The green fluorescent protein.

@article{Tsien1998TheGF,
  title={The green fluorescent protein.},
  author={Roger Tsien},
  journal={Annual review of biochemistry},
  year={1998},
  volume={67},
  pages={
          509-44
        }
}
  • R. Tsien
  • Published 1 July 1998
  • Biology
  • Annual review of biochemistry
In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology. Its amazing ability to generate a highly visible, efficiently emitting internal fluorophore is both intrinsically fascinating and tremendously valuable. High-resolution crystal structures of GFP offer unprecedented opportunities to understand and manipulate the relation between… 

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References

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We have cloned six fluorescent proteins homologous to the green fluorescent protein (GFP) from Aequorea victoria. Two of these have spectral characteristics dramatically different from GFP, emitting

Crystal Structure of the Aequorea victoria Green Fluorescent Protein

The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products. The

GREEN FLUORESCENT PROTEIN

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  • Biology
    Photochemistry and photobiology
  • 1995
This demonstration indicated that GFP could be used as a marker of gene expression and protein localization in living and fixed tissues and variations with more intense fluorescence or alterations in the excitation and emission spectra have been produced.

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Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1.

Proteins synthesized at a low temperature retained their fluorescence despite a shift to a higher temperature, and when a temperature-sensitive nsp1 mutant expressing GFP-nucleoplasmin was cultured at 23 degrees C and then shifted to 35 degrees C, this protein accumulated in novel nuclear-like compartments devoid of DNA.

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Using optimized combinatorial mutagenisis techniques and digital imaging Spectroscopy (DIS), we have insulated mutants of the cloned Aequorea victoria green fluorescent protein (GFP)that show

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    Proceedings of the National Academy of Sciences of the United States of America
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The availability of two visibly distinct colors should significantly extend the usefulness of GFP in molecular and cell biology by enabling in vivo visualization of differential gene expression and protein localization and measurement of protein association by fluorescence resonance energy transfer.

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Green fluorescence was observed in muscle, pancreas, kidney, heart and other organs in all the three transgenic mouse lines and it was demonstrated that the GFP expression could be quantified by measuring the fluorescence in tissue extracts.
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