N-acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo.
about
Non-standard amino acid incorporation into proteins using Escherichia coli cell-free protein synthesisPyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion toolExpanded cellular amino acid pools containing phosphoserine, phosphothreonine, and phosphotyrosineTranslation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins.The genetic incorporation of thirteen novel non-canonical amino acidsA Chemical Biology Approach to Reveal Sirt6-targeted Histone H3 Sites in Nucleosomes.Genomes by design.Expanding the genetic code of Mus musculus.Polyspecific pyrrolysyl-tRNA synthetases from directed evolutionCatalyst-free and site-specific one-pot dual-labeling of a protein directed by two genetically incorporated noncanonical amino acidsA genomically modified Escherichia coli strain carrying an orthogonal E. coli histidyl-tRNA synthetase•tRNAHis pair.Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog.Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acidsGenetic code flexibility in microorganisms: novel mechanisms and impact on physiology.Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids.A genetically encoded acrylamide functionality.A facile strategy for selective incorporation of phosphoserine into histones.Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation functionTransfer RNA misidentification scrambles sense codon recoding.Pyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.Upgrading protein synthesis for synthetic biology.Expanded genetic code technologies for incorporating modified lysine at multiple sites.Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion.Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in Escherichia coli.Acetylation Regulates Thioredoxin Reductase Oligomerization and Activity.Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.Continuous directed evolution of aminoacyl-tRNA synthetases.Chemical biology approaches for studying posttranslational modifications.Pyrrolysine Amber Stop-Codon Suppression: Development and Applications.Biochemical Characterization of the Lysine Acetylation of Tyrosyl-tRNA Synthetase in Escherichia coli.Evolving the N-Terminal Domain of Pyrrolysyl-tRNA Synthetase for Improved Incorporation of Noncanonical Amino Acids.Studying the Lysine Acetylation of Malate Dehydrogenase.Orthogonal Protein Translation Using Pyrrolysyl-tRNA Synthetases for Single- and Multiple-Noncanonical Amino Acid Mutagenesis.Kinetics of tRNA(Pyl) -mediated amber suppression in Escherichia coli translation reveals unexpected limiting steps and competing reactions.
P2860
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P2860
N-acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@ast
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@en
type
label
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@ast
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@en
prefLabel
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@ast
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@en
P2093
P1433
P1476
N-acetyl lysyl-tRNA synthetase ...... cificity in vitro and in vivo.
@en
P2093
Hee-Sung Park
Li-Tao Guo
Sangsik Lee
Takuya Umehara
P304
P356
10.1016/J.FEBSLET.2012.01.029
P407
P50
P577
2012-01-28T00:00:00Z