Shigeyuki Yokoyama
University of Tokyo
1125 Papers
10.8K Citations
Shigeyuki Yokoyama is an academic researcher from University of Tokyo. The author has contributed to research in topics: Transfer RNA & Thermus thermophilus. The author has an hindex of 107, co-authored 1113 publications. Previous affiliations of Shigeyuki Yokoyama include University of Tsukuba & RIKEN Brain Science Institute.
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Papers
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.
Neratur Krishnappagowda Lokanath,Ikuya Shiromizu,Noriyasu Ohshima,Yuichi Nodake,Mitsuaki Sugahara,Shigeyuki Yokoyama,Seiki Kuramitsu,Masashi Miyano,Naoki Kunishima +8 more
TL;DR: It is concluded that the oligomeric state of 2-deoxyribose-5-phosphate aldolase is important for the thermostability and not for the catalytic function.
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Efficient Decoding of the UAG Triplet as a Full-Fledged Sense Codon Enhances the Growth of a prfA-Deficient Strain of Escherichia coli
TL;DR: The results revealed the importance of "backup" stop triplets, UAA or UGA downstream of UAG, to avoid the deleterious impact of U AG reassignment on the proteome, and showed that the detrimental effect ofUAG reassignment could be alleviated by increasing the efficiency of Uag translation instead of reducing the number of UAKs in the genome.
Genetic encoding of non-natural amino acids in Drosophila melanogaster Schneider 2 cells.
TL;DR: An insect cell‐based system for incorporating non‐natural amino acids into proteins at specific sites is developed and 4‐azido‐L‐phenylalanine was incorporated into human interleukin‐8 at a specific site.
Structural Basis for Non-cognate Amino Acid Discrimination by the Valyl-tRNA Synthetase Editing Domain
TL;DR: Results indicate that the threonyl moiety and A76 of Thr-tRNAVal are recognized by the Lys-270, Thr-272, and Asp-279 side chains and by the Phe-264 side chain, respectively, of the ValRS editing domain.
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Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation
TL;DR: The solution structure of the C-terminal domain of DFF45, which is essential for its chaperone-like activity, consists of four alpha helices, which are folded in a novel helix-packing arrangement and reveals a large cluster of negatively charged residues on the molecular surface of D FF-C.
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