Results 51 to 60 of about 71,291 (119)

Genetic Encoding and Labeling of Aliphatic Azides and Alkynes in Recombinant Proteins via a Pyrrolysyl-tRNA Synthetase/tRNACUA Pair and Click Chemistry

open access: yes, 2016
Genetic Encoding and Labeling of Aliphatic Azides and Alkynes in Recombinant Proteins via a Pyrrolysyl-tRNA Synthetase/tRNACUA Pair and Click ...
Duy P. Nguyen (1278852)   +5 more
core   +1 more source

Genetic Code Expanded T Cell for Controllable Immunotherapy

open access: yesAdvanced Science, Volume 13, Issue 41, 22 July 2026.
Our GCE‐CAR‐T cells enables tight, dose‐dependent, and function‐preserving control of CAR expression at the translational level through amber codon suppression and genetic incorporation of ncAA. ABSTRACT Chimeric antigen receptor (CAR)‐T cell therapy has demonstrated curative potential against hematologic malignancies, but its clinical application ...
Xue Wang   +4 more
wiley   +1 more source

Genetic incorporation of D-Lysine into diketoreductase in Escherichia coli cells [PDF]

open access: yes, 2012
D-Lysine has been genetically introduced into diketoreductase in E. coli cells by utilization of an orthogonal Ph tRNA /Lysyl-tRNA synthetase pair.
Xin Yang   +4 more
core  

Genetic Incorporation of Histidine Derivatives Using an Engineered Pyrrolysyl-tRNA Synthetase

open access: yes, 2015
A polyspecific amber suppressor aminoacyl-tRNA synthetase/tRNA pair was evolved that genetically encodes a series of histidine analogues in both Escherichia coli and mammalian cells. In combination with tRNACUAPyl, a pyrrolysyl-tRNA synthetase mutant was
Han Xiao (373894)   +5 more
core   +1 more source

Aminoacylation of tRNA 2′- or 3′-hydroxyl by phosphoseryl- and pyrrolysyl-tRNA synthetases [PDF]

open access: yes, 2013
Class I and II aminoacyl-tRNA synthetases (AARSs) attach amino acids to the 2′- and 3′-OH of the tRNA terminal adenosine, respectively. One exception is phenylalanyl-tRNA synthetase (PheRS), which belongs to Class II but attaches phenylalanine to the 2 ...
O’Donoghue, Patrick   +5 more
core   +1 more source

Comparative evaluation of noncanonical amino acids as site‐specific NMR probes for the complex of E. coli SSB with single‐stranded DNA without isotope labelling

open access: yesThe FEBS Journal, Volume 293, Issue 12, Page 3601-3620, June 2026.
Genetic encoding of noncanonical amino acids (ncAA) enables their site‐specific installation in proteins. This work compares the nuclear magnetic resonance (NMR) performance of different ncAAs in a large protein−DNA complex (~ 100 kDa) without isotope labelling. The ncAAs deliver readily detectable NMR signals in the complex between E.
Sreelakshmi Mekkattu Tharayil   +7 more
wiley   +1 more source

Rapid Identification of Functional Pyrrolysyl-tRNA Synthetases via Fluorescence-Activated Cell Sorting

open access: yes, 2018
The orthogonal pyrrolysyl-tRNA synthetase/tRNACUA pair and their variants have provided powerful tools for expanding the genetic code to allow for engineering of proteins with augmented structure and function not present in Nature.
Andrew E. Lin, Qing Lin
core   +1 more source

The Engineering and Optimization of Pyrrolysyl-Synthetase as a Tool for Noncanonical Amino Acid Incorporation [PDF]

open access: yes, 2018
Since the discovery of pyrrolysine as the 22nd amino acid, the field of chemical biology has expanded tremendously with important developments made in genetic noncanonical amino acid (ncAA) incorporation based on the pyrrolysine incorporation machinery ...
Sharma, Vangmayee
core   +2 more sources

Facile Synthesis of H‐L‐Photo‐Lysine and Its Genetic Incorporation Into Proteins

open access: yesChemBioChem, Volume 27, Issue 10, 27 May 2026.
An efficient synthesis of a diazirine‐based noncanonical amino acid (ncAA), photo‐lysine (photoK), is reported, and its genetic incorporation into green fluorescent protein (GFP) is demonstrated. PhotoK‐enabled crosslinking is used to capture substrates and interaction partners of SIRT6 in vitro, in Escherichia coli, and in HEK293 cell lysates ...
Abu Hamza, Chiranjeev Sharma, Yana Cen
wiley   +1 more source

Aufklärung des Wirkmechanismus der Synthetase: Das Dimer der Pyrrolysyl‐tRNA‐Synthetase nutzt sekundäre Bindungsstellen in der Zelle

open access: yesAngewandte Chemie, Volume 138, Issue 18, 27 April 2026.
Das Dimer der Pyrrolysyl‐tRNA‐Synthetase zeigt im katalytischen Zyklus einen alternierenden Wirkmodus seiner Monomere, der durch die Belegung sekundärer Bindungsstellen an den Intermonomer‐Grenzflächen außerhalb der katalytischen Bindungsstelle realisiert wird.
Jessica Dröden   +6 more
wiley   +1 more source

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