Green fluorescent protein as a marker for gene expression.

  title={Green fluorescent protein as a marker for gene expression.},
  author={Martin Chalfie and Y Tu and Ghia M. Euskirchen and William W. Ward and Douglas C. Prasher},
  volume={263 5148},
A complementary DNA for the Aequorea victoria green fluorescent protein (GFP) produces a fluorescent product when expressed in prokaryotic (Escherichia coli) or eukaryotic (Caenorhabditis elegans) cells. Because exogenous substrates and cofactors are not required for this fluorescence, GFP expression can be used to monitor gene expression and protein localization in living organisms. 
Green Fluorescent Protein as a Reporter To Monitor Gene Expression and Food Colonization by Aspergillus flavus
ABSTRACT Transformants of Aspergillus flavus containing theAequorea victoria gfp gene fused to a viral promoter or the promoter region and 483 bp of the coding region of A. flavus aflR expressed
Red Fluorescent Protein (DsRed) as a Reporter inSaccharomyces cerevisiae
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The green fluorescent protein (GFP) of Aequorea victoria is a unique in vivo reporter for monitoring dynamic processes in cells or organisms. As a fusion tag GFP can be used to localize proteins, to
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The gene encoding the green fluorescent protein (GFP) from the jellyfish Aequorea victoria, ligated to the honeybee melittin signal peptide-encoding sequence, was inserted under transcriptional
Green Fluorescent Protein Green Fluorescent Protein
Green fluorescent protein (GFP) is a protein in the jellyfish Aequorea Victoria [8] that exhibits green fluorescence when exposed to light. The protein has 238 amino acids, three of them (Numbers 65
Green Fluorescent Protein Is Lighting Up Fungal Biology
Prasher cloned a cDNA for the green fluorescent protein (GFP) gene from the jellyfish Aequorea victoria in 1992 and shortly thereafter this gene or derivatives thereof were successfully expressed and conferred fluorescence to bacteria and yeast.


Firefly luciferase as a tool in molecular and cell biology.
The unique properties of firefly luciferase and the cloning of the gene for this enzyme have spawned a number of novel applications including its use as a reporter gene, as a model for the study of protein import into peroxisomes, and as a component of a heterologous gene expression system.
Primary structure of the Aequorea victoria green-fluorescent protein.
The cloning and sequencing of both cDNA and genomic clones of GFP from the cnidarian, Aequorea victoria, show three different restriction enzyme patterns which suggests that at least three different genes are present in the A. victoria population.
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A series of plasmid vectors which contain modular features particularly useful for studying gene expression in eukaryotic systems are described and used to analyze expression of several genes in the nematode Caenorhabditis elegans, demonstrating that lacZ can be expressed in a wide variety of different tissues and cell types.
Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.
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.
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Plasmid vectors are described that allow cloning of target DNAs at sites where they will be minimally transcribed by Escherichia coli RNA polymerase but selectively and actively transcribed by T7 RNA
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