Evidence map›Paper›PMID 19140678›Full record

ArticleJournal of proteome research2009

Evaluation of the variation in sample preparation for comparative proteomics using stable isotope labeling by amino acids in cell culture.

Guoan Zhang, David Fenyö, Thomas A Neubert

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-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

17 citing papers in PubMed, 51 citations in OpenAlex.

  1. Mass Spectrometry for Proteomics-Based Investigation.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Profound changes in cerebrospinal fluid proteome and metabolic profile are associated with congenital hydrocephalus.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Protein quantitation using mass spectrometry.Methods in molecular biology (Clifton, N.J.) · 2010
    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 at 2 institutions in 1 country.

Guoan ZhangKimmel Center for Biology and Medicine at the Skirball Institute and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA.
David Fenyö
Thomas A Neubert
Rockefeller University · USNew York University · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Protein Mass Spectrometry Core Facility for NeuroscienceP30NS050276 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NEUBERT, THOMAS A · 2005 to 2015
$7.9M
Q-TOF Mass SpectrometerS10RR017990 · NCRR · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NEUBERT, THOMAS A · 2003 to 2003
$500k
NCI NIH HHS 2P30 CA 016087NCI NIH HHS P30 CA016087NCRR NIH HHS S10 RR017990NINDS NIH HHS P30 NS050276
6 · The paper itself

Abstract

In comparative proteomic studies, it is important to know the variability associated with sample preparation. In this study, we report the strategy of using SILAC (stable isotope labeling by amino acids in cell culture) to evaluate the effect of the variation in sample preparation for quantitative proteomics. Variability can be measured when equal amounts of light and heavy SILAC samples undergo the same sample preparation procedures in parallel, and the two samples are mixed for relative protein quantitation by mass spectrometry. The high quantitative accuracy of SILAC allows for characterization of small variations. First, the reproducibility of immunoprecipitation (IP) and in-gel digestion was evaluated, and the impact of replicate number on quantitative accuracy was characterized. Second, we evaluated the overall variation in a comparative workflow involving three sequential sample preparation steps: IP, SDS-PAGE fractionation, and in-gel digestion. The evaluation of individual sample preparation steps was very valuable for experimental design: the optimal number of replicates for each step could be readily determined and the overall variation of the workflow could be predicted from the variation of the individual steps involved. By using informed experimental design, we demonstrated that the error associated with multiple steps of sample preparation in a comparative experiment can be limited to a reasonably low level.

Indexed as

Reproducibility of ResultsAmino AcidsAnimalsCell Line, TumorChromatography, LiquidEvaluation Studies as TopicImmunoprecipitationIsotope LabelingMiceProteomeRatsTandem Mass SpectrometryAmino AcidsProteome

Identifiers

PMID19140678
PMCPMC2693445
OpenAlexW2159938903

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.