Pyrrolysine is not hardwired for cotranslational insertion at UAG codons - Test2 - elhamkhani - TriplyDB

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

http://www.wikidata.org/entity/Q24685331

about

Carbon source-dependent expansion of the genetic code in bacteria Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase Stereochemical Basis for Engineered Pyrrolysyl-tRNA Synthetase and the Efficient in Vivo Incorporation of Structurally Divergent Non-native Amino Acids Towards reassigning the rare AGG codon in Escherichia coli Dual functions of codons in the genetic code Optimized orthogonal translation of unnatural amino acids enables spontaneous protein double-labelling and FRET Translation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins.Proteome labeling and protein identification in specific tissues and at specific developmental stages in an animal.Evolution of multiple, mutually orthogonal prolyl-tRNA synthetase/tRNA pairs for unnatural amino acid mutagenesis in Escherichia coli.Polyspecific pyrrolysyl-tRNA synthetases from directed evolution Reducing the genetic code induces massive rearrangement of the proteome.Adding pyrrolysine to the Escherichia coli genetic code.An expanded genetic code in mammalian cells with a functional quadruplet codon.Expanding the library and substrate diversity of the pyrrolysyl-tRNA synthetase to incorporate unnatural amino acids containing conjugated rings.Functional context, biosynthesis, and genetic encoding of pyrrolysine.Noncanonical secondary structure stabilizes mitochondrial tRNA(Ser(UCN)) by reducing the entropic cost of tertiary folding.The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity PylSn and the homologous N-terminal domain of pyrrolysyl-tRNA synthetase bind the tRNA that is essential for the genetic encoding of pyrrolysine The pyrrolysine translational machinery as a genetic-code expansion tool Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acids Genetically encoded cyclopropene directs rapid, photoclick-chemistry-mediated protein labeling in mammalian cells.Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology.[3'-32P]-labeling tRNA with nucleotidyltransferase for assaying aminoacylation and peptide bond formation.Efficient Reassignment of a Frequent Serine Codon in Wild-Type Escherichia coli.Misacylation of pyrrolysine tRNA in vitro and in vivo.Transfer RNA misidentification scrambles sense codon recoding.Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems.Pyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.Rewiring translation - Genetic code expansion and its applications.Expanded genetic code technologies for incorporating modified lysine at multiple sites.BMP2-modified injectable hydrogel for osteogenic differentiation of human periodontal ligament stem cells.Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.Single-Plasmid-Based System for Efficient Noncanonical Amino Acid Mutagenesis in Cultured Mammalian Cells.A versatile platform for single- and multiple-unnatural amino acid mutagenesis in Escherichia coli.Structural clones of UAG decoding RNA.Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.Designer tRNAs for efficient incorporation of non-canonical amino acids by the pyrrolysine system in mammalian cells.

P2860

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P2860

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

http://www.wikidata.org/entity/Q24685331

description

2007 nî lūn-bûn

@nan

2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@ast

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@en

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@nl

type

label

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@ast

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@en

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@nl

prefLabel

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@ast

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@en

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@nl

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P356

PNAS.0611634104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Pyrrolysine is not hardwired for cotranslational insertion at UAG codons

@en

P2093

Alexandre Ambrogelly

http://www.w3.org/2001/XMLSchema#string

Carina Frauer

http://www.w3.org/2001/XMLSchema#string

Carla Polycarpo

http://www.w3.org/2001/XMLSchema#string

Sarath Gundllapalli

http://www.w3.org/2001/XMLSchema#string

Stephanie Herring

http://www.w3.org/2001/XMLSchema#string

P2860

An aminoacyl-tRNA synthetase that specifically activates pyrrolysine

Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants

Expanding the genetic code

Exploring the limits of codon and anticodon size.

RNA-protein interactions in the yeast three-hybrid system: affinity, sensitivity, and enhanced library screening.

Nucleotides that determine Escherichia coli tRNA(Arg) and tRNA(Lys) acceptor identities revealed by analyses of mutant opal and amber suppressor tRNAs.

Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo.

Pyrrolysine and selenocysteine use dissimilar decoding strategies.

The direct genetic encoding of pyrrolysine.

Natural expansion of the genetic code.

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3141-6

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10.1073/PNAS.0611634104

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9

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104

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2007-02-27T00:00:00Z

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6445860

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17360621

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1805618

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