Evidence map›Paper›PMID 23019139›Full record

ReviewProteomics2013

A comparative analysis of computational approaches to relative protein quantification using peptide peak intensities in label-free LC-MS proteomics experiments.

Melissa M Matzke, Joseph N Brown, Marina A Gritsenko, Thomas O Metz, Joel G Pounds, Karin D Rodland, Anil K Shukla, Richard D Smith, Katrina M Waters, Jason E McDermott and 1 more

Open access · greenAbstract readComparative StudyReview
In one paragraph

Review in Proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Proteomics for Microalgae Extracts by High-Resolution Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Itaconic acid production is regulated by LaeA inMetabolic engineering communications · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Phosphoproteomic response of cardiac endothelial cells to ischemia and ultrasound.Biochimica et biophysica acta. Proteins and proteomics · 2021
    Article
  18. 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

11 authors at 1 institution in 1 country.

Melissa M MatzkePacific Northwest National Laboratory, Richland, WA 99352, USA.
Joseph N Brown
Marina A Gritsenko
Thomas O Metz
Joel G Pounds
Karin D Rodland
Anil K Shukla
Richard D Smith
Katrina M Waters
Jason E McDermott
Bobbie-Jo Webb-Robertson
Pacific Northwest National Laboratory · US

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
MOUSE BIOMARKER DISCOVERY AND VALIDATION STUDIESU54ES016015 · NIEHS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI POUNDS, JOEL G · 2007 to 2010
$5.8M
Adv.Proteomics & Metabolomics:Type 2 Diabet & Pre-DiabetR33DK071283 · NIDDK · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2007 to 2009
$1.6M
Adv.Proteomics &Metabolomics:Type 2 Diabet &Pre-DiabetR21DK071283 · NIDDK · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2005 to 2006
$656k
NCRR NIH HHS 5P41RR018522-10NCRR NIH HHS P41 RR018522NIDDK NIH HHS DK071283NIDDK NIH HHS R21 DK071283NIDDK NIH HHS R33 DK071283NIEHS NIH HHS U54 ES016015NIGMS NIH HHS (8 P41 GM103493-10NIGMS NIH HHS P41 GM103493PHS HHS U54-016015
6 · The paper itself

Abstract

Liquid chromatography coupled with mass spectrometry (LC-MS) is widely used to identify and quantify peptides in complex biological samples. In particular, label-free shotgun proteomics is highly effective for the identification of peptides and subsequently obtaining a global protein profile of a sample. As a result, this approach is widely used for discovery studies. Typically, the objective of these discovery studies is to identify proteins that are affected by some condition of interest (e.g. disease, exposure). However, for complex biological samples, label-free LC-MS proteomics experiments measure peptides and do not directly yield protein quantities. Thus, protein quantification must be inferred from one or more measured peptides. In recent years, many computational approaches to relative protein quantification of label-free LC-MS data have been published. In this review, we examine the most commonly employed quantification approaches to relative protein abundance from peak intensity values, evaluate their individual merits, and discuss challenges in the use of the various computational approaches.

Indexed as

Chromatography, LiquidData Interpretation, StatisticalHumansLinear ModelsMass SpectrometryProteomeProteomicsSoftwareProteome

Identifiers

PMID23019139
PMCPMC3775642
OpenAlexW2033884357

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.