Evidence map›Paper›PMID 31350722›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.

Frederik Lermyte, James Everett, Yuko P Y Lam, Christopher A Wootton, Jake Brooks, Mark P Barrow, Neil D Telling, Peter J Sadler, Peter B O'Connor, Joanna F Collingwood

Open 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. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  19. Review
  20. Review
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

10 authors at 2 institutions in 1 country.

Frederik LermyteSchool of Engineering, University of Warwick, Coventry, CV4 7AL, UK. f.lermyte@warwick.ac.uk.ORCID http://orcid.org/0000-0001-7371-4475
James EverettSchool of Engineering, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-1864-9700
Yuko P Y LamDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0001-5486-091X
Christopher A WoottonDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-3647-2611
Jake BrooksSchool of Engineering, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-4035-0369
Mark P BarrowDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-6474-5357
Neil D TellingInstitute for Science and Technology in Medicine, Keele University, Stoke-on-Trent, Staffordshire, ST4 7QB, UK.ORCID http://orcid.org/0000-0002-2683-5546
Peter J SadlerDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0001-9160-1941
Peter B O'ConnorDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-6588-6274
Joanna F CollingwoodSchool of Engineering, University of Warwick, Coventry, CV4 7AL, UK.ORCID http://orcid.org/0000-0002-8423-4183
University of Warwick · GBKeele University · GB

Funding

Engineering and Physical Sciences Research Council EP/N033140/1Engineering and Physical Sciences Research Council EP/N033191/1
6 · The paper itself

Abstract

Native top-down mass spectrometry is a fast, robust biophysical technique that can provide molecular-scale information on the interaction between proteins or peptides and ligands, including metal cations. Here we have analyzed complexes of the full-length amyloid β (1-42) monomer with a range of (patho)physiologically relevant metal cations using native Fourier transform ion cyclotron resonance mass spectrometry and three different fragmentation methods-collision-induced dissociation, electron capture dissociation, and infrared multiphoton dissociation-all yielding consistent results. Amyloid β is of particular interest as its oligomerization and aggregation are major events in the etiology of Alzheimer's disease, and it is known that interactions between the peptide and bioavailable metal cations have the potential to significantly damage neurons. Those metals which exhibited the strongest binding to the peptide (Cu

Indexed as

Amyloid beta-PeptidesMetalsHumansMass SpectrometryProtein BindingSpectroscopy, Fourier Transform InfraredAmyloid beta-PeptidesMetalsAmyloid betaCollision-induced dissociationElectron capture dissociationInfrared multiphoton dissociationMass spectrometryNative mass spectrometryNative top-downPeptide-metal complexRadical-directed dissociation

Identifiers

PMID31350722
PMCPMC6805827
OpenAlexW2964576316

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.