[14] Detection of protein-protein interactions by protein fragment complementation strategies
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RAPIDS, a method for sub-compartmental identification of protein interactomes
2022, Methods in EnzymologyCitation Excerpt :Abnormal protein interactions are linked to many human diseases. To study protein-protein interactions, affinity purification, chemical cross-linking, protein fragment complementation assays, and two-hybrid screening are employed (Bruckner, Polge, Lentze, Auerbach, & Schlattner, 2009; Dunham, Mullin, & Gingras, 2012; Michnick, Remy, Campbell-Valois, Vallee-Belisle, & Pelletier, 2000; Tang & Bruce, 2009). In the past decade, proximity-dependent labeling methods have emerged as effective complementary approaches to classical affinity purification and mass spectrometry-based protein interaction mapping.
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2019, Current Opinion in Chemical BiologyInferring Protein-Protein Interaction Networks From Mass Spectrometry-Based Proteomic Approaches: A Mini-Review
2019, Computational and Structural Biotechnology JournalCitation Excerpt :One of the primary goals of systems biology is to understand the functions of proteins from various organisms [1]. Some of the most widely used techniques to identify protein-protein interactions include yeast two-hybrid (Y2H) [2,3], protein-fragment complementation assay (PCA) [4], LUMIER [5], fluorescence resonance energy transfer (FRET) [6] etc. Mass spectrometry is a powerful tool for studying biomolecules such as proteins by their identification, quantification and further functional characterization [7–9].