Evidence map›Paper›PMID 26332448›Full record

ArticleThe European journal of neuroscience2016

Oligomeric α-synuclein and β-amyloid variants as potential biomarkers for Parkinson's and Alzheimer's diseases.

Stephanie M Williams, Philip Schulz, Michael R Sierks

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The European journal of neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

42 citing papers in PubMed, 71 citations in OpenAlex.

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  16. Alpha and Beta Synucleins: From Pathophysiology to Clinical Application as Biomarkers.Movement disorders : official journal of the Movement Disorder Society · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Stephanie M WilliamsChemical Engineering, The School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, 85287-6106, USA.
Philip SchulzChemical Engineering, The School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, 85287-6106, USA.
Michael R SierksChemical Engineering, The School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, 85287-6106, USA.
Arizona State University · US

Funding

Research Education ComponentP30AG019610 · NIA · SUN HEALTH RESEARCH INSTITUTE · PI GONZALEZ HERNANDEZ, GRACIELA · 2001 to 2020
$32.5M
National Brain and Tissue Resource for Parkinson's Disease and Related DisordersU24NS072026 · NINDS · BANNER SUN HEALTH RESEARCH INSTITUTE · PI BEACH, THOMAS G · 2011 to 2015
$7.8M
NIA NIH HHS P30 AG019610NIA NIH HHS P30 AG19610NINDS NIH HHS U24 NS072026
6 · The paper itself

Abstract

Oligomeric forms of α-synuclein and β-amyloid are toxic protein variants that are thought to contribute to the onset and progression of Parkinson's disease (PD) and Alzheimer's disease (AD), respectively. The detection of toxic variants in human cerebrospinal fluid (CSF) and blood has great promise for facilitating early and accurate diagnoses of these devastating diseases. Two hurdles that have impeded the use of these protein variants as biomarkers are the availability of reagents that can bind the different variants and a sensitive assay to detect their very low concentrations. We previously isolated antibody-based reagents that selectively bind two different oligomeric variants of α-synuclein and two of β-amyloid, and developed a phage-based capture enzyme-linked immunosorbent assay (ELISA) with subfemtomolar sensitivity to quantify their presence. Here, we used these reagents to show that these oligomeric α-synuclein variants are preferentially present in PD brain tissue, CSF and serum, and that the oligomeric β-amyloid variants are preferentially present in AD brain tissue, CSF, and serum. Some AD samples also had α-synuclein pathology and some PD samples also had β-amyloid pathology, and, very intriguingly, these PD cases also had a history of dementia. Detection of different oligomeric α-synuclein and β-amyloid species is an effective method for identifying tissue, CSF and sera from PD and AD samples, respectively, and samples that also contained early stages of other protein pathologies, indicating their potential value as blood-based biomarkers for neurodegenerative diseases.

Indexed as

AgedAged, 80 and overalpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesBiomarkersEnzyme-Linked Immunosorbent AssayFemaleHumansMaleParkinson DiseasePeptide FragmentsSensitivity and SpecificityTemporal Lobealpha-SynucleinAmyloid beta-PeptidesBiomarkersPeptide Fragmentsbrain tissuecerebrospinal fluidphage capture enzyme-linked immunosorbent assayserumsingle-chain variable fragments

Identifiers

PMID26332448
PMCPMC4718789
OpenAlexW2165027466

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.