ArticlePLoS biology2019
A new branched proximity hybridization assay for the quantification of nanoscale protein-protein proximity.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Proximity Ligation Assay: From a Foundational Principle to a Versatile Platform for Molecular and Translational Research.Biomolecules · 2025Review
- Site-directed conjugation of single-stranded DNA to affinity proteins: quantifying the importance of conjugation strategy.Chemical science · 2024Article
- An extracellular vesicular mutant KRAS-associated protein complex promotes lung inflammation and tumor growth.Journal of extracellular vesicles · 2023Article
- Regulatory guidelines and preclinical tools to study the biodistribution of RNA therapeutics.Advanced drug delivery reviews · 2022Review
- Branched Proximity Hybridization Assay for the Quantification of Nanoscale Protein-Protein Proximity.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Light-mediated discovery of surfaceome nanoscale organization and intercellular receptor interaction networks.Nature communications · 2021Article
- Aptamers against Immunoglobulins: Design, Selection and Bioanalytical Applications.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins are organized in nanoscale compartments. Their reorganization plays a crucial role in receptor activation and cell signaling. To monitor the organization and reorganization of membrane proteins, we developed a new branched proximity hybridization assay (bPHA) allowing better quantification of the nanoscale protein-protein proximity. In this assay, oligo-coupled binding probes, such as aptamer, nanobody, and antibodies, are used to translate the proximity of target proteins to the proximity of oligos. The closely positioned oligos then serve as a template for a maximum of 400-fold branched DNA (bDNA) signal amplification. The amplified bPHA signal is recorded by flow cytometer, thus enabling proximity studies with high throughput, multiplexing, and single-cell resolution. To demonstrate the potential of the bPHA method, we measured the reorganization of the immunoglobulin M (IgM)- and immunoglobulin D (IgD)-class B cell antigen receptor (BCR) on the plasma membrane and the recruitment of spleen tyrosine kinase (Syk) to the BCR upon B lymphocyte activation.
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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.