, Section of Neuroscience and Cell Biology, Università Politecnica delle Marche, Ancona, Italy; Center for Neurobiology of Aging, INRCA IRCCS, Ancona, Italy; Foundation for Molecular Medicine, Università Politecnica delle Marche, Ancona, Italy.
Daniela PuzzoDepartment Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy. Electronic address: danypuzzo@yahoo.it.
University of Catania · ITMarche Polytechnic University · ITUniversità Cattolica del Sacro Cuore · ITColumbia University · US

Funding

Extracellular tau oligomers and Alzheimer diseaseR01AG049402 · NIA · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ARANCIO, OTTAVIO · 2015 to 2019
$1.6M
NIA NIH HHS R01 AG049402
6 · The paper itself

Abstract

The increase of oligomeric amyloid-beta (oAβ) has been related to synaptic dysfunction, thought to be the earliest event in Alzheimer's disease pathophysiology. Conversely, the suppression of endogenous Aβ impaired synaptic plasticity and memory, suggesting that the peptide is needed in the healthy brain. However, different species, aggregation forms and concentrations of Aβ might differently influence synaptic function/dysfunction. Here, we have tested the contribution of monomeric and oligomeric Aβ42 and Aβ40 at 200 nM and 200 pM concentrations on hippocampal long-term potentiation and spatial memory. We found that, when at 200 nM, oAβ40, oAβ42, and monomeric Aβ42 impaired long-term potentiation and memory, whereas only oAβ42 200 pM enhanced synaptic plasticity and memory and rescued the detrimental effect due to depletion of endogenous Aβ. Interestingly, quantification of monomer-like and oligomer-like species carried out by transmission electron microscopy revealed an increase of the monomer/oligomer ratio in the oAβ42 200 pM preparation, suggesting that the content of monomers and oligomers depends on the final concentration of the solution.

Indexed as

Long-Term PotentiationAmyloid beta-PeptidesAnimalsFemaleHippocampusHumansMaleMice, Inbred C57BLPeptide FragmentsProtein AggregatesProtein IsoformsSpatial MemoryAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)Peptide FragmentsProtein AggregatesProtein IsoformsBeta amyloidHippocampusLong-term potentiationMemoryMonomersOligomers

Identifiers

PMID30092511
PMCPMC8948488
OpenAlexW2883225597

What OpenQuestion holds

Textmetadata
LicenceTDM
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.