Fluorescent proteins discovery

Shimomura, O. (1998). The discovery of green fluorescent protein. In Chalfie, M., and Kain, S. (eds.), Green Fluorescent Protein, pp. 3-15. Wiley-Liss, New York. 

Shimomura, O. (2005a). The discovery of aequorin and green fluorescent protein. J. Microscopy 217 3-15. 

FMNH2 requirement in bacterial luminescence Crystallization of Cypridina luciferin Crystallization of firefly luciferin Cypridina luciferin in fishes the first cross reaction discovered Structure of firefly luciferin Discovery of aequorin and GFP (green fluorescent protein) Structure of Cypridina luciferin Concept of photoprotein Structure of Latia luciferin Dioxetanone mechanism proposed in firefly and Cypridina luminescence... 

Shimomura O (2009) Discovery of green fluorescent protein (GFP) (Nobel lecture). Angew Chem Int Ed Engl 48 5590-5602... 

The discovery of Green Fluorescent Protein (GFP) and the development of technology that allows specific proteins to be tagged with GFP has fundamentally altered the types of question that can be asked using cell biological methods. It is now possible not only to study where a protein is within a cell, but also feasible to study the precise dynamics of protein movement within living cells. We have exploited these technical developments and applied them to the study of translation initiation factors in yeast, focusing particularly on the... 

The second major breakthrough for the application of fluorescent proteins was the isolation of the red fluorescent protein (RFP) drFP583 or DsRed from the Anthozoa and Discosoma sp., a mushroom-shaped anemone found in the warm waters of the Indo-Pacific ocean [13], The breakthrough was not only the discovery of the first true RFP, but equally important was the fact that it was discovered in a nonbioluminescent species and that the gene was cloned immediately. 

The isolation of fluorescent proteins from nonbioluminescent species has led to the discovery of a super family of GFP-like proteins [1, 14]. Recently, six additional GFP-like proteins were isolated from A. victoria-related jellyfish [14-16]. Furthermore, a large number of GFP-like proteins have been isolated from Anthozoa species, ranging in fluorescence from green to orange-red, as well as nonflu-orescent purple-blue chromoproteins [17-19],... 

Giuliano, K.A., and Taylor, D.L. 1998. Fluorescent-protein biosensors new tools for drug discovery. Trends Biotechnol. 16, 135-140. 

Kain SR. Green fluorescent protein (GFP) Applications in cell-based assays for drug discovery. Drug Discov Today 1999 4 304-12. 

Compared with fluorescent proteins and Q-dots, small fluorescence molecules have advantages such as less steric bulkiness, faster labeling, and easier handling,4 and thus have been widely utilized as popular tools for chemical, biological, and medical applications. Although the demand for useful fluorescence sensors is acute, for decades, the conventional target-oriented approach remains as the dominating approach for new fluorescence sensor development, if not the only one, which has limited the scope and speed of novel sensor discovery. 

Osamu Shimomura, Martin Chalfie, and Roger Y. Tsien each receives 1/3 of the Nobel Prize in chemistry for the discovery and development of the green fluorescent protein. 

Fluorescent spectroscopy, because of its high level of sensitivity, has long been a powerful method for studying protein behavior. Site-specific attachment of fluorophores to a unique cysteine in a protein of interest is a traditional route for the production of fluorescent proteins. In addition, the discovery of fluorescent proteins, such as the green fluorescent protein (GFP) from the jellyfish Aequorea victoria [62], has provided a genetic approach for the production of fluorescently labeled proteins. Both these methods, however,... 

Glowing Discoveries Research into bioluminescence led to the discovery of green fluorescent protein (GFP), which is found in some species of jellyfish. GFP emits a green light when exposed to UV light. Researchers have inserted GFP into various organisms, such as mice, for research purposes. Examples of what scientists are using GFP to study include cancer, malaria, and cellular processes. 

Osamu Shimomura (Japan), Martin Chalfie (United States), and Roger Y. Tsien (United States) for the discovery and development of the green fluorescent protein, GFR These three scientists received the prize for their work with a protein simply called green fluorescent protein, or GFR This protein was first observed way back in 1962 in a jellyfish. It eventually became a very important molecule in the biological sciences, as clever researchers have found ways to use GFP to study otherwise invisible chemical processes. Shimomura, Chalfie, and Tsien were at the forefront of the major discoveries that led to the understanding of GFP that researchers possess today. 

Green fluorescent protein (GFP), first isolated from biolumlnescent jellyfish, Is a protein containing 238 amino acid residues. The discovery of GFP has revolutionized the field of fluorescence microscopy, which enables biochemists to monitor the biosynthesis of proteins. The 2008 Nobel Prize in Chemistry was awarded to Martin Chalfie, Osamu Shimomura, and Roger Tsien for the discovery and development of GFP. The structural subunit of GFP responsible for fluorescence, called the fluorophore, results when three amino acid residues undergo cyclization. Identify the three amino acids that go into the biosynthesis of this fluorophore ... 

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