Evidence map›Paper›PMID 35234472›Full record

ArticleJournal of proteome research2022

Data-Independent Acquisition Protease-Multiplexing Enables Increased Proteome Sequence Coverage Across Multiple Fragmentation Modes.

Alicia L Richards, Kuei-Ho Chen, Damien B Wilburn, Erica Stevenson, Benjamin J Polacco, Brian C Searle, Danielle L Swaney

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  9. ProtView: A Versatile Tool forJournal of proteome research · 2023
    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

7 authors at 3 institutions in 1 country.

Alicia L RichardsQuantitative Biosciences Institute (QBI), University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0002-4869-2945
Kuei-Ho ChenQuantitative Biosciences Institute (QBI), University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0001-6541-0578
Damien B WilburnPelotonia Institute for Immuno-Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, Ohio 43210, United States.
Erica StevensonQuantitative Biosciences Institute (QBI), University of California San Francisco, San Francisco, California 94158, United States.
Benjamin J PolaccoQuantitative Biosciences Institute (QBI), University of California San Francisco, San Francisco, California 94158, United States.
Brian C SearlePelotonia Institute for Immuno-Oncology, The Ohio State University Comprehensive Cancer Center, Columbus, Ohio 43210, United States.
Danielle L SwaneyQuantitative Biosciences Institute (QBI), University of California San Francisco, San Francisco, California 94158, United States.
Gladstone Institutes · USThe Ohio State University · USUniversity of Washington · US

Funding

A universal multiplexing approach to unlock the hidden proteomeR01GM133981 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SWANEY, DANIELLE L · 2019 to 2022
$1.3M
Integrating 'omics', evolution, and structural biochemistry to understand animal fertilizationK99HD090201 · NICHD · UNIVERSITY OF WASHINGTON · PI WILBURN, DAMIEN BEAU · 2018 to 2020
$294k
NICHD NIH HHS K99 HD090201NIGMS NIH HHS R01 GM133981
6 · The paper itself

Abstract

The use of multiple proteases has been shown to increase protein sequence coverage in proteomics experiments; however, due to the additional analysis time required, it has not been widely adopted in routine data-dependent acquisition (DDA) proteomic workflows. Alternatively, data-independent acquisition (DIA) has the potential to analyze multiplexed samples from different protease digests, but has been primarily optimized for fragmenting tryptic peptides. Here we evaluate a DIA multiplexing approach that combines three proteolytic digests (Trypsin, AspN, and GluC) into a single sample. We first optimize data acquisition conditions for each protease individually with both the canonical DIA fragmentation mode (beam type CID), as well as resonance excitation CID, to determine optimal consensus conditions across proteases. Next, we demonstrate that application of these conditions to a protease-multiplexed sample of human peptides results in similar protein identifications and quantitative performance as compared to trypsin alone, but enables up to a 63% increase in peptide detections, and a 45% increase in nonredundant amino acid detections. Nontryptic peptides enabled noncanonical protein isoform determination and resulted in 100% sequence coverage for numerous proteins, suggesting the utility of this approach in applications where sequence coverage is critical, such as protein isoform analysis.

Indexed as

ProteomeProteomicsAmino Acid SequenceHumansPeptide HydrolasesPeptidesPeptide HydrolasesPeptidesProteomeCIDDIA-MSisoformslabel-free quantificationmultiplexingproteases

Identifiers

PMID35234472
PMCPMC9035370
OpenAlexW4220824959

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.