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 1998
  • Biology, Medicine
  • 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… Expand
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The green fluorescent protein (GFP) has recently attracted great attention because it is the only cloned protein that exhibits strong fluorescence without any extraneous chromophores [1]. When fusedExpand
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References

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TLDR
The GFP originally cloned from the jellyfish Aequorea victoria has several nonoptimal properties including low brightness, a significant delay between protein synthesis and fluorescence development, and complex photoisomerization, but can be re-engineered by mutagenesis to ameliorate these deficiencies and shift the excitation and emission wavelengths, creating different colors and new applications. Expand
Fluorescent proteins from nonbioluminescent Anthozoa species
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, emittingExpand
Photoactivation turns green fluorescent protein red
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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. TheExpand
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Green fluorescent protein is remarkable in that it autocatalyzes the formation of its own fluorophore and thus can be expressed in a variety of organisms in its fluorescent form. Expand
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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. Expand
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TLDR
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. Expand
Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein.
TLDR
A mutant of GFP with a significantly larger extinction coefficient for excitation at 488 nm with a re-engineered GFP gene sequence containing codons preferentially found in highly expressed human proteins yield an enhanced GFP which provides greater sensitivity in most systems. Expand
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