Fluorescent proteins from nonbioluminescent Anthozoa species
@article{Matz1999FluorescentPF, title={Fluorescent proteins from nonbioluminescent Anthozoa species}, author={Mikhail V. Matz and Arkady F. Fradkov and Yulii Aleksandrovich Labas and Aleksandr P. Savitsky and Andrey G. Zaraisky and Mikhail L. Markelov and Sergey A. Lukyanov}, journal={Nature Biotechnology}, year={1999}, volume={17}, pages={969-973} }
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 at yellow and red wavelengths. All the proteins were isolated from nonbioluminescent reef corals, demonstrating that GFP-like proteins are not always functionally linked to bioluminescence. The new proteins share the same β-can fold first observed in GFP, and this provided a basis for the…
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References
SHOWING 1-10 OF 36 REFERENCES
GREEN FLUORESCENT PROTEIN
- BiologyPhotochemistry 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.
Crystal Structure of the Aequorea victoria Green Fluorescent Protein
- Chemistry, BiologyScience
- 1996
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…
Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.
- Biology, ChemistryBiochemistry
- 1993
The characterization of the Aequorea victoria GFP chromophore is described, which is released as a hexapeptide upon digestion of the protein with papain, formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide.
Red-Shifted Excitation Mutants of the Green Fluorescent Protein
- Biology, ChemistryBio/Technology
- 1995
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…
Aequorea victoria bioluminescence moves into an exciting new era.
- Biology, EngineeringTrends in biotechnology
- 1998
Green‐fluorescent protein mutants with altered fluorescence excitation spectra
- Biology, ChemistryFEBS letters
- 1995
Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein.
- ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1997
A new understanding of proton redistribution in green fluorescent protein should enable engineering of environmentally sensitive fluorescent indicators and UV-triggered fluorescent markers of protein diffusion and trafficking in living cells.
The molecular structure of green fluorescent protein
- ChemistryNature Biotechnology
- 1996
The crystal structure of recombinant wild-type green fluorescent protein (GFP) has been solved to a resolution of 1.9 Å by multiwavelength anomalous dispersion phasing methods and the identification of the dimer contacts may allow mutagenic control of the state of assembly of the protein.
Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer.
- ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1996
The observed isotope effect suggests that the initial excited state process involves a proton transfer reaction that is followed by additional structural changes that may help to rationalize and motivate mutations that alter the absorption properties and improve the photo stability of GFP.