Articles with "renilla luciferase" as a keyword



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Trehalose radial networks protect Renilla luciferase helical layers against thermal inactivation.

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Published in 2017 at "International journal of biological macromolecules"

DOI: 10.1016/j.ijbiomac.2017.06.113

Abstract: Renilla luciferase (Rluc) from Renilla reniformis is an appropriate protein reporter for the detection of specific molecular targets due to its bioluminescent feature, although its relatively low stability limits the application. To investigate the effects… read more here.

Keywords: renilla; radial networks; trehalose radial; renilla luciferase ... See more keywords
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Kinetics, structure, and dynamics of Renilla luciferase solvated in binary mixtures of glycerol and water and the mechanism by which glycerol obstructs the enzyme emitter site.

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Published in 2018 at "International journal of biological macromolecules"

DOI: 10.1016/j.ijbiomac.2018.05.160

Abstract: Renilla Luciferase is a bioluminescent enzyme which is broadly implemented as protein reporter in biology-related researches. In this study, new evidences on the kinetics, structure, and dynamics of Renilla luciferase solvated in binary mixtures of… read more here.

Keywords: kinetics structure; structure dynamics; luciferase solvated; luciferase ... See more keywords
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A Split Renilla Luciferase Complementation Assay for the Evaluation of Hsp90/Aha1 Complex Disruptors and Their Activity at the Aha1 C-Terminal Domain.

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Published in 2022 at "ACS chemical biology"

DOI: 10.1021/acschembio.2c00854

Abstract: Disruption of interactions between Hsp90 and the cochaperone protein, Aha1, has emerged as a therapeutic strategy to inhibit Aha1-driven cancer metastasis and tau aggregation in models of tauopathy. A combination of split Renilla luciferase assays… read more here.

Keywords: interactions hsp90; split renilla; aha1; renilla luciferase ... See more keywords
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Medium-Throughput Detection of Hsp90/Cdc37 Protein–Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay

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Published in 2019 at "SLAS Discovery"

DOI: 10.1177/2472555219884033

Abstract: The protein-folding chaperone Hsp90 enables the maturation and stability of various oncogenic signaling proteins and is thus pursued as a cancer drug target. Folding in particular of protein kinases is assisted by the co-chaperone Cdc37.… read more here.

Keywords: protein; hsp90; cdc37; renilla luciferase ... See more keywords