Evidence map›Paper›PMID 21726088›Full record

ArticleJournal of proteome research2011

Rapid verification of candidate serological biomarkers using gel-based, label-free multiple reaction monitoring.

Hsin-Yao Tang, Lynn A Beer, Kurt T Barnhart, David W Speicher

Abstract read
In one paragraph

Article in Journal of proteome research, 2011. 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
–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

17 citing papers in PubMed.

  1. Trial
  2. Trial
  3. Article
  4. Proteomic Analysis of the Early Development of theMolecules (Basel, Switzerland) · 2020
    Article
  5. Article
  6. LC-SRM-Based Targeted Quantification of Urinary Protein Biomarkers.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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.

Hsin-Yao TangCenter for Systems and Computational Biology and Molecular and Cellular Oncogenesis Program, The Wistar Institute, Philadelphia, Pennsylvania, United States.
Lynn A Beer
Kurt T Barnhart
David W Speicher

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Aaron Robert Goldman · 1985 to 2026
$75.9M
RISK FACTORS AS PREDICTORS OF ECTOPIC PREGNANCYR01HD036455 · NICHD · UNIVERSITY OF PENNSYLVANIA · PI BARNHART, KURT T · 1999 to 2010
$4.1M
Identification of Ovarian Cancer Plasma BiomarkersR01CA131582 · NCI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 2009 to 2018
$4.1M
Discovery and validation of novel serological biomarkers of colon cancerR01CA120393 · NCI · WISTAR INSTITUTE · PI SPEICHER, DAVID W. · 2006 to 2010
$1.9M
Midcareer investigator award in patient oriented researchK24HD060687 · NICHD · UNIVERSITY OF PENNSYLVANIA · PI BARNHART, KURT T · 2009 to 2014
$956k
NCI NIH HHS CA10815NCI NIH HHS CA120393NCI NIH HHS CA131582NCI NIH HHS P30 CA010815NCI NIH HHS R01 CA120393NCI NIH HHS R01 CA131582NICHD NIH HHS HD036455NICHD NIH HHS K24 HD060687NICHD NIH HHS R01 HD036455
6 · The paper itself

Abstract

Stable isotope dilution-multiple reaction monitoring-mass spectrometry (SID-MRM-MS) has emerged as a promising platform for verification of serological candidate biomarkers. However, cost and time needed to synthesize and evaluate stable isotope peptides, optimize spike-in assays, and generate standard curves quickly becomes unattractive when testing many candidate biomarkers. In this study, we demonstrate that label-free multiplexed MRM-MS coupled with major protein depletion and 1D gel separation is a time-efficient, cost-effective initial biomarker verification strategy requiring less than 100 μL of serum. Furthermore, SDS gel fractionation can resolve different molecular weight forms of targeted proteins with potential diagnostic value. Because fractionation is at the protein level, consistency of peptide quantitation profiles across fractions permits rapid detection of quantitation problems for specific peptides from a given protein. Despite the lack of internal standards, the entire workflow can be highly reproducible, and long-term reproducibility of relative protein abundance can be obtained using different mass spectrometers and LC methods with external reference standards. Quantitation down to ~200 pg/mL could be achieved using this workflow. Hence, the label-free GeLC-MRM workflow enables rapid, sensitive, and economical initial screening of large numbers of candidate biomarkers prior to setting up SID-MRM assays or immunoassays for the most promising candidate biomarkers.

Indexed as

Amino Acid SequenceBiomarkersBlood ProteinsCathepsin DChromatography, High Pressure LiquidHumansImmunoassayMass SpectrometryMolecular Sequence DataPeptide FragmentsProteomicsReproducibility of ResultsSensitivity and SpecificityBiomarkersBlood ProteinsCathepsin DCTSD protein, humanPeptide Fragments

Identifiers

PMID21726088
PMCPMC3166403

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.