ArticleNature biotechnology2003
Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis.
Article in Nature biotechnology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 322 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
322 citing papers in PubMed.
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- Imaging Techniques for the Study of Protein Condensates and Filaments and Their Applications.International journal of molecular sciences · 2026Review
- Single-cell transcriptomics of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Oligomerization of transmembrane adenylyl cyclase isoforms.Molecular pharmacology · 2026Review
- Engineering a new tripartite split-ccGFP system from Corynactis californica for detecting protein-protein interactions.Scientific reports · 2025Article
- Mechanisms and Research Methods of Protein Modification in Virus Entry.Applied biochemistry and biotechnology · 2025Review
- A Molecular Recruitment Colocalization Platform for Visualizing Multi-Protein Interactions and Engineering Biomolecular Condensates in Living Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Clu1/Clu form mitochondria-associated granules upon metabolic transitions and regulate mitochondrial protein translation via ribosome interactions.PLoS genetics · 2025Article
- Dual DNA demethylation mechanisms implement epigenetic memory driven by the pioneer factor PAX7.Science advances · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Direct observation of fluorescent proteins in gels: A rapid, cost-efficient, and quantitative alternative to immunoblotting.Biology of the cell · 2025Article
- Bimolecular Fluorescence Complementation (BiFC) Technique for Exocytic Proteins in Murine Hippocampal Neurons.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Article
- Zinc metalloprotease FgM35, which targets the wheat zinc-binding protein TaZnBP, contributes to the virulence of Fusarium graminearum.Stress biology · 2024Article
- Novel Bimolecular Fluorescence Complementation (BiFC) Assay for Visualization of the Protein-Protein Interactions and Cellular Protein Complex Localizations.Molecular biotechnology · 2024Article
- Comprehensive Review on Bimolecular Fluorescence Complementation and Its Application in Deciphering Protein-Protein Interactions in Cell Signaling Pathways.Biomolecules · 2024Review
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- Powdery mildew effectors AVRMolecular plant pathology · 2024Article
262 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The specificity of biological regulatory mechanisms relies on selective interactions between different proteins in different cell types and in response to different extracellular signals. We describe a bimolecular fluorescence complementation (BiFC) approach for the simultaneous visualization of multiple protein interactions in the same cell. This approach is based on complementation between fragments of fluorescent proteins with different spectral characteristics. We have identified 12 bimolecular fluorescent complexes that correspond to 7 different spectral classes. Bimolecular complex formation between fragments of different fluorescent proteins did not differentially affect the dimerization efficiency of the bZIP domains of Fos and Jun or the subcellular sites of interactions between these domains. Multicolor BiFC enables visualization of interactions between different proteins in the same cell and comparison of the efficiencies of complex formation with alternative interaction partners.
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Registered trials
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