Evidence map›Paper›PMID 34384221›Full record

ArticleJournal of proteome research2021

Evaluation of the Sensitivity and Reproducibility of Targeted Proteomic Analysis Using Data-Independent Acquisition for Serum and Cerebrospinal Fluid Proteins.

Kyung-Cho Cho, Sungtaek Oh, Yuefan Wang, Liana S Rosenthal, Chan Hyun Na, Hui Zhang

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

8 citing papers in PubMed, 11 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 1 institution in 1 country.

Kyung-Cho ChoDepartment of Pathology, Johns Hopkins University, Baltimore, Maryland 21231, United States.ORCID 0000-0002-9448-4549
Sungtaek OhDepartments of Neurology, Johns Hopkins University, Baltimore, Maryland 21205, United States.
Yuefan WangDepartment of Pathology, Johns Hopkins University, Baltimore, Maryland 21231, United States.ORCID 0000-0001-5731-6143
Liana S RosenthalInstitute for Cell Engineering, Johns Hopkins University, Baltimore, Maryland 21205, United States.
Chan Hyun NaDepartments of Neurology, Johns Hopkins University, Baltimore, Maryland 21205, United States.ORCID 0000-0002-3622-2938
Hui ZhangDepartment of Pathology, Johns Hopkins University, Baltimore, Maryland 21231, United States.ORCID 0000-0001-8726-7098
Johns Hopkins University · US

Funding

Research Education ComponentP30AG066507 · NIA · JOHNS HOPKINS UNIVERSITY · PI MARILYN S. ALBERT · 2020 to 2026
$29.3M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
The Comprehensive Proteome Characterization Center at Johns Hopkins: High Precision Discovery and Confirmation of Genoproteomic TargetsU24CA210985 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2016 to 2020
$5.3M
University of Michigan Proteogenomics Data Analysis CenterU24CA210967 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHINNAIYAN, ARUL M, DHANASEKARAN, SARAVANA M · 2016 to 2020
$4.1M
Fourier Transform Orbitrap Fusion Lumos Tribrid Mass Spectrometer with ETDS10OD021844 · OD · JOHNS HOPKINS UNIVERSITY · PI PANDEY, AKHILESH · 2016 to 2016
$1.1M
NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA210967NCI NIH HHS U24 CA210985NIA NIH HHS P30 AG066507NIH HHS S10 OD021844
6 · The paper itself

Abstract

There is a need for targeted analysis of biological fluids for diagnosis, prognosis, or monitoring the progression of diseases. Cerebrospinal fluid (CSF) and serum have been widely used for the development of protein analysis for neurodegenerative diseases and other diseases, respectively. Recently, data-independent acquisition (DIA) mass spectrometry (MS) has been developed to increase the throughput over data-dependent acquisition (DDA) on screening of a large number of samples and discovery of candidate targets. When it comes to target validation, the analytical performance of targeted analysis is critical. However, the inter- and intralaboratory analytical performances of the DIA-MS for targeted proteomic analysis of CSF and serum samples have not yet been investigated. In this study, we showed that the DIA-MS approach allowed us to identify and quantify 1732 CSF and 424 serum proteins, with 90% of proteins identified and quantified in at least 50% of DIA-MS runs. To evaluate the sensitivity, linearity, and dynamic range of the DIA approach, we included the stable isotope-labeled (SI) peptides into CSF and serum samples with serial dilutions. The lower limit of quantification (LLOQ) of peptides was 0.1-0.5 fmol, and the dynamic range was over 3.53 orders of magnitude, with excellent linearity (

Indexed as

Cerebrospinal Fluid ProteinsProteomicsMass SpectrometryPeptidesProteomeReproducibility of ResultsCerebrospinal Fluid ProteinsPeptidesProteomecerebrospinal fluid (CSF)clinical proteomicsdata-independent acquisition (DIA)mass spectrometerquantitative proteomicsserum

Identifiers

PMID34384221
PMCPMC8631582
OpenAlexW3190003921

What OpenQuestion holds

Textmetadata
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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.