Results 231 to 240 of about 11,605 (288)

Luciferases with Tunable Emission Wavelengths

open access: yesAngewandte Chemie - International Edition, 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   +2 more
exaly   +7 more sources

De novo design of luciferases using deep learning [PDF]

open access: yesNature, 2023
De novo enzyme design has sought to introduce active sites and substrate-binding pockets that are predicted to catalyse a reaction of interest into geometrically compatible native scaffolds1,2, but has been limited by a lack of suitable protein ...
Hsien-Wei Yeh   +2 more
exaly   +2 more sources

Active-Site Properties of Phrixotrix Railroad Worm Green and Red Bioluminescence-Eliciting Luciferases

open access: yesJournal of Biochemistry, 2006
The luciferases of the railroad worm Phrixotrix (Coleoptera: Phengodidae) are the only beetle luciferases that naturally produce true red bioluminescence.
Vadim R Viviani, Yoshihiro Ohmiya
exaly   +2 more sources

Shining Light on the Secreted Luciferases of Marine Copepods: Current Knowledge and Applications

open access: yesPhotochemistry and Photobiology, 2019
Текст статьи не публикуется в открытом доступе в соответствии с политикой журнала.Copepod luciferases -a family of small secretory proteins of 18.4-24.3 kDa, including a signal peptide-are responsible for bright secreted bioluminescence of some marine ...
Svetlana V Marková   +2 more
exaly   +2 more sources

Few substitutions affect the bioluminescence spectra ofPhrixotrix (Coleoptera: Phengodidae) luciferases: a site-directed mutagenesis survey

open access: yesLuminescence, 2007
Phrixotrix (railroad worm) luciferases produce bioluminescence in the green and red regions of the spectrum, depending on the location of the lanterns, and are the only luciferases naturally producing red bioluminescence.
Vadim R Viviani   +1 more
exaly   +2 more sources

The Influence of the Loop between Residues 223‐235 in Beetle Luciferase Bioluminescence Spectra: A Solvent Gate for the Active Site of pH‐Sensitive Luciferases

open access: yesPhotochemistry and Photobiology, 2008
Beetle luciferases emit a wide range of bioluminescence colors, ranging from green to red. Firefly luciferases can shift the spectrum to red in response to pH and temperature changes, whereas click beetle and railroadworm luciferases do not. Despite many
Vadim R Viviani   +2 more
exaly   +2 more sources
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Bioluminescence assays: multicolor luciferase assay, secreted luciferase assay and imaging luciferase assay

Expert Opinion on Drug Discovery, 2010
By selecting the most appropriate bioluminescence assay, the researcher can study the underlying molecular mechanisms of a physiological system and the effects of a drug throughout the body.This review covers three luciferase assay systems: the multicolor luciferase assay, secreted luciferase assay and imaging luciferase assay. These assays are applied
Yoshihiro, Nakajima, Yoshihiro, Ohmiya
openaire   +2 more sources

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

Crystalline firefly luciferase

Biochimica et Biophysica Acta, 1956
Abstract 1. 1. The method for purification and crystallization of firefly luciferase is described. 2. 2. The crystalline enzyme is apparently homogenous as evidenced by ultracentrifugation a and electrophoretic determinations. The molecular weight is probably around 100,000 and the isoelectric point between pH 6.2 and 6.3. 3. 3.
A A, GREEN, W D, MCELROY
openaire   +2 more sources

Firefly luciferase inhibition

Journal of Photochemistry and Photobiology B: Biology, 2010
Firefly luciferase (Luc) is the most studied of the luciferase enzymes and the mechanism and kinetics of the reactions catalyzed by this enzyme have been relatively well characterized. Luc catalyzes the bioluminescent reaction involving firefly luciferin (D-LH(2)), adenosine triphosphate (ATP), magnesium ion and molecular oxygen with the formation of ...
João M. M. Leitão   +1 more
openaire   +3 more sources

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