Results 111 to 120 of about 1,475 (148)

Universal paralogs provide a window into evolution before the last universal common ancestor. [PDF]

Cell Genom
Goldman AD, Fournier GP, Kaçar B.
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Strategies to Expand the Genetic Code of Mammalian Cells. [PDF]

Chem Rev
Osgood AO, Huang Z, Szalay KH, Chatterjee A.   +3 more
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Correction to "Incorporation of Multiple β²‑Hydroxy Acids into a Protein in Vivo Using an Orthogonal Aminoacyl-tRNA Synthetase". [PDF]

ACS Cent Sci
Hamlish NX, Abramyan AM, Shah B, Zhang Z, Schepartz A.   +4 more
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Chemical Strategies for Controlling Sulfation in Biomacromolecules. [PDF]

ACS Chem Biol
Liu C, Liu X, Deng Y, Niu J.
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Machine Learning Enables Prediction of Pyrrolysyl-tRNA Synthetase Substrate Specificity

ACS Synthetic Biology, 2023
Knowledge about the substrate scope for a given enzyme is informative for elucidating biochemical pathways and also for expanding applications of the enzyme. However, no general methods are available to accurately predict the substrate specificity of an enzyme. Pyrrolysyl-tRNA synthetase (PylRS) is a powerful tool for incorporating various noncanonical
Qunfeng Zhang, Wenlong Zheng, Zhongdi Song, Qiang Zhang, Lirong Yang, Jianping Wu, Jianping Lin, Gang Xu, Haoran Yu   +8 more
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Thermophilic Pyrrolysyl-tRNA Synthetase Mutants for Enhanced Mammalian Genetic Code Expansion

ACS Synthetic Biology, 2020
Genetic code expansion (GCE) is a powerful technique for site-specific incorporation of noncanonical amino acids (ncAAs) into proteins in living cells, which is achieved through evolved aminoacyl-tRNA synthetase mutants. Stability is important for promoting enzyme evolution, and we found that many of the evolved synthetase mutants have reduced ...
Liming Hu, Xuewen Qin, Yujia Huang, Wenbing Cao, Chuchen Wang, Yong Wang, Xinyu Ling, Heqi Chen, Dan Wu, Yu Lin, Tao Liu   +10 more
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Specificity of Pyrrolysyl-tRNA Synthetase for Pyrrolysine and Pyrrolysine Analogs

Journal of Molecular Biology, 2009
Pyrrolysine, the 22nd amino acid, is encoded by amber (TAG=UAG) codons in certain methanogenic archaea and bacteria. PylS, the pyrrolysyl-tRNA synthetase, ligates pyrrolysine to tRNA(Pyl) for amber decoding as pyrrolysine. PylS and tRNA(Pyl) have potential utility in making tailored recombinant proteins.
Wen-Tai, Li, Anirban, Mahapatra, David G, Longstaff, Jonathan, Bechtel, Gang, Zhao, Patrick T, Kang, Michael K, Chan, Joseph A, Krzycki   +7 more
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Recognition of Non-α-amino Substrates by Pyrrolysyl-tRNA Synthetase

Journal of Molecular Biology, 2009
Pyrrolysyl-tRNA synthetase (PylRS), an aminoacyl-tRNA synthetase (aaRS) recently found in some methanogenic archaea and bacteria, recognizes an unusually large lysine derivative, L-pyrrolysine, as the substrate, and attaches it to the cognate tRNA (tRNA(Pyl)). The PylRS-tRNA(Pyl) pair interacts with none of the endogenous aaRS-tRNA pairs in Escherichia
Takatsugu, Kobayashi, Tatsuo, Yanagisawa, Kensaku, Sakamoto, Shigeyuki, Yokoyama   +3 more
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Improved pyrrolysyl-tRNA synthetase derived orthogonal translation systems

2023
BMBF, 031B0584A, IBÖM04: XenoGlue - Ein neuartiger Muschel-basierter fotoaktivierbarer Bioklebstoff für biomedizinische ...
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Generating Efficient Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetases for Structurally Diverse Non-Canonical Amino Acids

ACS Chemical Biology, 2022
Genetic code expansion (GCE) technologies commonly use the pyrrolysyl-tRNA synthetase (PylRS)/tRNAPyl pairs from Methanosarcina mazei (Mm) and Methanosarcina barkeri (Mb) for site-specific incorporation of non-canonical amino acids (ncAAs) into proteins. Recently a homologous PylRS/tRNAPyl pair from Candidatus Methanomethylophilus alvus Mx1201 (Ma) was
Savanna Avila-Crump, Marcus L. Hemshorn, Chloe M. Jones, Lea Mbengi, Kyle Meyer, Joshua A. Griffis, Subhashis Jana, Grace E. Petrina, Vinayak V. Pagar, P. Andrew Karplus, E. James Petersson, John J. Perona, Ryan A. Mehl, Richard B. Cooley   +13 more
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