Results 21 to 30 of about 810 (104)

Structural basis for the site-specific incorporation of lysine derivatives into proteins. [PDF]

open access: yesPLoS ONE, 2014
Posttranslational modifications (PTMs) of proteins determine their structure-function relationships, interaction partners, as well as their fate in the cell and are crucial for many cellular key processes.
Veronika Flügel   +2 more
doaj   +1 more source

Synthesis of non-linear protein dimers through a genetically encoded Thiol-ene reaction. [PDF]

open access: yesPLoS ONE, 2014
Site-specific incorporation of bioorthogonal unnatural amino acids into proteins provides a useful tool for the installation of specific functionalities that will allow for the labeling of proteins with virtually any probe.
Jessica Torres-Kolbus   +3 more
doaj   +1 more source

Ferritin Conjugates With Multiple Clickable Amino Acids Encoded by C-Terminal Engineered Pyrrolysyl-tRNA Synthetase

open access: yesFrontiers in Chemistry, 2021
This study reports the application of expanding genetic codes in developing protein cage-based delivery systems. The evolved Methanosarcina mazei pyrrolysyl-tRNA synthetase (PylRS)•tRNAPyl pairs derived from directed evolution are examined to probe their
Yi-Hui Wang   +9 more
doaj   +1 more source

Genetic Code Expansion System for Tight Control of Gene Expression in Bombyx mori Cell Lines

open access: yesInsects, 2021
Inducible gene expression systems are important tools for studying gene function and to control protein synthesis. With the completion of the detailed map of the silkworm (Bombyx mori) genome, the study of Bombyx mori has entered the post-genome era ...
Wei Lu   +4 more
doaj   +1 more source

First Report of ‘Candidatus Phytoplasma pyri’ Causing Peach Yellow Leaf Roll (PYLR) in Spain

open access: yesPlant Disease, 2014
‘Candidatus Phytoplasma prunorum,’ which causes European stone fruit yellows (ESFY), is the prevalent phytoplasma affecting Prunus spp. in Europe. It is closely related to ‘Ca. P. pyri,’ which causes pear decline (PD) in pear trees. Both phytoplasma belong to the ribosomal group 16Sr-X and are naturally transmitted by different species of Cacopsylla ...
J, Sabaté, A, Laviña, A, Batlle
openaire   +2 more sources

Incorporation of Amino Acids with Long-Chain Terminal Olefins into Proteins

open access: yesMolecules, 2016
The increasing need for site-specific protein decorations that mimic natural posttranslational modifications requires access to a variety of noncanonical amino acids with moieties enabling bioorthogonal conjugation chemistry.
Matthias P. Exner   +9 more
doaj   +1 more source

An evolved pyrrolysyl-tRNA synthetase with polysubstrate specificity expands the toolbox for engineering enzymes with incorporation of noncanonical amino acids

open access: yesBioresources and Bioprocessing, 2023
Aminoacyl-tRNA synthetase (aaRS) is a core component for genetic code expansion (GCE), a powerful technique that enables the incorporation of noncanonical amino acids (ncAAs) into a protein. The aaRS with polyspecificity can be exploited in incorporating
Ke Liu   +9 more
doaj   +1 more source

Pyrrolysyl-tRNA Synthetase with a Unique Architecture Enhances the Availability of Lysine Derivatives in Synthetic Genetic Codes

open access: yesMolecules, 2018
Genetic code expansion has largely relied on two types of the tRNA—aminoacyl-tRNA synthetase pairs. One involves pyrrolysyl-tRNA synthetase (PylRS), which is used to incorporate various lysine derivatives into proteins.
Atsushi Yamaguchi   +3 more
doaj   +1 more source

Pyrrolysyl-tRNA Synthetase, an Aminoacyl-tRNA Synthetase for Genetic Code Expansion

open access: yesCroatica Chemica Acta, 2016
Genetic code expansion (GCE) has become a central topic of synthetic biology. GCE relies on engineered aminoacyl‐tRNA synthetases (aaRSs) and a cognate tRNA species to allow codon reassignment by co-translational insertion of non-canonical amino acids ...
Ana Crnković   +3 more
doaj   +1 more source

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