T
Takanori Muto
Publications - 16
Citations - 1464
Takanori Muto is an academic researcher. The author has contributed to research in topics: Metabotropic glutamate receptor & Metabotropic glutamate receptor 7. The author has an hindex of 11, co-authored 16 publications receiving 1382 citations.
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Journal ArticleDOI
Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20.
Yoshito Abe,Toshihiro Shodai,Takanori Muto,Katsuyoshi Mihara,Hisayoshi Torii,Shuh Ichi Nishikawa,Toshiya Endo,Daisuke Kohda +7 more
TL;DR: In this article, the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase was reported.
Journal ArticleDOI
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
TL;DR: A general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements is proposed and revealed the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of theDimeric receptors on the cell surface.
Journal ArticleDOI
Domain architectures and characterization of an RNA-binding protein, TLS
Yuko Iko,Takashi S. Kodama,Nobuyuki Kasai,Takuji Oyama,Eugene Hayato Morita,Takanori Muto,Mika Okumura,Ritsuko Fujii,Toru Takumi,Shin-ichi Tate,Kosuke Morikawa +10 more
TL;DR: The domain organization of human TLS is examined by a combined approach using limited proteolysis, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, circular dichroism, inductively coupled plasma atomic emission spectroscopy, and NMR spectroscope to find that the RNA recognition motif (RRM) and zinc finger-like domains exclusively form protease-resistant core structures within the isolated TLS protein fragments.
Journal ArticleDOI
NMR identification of the Tom20 binding segment in mitochondrial presequences
TL;DR: In this paper, the chemical shift perturbation of the NMR signals of five different 15N-labeled presequence peptides by the addition of the cytosolic receptor domain of rat or yeast Tom20 was investigated.
Journal ArticleDOI
Crystallographic and Functional Studies of Very Short Patch Repair Endonuclease
Susan E. Tsutakawa,Takanori Muto,Tomohiko Kawate,Hisato Jingami,Naoki Kunishima,Mariko Ariyoshi,Daisuke Kohda,Masako Nakagawa,Kosuke Morikawa +8 more
TL;DR: VVsr endonuclease plays a crucial role in the repair of TG mismatched base pairs, which are generated by the spontaneous degradation of methylated cytidines; Vsr recognizes the mismatch and cleaves the phosphate backbone 5' to the thymidine.