Evidence map›Paper›PMID 18511480›Full record

ArticleMolecular & cellular proteomics : MCP2008

Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer.

Marcus Bantscheff, Markus Boesche, Dirk Eberhard, Toby Matthieson, Gavain Sweetman, Bernhard Kuster

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
13.5field-weighted citation impact, top 1% 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

91 citing papers in PubMed, 235 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Quantitative Proteomics Using Isobaric Labeling: A Practical Guide.Genomics, proteomics & bioinformatics · 2021
    Review
  7. Article
  8. The rise of single-cell proteomics.Analytical science advances · 2021
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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  20. Article

31 more citing papers are in PubMed but not listed here.

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.

Marcus BantscheffCellzome AG, Meyerhofstrasse 1, 69117 Heidelberg, Germany. marcus.bantscheff@cellzome.com
Markus Boesche
Dirk Eberhard
Toby Matthieson
Gavain Sweetman
Bernhard Kuster

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Isobaric stable isotope tagging reagents such as tandem mass tags or isobaric tags for relative and absolute quantification enable multiplexed quantification of peptides via reporter ion signals in the low mass range of tandem mass spectra. Until recently, the poor recovery of low mass fragments observed in tandem mass spectra acquired on ion trap mass spectrometers precluded the use of these reagents on this widely available instrument platform. The Pulsed Q Dissociation (PQD) technique allows negotiating this limitation but suffers from poor fragmentation efficiency, which has raised doubts in the community as to its practical utility. Here we show that by carefully optimizing instrument parameters such as collision energy, activation Q, delay time, ion isolation width, number of microscans, and number of trapped ions, low m/z fragment ion intensities can be generated that enable accurate peptide quantification at the 100 amol level. Side by side comparison of PQD on an LTQ Orbitrap with CID on a five-year old Q-Tof Ultima using complex protein digests shows that whereas precision of quantification of 10-15% can be achieved by both approaches, PQD quantifies twice as many proteins. PQD on an LTQ Orbitrap also outperforms "higher energy collision induced dissociation" on the same instrument using the recently introduced octapole collision cell in terms of lower limit of quantification. Finally, we demonstrate the significant analytical potential of iTRAQ quantification using PQD on an LTQ Orbitrap by quantitatively measuring the kinase interaction profile of the small molecule drug imatinib in K-562 cells. This article gives practical guidance for the implementation of PQD, discusses its merits, and for the first time, compares its performance to higher energy collision-induced dissociation.

Indexed as

BenzamidesCell Line, TumorHumansImatinib MesylateIsotope LabelingJurkat CellsPeptidesPiperazinesProtein Kinase InhibitorsProtein KinasesProteomicsPyrimidinesSensitivity and SpecificityTandem Mass SpectrometryBenzamidesImatinib MesylatePeptidesPiperazinesProtein Kinase InhibitorsProtein KinasesPyrimidines

Identifiers

PMID18511480
PMCPMC2556025
OpenAlexW2139208986

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.