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Incorporation of unnatural amino acids for synthetic biology
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1 of the 155 references listed on this page is in the Retraction Watch database as retracted (export 2026-10-28): 10.1126/science.1089509 (notice 2009-11-27).
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/anie.200454036openalex-snapshotAlternative Translations of a Single RNA Message: An Identity Switch of (2S,3R)‐4,4,4‐Trifluorovaline between Valine and Isoleucine Codons
inferredcites →https://doi.org/10.1002/anie.200700779openalex-snapshotHigh‐Throughput Screening for Methionyl‐tRNA Synthetases That Enable Residue‐Specific Incorporation of Noncanonical Amino Acids into Recombinant Proteins in Bacterial Cells
inferredcites →https://doi.org/10.1002/cbic.200400052openalex-snapshotCotranslational Incorporation of a Structurally Diverse Series of Proline Analogues in an Escherichia coli Expression System
inferredcites →https://doi.org/10.1002/cbic.200800164openalex-snapshotBiosynthesis and Stability of Coiled‐Coil Peptides Containing (2S,4R)‐5,5,5‐Trifluoroleucine and (2S,4S)‐5,5,5‐Trifluoroleucine
inferredcites →https://doi.org/10.1007/s002530100791openalex-snapshotIntroduction of specialty functions by the position-specific incorporation of nonnatural amino acids into proteins through four-base codon/anticodon pairs
inferredcites →https://doi.org/10.1016/0014-5793(95)00408-2openalex-snapshotRelaxing the substrate specificity of an aminoacyl‐tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids
inferredcites →https://doi.org/10.1016/j.bmcl.2007.07.107openalex-snapshotFluorinated chloramphenicol acetyltransferase thermostability and activity profile: Improved thermostability by a single-isoleucine mutant
inferredcites →https://doi.org/10.1016/s0040-4020(00)00833-4openalex-snapshotProtein Engineering by In Vivo Incorporation of Non-Natural Amino Acids: Control of Incorporation of Methionine Analogues by Methionyl-tRNA Synthetase
inferredcites →https://doi.org/10.1021/bi00189a013openalex-snapshotSubstrate Specificity Is Determined by Amino Acid Binding Pocket Size in Escherichia coli Phenylalanyl-tRNA Synthetase
inferredcites →https://doi.org/10.1021/bi011381bopenalex-snapshotElucidation of Solvent Exposure, Side-Chain Reactivity, and Steric Demands of the Trifluoromethionine Residue in a Recombinant Protein
inferredcites →https://doi.org/10.1021/bi026130xopenalex-snapshotAttenuation of the Editing Activity of theEscherichia coliLeucyl-tRNA Synthetase Allows Incorporation of Novel Amino Acids into Proteins in Vivo
inferredcites →https://doi.org/10.1021/bi980219eopenalex-snapshotEnzymes Harboring Unnatural Amino Acids: Mechanistic and Structural Analysis of the Enhanced Catalytic Activity of a Glutathione Transferase Containing 5-Fluorotryptophan,
inferredcites →https://doi.org/10.1021/ja016652kopenalex-snapshotBiosynthesis of a Highly Stable Coiled-Coil Protein Containing Hexafluoroleucine in an Engineered Bacterial Host
inferredcites →https://doi.org/10.1021/ja0177096openalex-snapshotA Designed Phenylalanyl-tRNA Synthetase Variant Allows Efficient in Vivo Incorporation of Aryl Ketone Functionality into Proteins
inferredcites →https://doi.org/10.1021/ja0626281openalex-snapshotDesign of a Bacterial Host for Site-Specific Incorporation of p-Bromophenylalanine into Recombinant Proteins
inferredcites →https://doi.org/10.1021/ja064661topenalex-snapshotSite-Specific Incorporation of a 19F-Amino Acid into Proteins as an NMR Probe for Characterizing Protein Structure and Reactivity
inferredcites →https://doi.org/10.1038/nbt1013openalex-snapshotThe site-specific incorporation of p-iodo-L-phenylalanine into proteins for structure determination
inferredcites →https://doi.org/10.1038/nmeth752openalex-snapshotPhoto-leucine and photo-methionine allow identification of protein-protein interactions in living cells
inferredcites →https://doi.org/10.1038/nprot.2007.52openalex-snapshotLabeling, detection and identification of newly synthesized proteomes with bioorthogonal non-canonical amino-acid tagging
inferredcites →https://doi.org/10.1073/pnas.0601637103openalex-snapshotSelective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
inferredcites →https://doi.org/10.1073/pnas.95.2.455openalex-snapshotResidue-specific bioincorporation of non-natural, biologically active amino acids into proteins as possible drug carriers: Structure and stability of the per -thiaproline mutant of annexin V
inferredcites →https://doi.org/10.1074/jbc.271.33.19991openalex-snapshotProbing the Structure and Function of the Tachykinin Neurokinin-2 Receptor through Biosynthetic Incorporation of Fluorescent Amino Acids at Specific Sites
inferredcites →https://doi.org/10.1074/jbc.m707355200openalex-snapshotSite-specific Incorporation of Keto Amino Acids into Functional G Protein-coupled Receptors Using Unnatural Amino Acid Mutagenesis
inferredcites →https://doi.org/10.1093/nar/gkl087openalex-snapshotIn vitro selection of tRNAs for efficient four-base decoding to incorporate non-natural amino acids into proteins in an Escherichia coli cell-free translation system
inferredcites →https://doi.org/10.1093/nar/gnj003openalex-snapshotFour-base codon mediated mRNA display to construct peptide libraries that contain multiple nonnatural amino acids
inferredcites →https://doi.org/10.1186/1471-2091-6-21openalex-snapshotNonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease
inferredcites →https://doi.org/10.1261/rna.666807openalex-snapshotImproved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 1: Minimizing misacylation
inferredcites →https://doi.org/10.1261/rna.667607openalex-snapshotImproved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 2: Evaluating suppression efficiency
inferredcites →https://doi.org/10.1263/jbb.102.511openalex-snapshotDesign of carrier tRNAs and selection of four-base codons for efficient incorporation of various nonnatural amino acids into proteins in Spodoptera frugiperda 21 (Sf21) insect cell-free translation system
inferredcites →https://doi.org/10.1263/jbb.99.473openalex-snapshotFour-base codon-mediated incorporation of nonnatural amino acids into proteins in a eukaryotic cell-free translation system
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/prot.23009openalex-snapshotIntegrating the intrinsic conformational preferences of noncoded α‐amino acids modified at the peptide bond into the noncoded amino acids database
inferred← citeshttps://doi.org/10.1007/bf03261880openalex-snapshotSite-Specific PEGylation of Therapeutic Proteins via Optimization of Both Accessible Reactive Amino Acid Residues and PEG Derivatives
inferred← citeshttps://doi.org/10.1007/s00726-012-1450-4openalex-snapshot4-[18F]Fluoro-N-methyl-N-(propyl-2-yn-1-yl)benzenesulfonamide ([18F]F-SA): a versatile building block for labeling of peptides, proteins and oligonucleotides with fluorine-18 via Cu(I)-mediated click chemistry
inferred← citeshttps://doi.org/10.1021/bm3005116openalex-snapshotModulating Supramolecular Assemblies and Mechanical Properties of Engineered Protein Materials by Fluorinated Amino Acids
inferred← citeshttps://doi.org/10.1039/c0mb00154fopenalex-snapshotEnhancing the thermal stability of a single-chain Fv fragment by in vivo global fluorination of the proline residues
inferred← citeshttps://doi.org/10.1039/c2ob06684jopenalex-snapshotSite specific chemoselective labelling of proteins with robust and highly sensitive Ru(ii) bathophenanthroline complexes
inferred← citeshttps://doi.org/10.1039/c2ob06922aopenalex-snapshotOrganic fluorine as a polypeptide building element: in vivo expression of fluorinated peptides, proteins and proteomes
inferred← citeshttps://doi.org/10.1039/c4ob00294fopenalex-snapshotZinc mediated allylations of chlorosilanes promoted by ultrasound: Synthesis of novel constrained sila amino acids
inferred← citeshttps://doi.org/10.1039/c5ob00375jopenalex-snapshotStereoselective Pd-catalyzed etherification and asymmetric synthesis of furanomycin and its analogues from a chiral aziridine
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