An engineered Tetrahymena tRNAGln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. (Q46001070)

18 December 2017

title

An engineered Tetrahymena tRNAGln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. (English)

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18 December 2017

author name string

Saks ME

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18 December 2017

Sampson JR

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18 December 2017

Nowak MW

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18 December 2017

Kearney PC

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18 December 2017

Du F

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18 December 2017

Abelson JN

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18 December 2017

Lester HA

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18 December 2017

Dougherty DA

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18 December 2017

language of work or name

English

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publication date

1 September 1996

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18 December 2017

Journal of Biological Chemistry

published in

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18 December 2017

volume

271

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18 December 2017

issue

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18 December 2017

page(s)

23169-23175

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18 December 2017

Genetic studies of the lac repressor. III. Additional correlation of mutational sites with specific amino acid residues

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A general method for site-specific incorporation of unnatural amino acids into proteins.

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Three Tetrahymena tRNA(Gln) isoacceptors as tools for studying unorthodox codon recognition and codon context effects during protein synthesis in vitro

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ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification

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Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase

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Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution

21 January 2018

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Enzymatic oligoribonucleotide synthesis with T4 RNA ligase

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Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor

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Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors

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A channeled tRNA cycle during mammalian protein synthesis

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Nonsense suppression in eukaryotes: the use of the Xenopus oocyte as an in vivo assay system

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An amber suppressor tRNA gene derived by site-specific mutagenesis: cloning and function in mammalian cells

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.38.23169

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18 December 2017

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18 December 2017