Search Results - "UENO, Takafumi"

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  1. 1

    Observation of gold sub-nanocluster nucleation within a crystalline protein cage by Maity, Basudev, Abe, Satoshi, Ueno, Takafumi

    Published in Nature communications (16-03-2017)
    “…Protein scaffolds provide unique metal coordination environments that promote biomineralization processes. It is expected that protein scaffolds can be…”
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  2. 2

    Porous Protein Crystals as Reaction Vessels by Ueno, Takafumi

    Published in Chemistry : a European journal (08-07-2013)
    “…Porous protein crystals have the potential to provide new porous materials due to their unique chemical environments composed of amino acid residues…”
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    Use of the confined spaces of apo-ferritin and virus capsids as nanoreactors for catalytic reactions by Maity, Basudev, Fujita, Kenta, Ueno, Takafumi

    Published in Current opinion in chemical biology (01-04-2015)
    “…•Ferritin cage and virus capsids as nanoreactor.•Catalytic reactions inside apo-ferritin cage.•Enzymatic reactions in virus capsid.•Protein cages versus…”
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    Controlled Uptake of an Iridium Complex inside Engineered apo‐Ferritin Nanocages: Study of Structure and Catalysis by Taher, Mohd, Maity, Basudev, Nakane, Taiki, Abe, Satoshi, Ueno, Takafumi, Mazumdar, Shyamalava

    Published in Angewandte Chemie International Edition (21-03-2022)
    “…The effect of the mutation at the core of the ferritin nanocage (apo‐rHLFr) on the uptake of IrCp* has been investigated by structural and spectroscopic…”
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  6. 6

    Site-Selective Protein Chemical Modification of Exposed Tyrosine Residues Using Tyrosine Click Reaction by Sato, Shinichi, Matsumura, Masaki, Kadonosono, Tetsuya, Abe, Satoshi, Ueno, Takafumi, Ueda, Hiroshi, Nakamura, Hiroyuki

    Published in Bioconjugate chemistry (20-05-2020)
    “…Targeting less abundant amino acid residues on the protein surface may realize site-selective protein modification of natural proteins. The relative…”
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  7. 7

    Importance of the Subunit–Subunit Interface in Ferritin Disassembly: A Molecular Dynamics Study by Li, Zhipeng, Maity, Basudev, Hishikawa, Yuki, Ueno, Takafumi, Lu, Diannan

    Published in Langmuir (25-01-2022)
    “…Ferritin is a spherical cage-like protein that is useful for loading large functional particles for various applications. To our knowledge, how pH affects the…”
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  8. 8

    An Individual-Level Meta-Analysis Using Real-World and Pivotal Studies on Mortality From the Use of Paclitaxel-Containing Devices in Japanese Femoropopliteal Disease Patients by Nakamura, Masato, Takata, Munenori, Yokoi, Hiroyoshi, Ueno, Takafumi, Suzuki, Yuka, Ikeda, Koji, Yamaguchi, Takuhiro

    Published in Circulation Journal (25-11-2021)
    “…Background:The effect of treatment with paclitaxel-containing devices (PTXD) on mortality in patients with peripheral artery disease remains…”
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    Optogenetic manipulation of activity and temporally controlled cell-specific ablation reveal a role for MCH neurons in sleep/wake regulation by Tsunematsu, Tomomi, Ueno, Takafumi, Tabuchi, Sawako, Inutsuka, Ayumu, Tanaka, Kenji F, Hasuwa, Hidetoshi, Kilduff, Thomas S, Terao, Akira, Yamanaka, Akihiro

    Published in The Journal of neuroscience (14-05-2014)
    “…Melanin-concentrating hormone (MCH) is a neuropeptide produced in neurons sparsely distributed in the lateral hypothalamic area. Recent studies have reported…”
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  10. 10

    Design of a Hierarchical Assembly at a Solid–Liquid Interface Using an Asymmetric Protein Needle by Kikuchi, Kosuke, Date, Koki, Ueno, Takafumi

    Published in Langmuir (14-02-2023)
    “…Design and control of processes for a hierarchical assembly of proteins remain challenging because it requires consideration of design principles with…”
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    Design of Multinuclear Gold Binding Site at the Two-fold Symmetric Interface of the Ferritin Cage by Hishikawa, Yuki, Maity, Basudev, Ito, Nozomi, Abe, Satoshi, Lu, Diannan, Ueno, Takafumi

    Published in Chemistry letters (05-07-2020)
    “…We have designed novel multinuclear metal-binding sites by introducing 96 Cys residues at the 2-fold symmetric interfaces in the protein cage of ferritin…”
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  15. 15

    A Photoactive Carbon-Monoxide-Releasing Protein Cage for Dose-Regulated Delivery in Living Cells by Fujita, Kenta, Tanaka, Yuya, Abe, Satoshi, Ueno, Takafumi

    Published in Angewandte Chemie International Edition (18-01-2016)
    “…Protein cages can serve as bioinorganic molecular templates for functionalizing metal compounds to regulate cellular signaling. We succeeded in developing a…”
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    Rh-Catalyzed Polymerization of Phenylacetylene: Theoretical Studies of the Reaction Mechanism, Regioselectivity, and Stereoregularity by Ke, Zhuofeng, Abe, Satoshi, Ueno, Takafumi, Morokuma, Keiji

    Published in Journal of the American Chemical Society (25-05-2011)
    “…Poly(phenylacetylene) (PPA) has versatile electrical and optical properties due to its intriguing π-conjugated backbone, configuration, stereoregularity, and…”
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    SYMPLICITY HTN-Japan – First Randomized Controlled Trial of Catheter-Based Renal Denervation in Asian Patients by Kario, Kazuomi, Ogawa, Hisao, Okumura, Ken, Okura, Takafumi, Saito, Shigeru, Ueno, Takafumi, Haskin, Russel, Negoita, Manuela, Shimada, Kazuyuki, on behalf of the SYMPLICITY HTN-Japan Investigators

    Published in Circulation Journal (2015)
    “…Background:SYMPLICITY HTN-Japan is a prospective, randomized, controlled trial comparing renal artery denervation (RDN) with standard pharmacotherapy for…”
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    Design of an In‐Cell Protein Crystal for the Environmentally Responsive Construction of a Supramolecular Filament by Abe, Satoshi, Pham, Thuc Toan, Negishi, Hashiru, Yamashita, Keitaro, Hirata, Kunio, Ueno, Takafumi

    Published in Angewandte Chemie International Edition (25-05-2021)
    “…Protein assemblies can be designed for development of nano–bio materials. This has been achieved by modulating protein–protein interactions. However,…”
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  20. 20

    The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design by Nguyen, Que Dan, Kikuchi, Kosuke, Maity, Basudev, Ueno, Takafumi

    “…Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can…”
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