Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Thermostabilization of firefly luciferase by in vivo directed evolution.

Protein engineering, design & selection : PEDS - 1 Nov 2011

Koksharov Mikhail I, Ugarova Natalia N

Abstract excerpt

Firefly luciferase is widely used in a number of areas of biotechnology and molecular biology. However, rapid inactivation of wild-type (WT) luciferases at elevated temperatures often hampers their application. A simple non-lethal in vivo screening scheme was used to identify thermostable mutants of luciferase in Escherichia coli colonies. This scheme allowed carrying out each cycle of mutagenesis in a rapid and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Biocatalysis
Share to Directed Molecular Evolution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Half-Life

Share to Hot Temperature

Share to Luciferases, Firefly

Share to Luminescent Measurements

Source

Identifiers

PMID: 21900306
DOI: 10.1093/protein/gzr044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thermostabilization of firefly luciferase by in vivo directed evolution.PMID 21900306Read ↗

Triple substitution G216N/A217L/S398M leads to the active and thermostable Luciola mingrelica firefly luciferase.Semantic proximity Read ↗

Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354.Semantic proximity Read ↗

Continuous Hypermutation and Evolution of Luciferase Variants.Semantic proximity Read ↗

Design and characterization of novel trypsin-resistant firefly luciferases by site-directed mutagenesis.Semantic proximity Read ↗

Expression and characterization of the Renilla luciferase with the cumulative mutation.Semantic proximity Read ↗

Glow-type conversion and characterization of a minimal luciferase via mutational analyses.Semantic proximity Read ↗

Directed molecular evolution reveals Gaussia luciferase variants with enhanced light output stability.Semantic proximity Read ↗

Elicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue.Semantic proximity Read ↗

Color-shifting mutations in the C-domain of L. mingrelica firefly luciferase provide new information about the domain alternation mechanism.Semantic proximity Read ↗

Thermostable red and green light-producing firefly luciferase mutants for bioluminescent reporter applications.Semantic proximity Read ↗

The effective role of positive charge saturation in bioluminescence color and thermostability of firefly luciferase.Semantic proximity Read ↗

Advanced Bioluminescence Reporter with Engineered Gaussia Luciferase via Sequence-Guided Mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.