Evidence map›Paper›PMID 19955079›Full record

ArticleMolecular & cellular proteomics : MCP2010

Sensitive plasma protein analysis by microparticle-based proximity ligation assays.

Spyros Darmanis, Rachel Yuan Nong, Maria Hammond, Jijuan Gu, Anders Alderborn, Johan Vänelid, Agneta Siegbahn, Sigrun Gustafsdottir, Olle Ericsson, Ulf Landegren and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
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  10. The Intriguing Landscape of Single-Cell Protein Analysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  11. Emerging Advances of Detection Strategies for Tumor-Derived Exosomes.International journal of molecular sciences · 2022
    Review
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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 2 institutions in 1 country.

Spyros DarmanisDepartment of Genetics and Pathology, Uppsala University, Uppsala, Sweden.
Rachel Yuan Nong
Maria Hammond
Jijuan Gu
Anders Alderborn
Johan Vänelid
Agneta Siegbahn
Sigrun Gustafsdottir
Olle Ericsson
Ulf Landegren
Masood Kamali-Moghaddam
Uppsala University · SEUppsala University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Detection of proteins released in the bloodstream from tissues damaged by disease can promote early detection of pathological conditions, differential diagnostics, and follow-up of therapy. Despite these prospects and a plethora of candidate biomarkers, efforts in recent years to establish new protein diagnostic assays have met with limited success. One important limiting factor has been the challenge of detecting proteins present at trace levels in complex bodily fluids. To achieve robust, sensitive, and specific detection, we have developed a microparticle-based solid-phase proximity ligation assay, dependent on simultaneous recognition of target proteins by three antibody molecules for added specificity. After capture on a microparticle, solid-phase pairs of proximity probes are added followed by washes, enabling detection and identification of rare protein molecules in blood while consuming small amounts of sample. We demonstrate that single polyclonal antibody preparations raised against target proteins of interest can be readily used to establish assays where detection depends on target recognition by three individual antibody molecules, recognizing separate epitopes. The assay was compared with state-of-the-art sandwich ELISAs for detection of vascular endothelial growth factor, interleukin-8 and interleukin-6, and it was found to be superior both with regard to dynamic range and minimal numbers of molecules detected. Furthermore, the assays exhibited excellent performance in undiluted plasma and serum as well as in whole blood, producing comparable results for nine different antigens. We thus show that solid-phase proximity ligation assay is suitable for validation of a variety of protein biomarkers over broad dynamic ranges in clinical samples.

Indexed as

MicrospheresBlood ProteinsEnzyme-Linked Immunosorbent AssayGrowth Differentiation Factor 15HumansImmunoassayBlood ProteinsGDF15 protein, humanGrowth Differentiation Factor 15

Identifiers

PMID19955079
PMCPMC2830843
OpenAlexW2137166024

What OpenQuestion holds

Textmetadata
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.