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A method for Boolean analysis of protein interactions at a molecular level

Author

Listed:
  • Doroteya Raykova

    (Uppsala University, Biomedical center)

  • Despoina Kermpatsou

    (Uppsala University, Biomedical center)

  • Tony Malmqvist

    (Atlas Antibodies AB)

  • Philip J. Harrison

    (Uppsala University, Biomedical center)

  • Marie Rubin Sander

    (Uppsala University, Biomedical center)

  • Christiane Stiller

    (Uppsala University, Biomedical center)

  • Johan Heldin

    (Uppsala University, Biomedical center)

  • Mattias Leino

    (Uppsala University, Biomedical center)

  • Sara Ricardo

    (University of Porto
    Institute for Research and Innovation in Health (i3S) of the University of Porto/Institute of Molecular Pathology and Immunology of the University of Porto (Ipatimup)
    University Institute of Health Sciences (IUCS), CESPU)

  • Anna Klemm

    (Uppsala University)

  • Leonor David

    (University of Porto
    Institute for Research and Innovation in Health (i3S) of the University of Porto/Institute of Molecular Pathology and Immunology of the University of Porto (Ipatimup))

  • Ola Spjuth

    (Uppsala University, Biomedical center)

  • Kalyani Vemuri

    (Uppsala University, Rudbeck Laboratory)

  • Anna Dimberg

    (Uppsala University, Rudbeck Laboratory)

  • Anders Sundqvist

    (Uppsala University, Biomedical center)

  • Maria Norlin

    (Uppsala University, Biomedical center)

  • Axel Klaesson

    (Uppsala University, Biomedical center)

  • Caroline Kampf

    (Atlas Antibodies AB)

  • Ola Söderberg

    (Uppsala University, Biomedical center)

Abstract

Determining the levels of protein–protein interactions is essential for the analysis of signaling within the cell, characterization of mutation effects, protein function and activation in health and disease, among others. Herein, we describe MolBoolean – a method to detect interactions between endogenous proteins in various subcellular compartments, utilizing antibody-DNA conjugates for identification and signal amplification. In contrast to proximity ligation assays, MolBoolean simultaneously indicates the relative abundances of protein A and B not interacting with each other, as well as the pool of A and B proteins that are proximal enough to be considered an AB complex. MolBoolean is applicable both in fixed cells and tissue sections. The specific and quantifiable data that the method generates provide opportunities for both diagnostic use and medical research.

Suggested Citation

  • Doroteya Raykova & Despoina Kermpatsou & Tony Malmqvist & Philip J. Harrison & Marie Rubin Sander & Christiane Stiller & Johan Heldin & Mattias Leino & Sara Ricardo & Anna Klemm & Leonor David & Ola S, 2022. "A method for Boolean analysis of protein interactions at a molecular level," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32395-w
    DOI: 10.1038/s41467-022-32395-w
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    References listed on IDEAS

    as
    1. Björn Koos & Gaëlle Cane & Karin Grannas & Liza Löf & Linda Arngården & Johan Heldin & Carl-Magnus Clausson & Axel Klaesson & M. Karoliina Hirvonen & Felipe M. S. de Oliveira & Vladimir O. Talibov & N, 2015. "Proximity-dependent initiation of hybridization chain reaction," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
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