Evidence map›Paper›PMID 29459625›Full record

ArticleScientific reports2018

Molecular subtypes of Alzheimer's disease.

Giuseppe Di Fede, Marcella Catania, Emanuela Maderna, Roberta Ghidoni, Luisa Benussi, Elisa Tonoli, Giorgio Giaccone, Fabio Moda, Anna Paterlini, Ilaria Campagnani and 6 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 83 citations in OpenAlex.

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  18. Recent update on the heterogeneity of the Alzheimer's disease spectrum.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
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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

16 authors at 5 institutions in 3 countries.

Giuseppe Di FedeIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Marcella CataniaIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Emanuela MadernaIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.ORCID 0000-0001-7281-4888
Roberta GhidoniMolecular Markers Laboratory, IRCCS Istituto Centro San Giovanni di Dio - Fatebenefratelli, Brescia, Italy.
Luisa BenussiMolecular Markers Laboratory, IRCCS Istituto Centro San Giovanni di Dio - Fatebenefratelli, Brescia, Italy.ORCID 0000-0003-2836-8141
Elisa TonoliMolecular Markers Laboratory, IRCCS Istituto Centro San Giovanni di Dio - Fatebenefratelli, Brescia, Italy.
Giorgio GiacconeIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Fabio ModaIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Anna PaterliniMolecular Markers Laboratory, IRCCS Istituto Centro San Giovanni di Dio - Fatebenefratelli, Brescia, Italy.
Ilaria CampagnaniIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Stefano SorrentinoIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.ORCID 0000-0002-5833-5183
Laura ColomboDepartment of Molecular Biochemistry and Pharmacology, IRCCS Istituto di Ricerche Farmacologiche "Mario Negri", Milan, Italy.
Adriana KubisIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Edoardo BistaffaIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy.
Bernardino GhettiDepartment of Pathology and Laboratory Medicine, Indiana University, Indianapolis, Indiana, USA.ORCID 0000-0002-1842-8019
Fabrizio TagliaviniIRCCS Foundation "Carlo Besta" Neurological Institute, Milan, Italy. fabrizio.tagliavini@istituto-besta.it.
Fondazione IRCCS Istituto Neurologico Carlo Besta · ITCentro San Giovanni di Dio Fatebenefratelli · ITIndiana University – Purdue University Indianapolis · USMario Negri Institute for Pharmacological Research · ITWroclaw Medical University · PL

Funding

Research Education ComponentP30AG010133 · NIA · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI SAYKIN, ANDREW J · 1991 to 2020
$37.3M
NIA NIH HHS P30 AG010133
6 · The paper itself

Abstract

Protein misfolding and aggregation is a central feature of several neurodegenerative disorders including Alzheimer's disease (AD), in which assemblies of amyloid β (Aβ) peptides accumulate in the brain in the form of parenchymal and/or vascular amyloid. A widely accepted concept is that AD is characterized by distinct clinical and neuropathological phenotypes. Recent studies revealed that Aβ assemblies might have structural differences among AD brains and that such pleomorphic assemblies can correlate with distinct disease phenotypes. We found that in both sporadic and inherited forms of AD, amyloid aggregates differ in the biochemical composition of Aβ species. These differences affect the physicochemical properties of Aβ assemblies including aggregation kinetics, resistance to degradation by proteases and seeding ability. Aβ-amyloidosis can be induced and propagated in animal models by inoculation of brain extracts containing aggregated Aβ. We found that brain homogenates from AD patients with different molecular profiles of Aβ are able to induce distinct patterns of Aβ-amyloidosis when injected into mice. Overall these data suggest that the assembly of mixtures of Aβ peptides into different Aβ seeds leads to the formation of distinct subtypes of amyloid having distinctive physicochemical and biological properties which result in the generation of distinct AD molecular subgroups.

Indexed as

Protein Aggregation, PathologicalAlzheimer DiseaseAmyloidAmyloid beta-PeptidesAnimalsBrainCerebral Amyloid AngiopathyChemical PhenomenaDisease Models, AnimalHumansMiceAmyloidAmyloid beta-Peptides

Identifiers

PMID29459625
PMCPMC5818536
OpenAlexW2795733020

What OpenQuestion holds

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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.