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Takeo Suzuki

Researcher at University of Tokyo

Publications -  129
Citations -  6119

Takeo Suzuki is an academic researcher from University of Tokyo. The author has contributed to research in topics: Transfer RNA & Mitochondrion. The author has an hindex of 34, co-authored 128 publications receiving 5278 citations. Previous affiliations of Takeo Suzuki include Kumamoto University.

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Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases.

TL;DR: A large number of nuclear factors involved in the biogenesis and function of mt tRNAs have been identified and characterized, including processing endonucleases, tRNA-modifying enzymes, and aminoacyl-tRNA synthetases, indicating the functional importance of mttRNAs for mitochondrial activity.
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Pimet, the Drosophila homolog of HEN1, mediates 2′-O-methylation of Piwi- interacting RNAs at their 3′ ends

TL;DR: It is shown that piRNAs in Drosophila are 2'-O-methylated at their 3' ends, and Pimet mediates piRNA 2'- O-methylation in Dosophila.
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Selective stabilization of mammalian microRNAs by 3' adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2.

TL;DR: In livers from GLD-2-null mice, the steady-state level of the mature form of miR-122 was specifically lower than in heterozygous mice, whereas no reduction of pre-miR- 122 was observed, demonstrating that 3'-terminal adenylation by GLd-2 is required for the selective stabilization of mi R-122 in the liver.
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Taurine as a constituent of mitochondrial tRNAs: new insights into the functions of taurine and human mitochondrial diseases

TL;DR: This is the first reported evidence that taurine is a constituent of biological macromolecules, unveiling the prospect of obtaining new insights into the functions and subcellular localization of this abundant amino acid.
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A complete landscape of post-transcriptional modifications in mammalian mitochondrial tRNAs

TL;DR: In mammalian mitochondria, 22 species of tRNAs encoded in mitochondrial DNA play crucial roles in the translation of 13 essential subunits of the respiratory chain complexes involved in oxidative phosphorylation, and comprehensively determined the post-transcriptional modifications in each tRNA by mass spectrometry.