Evidence map›Paper›PMID 21515431›Full record

ArticleJournal of proteomics2011

Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects.

Fabio Di Domenico, Rukhsana Sultana, Eugenio Barone, Marzia Perluigi, Chiara Cini, Cesare Mancuso, Jian Cai, William M Pierce, D Allan Butterfield

Abstract read
In one paragraph

Article in Journal of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.0field-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

50 citing papers in PubMed, 91 citations in OpenAlex.

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  15. SPR immunosensor combined with TiMikrochimica acta · 2020
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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 5 institutions in 2 countries.

Fabio Di DomenicoDepartment of Chemistry, Center of Membrane Sciences, Sanders-Brown Center on Aging, University of Kentucky, Lexington, KY 40506-0055, USA.
Rukhsana Sultana
Eugenio Barone
Marzia Perluigi
Chiara Cini
Cesare Mancuso
Jian Cai
William M Pierce
D Allan Butterfield
University of Kentucky · USSapienza University of Rome · ITUniversity of Louisville · USInstitute of Molecular Biology and Pathology · ITUniversità Cattolica del Sacro Cuore · IT

Funding

TROPIC, CHOLINERGIC AND PATHOLOGIC CHANGES IN ALZHEIMER'S DISEASEP01AG005119 · NIA · UNIVERSITY OF KENTUCKY · PI ST CLAIR, DARET K · 1985 to 2012
$15.4M
NIA NIH HHS AG-05119NIA NIH HHS P01 AG005119
6 · The paper itself

Abstract

Phosphorylation on tyrosine, threonine and serine residues represents one of the most important post-translational modifications and is a key regulator of cellular signaling of multiple biological processes that require a strict control by protein kinases and protein phosphatases. Abnormal protein phosphorylation has been associated with several human diseases including Alzheimer's disease (AD). One of the characteristic hallmarks of AD is the presence of neurofibrillary tangles, composed of microtubule-associated, abnormally hyperphosphorylated tau protein. However, several others proteins showed altered phosphorylation levels in AD suggesting that deregulated phosphorylation may contribute to AD pathogenesis. Phosphoproteomics has recently gained attention as a valuable approach to analyze protein phosphorylation, both in a quantitative and a qualitative way. We used the fluorescent phosphospecific Pro-Q Diamond dye to identify proteins that showed alterations in their overall phosphorylation in the hippocampus of AD vs. control (CTR) subjects. Significant changes were found for 17 proteins involved in crucial neuronal process such as energy metabolism or signal transduction. These phosphoproteome data may provide new clues to better understand molecular pathways that are deregulated in the pathogenesis and progression of AD.

Indexed as

ProteomicsAgedAged, 80 and overAlzheimer DiseaseEnergy MetabolismFemaleHippocampusHumansMaleMetabolic Networks and PathwaysNeurofibrillary TanglesNeuronsPhosphorylationProtein Processing, Post-TranslationalSignal Transductiontau Proteinstau Proteins

Identifiers

PMID21515431
PMCPMC3119855
OpenAlexW1979139472

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.