A facile strategy for selective incorporation of phosphoserine into histones.
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Non-standard amino acid incorporation into proteins using Escherichia coli cell-free protein synthesisFrom Chemical Mutagenesis to Post-Expression Mutagenesis: A 50 Year OdysseyRecent developments of engineered translational machineries for the incorporation of non-canonical amino acids into polypeptidesEfficient genetic encoding of phosphoserine and its nonhydrolyzable analogA flexible codon in genomically recoded Escherichia coli permits programmable protein phosphorylationRobust production of recombinant phosphoproteins using cell-free protein synthesisA chemical biology route to site-specific authentic protein modificationsRepurposing the translation apparatus for synthetic biologyChemical and biological tools for the preparation of modified histone proteinsTranslation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins.Engineering the elongation factor Tu for efficient selenoprotein synthesis.Negative regulation of NF-κB activity by brain-specific TRIpartite Motif protein 9.Improving cell-free protein synthesis through genome engineering of Escherichia coli lacking release factor 1In Vitro Selection Combined with Ribosomal Translation Containing Non-proteinogenic Amino Acids.Akt Kinase-Mediated Checkpoint of cGAS DNA Sensing PathwayChemical Methods for Encoding and Decoding of Posttranslational ModificationsTransfer RNA misidentification scrambles sense codon recoding.Expanding the genetic code of Salmonella with non-canonical amino acids.Touch, act and go: landing and operating on nucleosomes.Synthetic approaches to protein phosphorylation.Expanding the genetic code of Escherichia coli with phosphotyrosine.Dopamine and Cu+/2+ can induce oligomerization of α-synuclein in the absence of oxygen: Two types of oligomerization mechanisms for α-synuclein and related cell toxicity studies.Rewriting the Genetic Code.Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.Chemical biology approaches for studying posttranslational modifications.Effects of Heterologous tRNA Modifications on the Production of Proteins Containing Noncanonical Amino Acids.Expression of Recombinant Phosphoproteins for Signal Transduction Studies.A radical approach to posttranslational mutagenesis.Generation of phospho-ubiquitin variants by orthogonal translation reveals codon skipping.Genetic code expansion and live cell imaging reveal that Thr308 phosphorylation is irreplaceable and sufficient for Akt1 activity.Click chemistry for targeted protein ubiquitylation and ubiquitin chain formationPhosphorylation-Dependent Inhibition of Akt1
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A facile strategy for selective incorporation of phosphoserine into histones.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 26 March 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A facile strategy for selective incorporation of phosphoserine into histones.
@en
A facile strategy for selective incorporation of phosphoserine into histones.
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type
label
A facile strategy for selective incorporation of phosphoserine into histones.
@en
A facile strategy for selective incorporation of phosphoserine into histones.
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prefLabel
A facile strategy for selective incorporation of phosphoserine into histones.
@en
A facile strategy for selective incorporation of phosphoserine into histones.
@nl
P2093
P2860
P356
P1476
A facile strategy for selective incorporation of phosphoserine into histones
@en
P2093
Daeyoup Lee
Dieter Söll
Hee-Sung Park
Sangsik Lee
Seunghee Oh
P2860
P304
P356
10.1002/ANIE.201300531
P407
P50
P577
2013-03-26T00:00:00Z