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

Characterisation of a DNA polymerase highly mutated along the template binding interface.

Molecular biotechnology - 1 Sept 2010

Vichier-Guerre Sophie, Jestin Jean-Luc

Abstract excerpt

Phage display establishes a link between a polypeptide and its corresponding gene. It has been much used for the isolation of proteins binding to chosen molecular targets. A second link was designed more recently between a phage-displayed enzyme and its reaction product. Affinity chromatography for the product then allows the isolation of catalytically active enzymes and of their genes. Using this strategy, a...

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 Kinetics
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Templates, Genetic

Share to Thermus

Source

Identifiers

PMID: 20407851
DOI: 10.1007/s12033-010-9275-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterisation of a DNA polymerase highly mutated along the template binding interface.PMID 20407851Read ↗

A population of thermostable reverse transcriptases evolved from Thermus aquaticus DNA polymerase I by phage display.Semantic proximity Read ↗

Engineering of DNA polymerase I from Thermus thermophilus using compartmentalized self-replication.Semantic proximity Read ↗

Molecular diversity and catalytic activity of Thermus DNA polymerases.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 ↗

Selection of a T7 promoter mutant with enhanced in vitro activity by a novel multi-copy bead display approach for in vitro evolution.Semantic proximity Read ↗

Directed evolution of DNA polymerase, RNA polymerase and reverse transcriptase activity in a single polypeptide.Semantic proximity Read ↗

ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.Semantic proximity Read ↗

Dissection of two hallmarks of the open promoter complex by mutation in an RNA polymerase core subunit.Semantic proximity Read ↗

A phage display technique for a fast, sensitive, and systematic investigation of protein-protein interactions.Semantic proximity Read ↗

Functional display of human plasminogen-activator inhibitor 1 (PAI-1) on phages: novel perspectives for structure-function analysis by error-prone DNA synthesisSemantic proximity Read ↗

Directed evolution of the DnaK chaperone: mutations in the lid domain result in enhanced chaperone activity.Semantic proximity Read ↗

Mutations in the palm subdomain of Twa DNA polymerase to enhance PCR efficiency and its function analysis.Semantic proximity Read ↗

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