Evidence map›Paper›PMID 30118596›Full record

ArticleAnalytical chemistry2018

Improved Sensitivity and Separations for Phosphopeptides using Online Liquid Chromotography Coupled with Structures for Lossless Ion Manipulations Ion Mobility-Mass Spectrometry.

Christopher D Chouinard, Gabe Nagy, Ian K Webb, Tujin Shi, Erin S Baker, Spencer A Prost, Tao Liu, Yehia M Ibrahim, Richard D Smith

Abstract read
In one paragraph

Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Review
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  8. Targeted glucocorticoid analysis using ion mobility-mass spectrometry (IM-MS).Journal of mass spectrometry and advances in the clinical lab · 2022
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  12. 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

9 authors.

Christopher D ChouinardBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Gabe NagyBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Ian K WebbBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Tujin ShiBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Erin S BakerBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0001-5246-2213
Spencer A ProstBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Tao LiuBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0001-9529-6550
Yehia M IbrahimBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0001-6085-193X
Richard D SmithBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0002-2381-2349

Funding

Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
PNNL Proteome Characterization CenterU24CA210955 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI LIU, TAO, SMITH, RICHARD D · 2016 to 2020
$5.3M
NCI NIH HHS U24 CA210955NIGMS NIH HHS P41 GM103493
6 · The paper itself

Abstract

Phosphoproteomics greatly augments proteomics and holds tremendous potential for insights into the modulation of biological systems for various disease states. However, numerous challenges hinder conventional methods in terms of measurement sensitivity, throughput, quantification, and capabilities for confident phosphopeptide and phosphosite identification. In this work, we report the first example of integrating structures for lossless ion manipulations ion mobility-mass spectrometry (SLIM IM-MS) with online reversed-phase liquid chromatography (LC) to evaluate its potential for addressing the aforementioned challenges. A mixture of 51 heavy-labeled phosphopeptides was analyzed with a SLIM IM module having integrated ion accumulation and long-path separation regions. The SLIM IM-MS provided limits of detection as low as 50-100 pM (50-100 amol/μL) for several phosphopeptides, with the potential for significant further improvements. In addition, conventionally problematic phosphopeptide isomers could be resolved following an 18 m SLIM IM separation. The 2-D LC-IM peak capacity was estimated as ∼9000 for a 90 min LC separation coupled to an 18 m SLIM IM separation, considerably higher than LC alone and providing a basis for both improved identification and quantification, with additional gains projected with the future use of longer path SLIM IM separations. Thus, LC-SLIM IM-MS offers great potential for improving the sensitivity, separation, and throughput of phosphoproteomics analyses.

Indexed as

Amino Acid SequenceBacterial ProteinsChromatography, Reverse-PhaseHumansIon Mobility SpectrometryIsomerismMass SpectrometryPhosphopeptidesShewanellaBacterial ProteinsPhosphopeptides

Identifiers

PMID30118596
PMCPMC6211290

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Registered trials

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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.