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

Learning from directed evolution: Thermus aquaticus DNA polymerase mutants with translesion synthesis activity.

Chembiochem : a European journal of chemical biology - 4 Jul 2011

Obeid Samra, Schnur Andreas, Gloeckner Christian, Blatter Nina, Welte Wolfram, Diederichs Kay, Marx Andreas

Abstract excerpt

DNA is being constantly damaged by endo- and exogenous agents such as reactive oxygen species, chemicals, radioactivity, and ultraviolet radiation. Additionally, DNA is inherently labile, and this can result in, for example, the spontaneous hydrolysis of the glycosidic bond that connects the sugar and the nucleobase moieties in DNA; this results in abasic sites. It has long been obscure how cells achieve DNA...

Read the complete abstract on PubMed

Topics

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

Share to Directed Molecular Evolution
Share to DNA Damage

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutant Proteins

Share to Mutation

Share to Protein Conformation

Share to Taq Polymerase

Share to Thermus

Source

Identifiers

PMID: 21480455
DOI: 10.1002/cbic.201000783

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

Learning from directed evolution: Thermus aquaticus DNA polymerase mutants with translesion synthesis activity.PMID 21480455Read ↗

A single highly mutable catalytic site amino acid is critical for DNA polymerase fidelity.Semantic proximity Read ↗

Design and Discovery of New Combinations of Mutant DNA Polymerases and Modified DNA Substrates.Semantic proximity Read ↗

Directed DNA polymerase evolution: effects of mutations in motif C on the mismatch-extension selectivity of thermus aquaticus DNA polymerase.Semantic proximity Read ↗

DNA polymerase active site is highly mutable: evolutionary consequences.Semantic proximity Read ↗

Translesion DNA synthesis: little fingers teach tolerance.Semantic proximity Read ↗

A conservative isoleucine to leucine mutation causes major rearrangements and cold sensitivity in KlenTaq1 DNA polymerase.Semantic proximity Read ↗

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

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

Cold-sensitive mutants of Taq DNA polymerase provide a hot start for PCR.Semantic proximity Read ↗

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

Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase I.Semantic proximity Read ↗

An evolved, orthogonal ssDNA generator for targeted hypermutation of multiple genomic loci.Semantic proximity Read ↗

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