Evidence map›Paper›PMID 28432653›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Analyzing Glycopeptide Isomers by Combining Differential Mobility Spectrometry with Electron- and Collision-Based Tandem Mass Spectrometry.

J Larry Campbell, Takashi Baba, Chang Liu, Catherine S Lane, J C Yves Le Blanc, James W Hager

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Effective discrimination of gas-phase peptide conformers using TIMS-ECD-ToF MS/MS.Analytical methods : advancing methods and applications · 2021
    Article
  7. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Isomer Information from Ion Mobility Separation of High-Mannose Glycan Fragments.Journal of the American Society for Mass Spectrometry · 2018
    Article
  13. Article
  14. Review
  15. 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

6 authors.

J Larry CampbellSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada. larry.campbell@sciex.com.
Takashi BabaSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada.
Chang LiuSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada.
Catherine S LaneSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada.
J C Yves Le BlancSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada.
James W HagerSCIEX, 71 Four Valley Drive, Concord, ON, L4K 4V8, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Differential mobility spectrometry (DMS) has been employed to separate isomeric species in several studies. Under the right conditions, factors such as separation voltage, temperature, the presence of chemical modifiers, and residence time can combine to provide unique signal channels for isomeric species. In this study, we examined a set of glycopeptide isomers, MUC5AC-3 and MUC5AC-13, which bear an N-acetyl-galactosamine (GalNAc) group on either threonine-3 or threonine-13. When analyzed as a mixture, the resulting MS and MS/MS spectra yield fragmentation patterns that cannot discern these convolved species. However, when DMS is implemented during the analysis of this mixture, two features emerge in the DMS ionogram representing the two glycopeptide isomers. In addition, by locking in DMS parameters at each feature, we could observe several low intensity CID fragments that contain the GalNAc functionality-specific amino acid residues - identifying the DMS separation of each isomer without standards. Besides conventional CID MS/MS, we also implemented electron-capture dissociation (ECD) after DMS separation, and clearly resolved both isomers with this fragmentation method, as well. The electron energy used in these ECD experiments could be tuned to obtain maximum sequence coverage for these glycopeptides; this was critical as these ions were present as doubly protonated species, which are much more difficult to fragment efficiently via electron-transfer dissociation (ETD). Overall, the combination of DMS with electron- or collision-based MS/MS methods provided enhanced separation and sequence coverage for these glycopeptide isomers. Graphical Abstract ᅟ.

Indexed as

Collision-induced dissociationDifferential mobility spectrometryElectron-capture dissociationGlycopeptidesIsomer separation

Identifiers

PMID28432653
OpenAlexW2607295382

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.