Results 101 to 110 of about 71,291 (119)
Site-Specific Chemical Conjugation of Recombinant Proteins onto the AAV Capsid. [PDF]
Pham Q, Glicksman J, Chatterjee A.
europepmc +1 more source
Machine Learning Enables Prediction of Pyrrolysyl-tRNA Synthetase Substrate Specificity
Knowledge about the substrate scope for a given enzyme is informative for elucidating biochemical pathways and also for expanding applications of the enzyme.
Gang Xu, Haoran Yu, Lirong Yang
exaly +3 more sources
Genetic code expansion has largely focused on the reassignment of amber stop codons to insert single copies of non-canonical amino acids (ncAAs) into proteins.
John D Fisk, Margaret A Schmitt
exaly +2 more sources
Pyrrolysine analogues as substrates for pyrrolysyl-tRNA synthetase [PDF]
In certain methanogenic archaea a new amino acid, pyrrolysine (Pyl), is inserted at in-frame UAG codons in the mRNAs of some methyltransferases. Pyl is directly acylated onto a suppressor tRNAPyl by pyrrolysyl-tRNA synthetase (PylRS).
Carla Polycarpo +2 more
exaly +2 more sources
The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity [PDF]
Pyrrolysine (Pyl) is co-translationally inserted into a subset of proteins in the Methanosarcinaceae and in Desulfitobacterium hafniense programmed by an in-frame UAG stop codon. Suppression of this UAG codon is mediated by the Pyl amber suppressor tRNA,
Carla Polycarpo +2 more
exaly +2 more sources
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Acta Crystallographica Section F: Structural Biology Communications, 2006
Tatsuo Yanagisawa +2 more
exaly
Tatsuo Yanagisawa +2 more
exaly

