Evidence map›Paper›PMID 37774690›Full record

ArticleJournal of proteome research2023

Orbitrap Mass Spectrometry and High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Enable the in-Depth Analysis of Human Serum Proteoforms.

Jake T Kline, Michael W Belford, Cornelia L Boeser, Romain Huguet, Ryan T Fellers, Joseph B Greer, Sylvester M Greer, David M Horn, Kenneth R Durbin, Jean-Jacques Dunyach and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

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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

12 authors at 2 institutions in 1 country.

Jake T KlineDepartment of Biology, University of Oklahoma, Norman, Oklahoma 73019, United States.
Michael W BelfordThermo Scientific, San Jose, California 95134, United States.
Cornelia L BoeserThermo Scientific, San Jose, California 95134, United States.
Romain HuguetThermo Scientific, San Jose, California 95134, United States.
Ryan T FellersProteinaceous, Inc., Evanston, Illinois 60204, United States.
Joseph B GreerProteinaceous, Inc., Evanston, Illinois 60204, United States.
Sylvester M GreerThermo Scientific, San Jose, California 95134, United States.
David M HornThermo Scientific, San Jose, California 95134, United States.
Kenneth R DurbinProteinaceous, Inc., Evanston, Illinois 60204, United States.ORCID 0000-0001-7163-4877
Jean-Jacques DunyachThermo Scientific, San Jose, California 95134, United States.
Nagib AhsanDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID 0000-0002-6813-7527
Luca FornelliDepartment of Biology, University of Oklahoma, Norman, Oklahoma 73019, United States.ORCID 0000-0001-6334-1046
Thermo Fisher Scientific (United States) · USUniversity of Oklahoma · US

Funding

A multi-level mass spectrometry pipeline for the analysis of whole proteoforms and their complexesR35GM147397 · NIGMS · UNIVERSITY OF OKLAHOMA · PI Luca Fornelli · 2022 to 2026
$1.9M
NIGMS NIH HHS R35 GM147397
6 · The paper itself

Abstract

Blood serum and plasma are arguably the most commonly analyzed clinical samples, with dozens of proteins serving as validated biomarkers for various human diseases. Top-down proteomics may provide additional insights into disease etiopathogenesis since this approach focuses on protein forms, or proteoforms, originally circulating in blood, potentially providing access to information about relevant post-translational modifications, truncations, single amino acid substitutions, and many other sources of protein variation. However, the vast majority of proteomic studies on serum and plasma are carried out using peptide-centric, bottom-up approaches that cannot recapitulate the original proteoform content of samples. Clinical laboratories have been slow to adopt top-down analysis, also due to higher sample handling requirements. In this study, we describe a straightforward protocol for intact proteoform sample preparation based on the depletion of albumin and immunoglobulins, followed by simplified protein fractionation via polyacrylamide gel electrophoresis. After molecular weight-based fractionation, we supplemented the traditional liquid chromatography-tandem mass spectrometry (LC-MS

Indexed as

Ion Mobility SpectrometrySerumHumansMass SpectrometryProteinsProteomicsProteinsbiomarkersbloodFAIMSmass spectrometryOrbitrapPEPPIProtein depletionproteoformserumtop-down proteomics

Identifiers

PMID37774690
PMCPMC10629265
OpenAlexW4387160423

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.