Evidence map›Paper›PMID 29542338›Full record

ArticleExpert review of proteomics2018

Affinity enrichment for mass spectrometry: improving the yield of low abundance biomarkers.

Brianna Kim, Robyn Araujo, Marissa Howard, Ruben Magni, Lance A Liotta, Alessandra Luchini

Abstract read
In one paragraph

Article in Expert review of proteomics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–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

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Characterization ofMicroorganisms · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Review
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  13. Article
  14. Microfluidics for Peptidomics, Proteomics, and Cell Analysis.Nanomaterials (Basel, Switzerland) · 2021
    Review
  15. Review
  16. Observational
  17. Potential Inhibitory Effect ofAntibiotics (Basel, Switzerland) · 2020
    Article
  18. Article
  19. 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

6 authors.

Brianna Kima Ceres Nanosciences , Manassas , VA , USA.
Robyn Araujob School of Mathematical Sciences , Queensland University of Technology , Brisbane , Australia.
Marissa Howardc Center for Applied Proteomics and Molecular Medicine , George Mason University , Manassas , VA , USA.
Ruben Magnic Center for Applied Proteomics and Molecular Medicine , George Mason University , Manassas , VA , USA.
Lance A Liottac Center for Applied Proteomics and Molecular Medicine , George Mason University , Manassas , VA , USA.
Alessandra Luchinic Center for Applied Proteomics and Molecular Medicine , George Mason University , Manassas , VA , USA.

Funding

Protein painting identifies therapeutic targets at protein-protein interfacesR33CA206937 · NCI · GEORGE MASON UNIVERSITY · PI LIOTTA, LANCE ALLEN · 2016 to 2018
$1.2M
Nanotrap technology for one step preservation and amplification of cancer biomarkR33CA173359 · NCI · GEORGE MASON UNIVERSITY · PI LIOTTA, LANCE ALLEN · 2012 to 2014
$1.1M
Nanotechnology for One Step Concentration and Preservation of Labile Biomarkers iR21CA137706 · NCI · GEORGE MASON UNIVERSITY · PI LIOTTA, LANCE ALLEN · 2009 to 2010
$530k
Protein Painting reveals hidden protein-protein interaction domainsR21CA177535 · NCI · GEORGE MASON UNIVERSITY · PI LIOTTA, LANCE ALLEN · 2013 to 2014
$482k
Bridging adult to pediatric markers of tuberculosis disease severityR21HD097472 · NICHD · GEORGE MASON UNIVERSITY · PI LIOTTA, LANCE ALLEN · 2019 to 2020
$426k
NCI NIH HHS R21 CA137706NCI NIH HHS R21 CA177535NCI NIH HHS R33 CA173359NCI NIH HHS R33 CA206937NICHD NIH HHS R21 HD097472
6 · The paper itself

Abstract

introductionMass spectrometry (MS) is the premier tool for discovering novel disease-associated protein biomarkers. Unfortunately, when applied to complex body fluid samples, MS has poor sensitivity for the detection of low abundance biomarkers (≪10 ng/mL), derived directly from the diseased tissue cells or pathogens. Areas covered: Herein we discuss the strengths and drawbacks of technologies used to concentrate low abundance analytes in body fluids, with the aim to improve the effective sensitivity for MS discovery. Solvent removal by dry-down or dialysis, and immune-depletion of high abundance serum or plasma proteins, is shown to have disadvantages compared to positive selection of the candidate biomarkers by affinity enrichment. A theoretical analysis of affinity enrichment reveals that the yield for low abundance biomarkers is a direct function of the binding affinity (Association/Dissociation rates) used for biomarker capture. In addition, a high affinity capture pre processing step can effectively dissociate the candidate biomarker from partitioning with high abundance proteins such as albumin. Expert commentary: Properly designed high affinity capture materials can enrich the yield of low abundance (0.1-10 picograms/mL) candidate biomarkers for MS detection. Affinity capture and concentration, as an upfront step in sample preparation for MS, combined with MS advances in software and hardware that improve the resolution of the chromatographic separation can yield a transformative new class of low abundance biomarkers predicting disease risk or disease latency.

Indexed as

BiomarkersCommunicable DiseasesHumansLyme DiseaseMass SpectrometryNanotechnologyBiomarkersaffinity capturebiomarkercancerinfectious diseaselow abundancelyme diseaseMass spectrometrynanotechnology

Identifiers

PMID29542338
PMCPMC6081742

What OpenQuestion holds

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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.