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

Insertion of the T3 DNA polymerase thioredoxin binding domain enhances the processivity and fidelity of Taq DNA polymerase.

Nucleic acids research - 15 Aug 2003

Davidson John F, Fox Richard, Harris Dawn D, Lyons-Abbott Sally, Loeb Lawrence A

Abstract excerpt

Insertion of the T3 DNA polymerase thioredoxin binding domain (TBD) into the distantly related thermostable Taq DNA polymerase at an analogous position in the thumb domain, converts the Taq DNA polymerase from a low processive to a highly processive enzyme. Processivity is dependent on the presen...

Read the complete abstract on PubMed

Topics

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

Share to DNA-Directed DNA Polymerase
Share to DNA Replication
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Insertional

Share to Repetitive Sequences, Nucleic Acid

Share to Streptavidin

Share to Taq Polymerase

Share to Thioredoxins

Source

Open in PubMed Open full text

Identifiers

PMID: 12907710
DOI: 10.1093/nar/gkg667
PMCID: PMC169918

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12907710-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Insertion of the T3 DNA polymerase thioredoxin binding domain enhances the processivity and fidelity of Taq DNA polymerase.PMID 12907710Read ↗

Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase.Semantic proximity Read ↗

Structure of an open conformation of T7 DNA polymerase reveals novel structural features regulating primer-template stabilization at the polymerization active site.Semantic proximity Read ↗

Mutation of Phe102 to Ser in the carboxyl terminal helix of Escherichia coli thioredoxin affects the stability and processivity of T7 DNA polymerase.Semantic proximity Read ↗

DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN.Semantic proximity Read ↗

Thermostable DNA polymerase from Thermus thermophilus B35: preparation and study of a modified form of the enzyme with high affinity to ddNTP.Semantic proximity Read ↗

Generic expansion of the substrate spectrum of a DNA polymerase by directed evolution.Semantic proximity Read ↗

A DddA ortholog-based and transactivator-assisted nuclear and mitochondrial cytosine base editors with expanded target compatibility.Semantic proximity Read ↗

Genome Editing With Targeted DeaminasesSemantic proximity Read ↗

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