Evidence map›Paper›PMID 29227670›Full record

ArticleAnalytical chemistry2018

Expanding Proteoform Identifications in Top-Down Proteomic Analyses by Constructing Proteoform Families.

Leah V Schaffer, Michael R Shortreed, Anthony J Cesnik, Brian L Frey, Stefan K Solntsev, Mark Scalf, Lloyd M 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Intact Mass Proteomics Using a Proteoform Atlas.Journal of proteome research · 2025
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  2. Review
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  7. Mesh Fragmentation Improves Dissociation Efficiency in Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
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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 1 institution in 1 country.

Leah V SchafferDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0001-6339-9141
Michael R ShortreedDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Anthony J CesnikDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-5326-7134
Brian L FreyDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-0397-7269
Stefan K SolntsevDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-1061-1476
Mark ScalfDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Lloyd M SmithDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
University of Wisconsin–Madison · US

Funding

Research Training for Computation and Informatics in Biology and MedicineT15LM007359 · NLM · UNIVERSITY OF WISCONSIN-MADISON · PI Mark W. Craven, Colin Noel Dewey · 2002 to 2026
$22.6M
BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Intact Proteoform Identification and QuantificationR01GM114292 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GOULD, MICHAEL N, SMITH, LLOYD M · 2015 to 2018
$1.6M
NIGMS NIH HHS R01 GM114292NIGMS NIH HHS T32 GM008349NLM NIH HHS T15 LM007359
6 · The paper itself

Abstract

In top-down proteomics, intact proteins are analyzed by tandem mass spectrometry and proteoforms, which are defined forms of a protein with specific sequences of amino acids and localized post-translational modifications, are identified using precursor mass and fragmentation data. Many proteoforms that are detected in the precursor scan (MS1) are not selected for fragmentation by the instrument and therefore remain unidentified in typical top-down proteomic workflows. Our laboratory has developed the open source software program Proteoform Suite to analyze MS1-only intact proteoform data. Here, we have adapted it to provide identifications of proteoform masses in precursor MS1 spectra of top-down data, supplementing the top-down identifications obtained using the MS2 fragmentation data. Proteoform Suite performs mass calibration using high-scoring top-down identifications and identifies additional proteoforms using calibrated, accurate intact masses. Proteoform families, the set of proteoforms from a given gene, are constructed and visualized from proteoforms identified by both top-down and intact-mass analyses. Using this strategy, we constructed proteoform families and identified 1861 proteoforms in yeast lysate, yielding an approximately 40% increase over the original 1291 proteoform identifications observed using traditional top-down analysis alone.

Indexed as

Mass SpectrometryProteomeProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSoftwareProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID29227670
PMCPMC5807004
OpenAlexW2772477774

What OpenQuestion holds

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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.