Evidence map›Paper›PMID 28968100›Full record

ArticleJournal of proteome research2017

Elucidating Escherichia coli Proteoform Families Using Intact-Mass Proteomics and a Global PTM Discovery Database.

Yunxiang Dai, Michael R Shortreed, Mark Scalf, Brian L Frey, Anthony J Cesnik, Stefan Solntsev, Leah V Schaffer, Lloyd M Smith

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

  1. Intact Mass Proteomics Using a Proteoform Atlas.Journal of proteome research · 2025
    Article
  2. Article
  3. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Proteoforms and Proteoform Families: Past, Present, and Future.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  10. Mesh Fragmentation Improves Dissociation Efficiency in Top-down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Article
  11. Spritz: A Proteogenomic Database Engine.Journal of proteome research · 2021
    Article
  12. Article
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  14. Article
  15. 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

8 authors at 1 institution in 1 country.

Yunxiang DaiDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0001-7999-798X
Michael R ShortreedDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Mark ScalfDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Brian L FreyDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-0397-7269
Anthony J CesnikDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.ORCID 0000-0002-5326-7134
Stefan SolntsevDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Leah V SchafferDepartment 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

A proteoform family is a group of related molecular forms of a protein (proteoforms) derived from the same gene. We have previously described a strategy to identify proteoforms and elucidate proteoform families in complex mixtures of intact proteins. The strategy is based upon measurements of two properties for each proteoform: (i) the accurate proteoform intact-mass, measured by liquid chromatography/mass spectrometry (LC-MS), and (ii) the number of lysine residues in each proteoform, determined using an isotopic labeling approach. These measured properties are then compared with those extracted from a catalog of theoretical proteoforms containing protein sequences and localized post-translational modifications (PTMs) for the organism under study. A match between the measured properties and those in the catalog constitutes an identification of the proteoform. In the present study, this strategy is extended by utilizing a global PTM discovery database and is applied to the widely studied model organism Escherichia coli, providing the most comprehensive elucidation of E. coli proteoforms and proteoform families to date.

Indexed as

Multigene FamilyProtein Processing, Post-TranslationalChromatography, LiquidDatabases, ProteinEscherichia coliLysineProteomicsTandem Mass SpectrometryLysinedatabase searchE. coliintact-massNeuCodeproteoformproteoform familyPTM

Identifiers

PMID28968100
PMCPMC5679780
OpenAlexW2762321625

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.