Search Results - "Tochio, Hidehito"

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    Watching protein structure at work in living cells using NMR spectroscopy by Tochio, Hidehito

    Published in Current opinion in chemical biology (01-12-2012)
    “…► Advances in in-cell NMR spectroscopy of biomacromolecules. ► Escherichia coli, yeasts, Xenopus laevis oocytes and mammalian cell lines can be used. ►…”
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    Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism by Ariyoshi, Mariko, Shirakawa, Masahiro, Arita, Kyohei, Tochio, Hidehito, Nakamura, Yusuke

    Published in Nature (London) (09-10-2008)
    “…DNA methylation of CpG dinucleotides is an important epigenetic modification of mammalian genomes and is essential for the regulation of chromatin structure,…”
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    Real-Time Background-Free Selective Imaging of Fluorescent Nanodiamonds in Vivo by Igarashi, Ryuji, Yoshinari, Yohsuke, Yokota, Hiroaki, Sugi, Takuma, Sugihara, Fuminori, Ikeda, Kazuhiro, Sumiya, Hitoshi, Tsuji, Shigenori, Mori, Ikue, Tochio, Hidehito, Harada, Yoshie, Shirakawa, Masahiro

    Published in Nano letters (14-11-2012)
    “…Recent developments of imaging techniques have enabled fluorescence microscopy to investigate the localization and dynamics of intracellular substances of…”
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    The structural basis for receptor recognition of human interleukin-18 by Tsutsumi, Naotaka, Kimura, Takeshi, Arita, Kyohei, Ariyoshi, Mariko, Ohnishi, Hidenori, Yamamoto, Takahiro, Zuo, Xiaobing, Maenaka, Katsumi, Park, Enoch Y., Kondo, Naomi, Shirakawa, Masahiro, Tochio, Hidehito, Kato, Zenichiro

    Published in Nature communications (15-12-2014)
    “…Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation. The uncontrolled release of this…”
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    A Structured Monodisperse PEG for the Effective Suppression of Protein Aggregation by Muraoka, Takahiro, Adachi, Kota, Ui, Mihoko, Kawasaki, Shunichi, Sadhukhan, Nabanita, Obara, Haruki, Tochio, Hidehito, Shirakawa, Masahiro, Kinbara, Kazushi

    Published in Angewandte Chemie International Edition (25-02-2013)
    “…Part of the solution: A PEG with a discrete triangular structure exhibits hydrophilicity/hydrophobicity switching upon increasing temperatures, and suppresses…”
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    Structural Basis for the Multiple Interactions of the MyD88 TIR Domain in TLR4 Signaling by Ohnishi, Hidenori, Tochio, Hidehito, Kato, Zenichiro, Orii, Kenji E., Li, Ailian, Kimura, Takeshi, Hiroaki, Hidekazu, Kondo, Naomi, Shirakawa, Masahiro, Strominger, Jack L.

    “…Myeloid differentiating factor 88 (MyD88) and MyD88 adaptor-like (Mal) are adaptor molecules critically involved in the Toll-like receptor (TLR) 4 signaling…”
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    Pruning the ALS-Associated Protein SOD1 for in-Cell NMR by Danielsson, Jens, Inomata, Kohsuke, Murayama, Shuhei, Tochio, Hidehito, Lang, Lisa, Shirakawa, Masahiro, Oliveberg, Mikael

    Published in Journal of the American Chemical Society (17-07-2013)
    “…To efficiently deliver isotope-labeled proteins into mammalian cells poses a main challenge for structural and functional analysis by in-cell NMR. In this…”
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    Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints by Hou, Xue-Ni, Tochio, Hidehito

    Published in Biophysical reviews (01-02-2022)
    “…It has been over two decades since paramagnetic NMR started to form part of the essential techniques for structural analysis of proteins under physiological…”
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    Suppression of Nonspecific Protein–Nanodiamond Adsorption Enabling Specific Targeting of Nanodiamonds to Biomolecules of Interest by Sotoma, Shingo, Igarashi, Ryuji, Iimura, Jun, Kumiya, Yuta, Tochio, Hidehito, Harada, Yoshie, Shirakawa, Masahiro

    Published in Chemistry letters (2015)
    “…Applications of nanodiamonds (NDs) to bioimaging are restricted because of the nonspecific adsorption of biomolecules on the surface of NDs. Here, we show that…”
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    An innate interaction between IL-18 and the propeptide that inactivates its precursor form by Tsutsumi, Naotaka, Yokota, Ayumi, Kimura, Takeshi, Kato, Zenichiro, Fukao, Toshiyuki, Shirakawa, Masahiro, Ohnishi, Hidenori, Tochio, Hidehito

    Published in Scientific reports (16-04-2019)
    “…Uncontrolled secretion of mature interleukin (IL)-1β and IL-18 is responsible for severe autoinflammatory or autoimmune disorders and various allergic…”
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    Crystal structure of thymine DNA glycosylase conjugated to SUMO-1 by Shirakawa, Masahiro, Hiroaki, Hidekazu, Sugasawa, Kaoru, Maita, Nobuo, Tochio, Hidehito, Uchimura, Yasuhiro, Hanaoka, Fumio, Jee, Jun-Goo, Saitoh, Hisato, Baba, Daichi

    Published in Nature (16-06-2005)
    “…Members of the small ubiquitin-like modifier (SUMO) family can be covalently attached to the lysine residue of a target protein through an enzymatic pathway…”
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    Intracellular Phosphate Serves as a Signal for the Regulation of the PHO Pathway in Saccharomyces cerevisiae by Auesukaree, Choowong, Homma, Tomoyuki, Tochio, Hidehito, Shirakawa, Masahiro, Kaneko, Yoshinobu, Harashima, Satoshi

    Published in The Journal of biological chemistry (23-04-2004)
    “…In Saccharomyces cerevisiae, the phosphate signal transduction pathway (PHO pathway) is known to regulate the expression of several phosphate-responsive genes,…”
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    TRAM is involved in IL-18 signaling and functions as a sorting adaptor for MyD88 by Ohnishi, Hidenori, Tochio, Hidehito, Kato, Zenichiro, Kawamoto, Norio, Kimura, Takeshi, Kubota, Kazuo, Yamamoto, Takahiro, Funasaka, Tatsuyoshi, Nakano, Hiroshi, Wong, Richard W, Shirakawa, Masahiro, Kondo, Naomi

    Published in PloS one (07-06-2012)
    “…MyD88, a Toll/interleukin-1 receptor homology (TIR) domain-containing adaptor protein, mediates signals from the Toll-like receptors (TLR) or IL-1/IL-18…”
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    Plc1p, Arg82p, and Kcs1p, Enzymes Involved in Inositol Pyrophosphate Synthesis, Are Essential for Phosphate Regulation and Polyphosphate Accumulation in Saccharomyces cerevisiae by Auesukaree, Choowong, Tochio, Hidehito, Shirakawa, Masahiro, Kaneko, Yoshinobu, Harashima, Satoshi

    Published in The Journal of biological chemistry (01-07-2005)
    “…In Saccharomyces cerevisiae, the phosphate signal transduction PHO pathway is involved in regulating several phosphate-responsive genes such as PHO5, which…”
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