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

Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code.

PloS one - 1 Jan 2012

Nehring Sebastian, Budisa Nediljko, Wiltschi Birgit

Abstract excerpt

BACKGROUND: The suppression of amber stop codons with non-canonical amino acids (ncAAs) is used for the site-specific introduction of many unusual functions into proteins. Specific orthogonal aminoacyl-tRNA synthetase (o-aaRS)/amber suppressor tRNA(CUA) pairs (o-pairs) for the incorporation of ncAAs in S. cerevisiae were previously selected from an E. coli tyrosyl-tRNA synthetase/tRNA(CUA) mutant library....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acyl-tRNA Synthetases
Share to Codon, Terminator
Share to Eukaryota

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

Share to Genetic Code

Share to Genetic Engineering

Share to Genomic Library

Share to RNA, Transfer

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 22493661
DOI: 10.1371/journal.pone.0031992
PMCID: PMC3320878

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

Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code.PMID 22493661Read ↗

Continuous Hypermutation and Evolution of Noncanonical Amino Acid Synthases.Semantic proximity Read ↗

An Orthogonal Tyrosyl-tRNA Synthetase/tRNA Pair from a Thermophilic Bacterium for an Expanded Eukaryotic Genetic Code.Semantic proximity Read ↗

Directed evolution of aminoacyl-tRNA synthetases through in vivo hypermutation.Semantic proximity Read ↗

Incorporation of non-canonical amino acids into proteins in yeast.Semantic proximity Read ↗

Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion.Semantic proximity Read ↗

Two-Tier Screening Platform for Directed Evolution of Aminoacyl-tRNA Synthetases with Enhanced Stop Codon Suppression Efficiency.Semantic proximity Read ↗

An improved system for the generation and analysis of mutant proteins containing unnatural amino acids in Saccharomyces cerevisiae.Semantic proximity Read ↗

Progress toward the evolution of an organism with an expanded genetic code.Semantic proximity Read ↗

Genetic code expansion in mammalian cellsSemantic proximity Read ↗

Evolving Orthogonal Suppressor tRNAs To Incorporate Modified Amino Acids.Semantic proximity Read ↗

Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria.Semantic proximity Read ↗

Mutually orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs.Semantic proximity Read ↗

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