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

Raykova D, Kermpatsou D, Malmqvist T, Harrison PJ, Sander MR, Stiller C, Heldin J, Leino M, Ricardo S, Klemm A, David L, Spjuth O, Vemuri K, Dimberg A, Sundqvist A, Norlin M, Klaesson A, Kampf C, Söderberg O

Nat Commun 13 (1) 4755 [2022-08-13; online 2022-08-13]

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.

BioImage Informatics [Collaborative]

PubMed 35963857

DOI 10.1038/s41467-022-32395-w

Crossref 10.1038/s41467-022-32395-w

pii: 10.1038/s41467-022-32395-w
pmc: PMC9375095


Publications 8.1.0