ArticleNature communications2022
A method for Boolean analysis of protein interactions at a molecular level.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Molecular Boolean analyses of chemokine (C-C motif) receptor 1, αBiochemistry and biophysics reports · 2026Article
- Nano-Enabled Fluorescence Switching: A Novel Strategy for PDGFRβ Detection and TKI Therapy Monitoring.Research (Washington, D.C.) · 2026Article
- Ultrasensitive non-enzymatic protein detection using proximity immunoassay with photonic resonator absorption microscopy.Npj biosensing · 2026Article
- Antibody-oligonucleotide conjugates for spatial proteomics: principles, applications, and challenges.Acta biochimica et biophysica Sinica · 2025Article
- In Situ RAS:RAF Binding Correlates with Response to KRASG12C Inhibitors in KRASG12C-Mutant Non-Small Cell Lung Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025Article
- Creating Chemiluminescence Signature Arrays Coupled with Machine Learning for Alzheimer's Disease Serum Diagnosis.Research (Washington, D.C.) · 2025Article
- Multiplexed mapping of the interactome of GPCRs with receptor activity-modifying proteins.Science advances · 2024Article
- Article
- Expanding the GPCR-RAMP interactome.bioRxiv : the preprint server for biology · 2023Article
- DNA-based customized functional modules for signal transformation.Frontiers in chemistry · 2023Review
Corrections and comments
- Erratum issued
Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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