Evidence map›Paper›PMID 26503891›Full record

ArticleMolecular & cellular proteomics : MCP2016

Integrated Bottom-Up and Top-Down Proteomics of Patient-Derived Breast Tumor Xenografts.

Ioanna Ntai, Richard D LeDuc, Ryan T Fellers, Petra Erdmann-Gilmore, Sherri R Davies, Jeanne Rumsey, Bryan P Early, Paul M Thomas, Shunqiang Li, Philip D Compton and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.6field-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

46 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
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  6. AI-Assisted Processing Pipeline to Boost Protein Isoform Detection.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
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  14. Connecting aging biology and inflammation in the omics era.The Journal of clinical investigation · 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

17 authors at 7 institutions in 1 country.

Ioanna NtaiFrom the ‡Proteomics Center of Excellence, §Department of Chemistry, and.
Richard D LeDucFrom the ‡Proteomics Center of Excellence.
Ryan T FellersFrom the ‡Proteomics Center of Excellence.
Petra Erdmann-Gilmore‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110;
Sherri R Davies‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110;
Jeanne Rumsey‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110;
Bryan P EarlyFrom the ‡Proteomics Center of Excellence.
Paul M ThomasFrom the ‡Proteomics Center of Excellence, ¶Department of Molecular BiosciencesNorthwestern University, Evanston, IL 60208;
Shunqiang Li‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110;
Philip D ComptonFrom the ‡Proteomics Center of Excellence, ‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110;
Matthew J C Ellis**Department of Molecular & Cellular Biology, Baylor College of Medicine, Houston, TX 77030;
Kelly V Ruggles‡‡Center for Health Informatics and Bioinformatics, and Department of Biochemistry and Molecular Pharmacology, New York University Medical School, New York, NY 10016;
David Fenyö‡‡Center for Health Informatics and Bioinformatics, and Department of Biochemistry and Molecular Pharmacology, New York University Medical School, New York, NY 10016;
Emily S Boja§§Office of Cancer Clinical Proteomics Research, National Cancer Institute, Bethesda, MD 20892.
Henry Rodriguez§§Office of Cancer Clinical Proteomics Research, National Cancer Institute, Bethesda, MD 20892.
R Reid Townsend‖Department of Internal Medicine, Washington University School of Medicine, St Louis, MO 63110; rtownsend@wustl.edu n-kelleher@northwestern.edu.
Neil L KelleherFrom the ‡Proteomics Center of Excellence, §Department of Chemistry, and ¶Department of Molecular BiosciencesNorthwestern University, Evanston, IL 60208; rtownsend@wustl.edu n-kelleher@northwestern.edu.
Washington University in St. Louis · USNorthwestern University · USNational Cancer Institute · USBaylor College of Medicine · USColumbia University Irving Medical Center · USDigital Proteomics (United States) · USNew York University · US

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI TIMOTHY J. EBERLEIN · 2001 to 2026
$128.0M
Cancer Proteome Center at Washington Univ, Univ of North Carolina & Boise StateU24CA160035 · NCI · WASHINGTON UNIVERSITY · PI CHEN, XIAN, ELLIS, MATTHEW J · 2011 to 2016
$11.8M
Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENCI NIH HHS P30 CA091842NCI NIH HHS U24 CA160035NIGMS NIH HHS GM067193NIGMS NIH HHS R01 GM067193
6 · The paper itself

Abstract

Bottom-up proteomics relies on the use of proteases and is the method of choice for identifying thousands of protein groups in complex samples. Top-down proteomics has been shown to be robust for direct analysis of small proteins and offers a solution to the "peptide-to-protein" inference problem inherent with bottom-up approaches. Here, we describe the first large-scale integration of genomic, bottom-up and top-down proteomic data for the comparative analysis of patient-derived mouse xenograft models of basal and luminal B human breast cancer, WHIM2 and WHIM16, respectively. Using these well-characterized xenograft models established by the National Cancer Institute's Clinical Proteomic Tumor Analysis Consortium, we compared and contrasted the performance of bottom-up and top-down proteomics to detect cancer-specific aberrations at the peptide and proteoform levels and to measure differential expression of proteins and proteoforms. Bottom-up proteomic analysis of the tumor xenografts detected almost 10 times as many coding nucleotide polymorphisms and peptides resulting from novel splice junctions than top-down. For proteins in the range of 0-30 kDa, where quantitation was performed using both approaches, bottom-up proteomics quantified 3,519 protein groups from 49,185 peptides, while top-down proteomics quantified 982 proteoforms mapping to 358 proteins. Examples of both concordant and discordant quantitation were found in a ∼60:40 ratio, providing a unique opportunity for top-down to fill in missing information. The two techniques showed complementary performance, with bottom-up yielding eight times more identifications of 0-30 kDa proteins in xenograft proteomes, but failing to detect differences in certain posttranslational modifications (PTMs), such as phosphorylation pattern changes of alpha-endosulfine. This work illustrates the potency of a combined bottom-up and top-down proteomics approach to deepen our knowledge of cancer biology, especially when genomic data are available.

Indexed as

AnimalsBreast NeoplasmsChromatography, High Pressure LiquidFemaleGenotypeHeterograftsHumansMiceMolecular WeightPeptidesPolymorphism, Single NucleotideProteomeProteomicsTandem Mass SpectrometryTransplantation, HeterologousPeptidesProteome

Identifiers

PMID26503891
PMCPMC4762530
OpenAlexW2179083672

What OpenQuestion holds

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LicenceCC BY
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.