Results 271 to 280 of about 271,314 (298)
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Structure of bacterial luciferase

Current Opinion in Structural Biology, 1995
The generation of light by living organisms such as fireflies, glow-worms, mushrooms, fish, or bacteria growing on decaying materials has been a subject of fascination throughout the ages, partly because it occurs without the need for high temperatures.
T O, Baldwin   +6 more
openaire   +2 more sources

Luciferases with Tunable Emission Wavelengths

Angewandte Chemie, 2017
AbstractWe introduce luciferases whose emission maxima can be tuned to different wavelengths by chemical labeling. The luciferases are chimeras of NanoLuc with either SNAP‐tag or HaloTag7. Labeling of the self‐labeling tag with a fluorophore shifts the emission maximum of NanoLuc to that of the fluorophore.
Julien Hiblot   +9 more
openaire   +3 more sources

Measurement of Luciferase Rhythms

2014
Firefly luciferase (LUC) is a sensitive and versatile reporter for the analysis of gene expression. Transgenic plants carrying CLOCK GENE promoter:LUC fusions can be assayed with high temporal resolution. LUC measurement is sensitive, noninvasive, and nondestructive and can be readily automated, greatly facilitating genetic studies.
C Robertson, McClung, Qiguang, Xie
openaire   +2 more sources

Luciferases as Reporter Genes

2006
Luciferase is the ideal reporter gene to provide temporal and spatial information on promoter activity in Arabidopsis and other eukaryotes; the noninvasive detection of luminescence and short half-life of luciferase activity allow repeated measurements of individual seedlings over several days to assay dynamic changes in gene expression.
Megan M, Southern   +2 more
openaire   +2 more sources

Mechanical Control of Renilla Luciferase

Journal of the American Chemical Society, 2013
We report experiments where the activity of the enzyme luciferase from Renilla reniformis is controlled through a DNA spring attached to the enzyme. In the wake of previous work on kinases, these results establish that mechanical stress applied through the DNA springs is indeed a general method for the artificial control of enzymes, and for the ...
Chiao-Yu, Tseng, Giovanni, Zocchi
openaire   +2 more sources

Fabrication of a New Lineage of Artificial Luciferases from Natural Luciferase Pools

ACS Combinatorial Science, 2017
The fabrication of artificial luciferases (ALucs) with unique optical properties has a fundamental impact on bioassays and molecular imaging. In this study, we developed a new lineage of ALucs with unique substrate preferences by extracting consensus amino acids from the alignment of 25 copepod luciferase sequences available in natural luciferase pools.
Sung Bae Kim   +3 more
openaire   +2 more sources

Dual Luciferase Assay for Secreted Luciferases Based onGaussiaand NanoLuc

ASSAY and Drug Development Technologies, 2013
Just recently, NanoLuc, a new engineered luciferase based on the small subunit of the luciferase from Oplophorus gracilirostris was introduced. Like the luciferase from Gaussia princeps, this luciferase is secreted into the medium. Both luciferases are the smallest and brightest luciferases known and well-suited for reporter assays. In our experiments,
Kerstin, Heise   +4 more
openaire   +2 more sources

The Split Luciferase Complementation Assay

2010
A split luciferase complementation assay to study protein-protein interactions within Arabidopsis protoplasts in 96-well plates is described in this protocol. Two proteins of interest, a bait and prey, which are genetically fused to amino- and carboxy-terminal fragments of Renilla luciferase, are transiently expressed in protoplasts.
Naohiro, Kato, Jason, Jones
openaire   +2 more sources

[151] Bacterial luciferase

1955
Publisher Summary Bacterial luciferase is a flavoprotein which catalyzes the oxidation of reduced DPN by numerous oxidants such as FMN, ferricyanide, quinones, and various dyes. In the presence of FMN and a long-chain fatty aldehyde the oxidation of DPNH is accompanied by light emission.
Arda A. Green, William D. McElroy
openaire   +1 more source

Luciferase

RCSB Protein Data Bank, 2006
openaire   +1 more source

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