Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells - Test2 - elhamkhani - TriplyDB

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

http://www.wikidata.org/entity/Q24562667

about

Expanding the genetic code for biological studies Scorpion toxins specific for potassium (K+) channels: a historical overview of peptide bioengineering Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion Importance of single molecular determinants in the fidelity of expanded genetic codes Quasiracemic Crystallization as a Tool To Assess the Accommodation of Noncanonical Residues in Nativelike Protein Conformations Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells In vitro incorporation of nonnatural amino acids into protein using tRNA(Cys)-derived opal, ochre, and amber suppressor tRNAs A novel method for observing proteins in vivo using a small fluorescent label and multiphoton imaging Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 2: evaluating suppression efficiency.Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 1: minimizing misacylation Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity Transforming a pair of orthogonal tRNA-aminoacyl-tRNA synthetase from Archaea to function in mammalian cells.Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion Fluorescent analogs of biomolecular building blocks: design, properties, and applications.Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA Genetically encoded libraries of nonstandard peptides.In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression.Protein conjugation with genetically encoded unnatural amino acids.Noncanonical amino acids in the interrogation of cellular protein synthesis N-Terminally extended analogues of the K⁺ channel toxin from Stichodactyla helianthus as potent and selective blockers of the voltage-gated potassium channel Kv1.3.Designing novel spectral classes of proteins with a tryptophan-expanded genetic code.Phosphoproteomics in analyzing signaling pathways.The many applications of acid urea polyacrylamide gel electrophoresis to studies of tRNAs and aminoacyl-tRNA synthetases.Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog.Incorporation of 5-hydroxytryptophan into transferrin and its receptor allows assignment of the pH induced changes in intrinsic fluorescence when iron is released.Ribosomal synthesis of nonstandard peptides.Single-molecule imaging of a fluorescent unnatural amino acid incorporated into nicotinic receptors Glycosylated hydroxytryptophan in a mussel adhesive protein from Perna viridis Incorporation of unnatural amino acids for synthetic biology.Complete set of orthogonal 21st aminoacyl-tRNA synthetase-amber, ochre and opal suppressor tRNA pairs: concomitant suppression of three different termination codons in an mRNA in mammalian cells.Antibody microarrays utilizing site-specific antibody-oligonucleotide conjugates.Performance improvement of microbial fuel cell (MFC) using suitable electrode and Bioengineered organisms: A review.Designing logical codon reassignment - Expanding the chemistry in biology.Cellular encoding of Cy dyes for single-molecule imaging.The central role of tRNA in genetic code expansion.Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis.Expanding the genetic code in a mammalian cell line by the introduction of four-base codon/anticodon pairs.Codon reassignment to facilitate genetic engineering and biocontainment in the chloroplast of Chlamydomonas reinhardtii.Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms.Structure and activity of an aminoacyl-tRNA synthetase that charges tRNA with nitro-tryptophan.

P2860

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P2860

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

http://www.wikidata.org/entity/Q24562667

description

2004 nî lūn-bûn

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2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2004 թվականի հունիսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@ast

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@en

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@nl

type

label

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@ast

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@en

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@nl

prefLabel

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@ast

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@en

Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@nl

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

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Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells

@en

P2093

Badry Bursulaya

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

David S King

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

Feng Tian

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

Peter G Schultz

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

Sean Uryu

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

Zhiwen Zhang

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

P2860

Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells.

Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

2.9 Å crystal structure of ligand-free tryptophanyl-tRNA synthetase: Domain movements fragment the adenine nucleotide binding site

Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain

Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression

An expanded eukaryotic genetic code

Expanding the genetic code of Escherichia coli

Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli.

Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains

Addition of the keto functional group to the genetic code of Escherichia coli.

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8882-8887

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scholarly article

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10.1073/PNAS.0307029101

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24

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101

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2004-06-08T00:00:00Z

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8520299

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15187228

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428441

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