Evidence map›Paper›PMID 27466139›Full record

ArticleScientific reports2016

Altered protein phosphorylation as a resource for potential AD biomarkers.

Ana Gabriela Henriques, Thorsten Müller, Joana Machado Oliveira, Marta Cova, Cristóvão B da Cruz E Silva, Odete A B da Cruz E Silva

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Ana Gabriela HenriquesNeuroscience and Signalling Laboratory, Department of Medical Sciences and Insitute of Biomedicine - iBiMED, University of Aveiro, 3810-193 Aveiro, Portugal.
Thorsten MüllerCell Signaling in Neurodegeneration (CSIN), Medical Proteome-Center, Ruhr-University Bochum, 44801 Bochum, Germany.
Joana Machado OliveiraNeuroscience and Signalling Laboratory, Department of Medical Sciences and Insitute of Biomedicine - iBiMED, University of Aveiro, 3810-193 Aveiro, Portugal.
Marta CovaNeuroscience and Signalling Laboratory, Department of Medical Sciences and Insitute of Biomedicine - iBiMED, University of Aveiro, 3810-193 Aveiro, Portugal.
Cristóvão B da Cruz E SilvaLaboratório de Instrumentação e Física Experimental de Partículas - LIP, Av. Elias Garcia 14 - 1°, 1000-149 Lisboa, Portugal.
Odete A B da Cruz E SilvaNeuroscience and Signalling Laboratory, Department of Medical Sciences and Insitute of Biomedicine - iBiMED, University of Aveiro, 3810-193 Aveiro, Portugal.
University of Aveiro · PTLIP - Laboratory of Instrumentation and Experimental Particle Physics · PTRuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amyloidogenic peptide, Aβ, provokes a series of events affecting distinct cellular pathways regulated by protein phosphorylation. Aβ inhibits protein phosphatases in a dose-dependent manner, thus it is expected that the phosphorylation state of specific proteins would be altered in response to Aβ. In fact several Alzheimer's disease related proteins, such as APP and TAU, exhibit pathology associated hyperphosphorylated states. A systems biology approach was adopted and the phosphoproteome, of primary cortical neuronal cells exposed to Aβ, was evaluated. Phosphorylated proteins were recovered and those whose recovery increased or decreased, upon Aβ exposure across experimental sets, were identified. Significant differences were evident for 141 proteins and investigation of their interactors revealed key protein clusters responsive to Aβ treatment. Of these, 73 phosphorylated proteins increased and 68 decreased upon Aβ addition. These phosphorylated proteins represent an important resource of potential AD phospho biomarkers that should be further pursued.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorBiomarkersComputational BiologyHumansNeuronsPhosphoproteinsPhosphorylationProtein Interaction MappingProtein Interaction MapsProteomeProteomicsWorkflowAmyloid beta-PeptidesAmyloid beta-Protein PrecursorBiomarkersPhosphoproteinsProteome

Identifiers

PMID27466139
PMCPMC4964585
OpenAlexW2503550225

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.