Evidence map›Paper›PMID 32126768›Full record

ArticleJournal of proteome research2020

Full-Featured, Real-Time Database Searching Platform Enables Fast and Accurate Multiplexed Quantitative Proteomics.

Devin K Schweppe, Jimmy K Eng, Qing Yu, Derek Bailey, Ramin Rad, Jose Navarrete-Perea, Edward L Huttlin, Brian K Erickson, Joao A Paulo, Steven P Gygi

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 197 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
197citing papers in PubMed, 1 pooled it
18.9field-weighted citation impact, top 1% 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

197 citing papers in PubMed, 1 synthesis or guideline pooled it, 288 citations in OpenAlex.

  1. Pooled it
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  11. SLC16A6 is a tyrosine transporter for the melanosome.bioRxiv : the preprint server for biology · 2026
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137 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Devin K SchweppeHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0002-3241-6276
Jimmy K EngUniversity of Washington Proteomics Resource, Seattle, Washington 98109, United States.ORCID 0000-0001-6352-6737
Qing YuHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0003-0468-5353
Derek BaileyThermo Scientific LSMS, San Jose, California 95134, United States.
Ramin RadHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.
Jose Navarrete-PereaHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0001-6265-6214
Edward L HuttlinHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0002-1822-1173
Brian K EricksonHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0002-1150-5042
Joao A PauloHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.
Steven P GygiHarvard Medical School, Department of Cell Biology, Cambridge, Massachusetts 02155, United States.ORCID 0000-0001-7626-0034
Harvard University · USThermo Fisher Scientific (United States) · USUniversity of Washington · US

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Advancing Multiplexed Isobaric Tag-based Strategies for Proteome ProfilingR01GM132129 · NIGMS · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2019 to 2023
$1.7M
NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM132129
6 · The paper itself

Abstract

Multiplexed quantitative analyses of complex proteomes enable deep biological insight. While a multitude of workflows have been developed for multiplexed analyses, the most quantitatively accurate method (SPS-MS3) suffers from long acquisition duty cycles. We built a new, real-time database search (RTS) platform, Orbiter, to combat the SPS-MS3 method's longer duty cycles. RTS with Orbiter eliminates SPS-MS3 scans if no peptide matches to a given spectrum. With Orbiter's online proteomic analytical pipeline, which includes RTS and false discovery rate analysis, it was possible to process a single spectrum database search in less than 10 ms. The result is a fast, functional means to identify peptide spectral matches using Comet, filter these matches, and more efficiently quantify proteins of interest. Importantly, the use of Comet for peptide spectral matching allowed for a fully featured search, including analysis of post-translational modifications, with well-known and extensively validated scoring. These data could then be used to trigger subsequent scans in an adaptive and flexible manner. In this work we tested the utility of this adaptive data acquisition platform to improve the efficiency and accuracy of multiplexed quantitative experiments. We found that RTS enabled a 2-fold increase in mass spectrometric data acquisition efficiency. Orbiter's RTS quantified more than 8000 proteins across 10 proteomes in half the time of an SPS-MS3 analysis (18 h for RTS, 36 h for SPS-MS3).

Indexed as

ProteomeProteomicsDatabases, FactualMass SpectrometryPeptidesPeptidesProteomeadaptive instrument controlC#CometFusion APIintelligent data acquisitionmultiplexed proteomicsreal-time FDR filteringreal-time searchingsmart TMT

Identifiers

PMID32126768
PMCPMC7295121
OpenAlexW3009182715

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.