 帝京大学薬学部 |
研究室ページ | English | |
| 生体分子化学研究室 | ||
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論文リスト | |
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Ito, G., Tomita, T. and Utsunomiya-Tate, N. "LRRK2-mediated phosphorylation and thermal stability of Rab12 are regulated by bound nucleotides." Biochem. Biophys. Res. Commun., 667, 43-49 (2023) | |
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Ito, G. and Utsunomiya-Tate, N. "Overview of the Impact of Pathogenic LRRK2 Mutations in Parkinson's Disease." Biomolecules, 13(5), 845 (2023) | |
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Ito, K., Araki, M., Katai, Y., Nishimura, Y., Imotani, S., Inoue, H., Ito, G. and Tomita, T. "Pathogenic LRRK2 compromises the subcellular distribution of lysosomes in a Rab12-RILPL1-dependent manner." FASEB J., 37(5), e22930 (2023) | |
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Iguchi, A., Takatori, S., Kimura, S., Muneto, H., Wang, K., Etani, H., Ito, G., Sato, H., Hori, Y., Sasaki, J., Saito, T., Saido, TC., Ikezu, T., Takai, T., Sasaki, T. and Tomita, T. "INPP5D modulates TREM2 loss-of-function phenotypes in a β-amyloidosis mouse model." iScience, 26(4), 106375 (2023)
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Sato, W., Watanabe-Takahashi, M., Murata, T., Utsunomiya-Tate, N., Motoyama, J., Anzai, M., Ishihara, S., Nishioka, N., Uchiyama, H., Togashi, J., Nishihara, S., Kawasaki, K., Saito, T., Saido, TC., Funamoto, S. and Nishikawa, K. "A tailored tetravalent peptide displays dual functions to inhibit amyloid β production and aggregation." Commun. Biol., 6, 383 (2023) | |
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Murata, T., Ito, G. and Utsunomiya-Tate, N. "Site-specific amino acid D-isomerization of Tau R2 and R3 peptides changes the fibril morphology, resulting in attenuation of Tau aggregation inhibitor potency." Biochem. Biophys. Res. Commun. 654, 18-25 (2023) |
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Ito, G. and Ustunomiya-Tate, N. "A dementia-inclusive symbiotic society." Impact Volume2023, No. 2, 33-35 (2023) |
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Murata, T., Tochio, N. and Utsunomiya-Tate, N. "Physicochemical characterization of the G51D mutation of a-synuclein that is responsible for its severe cytotoxicity." Neurosci. Lett., 760, 136077 (2021) |
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Murata, T., Unno, Y., Fukuda, M. and Utsunomiya-Tate, N. “The dynamical structure of Rab 35 is stabilized in the presence of GTP under the physiological condition.” Biochem. Biophys. Rep. 23, 100776-100782 (2020) |
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Tochio, N., Murata, T. and Utsunomiya-Tate, N. "Effect of site-specific amino acid D-isomerization on b-sheet transition and fibril formation profiles of Tau microtuble-binding repeat peptides." Biochem. Biophys. Commun. Res. 508, 184-190 (2019) |
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Ikura, T., Tochio, N., Kawasaki, R., Matsuzaki, M., Narita, A., Kikumoto, M., Utsunomiya-Tate, N. and Ito, N. "The trans isomer of Tau peptide is prone to aggregate, and the WW domain of Pin1 drastically decreases its aggregation." FEBS Lett. 592, 3082-3091 (2018) | |
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Watanabe, H., Watanabe, Y., Tashiro, Y., Mushiroda, T., Ozeki, T., Sueki, H., Yamamoto, T., Utsunomiya-Tate, N., Gouda, H. and Kusakabe, Y. "A docking model of dapsone bound to HLA-B* 13:01 explains the risk of dapsone hypersensitivity syndorome." J. of Dermatological Science 88, 320-329 (2017) |
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Tadokoro. S., Shibata, T., Itoh, Y., Amano T., Nakanishi, M., Hirashima, N. and Utsunomiya-Tate, N. “Phosphorylation of syntaxin-3 at Thr 14 negatively regulates exocytosis in RBL-2H3 mast cells.” Cell Biol. Int. 40, 589-596 (2016) |
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Tadokoro, S., Hirashima, N. and Utsunomiya-Tate, N. “Effect of Complexin 2 on Membrane Fusion between Liposomes containing Mast Cell SNARE Proteins.” Biol. Pharm. Bull. 39, 446-449 (2016) |
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Wang, J., Tochio, N., Kawasaki, R., Tamari,Y., Xu, N., Uewaki, J., Utsunomiya-Tate, N. and Tate, S. "Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif on the Active Site ofHuman Pin1 PPlase.” Biochemistry 54, 5343-5253 (2015) |
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Xu, H., Tochio, N., Wang, J., Tamari, Y., Uewaki, J., Utsunomiya-Tate, N., Igarashi, K., Shiraki, T., Kobayashi, N. and Tate, S. “ The C113D mutation in Human Pin 1 causes allosteric structural changes in the phosphate binding pocket of the PPlase domain through the Tug of war in the Dual-Histidine motif.” Biochemistry 53, 5568-5578 (2014) | |
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Sugiki, T. and Utsunomiya-Tate, N.,“Site-specific aspartic acid isomerization regurates self-assembly and neurotoxicity of amyloid ・・ Biochem. Biophys. Res. Commun. 441, 493-498 (2013) | |
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"Preferential domain orientation HMGB2 determined by the weak intramolecular interactions mediated by the interdomain linker."Uewaki, J., Kamikubo, H., Kurita, J., Hiroguchi, N., Moriuchi, H., Yosgida, K., Kataoka, M., Utusnomiya-Tate, N. and Tate, S. Chem Phys. 419, 212-223 (2013) |
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"Ｔｅｔｒａｍｅｒｉｃ ｉｎｔｅｒａｃｔｉｏｎ ｏｆ ｔｈｅ ｅｃｏｅｎｚｙｍｅ CD38 in the cell surface enables its catalytic and raft-association."Hara-yokoyama. M., Utsunomiya-Tate, N., et.al Structure, 20, 1585-1595 (2012) |
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"D-Ser-containing humanin shows promorion of fibril formation." Hayashi, K., Sasabe, J., Chiba, T., Aiso, S. andUtsunomiya-Tate, N. Amno Acids, 42, 2293-2297 (2012) |
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"Controlled suricture and properties of silicate nanoparticle networks for incorporation of biosystem components." Sakai-Kato, K., Hasegawa, T., Takeoka, A., Kato, M., Toyo'oka, T.,Utsunnomiya-Tate,N.And Kawanishi,T. Nanotechnology, 22, 1-8 (2011) | |
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"Stabilitu of folding structure of Zic zinc finger protein." Sakai-Kato, K., Umezawa, Y., Mikoshiba, K., Aruga, J. and Utsunimoiya-Tate, N Bioche. Biophy. Res. Commun. 384, 362-265 (2009)Ｂｉｏｃｈｅ． |
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"Ｓｃｒｅｅｎｉｎｇ ｓｙｓtem for D-Asp-containing proteins using D-aspartul endopepyidase and two-dimensional gel electrophoresis." Sakai-Kato, K., Kinouchi, T., Fuii, N., Imai, K. and Utsunomiya-Tate, N. Amino Acids, 36, 125-129 (2009) |
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"Structure requirements for tha flavonoid fisetin in inhibiting fibril formation of amyloid βprotein," Akaishi, T., Morimoto, T., Shibao, M., Sakai-Kato, K., Utsunomiya-Tate, N., Abe, K. Neurosci, Lett. 444, 280-285 (2009) |
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"Functional and structural basis of the nuclear localization signal in ZIC3 zinc finger domain." Hatayama, M., Tomizawa, T., Sakai-Kato, K., Kose, S., Imamoto, N., Yokoyama, S., Utsunomiya-Tate, N., Mikoshiba, K. et.al. Human Mol. Genet. 17, 3459-3473 (2009) |
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"CD spectra show the relational style between Zic-, Gli-, Glis-zinc finger protein and ＤＮＡ．” Ｓaｋａｉ−Ｋａｔｏ， Ｋ．， Ｉｓｈｉｇｕｒｏ， Ａ．， Ｍｉｋｏｓｈｉｂａ， Ｋ．，Aruga, J., Utsunomiya-Tate, N. Biochimica Biophysica Acta 1784, 1011-1019 (2008) |
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"Racemization of amyloid βAsp1 residue blockes the acceleration of fibril formation caused by racemaization of the Asp23 residue." Sakai-Kato, K., Naito, M. And Utsunomiya-Tate､N. Bioshem Biophys Res. Commun. 364, 464-469 (2007) |
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"Chimeric structural stabilities in coiled-coil structure of the NECK domain in Hyuman lectin-like oxidized low-density lipoprotein receptor 1 (LOX-1)," Ishigaki, T., Ojki, I., Utsunomiya-Tate. N. and Tate, S. J.Biochem. 141, 855-866 (2007) |
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"Cationic starch derivatives as dynamic coating additives for protein analysis in capillary electrphoresis." Sakai-Kato, K., Kato, M., Homma, H., Toyo'oka, T and Utsunoimiya-Tate, N. J. Chromatogr. A, 1111. 127-132 (2006) |
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"Creation of P450 chip for high-throughput analysis." Sakai-Kato, K., Kato, M., Homma, H., Toyo'oka, T and Utsunoimiya-Tate, N. Sakai-Kato, K., Anal. Chem. 77, 7080-7083 (2006) |
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"Molecular-orientation analysis based on alignment-induced TROSY chemical shift changes." Tate, S., Sgimahaea, H. and Utsunomiya-Tate, N. J. Mａｇｎｅｔｉｃ Rｅｓｏｎａｎｃｅ 171、284-292 (2004) |
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"Ｍｅａｓｕｒｅｍｅｎｔ of 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning." Kurita, J., Shimahara, H., Utsunomiya-Tate, N., and Tate, S. J. Mａｇｎｅｔｉｃ Resonance 163, 163-173 (2003) |
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"Reelin molecules asemble together to form a large complex, which is inhibited by the function-blocking CR50 antibody." Utsunomiya-Tate, N., Kubo, K., Tate, S., Kainosho, M., Katayama, E., Nakajima, K. and Mikoshiba, K. Proc. Natl. Acad. Sci. USA 97, 9729-9734 (2000) |
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著書リスト・その他 | |
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1.
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教科書 「薬学生の物理化学」 楯 直子 平嶋尚英 共編 培風館 （２０２１年） | |
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2.
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教科書 「医療コミュニケーション ： 帝京大学医療コミュニケーション運営委員会編」（京都廣川書店） 編集者 ： 楯 直子 (２０１８年） |
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3.
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特集 「患者中心の医療を実現するためのコミュニケーション教育 ― 帝京大学の取り組み―」 MISSION IN LIFE 65巻 楯 直子 （２０１５年） |
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4.
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薬学生のための基礎シリーズ7 基礎化学 楯 直子 平嶋尚英 共編、培風館 （2014年） |
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5.
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アミロイドβペプチドの凝集に及ぼすD-アスパラギン酸に影響 加藤くみ子、楯 直子 京都大学原子炉研究所レポｰト （2008年） |
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6.
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講義室「恩師 坪井正道先生」 楯 直子 日本薬学会ファルマシア 44巻、224 （2008年） |
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7.
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医薬品の陰の立役者、「物理化学」を学ぶ 楯 直子 リクルート進学ネット （2007年） |
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8.
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分子腎臓学：研究手法の原理と具体的方法：cDNAクローニングにより遺伝子が得られたら何を調べるか-変異導入 楯 直子 腎と透析 第45巻増刊 106−110 （1998年） |
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9.
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Clinical Neuroscience ：シナプス - 構造と機能 ； トランスポーター作用薬 楯 直子、遠藤 仁 臨床神経科学 14巻、936−937 （1996年） |
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10.
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糖 - その多様性を探る ； 磁化移動を利用した糖鎖構造解析 - 2次元NMRによる解析 稲垣冬彦、楯 直子 化学増刊122号、133−142 （化学同人） （1992年） |
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蛍光ストップト・フロー法 楯（宇都宮）直子、中西 守、 臨床検査 33巻、949 （医学書院） （1989年） |
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