<i>Aequorea</i> green fluorescent protein

Inouye, Satoshi; Tsuji, Frederick I.

doi:10.1016/0014-5793(94)80472-9

Cited by 361 publications

(87 citation statements)

References 28 publications

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“…Photographs were taken by using Kodak Echtachrome 400, and films were subsequently processed to enhance sensitivity. ing GFP in E. coli carrying pHis-AGP at 37°C (9). Strong green fluorescence in single cells was readily detectable under the microscope (data not shown).…”

Section: Methodsmentioning

confidence: 95%

“…Molecular cloning and expression of GFP cDNA in Escherichia coli have led to amino acid-sequence determination of the protein and to the location of the chromophore in the primary structure (7,8). GFP expressed in E. coli has also been shown to possess spectroscopic properties identical to the native protein (8)(9)(10). Recent studies have indicated that formation of the chromophore may depend on molecular oxygen or temperature (10)(11)(12).…”

mentioning

confidence: 99%

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Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells.

Ogawa

Inouye

Tsuji

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

227

145

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Section: Methodsmentioning

confidence: 95%

mentioning

confidence: 99%

Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells.

Ogawa

Inouye

Tsuji

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

227

145

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“…57,58) The emission is due to the presence of a chromophore, formed spontaneously by posttranslational cyclization of the tripeptide Ser65-Tyr66-Gly67 in the protein chain. [59][60][61] It consists of an imidazolone ring structure, and the light emitter is the singlet excited-state of the phenolate anion of the chromophore.…”

Section: Luciferinmentioning

confidence: 99%

Basic and Applied Aspects of Color Tuning of Bioluminescence Systems

Ohmiya

2005

Jpn. J. Appl. Phys.

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V. Viviani et al. [Biochemistry 38 (1999) 8271] were the first to succeed in cloning the red-emitting enzyme from the South American railroad worm, which is the only bioluminescent organism known to emit a red-colored light. The application of red bioluminescence has been our goal because the transmittance of longer-wavelength light is superior to that of the other colors for visualization of biological functions in living cells. Now, different color luciferases, which emit with wavelength maxima ranging from 400 to 630 nm, are available and are being used. For example, based on different color luciferases, Nakajima et al. developed a tricolor reporter in vitro assay system based on these different color luciferases in which the expression of three genes can be monitored simultaneously. On the other hand, bioluminescence resonance energy transfer (BRET) is a natural phenomenon caused by the intermolecular interaction between a bioluminescent protein and a fluorophore on a second protein, resulting in the light from the bioluminescence reaction having the spectrum of the fluorophore. Otsuji et al. [Anal. Biochem. 329 (2004) 230] showed that the change in the efficiency of energy transfer in intramolecular BRET can quantify cellular functions in living cells. In this review, I introduce the basic mechanisms of color tuning in bioluminescent systems and new applications based on color tuning in the life sciences.

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“…Advances in the development of proteins conjugated with green fluorescent protein (GFP) have since provided the opportunity for real time optical analysis of protein trafficking events in individual cells (13)(14)(15). Green fluorescent protein is a naturally occurring protein isolated from several different species of jellyfish (Aequoria) and sea cucumbers (Renilla).…”

mentioning

confidence: 99%

Visualization of Agonist-induced Sequestration and Down-regulation of a Green Fluorescent Protein-tagged β2-Adrenergic Receptor

Kallal

Gagnon

Penn

et al. 1998

Journal of Biological Chemistry

158

126

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To date, the visualization of ␤ 2 -adrenergic receptor (␤ 2 AR) trafficking has been largely limited to immunocytochemical analyses of acute internalization events of epitope-tagged receptors in various transfection systems. The development of a ␤ 2 AR conjugated with green fluorescent protein (␤ 2 AR-GFP) provides the opportunity for a more extensive optical analysis of ␤ 2 AR sequestration, down-regulation, and recycling in cells. Here we demonstrate that stable expression of ␤ 2 AR-GFP in HeLa cells enables a detailed temporal and spatial analysis of these events. Time-dependent colocalization of ␤ 2 AR-GFP with rhodamine-labeled transferrin and rhodamine-labeled dextran following agonist exposure demonstrates receptor distribution to early endosomes (sequestration) and lysosomes (down-regulation), respectively. The observed temporal distribution of ␤ 2 AR-GFP was consistent with measures of receptor sequestration and down-regulation generated by radioligand-receptor binding assays. Cells stimulated with different ␤-agonists revealed time courses of ␤ 2 AR-GFP redistribution reflective of the intrinsic activity of each agonist.

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Aequorea green fluorescent protein

Cited by 361 publications

References 28 publications

Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells.

Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells.

Basic and Applied Aspects of Color Tuning of Bioluminescence Systems

Visualization of Agonist-induced Sequestration and Down-regulation of a Green Fluorescent Protein-tagged β2-Adrenergic Receptor

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