Evidence map›Paper›PMID 32058701›Full record

ArticleAnalytical chemistry2020

Deep Proteomics Using Two Dimensional Data Independent Acquisition Mass Spectrometry.

Kyung-Cho Cho, David J Clark, Michael Schnaubelt, Guo Ci Teo, Felipe da Veiga Leprevost, William Bocik, Emily S Boja, Tara Hiltke, Alexey I Nesvizhskii, Hui Zhang

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.7field-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

22 citing papers in PubMed, 37 citations in OpenAlex.

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  14. COVIDomics: The Proteomic and Metabolomic Signatures of COVID-19.International journal of molecular sciences · 2022
    Review
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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 4 institutions in 1 country.

Kyung-Cho ChoDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0002-9448-4549
David J ClarkDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0003-0527-8469
Michael SchnaubeltDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Guo Ci TeoDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Felipe da Veiga LeprevostDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
William BocikAntibody Characterization Laboratory, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, Frederick, Maryland 21701, United States.
Emily S BojaOffice of Cancer Clinical Proteomics Research, National Cancer Institute, Bethesda, Maryland 20892, United States.
Tara HiltkeOffice of Cancer Clinical Proteomics Research, National Cancer Institute, Bethesda, Maryland 20892, United States.
Alexey I NesvizhskiiDepartment of Pathology, University of Michigan, Ann Arbor, Michigan 48109, United States.
Hui ZhangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0001-8726-7098
Johns Hopkins University · USUniversity of Michigan · USCancer Clinic · USFrederick National Laboratory for Cancer Research · US

Funding

Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
COMPUTATIONAL TOOLS FOR MASS SPECTROMETRY-BASED INTERACTOME DATAR01GM094231 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Alexey I Nesvizhskii · 2010 to 2026
$5.4M
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
NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA210967NCI NIH HHS U24 CA210985NIGMS NIH HHS R01 GM094231
6 · The paper itself

Abstract

Methodologies that facilitate high-throughput proteomic analysis are a key step toward moving proteome investigations into clinical translation. Data independent acquisition (DIA) has potential as a high-throughput analytical method due to the reduced time needed for sample analysis, as well as its highly quantitative accuracy. However, a limiting feature of DIA methods is the sensitivity of detection of low abundant proteins and depth of coverage, which other mass spectrometry approaches address by two-dimensional fractionation (2D) to reduce sample complexity during data acquisition. In this study, we developed a 2D-DIA method intended for rapid- and deeper-proteome analysis compared to conventional 1D-DIA analysis. First, we characterized 96 individual fractions obtained from the protein standard, NCI-7, using a data-dependent approach (DDA), identifying a total of 151,366 unique peptides from 11,273 protein groups. We observed that the majority of the proteins can be identified from just a few selected fractions. By performing an optimization analysis, we identified six fractions with high peptide number and uniqueness that can account for 80% of the proteins identified in the entire experiment. These selected fractions were combined into a single sample which was then subjected to DIA (referred to as 2D-DIA) quantitative analysis. Furthermore, improved DIA quantification was achieved using a hybrid spectral library, obtained by combining peptides identified from DDA data with peptides identified directly from the DIA runs with the help of DIA-Umpire. The optimized 2D-DIA method allowed for improved identification and quantification of low abundant proteins compared to conventional unfractionated DIA analysis (1D-DIA). We then applied the 2D-DIA method to profile the proteomes of two breast cancer patient-derived xenograft (PDX) models, quantifying 6,217 and 6,167 unique proteins in basal- and luminal- tumors, respectively. Overall, this study demonstrates the potential of high-throughput quantitative proteomics using a novel 2D-DIA method.

Indexed as

ProteomicsHumansMass SpectrometryPeptidesProteinsPeptidesProteins

Identifiers

PMID32058701
PMCPMC7255061
OpenAlexW3006506703

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.