Evidence map›Paper›PMID 23642296›Full record

ArticleJournal of proteome research2013

Evaluation and optimization of mass spectrometric settings during data-dependent acquisition mode: focus on LTQ-Orbitrap mass analyzers.

Anastasia Kalli, Geoffrey T Smith, Michael J Sweredoski, Sonja Hess

Abstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. An Enzymatic and Proteomic Analysis ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  6. A planar quadrupole device for transmitting and trapping ions in high vacuum.Rapid communications in mass spectrometry : RCM · 2023
    Article
  7. Article
  8. Article
  9. Establishing Quality Control Procedures for Large-Scale Plasma Proteomics Analyses.Journal of the American Society for Mass Spectrometry · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Biological Applications for LC-MS-Based Proteomics.Advances in experimental medicine and biology · 2021
    Article
  20. Review
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.

Anastasia KalliProteome Exploration Laboratory, Division of Biology, Beckman Institute, California Institute of Technology, Pasadena, California 91125, USA.
Geoffrey T Smith
Michael J Sweredoski
Sonja Hess

Funding

Purchase of a Liquid Chromatograph-Orbitrap VELOS mass spectrometerS10RR029594 · NCRR · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HESS, SONJA · 2011 to 2011
$600k
NCRR NIH HHS RR10565784NCRR NIH HHS S10 RR029594
6 · The paper itself

Abstract

Mass-spectrometry-based proteomics has evolved as the preferred method for the analysis of complex proteomes. Undoubtedly, recent advances in mass spectrometry instrumentation have greatly enhanced proteomic analysis. A popular instrument platform in proteomics research is the LTQ-Orbitrap mass analyzer. In this tutorial, we discuss the significance of evaluating and optimizing mass spectrometric settings on the LTQ-Orbitrap during CID data-dependent acquisition (DDA) mode to improve protein and peptide identification rates. We focus on those MS and MS/MS parameters that have been systematically examined and evaluated by several researchers and are commonly used during DDA. More specifically, we discuss the effect of mass resolving power, preview mode for FTMS scan, monoisotopic precursor selection, signal threshold for triggering MS/MS events, number of microscans per MS/MS scan, number of MS/MS events, automatic gain control target value (ion population) for MS and MS/MS, maximum ion injection time for MS/MS, rapid and normal scan rate, and prediction of ion injection time. We furthermore present data from the latest generation LTQ-Orbitrap system, the Orbitrap Elite, along with recommended MS and MS/MS parameters. The Orbitrap Elite outperforms the Orbitrap Classic in terms of scan speed, sensitivity, dynamic range, and resolving power and results in higher identification rates. Several of the optimized MS parameters determined on the LTQ-Orbitrap Classic and XL were easily transferable to the Orbitrap Elite, whereas others needed to be reevaluated. Finally, the Q Exactive and HCD are briefly discussed, as well as sample preparation, LC-optimization, and bioinformatics analysis. We hope this tutorial will serve as guidance for researchers new to the field of proteomics and assist in achieving optimal results.

Indexed as

Computational BiologyHumansPeptidesProteinsProteomicsTandem Mass SpectrometryPeptidesProteins

Identifiers

PMID23642296
PMCPMC3748959

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Registered trials

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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.