Evidence map›Paper›PMID 34355254›Full record

ArticleAnalytical and bioanalytical chemistry2022

Accurate characterization of β-amyloid (Aβ40, Aβ42) standards using species-specific isotope dilution by means of HPLC-ICP-MS/MS.

Martin Schaier, Gerrit Hermann, Gunda Koellensperger, Sarah Theiner

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
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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

4 authors.

Martin SchaierInstitute of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 38, 1090, Vienna, Austria.
Gerrit HermannInstitute of Analytical Chemistry, Department of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria.
Gunda KoellenspergerInstitute of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 38, 1090, Vienna, Austria.
Sarah TheinerInstitute of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 38, 1090, Vienna, Austria. sarah.theiner@univie.ac.at.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amyloid β peptide, as one of the main components in senile plaque, represents a defining pathological feature for Alzheimer's disease, and is therefore commonly used as a biomarker for this disease in clinical analysis. However, the selection of suitable standards is limited here, since only a few are commercially available, and these suffer from varying purity. Hence, the accurate characterization of these standards is of great importance. In this study, we developed a method for the traceable quantification of the peptide content using species-specific isotope dilution and ICP-MS/MS detection. It is based on the separation of the sulfur-containing amino acids methionine and cysteine after oxidation and hydrolysis of the peptide. Using a strong anion exchange column, both amino acids could be separated from each other, as well as from their oxidized forms and sulfate. The sulfur content was determined via ICP-MS/MS using oxygen as reaction gas. Species-specific isotope dilution was enabled by using a

Indexed as

Amyloid beta-PeptidesTandem Mass SpectrometryChromatography, High Pressure LiquidIsotopesPeptide FragmentsAmyloid beta-Peptidesamyloid beta-protein (1-42)IsotopesPeptide FragmentsAlzheimer’s diseaseAmyloid beta peptideICP-MSSpeciation analysisSpecies-specific isotope dilutionTraceability

Identifiers

PMID34355254
PMCPMC8748378

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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.