Matches in SemOpenAlex for { <https://semopenalex.org/work/W97567589> ?p ?o ?g. }
Showing items 1 to 71 of
71
with 100 items per page.
- W97567589 abstract "The genetic code of most organisms was evolved to encode 20 amino acids. Although the ability to encode 20 amino acids provides the basis to translate proteins necessary for life, researchers are also limited to these 20 amino acids for conventional site-directed mutagenesis. The ability to encode unnatural amino acids provides researchers the ability to circumvent the limitation imposed by the genetic code. Genetically encoding unnatural amino acids provides researchers the means to not only mimic naturally occurring posttranslational modifications but also the ability to encode amino acids with new physical or chemical properties to study biological processes. The incorporation of unnatural amino acids into proteins had been developed in Escherichia coli and also in yeast. We have developed a methodology to genetically incorporate unnatural amino acids in mammalian cells in response to an amber codon (UAG). The incorporation of unnatural amino acids is high in E. coli and yeast, but the incorporation in mammalian cells is relatively low. In addition to developing the system to incorporate unnatural amino acids in mammalian cells, we have also improved suppression efficiencies by modifying the synthetase and unnatural amino acid. To incorporate unnatural amino acids in response to an amber codon, the tRNA anticodon is mutated from a GUA to a CUA. We were able to show that engineering the anticodon-binding domain of the synthetase could enhance the recognition of the tRNA and thus increased suppression efficiencies. Furthermore, by masking the carboxyl group of the amino acid by an ester group, we were able to increase the bioavailability of an unnatural amino acid to further increase suppression efficiencies. Most evolved synthetases aminoacylate unnatural amino acids that are structurally similar to the native substrate of the wild- type synthetase. We were able to adapt Methanosarcina mazei pyrrolysine synthetase (PylRS) to charge a considerable disparate amino acid from its native substrate, O-methyl-L-tyrosine. In addition, the X-ray crystal structure was solved for the evolved PylRS complexed with O-methyl-L-tyrosine at 1.75A. This multifaceted approach provides the basis to engineer the PylRS to incorporate a significantly diverse selection of unnatural amino acids than previously anticipated" @default.
- W97567589 created "2016-06-24" @default.
- W97567589 creator A5075720029 @default.
- W97567589 date "2011-01-01" @default.
- W97567589 modified "2023-09-27" @default.
- W97567589 title "Unnatural amino acid incorporation for genetic code expansion in mammalian cells" @default.
- W97567589 hasPublicationYear "2011" @default.
- W97567589 type Work @default.
- W97567589 sameAs 97567589 @default.
- W97567589 citedByCount "0" @default.
- W97567589 crossrefType "journal-article" @default.
- W97567589 hasAuthorship W97567589A5075720029 @default.
- W97567589 hasConcept C104317684 @default.
- W97567589 hasConcept C105580179 @default.
- W97567589 hasConcept C10853874 @default.
- W97567589 hasConcept C149364088 @default.
- W97567589 hasConcept C153957851 @default.
- W97567589 hasConcept C16318435 @default.
- W97567589 hasConcept C20580545 @default.
- W97567589 hasConcept C2779222958 @default.
- W97567589 hasConcept C2779315393 @default.
- W97567589 hasConcept C2910418148 @default.
- W97567589 hasConcept C501734568 @default.
- W97567589 hasConcept C515207424 @default.
- W97567589 hasConcept C547475151 @default.
- W97567589 hasConcept C55493867 @default.
- W97567589 hasConcept C67705224 @default.
- W97567589 hasConcept C86803240 @default.
- W97567589 hasConceptScore W97567589C104317684 @default.
- W97567589 hasConceptScore W97567589C105580179 @default.
- W97567589 hasConceptScore W97567589C10853874 @default.
- W97567589 hasConceptScore W97567589C149364088 @default.
- W97567589 hasConceptScore W97567589C153957851 @default.
- W97567589 hasConceptScore W97567589C16318435 @default.
- W97567589 hasConceptScore W97567589C20580545 @default.
- W97567589 hasConceptScore W97567589C2779222958 @default.
- W97567589 hasConceptScore W97567589C2779315393 @default.
- W97567589 hasConceptScore W97567589C2910418148 @default.
- W97567589 hasConceptScore W97567589C501734568 @default.
- W97567589 hasConceptScore W97567589C515207424 @default.
- W97567589 hasConceptScore W97567589C547475151 @default.
- W97567589 hasConceptScore W97567589C55493867 @default.
- W97567589 hasConceptScore W97567589C67705224 @default.
- W97567589 hasConceptScore W97567589C86803240 @default.
- W97567589 hasLocation W975675891 @default.
- W97567589 hasOpenAccess W97567589 @default.
- W97567589 hasPrimaryLocation W975675891 @default.
- W97567589 hasRelatedWork W2000144032 @default.
- W97567589 hasRelatedWork W2039549031 @default.
- W97567589 hasRelatedWork W2056473913 @default.
- W97567589 hasRelatedWork W2061377697 @default.
- W97567589 hasRelatedWork W2063340676 @default.
- W97567589 hasRelatedWork W2065073611 @default.
- W97567589 hasRelatedWork W2102971391 @default.
- W97567589 hasRelatedWork W2148123458 @default.
- W97567589 hasRelatedWork W2156370777 @default.
- W97567589 hasRelatedWork W280247641 @default.
- W97567589 hasRelatedWork W3112210423 @default.
- W97567589 hasRelatedWork W1885074239 @default.
- W97567589 hasRelatedWork W2592303599 @default.
- W97567589 hasRelatedWork W2759033518 @default.
- W97567589 hasRelatedWork W2784883230 @default.
- W97567589 hasRelatedWork W2844378069 @default.
- W97567589 hasRelatedWork W302314857 @default.
- W97567589 hasRelatedWork W3095371396 @default.
- W97567589 hasRelatedWork W3105078088 @default.
- W97567589 hasRelatedWork W3137920361 @default.
- W97567589 isParatext "false" @default.
- W97567589 isRetracted "false" @default.
- W97567589 magId "97567589" @default.
- W97567589 workType "article" @default.