Evidence map›Paper›PMID 25261218›Full record

ArticleJournal of the American Society for Mass Spectrometry2014

Comparison of data acquisition strategies on quadrupole ion trap instrumentation for shotgun proteomics.

Jesse D Canterbury, Gennifer E Merrihew, Michael J MacCoss, David R Goodlett, Scott A Shaffer

Open access · greenAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteomic Technology.Advances in experimental medicine and biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Improving Precursor Selectivity in Data-Independent Acquisition Using Overlapping Windows.Journal of the American Society for Mass Spectrometry · 2019
    Article
  15. Article
  16. Maillard Proteomics: Opening New Pages.International journal of molecular sciences · 2017
    Review
  17. Article
  18. Article
  19. Review
  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

5 authors at 4 institutions in 1 country.

Jesse D CanterburyDepartment of Genome Sciences, University of Washington, Seattle, WA, 98195, USA.
Gennifer E Merrihew
Michael J MacCoss
David R Goodlett
Scott A Shaffer
University of Washington · USThermo Fisher Scientific (United States) · USUniversity of Maryland, Baltimore · USUniversity of Massachusetts Chan Medical School · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI SALVESEN, GUY S. · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Analysis of Protein Dynamics in C. elegans by mLC/MS/MSR01DK069386 · NIDDK · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2006 to 2013
$2.3M
NCRR NIH HHS P41 RR011823NIDDK NIH HHS R01 DK069386NIGMS NIH HHS P41 GM103533
6 · The paper itself

Abstract

The most common data collection in shotgun proteomics is via data-dependent acquisition (DDA), a process driven by an automated instrument control routine that directs MS/MS acquisition from the highest abundant signals to the lowest. An alternative to DDA is data-independent acquisition (DIA), a process in which a specified range in m/z is fragmented without regard to prioritization of a precursor ion or its relative abundance in the mass spectrum, thus potentially offering a more comprehensive analysis of peptides than DDA. In this work, we evaluate both DDA and DIA on three different linear ion trap instruments: an LTQ, an LTQ modified with an electrodynamic ion funnel, and an LTQ Velos. These instruments represent both older (LTQ) and newer (LTQ Velos) ion trap designs (i.e., linear versus dual ion traps, respectively), and allow direct comparison of peptide identifications using both DDA and DIA analysis. Further, as the LTQ Velos has an enhanced "S-lens" ion guide to improve ion flux, we found it logical to determine if the former LTQ model could be leveraged by improving sensitivity by modifying with an electrodynamic ion guide of significantly different design to the S-lens. We find that the ion funnel enabled LTQ identifies more proteins in the insoluble fraction of a yeast lysate than the other two instruments in DIA mode, whereas the faster scanning LTQ Velos performs better in DDA mode. We explore reasons for these results, including differences in scan speed, source ion optics, and linear ion trap design.

Indexed as

Databases, ProteinFungal ProteinsPeptide MappingProteomicsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryYeastsFungal Proteins

Identifiers

PMID25261218
PMCPMC4417682
OpenAlexW1966552971

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.