Evidence map›Paper›PMID 26941048›Full record

ArticleJournal of proteome research2016

Elucidating Proteoform Families from Proteoform Intact-Mass and Lysine-Count Measurements.

Michael R Shortreed, Brian L Frey, Mark Scalf, Rachel A Knoener, Anthony J Cesnik, Lloyd M Smith

Erratum issuedAbstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 56 citations in OpenAlex.

  1. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Review
  3. Review
  4. Article
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  7. Intact Mass Proteomics Using a Proteoform Atlas.Journal of proteome research · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Proteoforms and Proteoform Families: Past, Present, and Future.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Article
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  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Michael R ShortreedDepartment 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.
Mark ScalfDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Rachel A KnoenerDepartment 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.
Lloyd M SmithDepartment of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.
University of Wisconsin–Madison · USEnergy Center of Wisconsin · 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
Intact Proteoform Identification and QuantificationR01GM114292 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GOULD, MICHAEL N, SMITH, LLOYD M · 2015 to 2018
$1.6M
A Mechanical Nanomembrane Detector for Time-of-Flight Mass SpectrometryR01GM103315 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SMITH, LLOYD M · 2012 to 2014
$889k
NIGMS NIH HHS R01 GM103315NIGMS NIH HHS R01GM103315NIGMS NIH HHS R01 GM114292NIGMS NIH HHS R01GM114292NLM NIH HHS T15 LM007359
6 · The paper itself

Abstract

Proteomics is presently dominated by the "bottom-up" strategy, in which proteins are enzymatically digested into peptides for mass spectrometric identification. Although this approach is highly effective at identifying large numbers of proteins present in complex samples, the digestion into peptides renders it impossible to identify the proteoforms from which they were derived. We present here a powerful new strategy for the identification of proteoforms and the elucidation of proteoform families (groups of related proteoforms) from the experimental determination of the accurate proteoform mass and number of lysine residues contained. Accurate proteoform masses are determined by standard LC-MS analysis of undigested protein mixtures in an Orbitrap mass spectrometer, and the lysine count is determined using the NeuCode isotopic tagging method. We demonstrate the approach in analysis of the yeast proteome, revealing 8637 unique proteoforms and 1178 proteoform families. The elucidation of proteoforms and proteoform families afforded here provides an unprecedented new perspective upon proteome complexity and dynamics.

Indexed as

Chromatography, LiquidLysineMass SpectrometryMolecular WeightMultiprotein ComplexesProtein Interaction MappingProteomicsRibosomal ProteinsRibosome Subunits, Large, EukaryoticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsLysineMultiprotein ComplexesRibosomal ProteinsSaccharomyces cerevisiae Proteinsdatabase searchNeuCodeproteoformproteoform familyproteomicsPTMtop-down

Identifiers

PMID26941048
PMCPMC4917391
OpenAlexW2289907074

What OpenQuestion holds

Textmetadata
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.