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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Green fluorescent protein from the jellyfish Aequorea victoria and GFP-like proteins from Anthozoa species contain light-absorbing chromophores within their protein sequences, aimed at providing information for rational design of variants with desired fluorescence properties. Expand
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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… Expand
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Recognized increased opportunities to understand the relation between GFP structure and its spectroscopic function become available because of the higher resolution of its structure. Expand
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Green fluorescent protein (GFP) was discovered, purified, and characterized by Shimomura in a jellyfish beginning in 1962 and has revolutionized cell biology and led to the new field of in vivo cell biology. 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 fused… Expand
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The use of S65T GFP is described, unique in having increased fluorescence intensity, faster fluorophore formation, and altered excitation and emission spectra than that of the wild-type protein. Expand
Focus on Fluorescent Proteins
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The mechanisms for this self-catalyzed amino-acid modifications leading to the chromophore formation are best characterized for the GFP although some work was carried out on other proteins as well. Expand
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References

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Understanding, improving and using green fluorescent proteins.
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, emitting… Expand
Photoactivation turns green fluorescent protein red
TLDR
The use of GFP photoactivation is reported here the first direct measurements of protein diffusion in the cytoplasm of living bacteria, and enables regional, non-invasive marking of proteins in vivo. Expand
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… Expand
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  • Biology, Medicine
  • Current opinion in structural biology
  • 1997
TLDR
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
GREEN FLUORESCENT PROTEIN
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  • Chemistry, Medicine
  • Photochemistry and photobiology
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TLDR
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
Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1.
TLDR
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. Expand
Red-Shifted Excitation Mutants of the Green Fluorescent Protein
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… Expand
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  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1994
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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