A slow but steady nanoLuc: R162A mutation results in a decreased, but stable, nanoLuc activity-Reference-Cited by-同舟云学术

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A slow but steady nanoLuc: R162A mutation results in a decreased, but stable, nanoLuc activity

Published:2024-06 Issue: Volume:269 Page:131864
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Ahmed Wesam S.^ORCID,Geethakumari Anupriya M.^ORCID,Sultana Asfia^ORCID,Fatima Asma^ORCID,Philip Angelin M.^ORCID,Uddin S.M. Nasir^ORCID,Biswas Kabir H.^ORCID

Funder

Hamad Bin Khalifa University

Publisher

Elsevier BV

Reference85 articles.

1. In Memoriam Dr Marlene Deluca;Kricka,1989

2. Effects of synonymous mutations on kinetic properties and structure of firefly luciferase: molecular dynamics simulation, molecular docking, RNA folding, and experimental study;Mortazavi;Int. J. Biol. Macromol.,2023

3. Mutation of conserved residues K329 and R330 on the surface of firefly luciferase: effect on proteolytic degradation;Jarchi;Int. J. Biol. Macromol.,2018

4. Bifunctional role of leucine 300 of firefly luciferase in structural rigidity;Yousefi;Int. J. Biol. Macromol.,2017

5. Biosynthetic bifunctional enzyme complex with high-efficiency luciferin-recycling to enhance the bioluminescence imaging;Sun;Int. J. Biol. Macromol.,2019

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