Evidence map›Paper›PMID 33844503›Full record

ArticleAnalytical chemistry2021

Deeper Protein Identification Using Field Asymmetric Ion Mobility Spectrometry in Top-Down Proteomics.

Vincent R Gerbasi, Rafael D Melani, Susan E Abbatiello, Michael W Belford, Romain Huguet, John P McGee, Dawson Dayhoff, Paul M Thomas, Neil L Kelleher

Abstract read
In one paragraph

Article in Analytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
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  4. Top-down proteomics.Nature reviews. Methods primers · 2024
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  18. Affinity-Based Interactome Analysis of Endogenous LINE-1 Macromolecules.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
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  20. Article
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.

Vincent R GerbasiNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.
Rafael D MelaniNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.ORCID 0000-0002-0349-235X
Susan E AbbatielloNortheastern University, Boston, Massachusetts 02115, United States.
Michael W BelfordThermo Fisher Scientific, San Jose, California 98665, United States.
Romain HuguetThermo Fisher Scientific, San Jose, California 98665, United States.
John P McGeeNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.ORCID 0000-0002-0527-8904
Dawson DayhoffNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.
Paul M ThomasNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.ORCID 0000-0003-2887-4765
Neil L KelleherNorthwestern University, National Resource for Translational and Developmental Proteomics, Evanston, Illinois 60208, United States.ORCID 0000-0002-8815-3372

Funding

TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Renewable and Specific Affinity Reagents for Mapping Proteoforms in Human TissuesUH3CA246635 · NCI · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2019 to 2021
$1.4M
NCI NIH HHS UH3 CA246635NIGMS NIH HHS P41 GM108569
6 · The paper itself

Abstract

Field asymmetric ion mobility spectrometry (FAIMS), when used in proteomics studies, provides superior selectivity and enables more proteins to be identified by providing additional gas-phase separation. Here, we tested the performance of cylindrical FAIMS for the identification and characterization of proteoforms by top-down mass spectrometry of heterogeneous protein mixtures. Combining FAIMS with chromatographic separation resulted in a 62% increase in protein identifications, an 8% increase in proteoform identifications, and an improvement in proteoform identification compared to samples analyzed without FAIMS. In addition, utilization of FAIMS resulted in the identification of proteins encoded by lower-abundance mRNA transcripts. These improvements were attributable, in part, to improved signal-to-noise for proteoforms with similar retention times. Additionally, our results show that the optimal compensation voltage of any given proteoform was correlated with the molecular weight of the analyte. Collectively these results suggest that the addition of FAIMS can enhance top-down proteomics in both discovery and targeted applications.

Indexed as

Ion Mobility SpectrometryProteomicsMass SpectrometryProteinsProteins

Identifiers

PMID33844503
PMCPMC8130575

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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.