Evidence map›Paper›PMID 34170114›Full record

ArticleAnalytical chemistry2021

Proteoform Differentiation using Tandem Trapped Ion Mobility, Electron Capture Dissociation, and ToF Mass Spectrometry.

Kevin Jeanne Dit Fouque, Desmond Kaplan, Valery G Voinov, Frederik H V Holck, Ole N Jensen, Francisco Fernandez-Lima

Open access · greenAbstract 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Linker H1 Histone Direct Top-Down Proteoform Analysis.Journal of proteome research · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Chemical science · 2023
    Article
  14. Enhancing the Depth of Analyses with Next-Generation Ion Mobility Experiments.Annual review of analytical chemistry (Palo Alto, Calif.) · 2023
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Effective discrimination of gas-phase peptide conformers using TIMS-ECD-ToF MS/MS.Analytical methods : advancing methods and applications · 2021
    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

6 authors at 3 institutions in 2 countries.

Kevin Jeanne Dit FouqueDepartment of Chemistry and Biochemistry, Florida International University, Miami, Florida 33199, United States.
Desmond KaplanKapScience, LLC., Tewksbury, Massachusetts 01876, United States.
Valery G Voinove-MSion, Inc., Corvallis, Oregon 97330, United States.
Frederik H V HolckDepartment of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, DK-5230 Odense M, Denmark.
Ole N JensenDepartment of Biochemistry & Molecular Biology and VILLUM Center for Bioanalytical Sciences, University of Southern Denmark, DK-5230 Odense M, Denmark.ORCID 0000-0003-1862-8528
Francisco Fernandez-LimaDepartment of Chemistry and Biochemistry, Florida International University, Miami, Florida 33199, United States.ORCID 0000-0002-1283-4390
Florida International University · USUniversity of Southern Denmark · DKOregon State University · US

Funding

Development of Multidimensional, Linear and Differential Ion Mobility MS Separations for Middle-Down ProteoformsR01GM134247 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI FERNANDEZ-LIMA, FRANCISCO · 2019 to 2022
$1.7M
NIGMS NIH HHS R01 GM134247
6 · The paper itself

Abstract

Comprehensive characterization of post-translationally modified histone proteoforms is challenging due to their high isobaric and isomeric content. Trapped ion mobility spectrometry (TIMS), implemented on a quadrupole/time-of-flight (Q-ToF) mass spectrometer, has shown great promise in discriminating isomeric complete histone tails. The absence of electron activated dissociation (ExD) in the current platform prevents the comprehensive characterization of unknown histone proteoforms. In the present work, we report for the first time the use of an electromagnetostatic (EMS) cell devised for nonergodic dissociation based on electron capture dissociation (ECD), implemented within a nESI-TIMS-Q-ToF mass spectrometer for the characterization of acetylated (AcK18 and AcK27) and trimethylated (TriMetK4, TriMetK9 and TriMetK27) complete histone tails. The integration of the EMS cell in a TIMS-q-TOF MS permitted fast mobility-selected top-down ECD fragmentation with near 10% efficiency overall. The potential of this coupling was illustrated using isobaric (AcK18/TriMetK4) and isomeric (AcK18/AcK27 and TriMetK4/TriMetK9) binary H3 histone tail mixtures, and the H3.1 TriMetK27 histone tail structural diversity (e.g., three IMS bands at

Indexed as

ElectronsIon Mobility SpectrometryCell DifferentiationIonsMass SpectrometryIons

Identifiers

PMID34170114
PMCPMC8568060
OpenAlexW3176924235

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.