ArticlePloS one2014
A protein L-based immunodiagnostic approach utilizing time-resolved Förster resonance energy transfer.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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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.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Whole Blood as a Sample Matrix in Homogeneous Time-Resolved Assay-Förster Resonance Energy Transfer-Based Antibody Detection.Diagnostics (Basel, Switzerland) · 2024Article
- Immunoassay System Based on the Technology of Time-Resolved Fluorescence Resonance Energy Transfer.Sensors (Basel, Switzerland) · 2024Article
- Article
- Article
- Resonance Energy Transfer-Based Biosensors for Point-of-Need Diagnosis-Progress and Perspectives.Sensors (Basel, Switzerland) · 2021Review
- Urine and Free Immunoglobulin Light Chains as Analytes for Serodiagnosis of Hantavirus Infection.Viruses · 2019Article
- Article
- Immunoassay for serodiagnosis of Zika virus infection based on time-resolved Förster resonance energy transfer.PloS one · 2019Article
- Competitive Homogeneous Immunoassay for Rapid Serodiagnosis of Hantavirus Disease.Journal of clinical microbiology · 2015Article
- Rapid homogeneous immunoassay based on time-resolved Förster resonance energy transfer for serodiagnosis of acute hantavirus infection.Journal of clinical microbiology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chelated lanthanides such as europium (Eu) have uniquely long fluorescence emission half-lives permitting their use in time-resolved fluorescence (TRF) assays. In Förster resonance energy transfer (FRET) a donor fluorophore transfers its emission energy to an acceptor fluorophore if in sufficiently close proximity. The use of time-resolved (TR) FRET minimizes the autofluorescence of molecules present in biological samples. In this report, we describe a homogenous immunoassay prototype utilizing TR-FRET for detection of antibodies in solution. The assay is based on labeled protein L, a bacterial protein that binds to immunoglobulin (Ig) light chain, and labeled antigen, which upon association with the same Ig molecule produce a TR-FRET active complex. We show that the approach is functional and can be utilized for both mono- and polyvalent antigens. We also compare the assay performance to that of another homogenous TR-FRET immunoassay reported earlier. This novel assay may have wide utility in infectious disease point-of-care diagnostics.
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Registered trials
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.