Evidence map›Paper›PMID 24651194›Full record

ReviewNature chemistry2014

The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics.

Francesco Lanucara, Stephen W Holman, Christopher J Gray, Claire E Eyers

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 289 papers.

0numbers the graph read from it
0cells of the map it votes in
289citing 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

289 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Direct Comparison of MRM-MS and PRM-MS Methods for Quantitative Ganglioside Analysis.Journal of the American Society for Mass Spectrometry · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Application of Ion Mobility Mass Spectrometry in Lipidomics.Advances in experimental medicine and biology · 2026
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

229 more citing papers are in PubMed but not listed here.

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

4 authors.

Francesco Lanucara1] Protein Function Group, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK [2] Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Stephen W Holman1] Protein Function Group, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK [2] Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Christopher J GrayMichael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Claire E Eyers1] Protein Function Group, Department of Biochemistry, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK [2] Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/F00561X/1Biotechnology and Biological Sciences Research Council BB/G009058/1Biotechnology and Biological Sciences Research Council BB/H007113/1
6 · The paper itself

Abstract

Mass spectrometry is a vital tool for molecular characterization, and the allied technique of ion mobility is enhancing many areas of (bio)chemical analysis. Strong synergy arises between these two techniques because of their ability to ascertain complementary information about gas-phase ions. Ion mobility separates ions (from small molecules up to megadalton protein complexes) based on their differential mobility through a buffer gas. Ion mobility-mass spectrometry (IM-MS) can thus act as a tool to separate complex mixtures, to resolve ions that may be indistinguishable by mass spectrometry alone, or to determine structural information (for example rotationally averaged cross-sectional area), complementary to more traditional structural approaches. Finally, IM-MS can be used to gain insights into the conformational dynamics of a system, offering a unique means of characterizing flexibility and folding mechanisms. This Review critically describes how IM-MS has been used to enhance various areas of chemical and biophysical analysis.

Indexed as

BiophysicsIonsMass SpectrometryMolecular ConformationIons

Identifiers

PMID24651194

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.