Evidence map›Paper›PMID 29949061›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

Initial Protein Unfolding Events in Ubiquitin, Cytochrome c and Myoglobin Are Revealed with the Use of 213 nm UVPD Coupled to IM-MS.

Alina Theisen, Rachelle Black, Davide Corinti, Jeffery M Brown, Bruno Bellina, Perdita E Barran

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2019. 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-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, 50 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. The Role of Nanobubbles in Protein Unfolding during Electrothermal Supercharging.Journal of the American Society for Mass Spectrometry · 2025
    Article
  4. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  5. Article
  6. Review
  7. FTflow: An Open-Source Python GUI for FT-IM-MS Experiments.Journal of the American Society for Mass Spectrometry · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Synchronized Stepped Frequency Modulation for Multiplexed Ion Mobility Measurements.Journal of the American Society for Mass Spectrometry · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Alina TheisenMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Rachelle BlackMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Davide CorintiDipartimento di Chimica e Tecnologie del Farmaco, Università di Roma "La Sapienza", 00185, Rome, Italy.
Jeffery M BrownWaters Corporation, Stamford Avenue, Altrincham Road, Wilmslow, SK9 4AX, UK.
Bruno BellinaMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Perdita E BarranMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology and Photon Science Institute, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK. perdita.barran@manchester.ac.uk.
University of Manchester · GBSapienza University of Rome · ITWaters (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L002655/1Biotechnology and Biological Sciences Research Council BB/L016486/1Biotechnology and Biological Sciences Research Council BB/M017702/1
6 · The paper itself

Abstract

The initial stages of protein unfolding may reflect the stability of the entire fold and can also reveal which parts of a protein can be perturbed, without restructuring the rest. In this work, we couple UVPD with activated ion mobility mass spectrometry to measure how three model proteins start to unfold. Ubiquitin, cytochrome c and myoglobin ions produced via nESI from salty solutions are subjected to UV irradiation pre-mobility separation; experiments are conducted with a range of source conditions which alter the conformation of the precursor ion as shown by the drift time profiles. For all three proteins, the compact structures result in less fragmentation than more extended structures which emerge following progressive in-source activation. Cleavage sites are found to differ between conformational ensembles, for example, for the dominant charge state of cytochrome c [M + 7H]

Indexed as

Protein UnfoldingAnimalsCattleCytochromes cIon Mobility SpectrometryMyoglobinUbiquitinUltraviolet RaysCytochromes cMyoglobinUbiquitinCytochrome cIM-MSMyoglobinUbiquitinUVPD

Identifiers

PMID29949061
PMCPMC6318241
OpenAlexW2805030819

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.