A method for Boolean analysis of protein interactions at a molecular level.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
13 08 2022
13 08 2022
Historique:
received:
01
07
2021
accepted:
29
07
2022
entrez:
13
8
2022
pubmed:
14
8
2022
medline:
17
8
2022
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 35963857
doi: 10.1038/s41467-022-32395-w
pii: 10.1038/s41467-022-32395-w
pmc: PMC9375095
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4755Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2022. The Author(s).
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