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A general purpose RNA-cleaving DNA enzyme.
An in vitro selection procedure was used to develop a DNA enzyme that can be made to cleave almost any targeted RNA substrate under simulated physiological conditions. The enzyme is comprised of aExpand
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Mechanism and utility of an RNA-cleaving DNA enzyme.
We previously reported the in vitro selection of a general-purpose RNA-cleaving DNA enzyme that exhibits a catalytic efficiency (kcat/KM) exceeding that of any other known nucleic acid enzymeExpand
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Addition of p-azido-L-phenylalanine to the genetic code of Escherichia coli.
We report the selection of a new orthogonal aminoacyl tRNA synthetase/tRNA pair for the in vivo incorporation of a photocrosslinker, p-azido-l-phenylalanine, into proteins in response to the amberExpand
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An expanded genetic code with a functional quadruplet codon.
With few exceptions the genetic codes of all known organisms encode the same 20 amino acids, yet all that is required to add a new building block are a unique tRNA/aminoacyl-tRNA synthetase pair, aExpand
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RNA cleavage by a DNA enzyme with extended chemical functionality.
In vitro selection techniques were applied to the development of a DNA enzyme that contains three catalytically essential imidazole groups and catalyzes the cleavage of RNA substrates. Nucleic acidExpand
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An efficient system for the evolution of aminoacyl-tRNA synthetase specificity
A variety of strategies to incorporate unnatural amino acids into proteins have been pursued, but all have limitations with respect to technical accessibility, scalability, applicability to in vivoExpand
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Generation of a bacterium with a 21 amino acid genetic code.
We have generated a completely autonomous bacterium with a 21 amino acid genetic code. This bacterium can biosynthesize a nonstandard amino acid from basic carbon sources and incorporate this aminoExpand
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Directed evolution of the site specificity of Cre recombinase
  • S. Santoro, P. Schultz
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 19 March 2002
Cre recombinase from bacteriophage P1 recognizes a 34-bp recombination site, loxP, with exquisite sequence specificity and catalyzes the site-specific insertion, excision, or rearrangement of DNA. ToExpand
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An archaebacteria-derived glutamyl-tRNA synthetase and tRNA pair for unnatural amino acid mutagenesis of proteins in Escherichia coli.
The addition of novel amino acids to the genetic code of Escherichia coli involves the generation of an aminoacyl-tRNA synthetase and tRNA pair that is 'orthogonal', meaning that it functionsExpand
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Site-specific recombination of asymmetric lox sites mediated by a heterotetrameric Cre recombinase complex.
Previous reports have demonstrated that new Cre recombinase specificities can be developed for symmetrically designed lox mutants through directed evolution. The development of Cre variants thatExpand
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