Results 1 to 10 of about 5,761 (165)

Coelenterazine Analogs for Bioassays and Molecular Imaging [PDF]

open access: yesSensors
Coelenterazine (CTZ) is a common substrate of marine luciferases upon emission of bioluminescence (BL) in living organisms. Because CTZ works as a “luminophore” in the process of BL emission, the chemical modification has been centered for improving the ...
Sung-Bae Kim   +3 more
doaj   +4 more sources

Coelenterazine sulfotransferase from Renilla muelleri.

open access: yesPLoS ONE, 2022
The luciferin sulfokinase (coelenterazine sulfotransferase) of Renilla was previously reported to activate the storage form, luciferyl sulfate (coelenterazine sulfate) to luciferin (coelenterazine), the substrate for the luciferase bioluminescence ...
George Tzertzinis   +7 more
doaj   +3 more sources

Fast kinetics of photoprotein emitting species [PDF]

open access: yesScientific Reports
Coelenterazine is the most common substrate for light-emitting reactions identified in luminous marine organisms. Among bioluminescent proteins engaging coelenterazine as a luciferin, Ca2+-regulated photoproteins form stable enzyme-substrate complexes ...
Elena V. Eremeeva   +4 more
doaj   +2 more sources

Availability and occurrence of coelenterazine in a Swedish fjord to maintain Amphiura filiformis bioluminescence [PDF]

open access: yesScientific Reports
The bioluminescent European brittle star Amphiura filiformis produces blue light at the arm-spine level thanks to a biochemical reaction involving coelenterazine as substrate and a Renilla-like luciferase as an enzyme.
Constance Coubris   +3 more
doaj   +2 more sources

Coelenterazine Indicators for the Specific Imaging of Human and Bovine Serum Albumins

open access: yesSensors, 2023
Albumin assays in serum are important for the prognostic assessment of many life-threatening diseases, such as heart failure, liver disease, malnutrition, inflammatory bowel disease, infections, and kidney disease. In this study, synthetic coelenterazine
Nobuo Kitada   +2 more
exaly   +3 more sources

Insights into the bioluminescence systems of three sea pens (Cnidaria: Anthozoa): from de novo transcriptome analyses to biochemical assays [PDF]

open access: yesOpen Biology
Bioluminescence is the production of visible light by living organisms. It occurs through the oxidation of luciferin substrates catalysed by luciferase enzymes.
Laurent Duchatelet   +10 more
doaj   +2 more sources

Design of Ctenophore Ca2+-Regulated Photoprotein Berovin Capable of Being Converted into Active Protein Under Physiological Conditions: Computational and Experimental Approaches [PDF]

open access: yesLife
Here, we describe (1) the AlphaFold-based structural modeling approach to identify amino acids of the photoprotein berovin that are crucial for coelenterazine binding, and (2) the production and characterization of berovin mutants with substitutions of ...
Ludmila P. Burakova   +4 more
doaj   +2 more sources

Advanced Bioluminescence Reporter with Engineered Gaussia Luciferase via Sequence-Guided Mutagenesis [PDF]

open access: yesBiosensors
Gaussia luciferase (GLuc) is the preeminent secreted luciferase widely used in cell-based reporter assays. By employing sequence-guided mutagenesis informed by alignments of diverse copepod luciferase sequences, we identified key amino acids that ...
Vinayakumar Gedi   +3 more
doaj   +2 more sources

Maintain the light, long-term seasonal monitoring of luminous capabilities in the brittle star Amphiura filiformis [PDF]

open access: yesScientific Reports
The European brittle star Amphiura filiformis emits blue light, via a Renilla-like luciferase, which depends on the dietary acquisition of coelenterazine.
Constance Coubris   +7 more
doaj   +2 more sources

The key residue responsible for the red shift of bioluminescence spectra of light-sensitive Ca2+-regulated photoproteins of ctenophores [PDF]

open access: yesScientific Reports
Isoforms of some ctenophore photoproteins show different maxima of bioluminescence spectra— the ones of mnemiopsin and bolinopsin have λmax at 490 and 500 nm, while λmax for velamin isoforms are at 500 and 508 nm.
Ludmila P. Burakova, Eugene S. Vysotski
doaj   +2 more sources

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