ArticleBioTechniques2010
The nuclear translocation assay for intracellular protein-protein interactions and its application to the Bcr coiled-coil domain.
Article in BioTechniques, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- ReLo is a simple and rapid colocalization assay to identify and characterize direct protein-protein interactions.Nature communications · 2024Article
- Visualizing protein-protein interactions in plants by rapamycin-dependent delocalization.The Plant cell · 2021Article
- Controlled access of p53 to the nucleus regulates its proteasomal degradation by MDM2.Molecular pharmaceutics · 2013Article
- Utilizing the estrogen receptor ligand-binding domain for controlled protein translocation to the insoluble fraction.Pharmaceutical research · 2012Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Changing the subcellular location of the oncoprotein Bcr-Abl using rationally designed capture motifs.Pharmaceutical research · 2012Article
- Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.PloS one · 2012Article
- Disruption of Bcr-Abl coiled coil oligomerization by design.The Journal of biological chemistry · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein interactions are critical for normal biological processes and molecular pathogenesis. While it is important to study these interactions, there are limited assays that are performed inside the cell, in the native cell environment, where the majority of protein-protein interactions take place. Here we present a method of studying protein interactions intracellularly using one protein of interest fused to a localization-controllable enhanced GFP (EGFP) construct and the other protein of interest fused to the red fluorescent protein, DsRed. Nuclear translocation of the EGFP construct is induced by addition of a ligand, and the difference in nuclear localization between the induced and noninduced states of the DsRed construct provides an indication of the interaction between the two proteins. This assay, the nuclear translocation assay (NTA), is introduced here as broadly applicable for studying protein interactions in the native environment inside cells and is demonstrated using forms of the coiled-coil domain from the breakpoint cluster region (Bcr) protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.