Evidence map›Paper›PMID 21692493›Full record

ArticleAnalytical chemistry2011

Ultrasensitive identification of localization variants of modified peptides using ion mobility spectrometry.

Yehia M Ibrahim, Alexandre A Shvartsburg, Richard D Smith, Mikhail E Belov

Abstract readEvaluation Study
In one paragraph

Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of Mobility-ResolvedAnalytical chemistry · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Spatial Ion Peak Compression and its Utility in Ion Mobility Spectrometry.Journal of the American Society for Mass Spectrometry · 2016
    Article
  13. Article
  14. Review
  15. Automated deconvolution of overlapped ion mobility profiles.Journal of the American Society for Mass Spectrometry · 2014
    Article
  16. Article
  17. Article
  18. Review
  19. 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

4 authors at 1 institution in 1 country.

Yehia M IbrahimBiological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.
Alexandre A Shvartsburg
Richard D Smith
Mikhail E Belov
Pacific Northwest National Laboratory · US

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
NCRR NIH HHS P41 RR018522NCRR NIH HHS RR18522
6 · The paper itself

Abstract

Localization of the modification sites on peptides is challenging, particularly when multiple modifications or mixtures of localization isomers (variants) are involved. Such variants commonly coelute in liquid chromatography and may be undistinguishable in tandem mass spectrometry (MS/MS) for lack of unique fragments. Here, we have resolved the variants of singly and doubly phosphorylated peptides employing drift tube ion mobility spectrometry (IMS) coupled to time-of-flight mass spectrometry. Even with a moderate IMS resolving power of ∼80-100, substantial separation was achieved for both 2+ and 3+ ions normally generated by electrospray ionization, including for the variants indistinguishable by MS/MS. Variants often exhibit a distribution of 3-D conformers, which can be adjusted for optimum IMS separation by prior field heating of ions in a funnel trap. The peak assignments were confirmed using MS/MS after IMS separation, but known species could be identified using just the ion mobility "tag". Avoiding the MS/MS step lowers the detection limit of localization variants to <100 amol, an order of magnitude better than that provided by electron transfer dissociation in an Orbitrap MS.

Indexed as

Amino Acid SequenceChromatography, LiquidEquipment DesignIsomerismMass SpectrometryMolecular ConformationMolecular Sequence DataPeptidesSensitivity and SpecificityPeptides

Identifiers

PMID21692493
PMCPMC3136632
OpenAlexW2045319872

What OpenQuestion holds

Textmetadata
LicenceTDM
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.