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10.1016/j.jmb.2015.03.005

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suck abstract from ncbi

pmid25772494
      J+Mol+Biol 2015 ; 427 (11 ): 2039-2055
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  • Bimolecular Fluorescence Complementation (BiFC) Analysis: Advances and Recent Applications for Genome-Wide Interaction Studies #MMPMID25772494
  • Miller KE ; Kim Y ; Huh WK ; Park HO
  • J Mol Biol 2015[Jun]; 427 (11 ): 2039-2055 PMID25772494 show ga
  • Complex protein networks are involved in nearly all cellular processes. To uncover these vast networks of protein interactions, various high-throughput screening technologies have been developed. Over the last decade, bimolecular fluorescence complementation (BiFC) assay has been widely used to detect protein-protein interactions (PPIs) in living cells. This technique is based on the reconstitution of a fluorescent protein in vivo. Easy quantification of the BiFC signals allows effective cell-based high-throughput screenings for protein binding partners and drugs that modulate PPIs. Recently, with the development of large screening libraries, BiFC has been effectively applied for genome-wide PPI studies and has uncovered novel protein interactions, providing new insight into protein functions. In this review, we describe the development of reagents and methods used for BiFC-based screens in yeast, plants, and mammalian cells. We also discuss the advantages and drawbacks of these methods and highlight the application of BiFC in large-scale studies.
  • |*Molecular Probe Techniques [MESH]
  • |Animals [MESH]
  • |Arabidopsis Proteins/metabolism [MESH]
  • |Fluorescent Dyes/metabolism [MESH]
  • |Genome-Wide Association Study [MESH]
  • |Green Fluorescent Proteins/metabolism [MESH]
  • |High-Throughput Screening Assays/*methods [MESH]
  • |Humans [MESH]
  • |Mammals [MESH]
  • |Protein Interaction Mapping/*methods [MESH]
  • |Proteomics/methods [MESH]
  • |Telomere/metabolism [MESH]


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