Evidence map›Paper›PMID 31117399›Full record

ArticleAnalytical chemistry2019

Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device.

Charles Eldrid, Jakub Ujma, Symeon Kalfas, Nick Tomczyk, Kevin Giles, Mike Morris, Konstantinos Thalassinos

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  12. Review
  13. Revealing the Fates of Proteins in the Gas Phase.International journal of mass spectrometry · 2024
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Resolving Hidden Solution Conformations of Hemoglobin Using IMS-IMS on a Cyclic Instrument.Journal of the American Society for Mass Spectrometry · 2023
    Article
  20. 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

7 authors.

Charles EldridInstitute of Structural and Molecular Biology, Division of Biosciences , University College London , London , WC1E 6BT , United Kingdom.ORCID 0000-0001-5306-3644
Jakub UjmaWaters Corporation , Wilmslow , SK9 4AX , United Kingdom.
Symeon KalfasInstitute of Structural and Molecular Biology, Division of Biosciences , University College London , London , WC1E 6BT , United Kingdom.
Nick TomczykWaters Corporation , Wilmslow , SK9 4AX , United Kingdom.
Kevin GilesWaters Corporation , Wilmslow , SK9 4AX , United Kingdom.ORCID 0000-0001-5693-1064
Mike MorrisWaters Corporation , Wilmslow , SK9 4AX , United Kingdom.
Konstantinos ThalassinosInstitute of Structural and Molecular Biology, Division of Biosciences , University College London , London , WC1E 6BT , United Kingdom.ORCID 0000-0001-5072-8428

Funding

Biotechnology and Biological Sciences Research Council BB/L015382/1
6 · The paper itself

Abstract

Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into "conformational families". Increasing the IM resolving power should allow finer structural information to be obtained and can be achieved by increasing the length of the IM separator. This, however, increases the time that protein ions spend in the gas phase and previous experiments have shown that the initial conformations of small proteins can be lost within tens of milliseconds. Here, we report on investigations of protein ion stability using a multipass traveling wave (TW) cyclic IM (cIM) device. Using this device, minimal structural changes were observed for Cytochrome C after hundreds of milliseconds, while no changes were observed for a larger multimeric complex (Concanavalin A). The geometry of the instrument (Q-cIM-ToF) also enables complex tandem IM experiments to be performed, which were used to obtain more detailed collision-induced unfolding pathways for Cytochrome C. The instrument geometry provides unique capabilities with the potential to expand the field of protein analysis via IM-MS.

Identifiers

PMID31117399
PMCPMC7006968

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.