Evidence map›Paper›PMID 22532456›Full record

ArticleProteomics. Clinical applications2012

Analysis of a membrane-enriched proteome from postmortem human brain tissue in Alzheimer's disease.

Laura E Donovan, Lenora Higginbotham, Eric B Dammer, Marla Gearing, Howard D Rees, Qiangwei Xia, Duc M Duong, Nicholas T Seyfried, James J Lah, Allan I Levey

Abstract readValidation Study
In one paragraph

Article in Proteomics. Clinical applications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 82 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

10 authors at 1 institution in 1 country.

Laura E DonovanDepartment of Neurology, Emory University School of Medicine, Atlanta, Georgia, USA.
Lenora Higginbotham
Eric B Dammer
Marla Gearing
Howard D Rees
Qiangwei Xia
Duc M Duong
Nicholas T Seyfried
James J Lah
Allan I Levey
Emory University · US

Funding

The Emory Alzheimer's Disease CenterP50AG025688 · NIA · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2005 to 2019
$25.7M
ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2008 to 2018
$6.8M
TRAINING IN TRANSLATIONAL RESEARCH IN NEUROLOGYT32NS007480 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2000 to 2020
$4.5M
NIA NIH HHS AG025688NIA NIH HHS P01AG1449NIA NIH HHS P50 AG025688NINDS NIH HHS NS055077NINDS NIH HHS P30 NS055077NINDS NIH HHS T32 NS007480NINDS NIH HHS T32NS007480
6 · The paper itself

Abstract

purposeThe present study is a discovery mode proteomics analysis of the membrane-enriched fraction of postmortem brain tissue from Alzheimer's disease (AD) and control cases. This study aims to validate a method to identify new proteins that could be involved in the pathogenesis of AD and potentially serve as disease biomarkers. EXPERIMENTAL

designLiquid chromatography-tandem mass spectrometry (LC-MS/MS) was used to analyze the membrane-enriched fraction of human postmortem brain tissue from five AD and five control cases of similar age. Biochemical validation of specific targets was performed by immunoblotting.

resultsOne thousand seven hundred and nine proteins were identified from the membrane-enriched fraction of frontal cortex. Label-free quantification by spectral counting and G-test analysis identified 13 proteins that were significantly changed in disease. In addition to Tau (MAPT), two additional proteins found to be enriched in AD, ubiquitin carboxy-terminal hydrolase 1 (UCHL1), and syntaxin-binding protein 1 (Munc-18), were validated through immunoblotting. DISCUSSION AND CLINICAL RELEVANCE: Proteomic analysis of the membrane-enriched fraction of postmortem brain tissue identifies proteins biochemically altered in AD. Further analysis of this subproteome may help elucidate mechanisms behind AD pathogenesis and provide new sources of biomarkers.

Indexed as

AgedAlzheimer DiseaseAutopsyBiomarkersBrain ChemistryCase-Control StudiesCell MembraneChromatography, LiquidFemaleFrontal LobeHumansMaleMiddle AgedMunc18 ProteinsProteomeProteomicsBiomarkersMAPT protein, humanMunc18 ProteinsProteomeSTXBP1 protein, humantau ProteinsUbiquitin ThiolesteraseUCHL1 protein, human

Identifiers

PMID22532456
PMCPMC3338199
OpenAlexW2097925533

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.