Evidence map›Paper›PMID 31999103›Full record

ArticleAnalytical chemistry2020

Top-Down Characterization of Denatured Proteins and Native Protein Complexes Using Electron Capture Dissociation Implemented within a Modified Ion Mobility-Mass Spectrometer.

Jonathan P Williams, Lindsay J Morrison, Jeffery M Brown, Joseph S Beckman, Valery G Voinov, Frederik Lermyte

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

32 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  7. Article
  8. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
    Article
  9. Review
  10. Article
  11. Article
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  13. Article
  14. Review
  15. Article
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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

6 authors at 3 institutions in 2 countries.

Jonathan P WilliamsWaters Corporation, Stamford Avenue, Altrincham Road, Wilmslow SK9 4AX, United Kingdom.
Lindsay J MorrisonWaters Corporation, Stamford Avenue, Altrincham Road, Wilmslow SK9 4AX, United Kingdom.
Jeffery M BrownWaters Corporation, Stamford Avenue, Altrincham Road, Wilmslow SK9 4AX, United Kingdom.ORCID 0000-0001-8569-7174
Joseph S Beckmane-MSion Inc., 2121 NE Jack London Drive, Corvallis, Oregon 97330, United States.
Valery G Voinove-MSion Inc., 2121 NE Jack London Drive, Corvallis, Oregon 97330, United States.
Frederik LermyteSchool of Engineering, University of Warwick, Coventry CV4 7AL, United Kingdom.ORCID 0000-0001-7371-4475
Waters (United Kingdom) · GBOregon State University · USUniversity of Warwick · GB

Funding

Practical Mass Spectrometry Upgrade for Identifying Fragile Protein Modifications by ECDR44GM122131 · NIGMS · E-MSION, INC. · PI VOINOV, VALERY G. · 2017 to 2018
$1.8M
Practical Mass Spectrometry Upgrade for Identifying Fragile Protein Modifications by ECDR43GM122131 · NIGMS · E-MSION, INC. · PI VOINOV, VALERY G. · 2017 to 2017
$225k
NIGMS NIH HHS R43 GM122131NIGMS NIH HHS R44 GM122131
6 · The paper itself

Abstract

Electron-based fragmentation methods have revolutionized biomolecular mass spectrometry, in particular native and top-down protein analysis. Here, we report the use of a new electromagnetostatic cell to perform electron capture dissociation (ECD) within a quadrupole/ion mobility/time-of-flight mass spectrometer. This cell was installed between the ion mobility and time-of-flight regions of the instrument, and fragmentation was fast enough to be compatible with mobility separation. The instrument was already fitted with electron transfer dissociation (ETD) between the quadrupole and mobility regions prior to modification. We show excellent fragmentation efficiency for denatured peptides and proteins without the need to trap ions in the gas phase. Additionally, we demonstrate native top-down backbone fragmentation of noncovalent protein complexes, leading to comparable sequence coverage to what was achieved using the instrument's existing ETD capabilities. Limited collisional ion activation of the hemoglobin tetramer before ECD was reflected in the observed fragmentation pattern, and complementary ion mobility measurements prior to ECD provided orthogonal evidence of monomer unfolding within this complex. The approach demonstrated here provides a powerful platform for both top-down proteomics and mass spectrometry-based structural biology studies.

Indexed as

Protein DenaturationAmino Acid SequenceAnimalsCattleHumansMass SpectrometryModels, MolecularProtein MultimerizationProteinsProtein Structure, QuaternaryProteins

Identifiers

PMID31999103
PMCPMC7847745
OpenAlexW3004221282

What OpenQuestion holds

Textmetadata
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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.