Evidence map›Paper›PMID 24845359›Full record

ArticleJournal of the American Society for Mass Spectrometry2014

Large-scale collision cross-section profiling on a traveling wave ion mobility mass spectrometer.

Christopher B Lietz, Qing Yu, Lingjun Li

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. The Potential for Ion Mobility in Pharmaceutical and Clinical Analyses.Advances in experimental medicine and biology · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Identification, Quantitation, and Imaging of the Crustacean Peptidome.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Advanced Multidimensional Separations in Mass Spectrometry: Navigating the Big Data Deluge.Annual review of analytical chemistry (Palo Alto, Calif.) · 2016
    Article
  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

3 authors.

Christopher B LietzDepartment of Chemistry, University of Wisconsin, Madison, WI, 53705, USA.
Qing Yu
Lingjun Li

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Mass Spectrometric Studies of Neuropeptides in FeedingR56DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$216k
NIDDK NIH HHS 1R01DK071801NIDDK NIH HHS 1R56DK071801NIDDK NIH HHS R01 DK071801NIDDK NIH HHS R56 DK071801NIGMS NIH HHS T32 GM008505NIGMS NIH HHS T32-GM008505
6 · The paper itself

Abstract

Ion mobility (IM) is a gas-phase electrophoretic method that separates ions according to charge and ion-neutral collision cross-section (CCS). Herein, we attempt to apply a traveling wave (TW) IM polyalanine calibration method to shotgun proteomics and create a large peptide CCS database. Mass spectrometry methods that utilize IM, such as HDMS(E), often use high transmission voltages for sensitive analysis. However, polyalanine calibration has only been demonstrated with low voltage transmission used to prevent gas-phase activation. If polyalanine ions change conformation under higher transmission voltages used for HDMS(E), the calibration may no longer be valid. Thus, we aimed to characterize the accuracy of calibration and CCS measurement under high transmission voltages on a TW IM instrument using the polyalanine calibration method and found that the additional error was not significant. We also evaluated the potential error introduced by liquid chromatography (LC)-HDMS(E) analysis, and found it to be insignificant as well, validating the calibration method. Finally, we demonstrated the utility of building a large-population peptide CCS database by investigating the effects of terminal lysine position, via LysC or LysN digestion, on the formation of two structural sub-families formed by triply charged ions.

Indexed as

Amino Acid SequenceBradykininCalibrationGasesIonsMass SpectrometryMolecular Sequence DataPeptide FragmentsPeptidesProteomicsSaccharomyces cerevisiae ProteinsBradykininGasesIonsPeptide FragmentsPeptidespolyalanineSaccharomyces cerevisiae Proteins

Identifiers

PMID24845359
PMCPMC4224635

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.