{"id":19,"date":"2017-08-18T11:02:47","date_gmt":"2017-08-18T02:02:47","guid":{"rendered":"http:\/\/organellezone.sakura.ne.jp\/site\/?page_id=19"},"modified":"2021-10-12T11:35:26","modified_gmt":"2021-10-12T02:35:26","slug":"achievement","status":"publish","type":"page","link":"http:\/\/organellezone.org\/achievement\/","title":{"rendered":"\u7814\u7a76\u6210\u679c"},"content":{"rendered":"<div class=\"btns\">\n<ul>\n<li><a href=\"#2021\">\u25bc 2021\u5e74<\/a><\/li>\n<li><a href=\"#2020\">\u25bc 2020\u5e74<\/a><\/li>\n<li><a href=\"#2019\">\u25bc 2019\u5e74<\/a><\/li>\n<li><a href=\"#2018\">\u25bc 2018\u5e74<\/a><\/li>\n<li><a href=\"#2017\">\u25bc 2017\u5e74<\/a><\/li>\n<\/ul>\n<\/div>\n<h2 id=\"2021\">2021\u5e74<\/h2>\n<h3 class=\"achievementtitle\">\u4e2d\u5c71\u548c\u4e45<small>\uff08\u4eac\u90fd\u5927\u5b66\u5927\u5b66\u9662\u3000\u85ac\u5b66\u7814\u7a76\u79d1\uff09<\/small><\/h3>\n<ol>\n<li>Noguchi, T., Nakamura, K., Satoda, Y., Katoh, Y. &#038; <span style=\"text-decoration: underline;\">Nakayama, K.<\/span> (2021) CCRK\/CDK20 regulates ciliary retrograde protein trafficking via interacting with BROMI\/TBC1D32.<strong><em>PLoS ONE<\/em> 16,<\/strong> e0258497.<\/li>\n<li>Inoue, H., Takatsu, H., Hamamoto, A., Takayama, M., Nakabuchi, R., Muranaka, Y., Yagi, T., <span style=\"text-decoration: underline;\">Nakayama, K.<\/span> &amp; Shin, H.-W.(2021)The interaction of ATP11C-b with ezrin contributes to its polarized localization.<strong><em>J. Cell Sci.<\/em> 134,<\/strong> jcs258523.<\/li>\n<li>Fujisawa, S., Qiu, H., Nozaki, S., Chiba, S., Katoh, Y. &amp; <span style=\"text-decoration: underline;\">Nakayama, K.<\/span> (2021) ARL3 and ARL13B GTPases participate in distinct steps of INPP5E targeting to the ciliary membrane. <strong><em>Biol. Open 10<\/em>,<\/strong> bio058843.<\/li>\n<li>Ishida, Y., Kobayashi, T., Chiba, S., Katoh, Y. &amp; <span style=\"text-decoration: underline;\">Nakayama, K.<\/span> (2021) Molecular basis of ciliary defects caused by compound heterozygous <em>IFT144\/WDR19<\/em> mutations found in cranioectodermal dysplasia. <strong><em>Hum. Mol. Genet.,<\/em> 30,<\/strong> 213-225.<\/li>\n<li>Qiu, H., Fujisawa, S., Nozaki, S., Katoh, Y. &amp; <span style=\"text-decoration: underline;\">Nakayama, K.<\/span> (2021) Interaction of INPP5E with ARL13B is essential for its ciliary membrane retention but dispensable for its ciliary entry. <strong><em>Biol. Open <\/em> 10,<\/strong> bio057653.<\/li>\n<li>Kobayashi, T., Ishida, Y., Hirano, T., Katoh, Y. &amp;\u00a0<span style=\"text-decoration: underline;\">Nakayama, K.<\/span>\u00a0(2021) Cooperation of the IFT-A complex with the IFT-B complex is required for ciliary retrograde protein trafficking and GPCR import. <strong><em>Mol. Biol. Cell,<\/em> 32,<\/strong> 45-56.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u897f\u982d\u82f1\u8d77<small>\uff08\u5bae\u5d0e\u5927\u5b66\u3000\u533b\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Sugiyama, T., Murao, N., Kadowaki, H., Takao, K., Miyakawa, T., Matsushita, Y., Katagiri, T., Futatsugi, A., Shinmyo, Y., Kawasaki, H., Sakai, J., Shiomi, K., Nakazato, M., Takeda, K., Mikoshiba, K., Ploegh, H.L., Ichijo, H., <span style=\"text-decoration: underline;\">Nishitoh, H.<\/span> (2021) ERAD components Derlin-1 and Derlin-2 are essential for postnatal brain development and motor function. <em><strong>iScience<\/strong><\/em>, 24:102758.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e2d\u91ce\u660e\u5f66<small>\uff08\u7406\u5316\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Shimizu, Y., Takagi, J., Ito, E., Ito, Y., Ebine, K., Komatsu, Y., Goto, Y., Sato, M., Toyooka, K., Ueda, T., <u>Kurokawa, K.<\/u>, Uemura, T., and <span class=\"double\">Nakano, A.<\/span> (2021). Cargo sorting zones in the <em>trans<\/em>-Golgi network visualized by super-resolution confocal live imaging microscopy in plants. <strong><em>Nat. Commun.<\/em><\/strong> <strong>12<\/strong>:1901.<\/li>\n<li>\n<p>Rizzo, R., Russo, D., <u>Kurokawa, K.<\/u>, Sahu, P., Lombardi, B., Supino, D., Zhukovsky, M. A., Vocat, A., Pothukuchi, P., Kunnathully, V., Capolupo, L., Boncompain, G., Vitagliano, C., Marino, F. Z., Aquino, G., Montariello, D., Henklein, P., Mandrich, L., Botti, G., Clausen, H., Mandel, U., Yamaji, T., Hanada, K., Budillon, A., Perez, F., Parashuraman, S., Hannun, Y. A., <span class=\"double\">Nakano, A.<\/span>, Corda, D., D\u2019Angelo, G., and Luini, A. (2021). Golgi maturation-dependent glycoenzyme recycling controls glycosphingolipid biosynthesis and cell growth via GOLPH3. <strong><em>EMBO J<\/em><em>.<\/em><\/strong> <strong>40<\/strong>:e107238.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u52a0\u85e4\u85ab<small>\uff08\u7523\u696d\u6280\u8853\u7dcf\u5408\u7814\u7a76\u6240\u3000\u30d0\u30a4\u30aa\u30e1\u30c7\u30a3\u30ab\u30eb\u7814\u7a76\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Ohzono T.. <u>Katoh K<\/u>., Terentjev E.M. (2021)<br \/>\nMicroscopy of diffuse nematic-isotropic transition in main-chain nematic liquid crystal elastomers. <em>Macromolecules <\/em>(in press)<\/p>\n<\/li>\n<li>\n<p>Ohzono T., <u>Katoh K.<\/u>, Minamikawa H., Saed M. O., Terentjev E.M. (2021)<br \/>\nInternal constraints and arrested relaxation in main-chain nematic elastomers<br \/>\n<em>Nat Commun<\/em> 12, 787 (2021). https:\/\/doi.org\/10.1038\/s41467-021-21036-3<\/p>\n<\/li>\n<\/ol>\n<h2 id=\"2020\">2020\u5e74<\/h2>\n<h3 class=\"achievementtitle\">\u4e2d\u91ce\u660e\u5f66<small>\uff08\u7406\u5316\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Fujii, S., <u>Kurokawa, K.<\/u>, Tago, T., Inaba, R., Takiguchi, A., <span class=\"double\">Nakano, A.<\/span>, Satoh, T., and Satoh, A. (2020). Sec71 separates Golgi stacks in <em>Drosophila<\/em> S2 cells. <strong><em>J. Cell Sci.<\/em><\/strong> <strong>133<\/strong>:jcs245571.<\/li>\n<li>Kanazawa, T., Morinaka, H., Ebine, K., Shimada, T. L., Ishida, S., Minamino, N., Yamaguchi, K., Shigenobu, S., Kohchi, T., <span class=\"double\">Nakano, A.<\/span>, and Ueda, T. (2020). The liverwort oil body is formed by redirection of the secretory pathway. <strong><em>Nat. Commun.<\/em> 11<\/strong>:6152.<\/li>\n<li>Rodriguez-Gallardo, S.\u2020, <u>Kurokawa, K.<\/u>\u2020, Sabido-Bozo, S., Cortes-Gomez, A., Ikeda, A., Zoni, V., Aguilera-Romero, A., Maria Perez-Linero, A., Lopez, S., Waga, M., Araki, M., Nakano, M., Riezman, H., Funato, K., Vanni, S., <span class=\"double\">Nakano, A.<\/span>, and Mu\u00f1iz, M. (2020). Ceramide chain length-dependent protein sorting into selective endoplasmic reticulum exit sites. <strong><em>Sci. Adv.<\/em> 6<\/strong>:eaba8237. (\u2020 equal contribution)<\/li>\n<li>Ikeda, A., Schlarmann, P., <u>Kurokawa, K.<\/u>, <span class=\"double\">Nakano, A.<\/span>, Riezman, H., and Funato, K. (2020). Tricalbins are required for nonvesicular ceramide transport at ER-Golgi contacts and modulate lipid droplet biogenesis. <strong><em>iScience<\/em> 23<\/strong>:101603.<\/li>\n<li>Murakami-Sekimata, A., Sekimata, M., Sato, N., Hayasaka, Y., and <span class=\"double\">Nakano, A.<\/span> (2020). Deletion of <em>pin4 <\/em>suppresses the protein transport defects caused by <em>sec12-4<\/em> mutation in <em>Saccharomyces cerevisiae<\/em>. <strong><em>Microbial Physiol. <\/em>30<\/strong>:25-35.<\/li>\n<li>\n<p>Fujii, S., <u>Kurokawa, K.<\/u>, Inaba, R., Hiramatsu, N., Tago, T., Nakamura, Y., <span class=\"double\">Nakano, A.<\/span>, Satoh, T., and Satoh, A. K. (2020). Recycling endosomes attach to the trans-side of Golgi stacks in <em>Drosophila<\/em> and mammalian cells. <strong><em>J. Cell Sci.<\/em><\/strong> <strong>133<\/strong>: jcs236935.<\/p>\n<\/li>\n<li><u>Kurokawa, K.<\/u> and <span class=\"double\">Nakano, A.<\/span> (2020). Live-cell imaging by super-resolution confocal live imaging microscopy (SCLIM): simultaneous three-color and four-dimensional live cell imaging with high space and time resolution. <strong><em>Bio-protocol<\/em><\/strong> <strong>10<\/strong>:e3732.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u52a0\u85e4\u85ab<small>\uff08\u7523\u696d\u6280\u8853\u7dcf\u5408\u7814\u7a76\u6240\u3000\u30d0\u30a4\u30aa\u30e1\u30c7\u30a3\u30ab\u30eb\u7814\u7a76\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Higaki T., Akita K., <u>Katoh K<\/u> (2020)<br \/>\nCoefficient of variation as an image-intensity metric for cytoskeleton bundling<br \/>\n<em>Sci. Rep.<\/em> 10, 22187. https:\/\/doi.org\/10.1038\/s41598-020-79136-x<\/p>\n<\/li>\n<li>\n<p>Yamaguchi H., Honda S., Torii S., Shimizu K., <u>Katoh K.<\/u>, Miyake K., Miyake N., Fujikake N.,<br \/>\nSakurai H.T., Arakawa S., Shimizu S.(2020)<br \/>\nWipi3 is essential for alternative autophagy and its loss causes neurodegeneration. <em>Nat Commun <\/em>11, 5311. <a href=\"https:\/\/doi.org\/10.1038\/s41467-020-18892\" target=\"_blank\" rel=\"noopener\">https:\/\/doi.org\/10.1038\/s41467-020-18892<\/a><\/p>\n<\/li>\n<li>Ueno Y., Matsuda K., <u>Katoh K.<\/u>, Kuzuya A., Kakugo A., Konagaya A. (2020)\u00a0 Modeling a Microtubule Filaments Mesh Structure from Confocal Microscopy Imaging. <em>Micromachines<\/em> 11 (9), 844 https:\/\/doi.org\/10.3390\/mi11090844<\/li>\n<li>\n<p>Pelc R., Hostounsk\u00fd Z., Otaki T., <u>Katoh K.<\/u> (2020)\u00a0 Conventional, Apodized, and Relief Phase-Contrast Microscopy. In: Pelc R., Walz W., Doucette J. (eds) Neurohistology and Imaging Techniques. Neuromethods, vol 153. Humana, New York, NY.<br \/>\n<a href=\"https:\/\/doi.org\/10.1007\/978-1-0716-0428-1_10\" target=\"_blank\" rel=\"noopener\">https:\/\/doi.org\/10.1007\/978-1-0716-0428-1_10<\/a><\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6728\u4e0b\u30bf\u30ed\u30a6<small>\uff08\u5927\u962a\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Kobayashi, A.*, Hirata, T.*, Nishikaze, T., Ninomiya, A., Maki, Y., Takada, Y., Kitamoto, T., and <span style=\"text-decoration: underline;\">Kinoshita, T.<\/span> (2020) \u03b12, 3-linkage of sialic acid to a GPI-anchor and an unpredicted GPI attachment site in human prion protein. <strong><em>J. Biol. Chem.<\/em><\/strong>, 295(22):7789-7798.<\/p>\n<\/li>\n<li>\n<p>Lee, G.-H., Fujita, M., Nakanishi, H., Miyata, H., Ikawa, M., Maeda, Y., Murakami, Y., and <span style=\"text-decoration: underline;\">Kinoshita, T.<\/span> (2020) PGAP6, a GPI-specific phospholipase A2, has narrow substrate specificity against GPI-anchored proteins. <strong><em>J. Biol. Chem.<\/em><\/strong>, 295(42):14501-14509.<\/p>\n<\/li>\n<li>\n<p>Langemeijer, S., Schaap, C., Preijers, F., Jansen, J. H., Blijlevens, N., Inoue, N., Muus, P., <span style=\"text-decoration: underline;\">Kinoshita, T.<\/span>, and Murakami, Y. (2020) Paroxysmal nocturnal hemoglobinuria caused by CN-LOH of constitutional\u00a0<em>PIGB<\/em>\u00a0mutation and 70-kb microdeletion on 15q. <strong><em>Blood Adv<\/em><\/strong><em>.<\/em>, 4(22):5755-5761.<\/p>\n<\/li>\n<li>Guo, X.-Y., Liu, Y.-S., Gao, X.-D., <span style=\"text-decoration: underline;\">Kinoshita, T.<\/span>, and Fujita, M. (2020) Calnexin mediates the maturation of GPI-anchors through ER retention. <strong><em>J. Biol. Chem.<\/em><\/strong>, in press.<\/li>\n<li>\n<p>Okuda, T., Yonekawa, T., Murakami, Y., <span style=\"text-decoration: underline;\">Kinoshita, T.<\/span>, Matsushita, K., Koike, Y., Inoue, M., Uchida, K., Yodoya, N., Ohashi, H., Sawada, H., Iwamoto, S., Mitani, Y., and Hirayama, M. (2020) PIGO variants in a boy with features of Mabry syndrome who also exhibits Fryns syndrome with peripheral neuropathy. <strong><em>Am. J. Med. Genet. A<\/em><\/strong>, in press.<\/p>\n<\/li>\n<li>\n<p><u>Kinoshita, T.<\/u>\u00a0(2020) Biosynthesis and biology of mammalian GPI-anchored proteins.\u00a0<strong><em>Open Biol.<\/em><\/strong>, 10: 190290. (Review)<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32156170\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32156170<\/a><\/p>\n<\/li>\n<li>\n<p>Wang, Y., Maeda, Y., Liu, Y.-S., Takada, Y., Ninomiya, A., Hirata, T., Fujita, M., Murakami, Y., and\u00a0<u>Kinoshita, T.<\/u>\u00a0(2020) Cross-talks of glycosylphosphatidylinositol biosynthesis with glycosphingolipid biosynthesis and ER-associated degradation.\u00a0<strong><em>Nat. Commun.<\/em><\/strong>, 11:860.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32054864\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32054864<\/a><\/p>\n<\/li>\n<li>\n<p>Nguyen, T. T. M., Murakami, Y., Mobilio, S., Niceta, M., Zampino, G., Philippe, C., Moutton, S., Zaki, M. S., James, K., Musaev, D., Mu, W., Baranano, K., Nance, J. R., Rosenfeld, J. A., Braverman, N., Ciolfi, A., Millan, F., Person, R. E., Bruel, A.-L., Thauvin-Robinet, C., Ververi, A., DeVile, C., Male, A., Efthymiou, S., Maroofian, R., Houlden, H., Maqbool, S., Rahman, F., Baratang, N. V., Rousseau, J., St-Denis, A., Elrick, M. J., Anselm, I., Rodan, L.H., Tartaglia, M., Gleeson, J.,\u00a0<u>Kinoshita, T.,<\/u>\u00a0and Campeau, P. M. (2020) Bi-allelic variants in the GPI transamidase subunit PIGK cause a neurodevelopmental syndrome with hypotonia and cerebellar atrophy and epilepsy.\u00a0<strong><em>Am. J. Hum. Genet.<\/em><\/strong>, in press.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32220290\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/32220290<\/a><\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e2d\u5c71\u548c\u4e45<small>\uff08\u4eac\u90fd\u5927\u5b66\u5927\u5b66\u9662\u3000\u85ac\u5b66\u7814\u7a76\u79d1\uff09<\/small><\/h3>\n<ol>\n<li>Nakamura, K., Noguchi, T., Takahara, M., Omori, Y., Furukawa, T., Katoh, Y., and <u>Nakayama, K.<\/u> (2020) Anterograde trafficking of ciliary MAP kinase-like ICK\/CILK1 by the intraflagellar transport machinery is required for intraciliary retrograde protein trafficking. <strong><em>J. Biol. Chem.<\/em>, 295,<\/strong> 13363-13376.<\/li>\n<li>\n<p>Okazaki, M., Kobayashi, T., Chiba, S., Takei, R., Liang, L., <u>Nakayama, K.<\/u>, and Katoh, Y. (2020) Formation of the B9-domain protein complex MKS1\u2013B9D2\u2013B9D1 is essential as a diffusion barrier for ciliary membrane proteins. <strong><em>Mol. Biol. Cell<\/em>, 31,<\/strong> 2259-2268.<\/p>\n<\/li>\n<li>\n<p>Katoh, Y., Chiba, S., and <u>Nakayama, K.<\/u> (2020) Practical method for super-resolution imaging of primary cilia and centrioles by expansion microscopy using an amplibody for fluorescence signal amplification. <strong><em>Mol. Biol. Cell<\/em>, 31,<\/strong> 2195-2206.<\/p>\n<\/li>\n<li>\n<p>Okamoto, S., Naito, T., Shigetomi, R., Kosugi, Y., <u>Nakayama, K.<\/u>, Takatsu, H., and Shin, H.-W. (2020) The N- or C-terminal cytoplasmic regions of P4-ATPases determine their cellular localization.<strong><em> Mol. Biol. Cell<\/em>, 31,<\/strong> 2115\u20132124.<\/p>\n<\/li>\n<li>\n<p><u>Nakayama, K.<\/u> and Katoh, Y. (2020) Architecture of the IFT ciliary trafficking machinery and interplay between its components. <strong><em>Crit. Rev. Biochem. Mol. Biol.<\/em>, 55,<\/strong> 179-196.<\/p>\n<\/li>\n<li>\n<p>Tone, T., <u>Nakayama, K.<\/u>, Takatsu, H., and Shin, H.-W. (2020) ATPase reaction cycle of P4-ATPases affects their transport from the endoplasmic reticulum. <strong><em>FEBS Lett.<\/em>, 594,<\/strong> 412-423.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u5c3e\u91ce\u96c5\u54c9<small>\uff08\u56fd\u7acb\u304c\u3093\u7814\u7a76\u30bb\u30f3\u30bf\u30fc\u7814\u7a76\u6240\u3000\u81e8\u5e8a\u30d7\u30ed\u30c6\u30aa\u30fc\u30e0\u89e3\u6790\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Yoshida, S., Aoki, K., Fujiwara, K., Nakakura, T., Kawamura, A., Yamada, K., <span style=\"text-decoration: underline;\">Ono, M.<\/span>, Yogosawa, S., Yoshida, K. (2020) The novel ciliogenesis regulator DYRK2 governs Hedgehog signaling during mouse embryogenesis. <em><strong>Elife<\/strong><\/em>, 9, e57381.<\/p>\n<\/li>\n<li>Gao, Y., Nihira, N.T., Bu, X., Chu, C., Zhang, J., Kolodziejczyk, A., Fan, Y., Chan, N.T., Ma, L., Liu, J., Wang, D., Dai, X., Liu, H., <span style=\"text-decoration: underline;\">Ono, M.<\/span>, Nakanishi, A., Inuzuka, H., North, B.J., Huang, Y.H., Sharma, S., Geng, Y., Xu, W., Liu, X.S., Li, L., Miki, Y., Sicinski, P., Freeman, G.J., Wei, W. (2020) Acetylation-dependent regulation of PD-L1 nuclear translocation dictates the efficacy of anti-PD-1 immunotherapy. <em><strong>Nat Cell Biol.<\/strong><\/em>, Epub ahead.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7530\u6751\u5eb7<small>\uff08\u5c71\u5f62\u5927\u5b66\u3000\u7406\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Nakamura, S., Matsui, A., Akabane, S. <u>Tamura, Y.<\/u>, Hatano, Z., Miyano, Y., Omote, H., Kajikawa, M., Maenaka, K., Moriyama, Y., Endo, T., &amp; Oka T. (2020) The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain. <strong><em>Commun Biol.<\/em><\/strong>, 3: 99.<\/p>\n<\/li>\n<li>\n<p>Kudo S., Shiino H., Furuta S., <u>Tamura Y<\/u>.* (2020) Yeast transformation stress, together with loss of Pah1, phosphatidic acid phosphatase, leads to Ty1 retrotransposon insertion into the <em>INO4<\/em> gene <strong><em>FASEB J.<\/em><\/strong>, 34(3): 4749-4763.<\/p>\n<\/li>\n<li>\n<p>Watanabe Y., <u>Tamura Y.<\/u>, Kakuta C., Watanabe S., and Endo T.* (2020) Structural basis for inter-organelle phospholipid transport mediated by VAT-1<strong><em> JBC.<\/em><\/strong>, 295(10): 3257-3268.<\/p>\n<\/li>\n<li>\n<p><u>Tamura Y<\/u>. Kawano S. and Endo T*. (2020) Lipid homeostasis in mitochondria. <strong><em>Biol Chem.<\/em><\/strong>, in press (DOI: 10.1515\/hsz-2020-0121.).<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4eca\u6cc9\u548c\u5247<small>\uff08\u5e83\u5cf6\u5927\u5b66\u5927\u5b66\u9662\u533b\u6b6f\u85ac\u4fdd\u5065\u5b66\u7814\u7a76\u79d1\u3000\u5206\u5b50\u7d30\u80de\u60c5\u5831\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Okamoto, T., <u>Imaizumi, K.<\/u>, and Kaneko, M. (2020) The Role of Tissue-Specific Ubiquitin Ligases, RNF183, RNF186, RNF182 and RNF152, in Disease and Biological Function. <strong><em>Int J Mol Sci<\/em><\/strong><em>,<\/em> 21:3921.<\/li>\n<li>Matsuhisa, K., Saito, A., Cai, L., Kaneko, M., Okamoto, T., Sakaue, F., Asada, R., Urano, F., Yanagida, K., Okochi, M., Kudo, Y., Matsumoto, M., Nakayama, K. I., and <u>Imaizumi, K.<\/u> (2020) Production of BBF2H7-derived small peptide fragments via endoplasmic reticulum stress-dependent regulated intramembrane proteolysis. <strong><em>FASEB J<\/em><\/strong><em>,<\/em> 34:865-880.<\/li>\n<li>Okamoto, T., Wu, Y., Matsuhisa, K., Saito, A., Sakaue, F., <u>Imaizumi, K.<\/u>, and Kaneko, M. (2020) Hypertonicity-responsive ubiquitin ligase RNF183 promotes Na, K-ATPase lysosomal degradation through ubiquitination of its beta1 subunit. <strong><em>Biochem Biophys Res Commun<\/em><\/strong><em>,<\/em> 521:1030-1035.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u77e2\u6728\u5b8f\u548c<small>\uff08\u540d\u53e4\u5c4b\u5e02\u7acb\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li><u>Yagi, H.<\/u>, Yagi-Utsumi, M., Honda, R., Ohta, Y., Saito, T., Nishio, M., Ninagawa, S., Suzuki, K., Anzai, T., Kamiya, Y., Aoki, K., Nakanishi, M., Satoh, T. and Kato, K. (2020) Improved secretion of glycoproteins using an N-glycan-restricted passport sequence tag recognized by cargo receptor. <strong><em>Nature Commun.<\/em><\/strong>, 11, Article number: 1368<\/li>\n<li>George, G., Ninagawa, S., <u>Yagi, H.<\/u>, Saito, T., Ishikawa, T., Sakuma, T., Yamamoto, T., Imami, K., Ishihama, Y., Kato, K., Okada, T. and Mori, K. (2020) EDEM2 stably disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD. <strong><em>eLife<\/em><\/strong>, 9, e53455<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u82b1\u7530\u8ce2\u592a\u90ce<small>\uff08\u56fd\u7acb\u611f\u67d3\u75c7\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Morimoto, K., Suzuki, N., Tanida, I., Kakuta, S., Furuta, Y., Uchiyama, Y., <span style=\"text-decoration: underline;\">Hanada, K.<\/span>, Suzuki, Y., Yamaj, T. (2020) Blood group P1 antigen-bearing glycoproteins are functional but less efficient receptors of Shiga toxin than conventional glycolipid-based receptors, <em><strong>J. Biol. Chem.<\/strong><\/em>, in press.<\/li>\n<li><span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2020) Organelle contacts: sub-organelle zones to facilitate rapid and accurate inter-organelle trafficking of lipids. <em><strong>Traffic<\/strong><\/em>, 21, 189-196. doi: org\/10.1111\/tra.12716 (invited commentary)<\/li>\n<li>Tachida, Y., Kumagai, K., Sakai, S., Ando, S., Yamaji, T., and <span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2020) Chlamydia trachomatis-infected human cells convert ceramide to sphingomyelin without sphingomyelin synthases 1 and 2. <em><strong>FEBS Let.<\/strong><\/em>, 594, 519-529. (T.Y. and K.H. are co-correspondence) doi: org\/10.1002\/1873-3468.13632.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u897f\u982d\u82f1\u8d77<small>\uff08\u5bae\u5d0e\u5927\u5b66\u3000\u533b\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Kato, H., Okabe, K., Miyake, M., Hattori, K., Fukaya, T., Tanimoto, K., Beini, S., Mizuguchi, M., Torii, S., Arakawa, S., Ono, M., Saito, Y., Sugiyama, T., Funatsu, T., Sato, K., Shimizu, S., Oyadomari, S., Ichijo, H., Kadowaki, H., <span style=\"text-decoration: underline;\">Nishitoh, H.<\/span> (2020) ER-resident sensor PERK is essential for mitochondrial thermogenesis in brown adipose tissue. <strong><em>Life Sci. Alliance<\/em><\/strong> DOI:10.26508\/lsa.201900576<\/p>\n<\/li>\n<\/ol>\n<h2 id=\"2019\">2019\u5e74<\/h2>\n<h3 class=\"achievementtitle\">\u52a0\u85e4\u85ab<small>\uff08\u7523\u696d\u6280\u8853\u7dcf\u5408\u7814\u7a76\u6240\u3000\u30d0\u30a4\u30aa\u30e1\u30c7\u30a3\u30ab\u30eb\u7814\u7a76\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Ishida K., Goto S., Ishimura M., Amanuma M., Hara Y., Suzuki R., <u>Katoh K.<\/u>, Morita E. (2019)<br \/>\nFunctional Correlation between Subcellular Localizations of Japanese Encephalitis Virus Capsid Protein and Virus Production.<br \/>\n<em>J Virol <\/em>93:e00612-19. https:\/\/doi.org\/10.1128\/JVI.00612-19<\/p>\n<\/li>\n<li>\n<p>Morita, M, Ota, Y, <u>Katoh, K<\/u>, Noda, N (2019)\u00a0 Bacterial Cell Culture at the Single-cell Level Inside Giant Vesicles.<br \/>\n<em>JOVE-JOURNAL OF VISUALIZED EXPERIMENTS,<\/em> (146):10.3791\/59555<\/p>\n<\/li>\n<li>Tanaka, M., Fujii, Y., Hirano, K., Higaki, T., Nagasaki, A., Ishikawa, R., Okajima, T., <span style=\"text-decoration: underline;\">Katoh, K<\/span>\u00a0(2019). Fascin in lamellipodia contributes to cell elasticity by controlling the orientation of filamentous actin. <strong><em>Genes to Cells.<\/em><\/strong> 24, p202-213, https:\/\/doi.org\/10.1111\/gtc.12671<\/li>\n<li>Takata, H., Madung, M., <span style=\"text-decoration: underline;\">Katoh, K.<\/span>, Fukui, K.(2019) Cdk1-dependent phosphorylation of KIF4A at S1186 triggers lateral chromosome compaction during early mitosis. <strong><em>PLoS One\u00a0<\/em><\/strong>13(12): e0209614\u00a0 doi.org\/10.1371\/journal.pone.0209614<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7530\u6751\u5eb7<small>\uff08\u5c71\u5f62\u5927\u5b66\u3000\u7406\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Matsumoto S., Nakatsukasa K., Kakuta C., <u>Tamura Y.<\/u>, Esaki M., and Endo T. (2019) Msp1 Clears Mistargeted Proteins by Facilitating Their Transfer from Mitochondria to the ER <strong><em>Mol. Cell.<\/em><\/strong>, 76: 191-205.<\/p>\n<\/li>\n<li>\n<p>Wang C., Taki M., Sato Y., <u>Tamura Y.<\/u>, Yaginuma H., Okada Y., and Yamaguchi S. (2019) A photostable fluorescent marker for the superresolution live imaging of the dynamic structure of the mitochondrial cristae <strong><em>PNAS.<\/em><\/strong>, 116: 15817-15822.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4eca\u6cc9\u548c\u5247<small>\uff08\u5e83\u5cf6\u5927\u5b66\u5927\u5b66\u9662\u533b\u6b6f\u85ac\u4fdd\u5065\u5b66\u7814\u7a76\u79d1\u3000\u5206\u5b50\u7d30\u80de\u60c5\u5831\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Wu, Y., Kimura, Y., Okamoto, T., Matsuhisa, K., Asada, R., Saito, A., Sakaue, F., <u>Imaizumi, K.<\/u>, and Kaneko, M. (2019) Inflammatory bowel disease-associated ubiquitin ligase RNF183 promotes lysosomal degradation of DR5 and TRAIL-induced caspase activation. <strong><em>Sci Rep<\/em><\/strong><em>,<\/em> 9:20301.<\/p>\n<\/li>\n<li>Maeoka, Y., Okamoto, T., Wu, Y., Saito, A., Asada, R., Matsuhisa, K., Terao, M., Takada, S., Masaki, T., <u>Imaizumi, K.<\/u>, and Kaneko, M. (2019) Renal medullary tonicity regulates RNF183 expression in the collecting ducts via NFAT5. <strong><em>Biochem Biophys Res Commun<\/em><\/strong><em>,<\/em> 514:436-442.<\/li>\n<li>Osaki, Y., Matsuhisa, K., Che, W., Kaneko, M., Asada, R., Masaki, T., <u>Imaizumi, K.<\/u>, and Saito, A. (2019) Calnexin promotes the folding of mutant iduronate 2-sulfatase related to mucopolysaccharidosis type II. <strong><em>Biochem Biophys Res Commun<\/em><\/strong><em>,<\/em> 514:217-223.<\/li>\n<li>Maeoka, Y., Wu, Y., Okamoto, T., Kanemoto, S., Guo, X. P., Saito, A., Asada, R., Matsuhisa, K., Masaki, T., <u>Imaizumi, K.<\/u>, and Kaneko, M. (2019) NFAT5 up-regulates expression of the kidney-specific ubiquitin ligase gene Rnf183 under hypertonic conditions in inner-medullary collecting duct cells. <strong><em>J Biol Chem<\/em><\/strong>, 294:101-115.<\/li>\n<li>Ariyasu, D., Kubo, E., Higa, D., Shibata, S., Takaoka, Y., Sugimoto, M., <u>Imaizumi, K.<\/u>, Hasegawa, T., and Araki, K. (2019) Decreased Activity of the Ghrhr and Gh Promoters Causes Dominantly Inherited GH Deficiency in Humanized GH1 Mouse Models.<strong><em>Endocrinology<\/em><\/strong>, 160:2673-<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u77e2\u6728\u5b8f\u548c<small>\uff08\u540d\u53e4\u5c4b\u5e02\u7acb\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Yogo, R., Yamaguchi, Y., Watanabe, H., <u>Yagi, H.<\/u>, Satoh, T., Nakanishi, M., Onitsuka, M., Omasa, T., Shimada,M., Maruno,T., Torisu, T., Watanabe, S., Higo, D., Uchihashi, T., Yanaka, S., Uchiyama, S., and Kato, K. (2019) The Fab portion of immunoglobulin G contributes to its binding to Fc\u03b3 receptor III. <strong><em>Sci. Rep.<\/em><\/strong>, 9, Article number: 11957<\/p>\n<\/li>\n<li>\n<p>Yanaka, S., Yogo, R., Inoue, R., Sugiyama, M., Itoh, S.G., Okumura, H., Miyanoiri, Y., <u>Yagi, H.<\/u>, Satoh, T., Yamaguchi, T. and Kato, K. (2019) Dynamic views of the Fc region of immunoglobulin G provided by experimental and computational observations. <strong><em>Antibodies<\/em><\/strong>, 8, 39<\/p>\n<\/li>\n<li>\n<p>Harada, Y., Kizuka, Y., Tokoro, Y., Kondo, K., <u>Yagi, H.<\/u>, Kato, K., Inoue, H., Taniguchi, N. and Maruyama, I. (2019) N-glycome inheritance from cells to extracellular vesicles in B16 melanomas. <strong><em>FEBS Lett.<\/em><\/strong>, 593, 942-951<\/p>\n<\/li>\n<li>\n<p>Narentuya, Y., Takeda-Uchimura, T., Foyez, Z., Zhang, T., Akama, O., <u>Yagi, H.<\/u>, Kato, K., Komatsu, Y., Kadomatsu, K. and Uchimura, K. (2019) GlcNAc6ST3 is a keratan sulfate sulfotransferase for the protein- tyrosine phosphatase PTPRZ in the adult brain. <strong><em>Sci. Rep.<\/em><\/strong>, 9, Article number: 4387<\/p>\n<\/li>\n<li>\n<p>Harada, Y., Suzuki, T., Fukushige, T., Kizuka, Y., <u>Yagi, H.<\/u>, Yamamoto, M., Kondo, K., Inoue, H., Kato, K., Taniguchi, N., Kanekura, T., Dohmae, N. and Maruyama, I. (2019) Generation of the heterogeneity of extracellular vesicles by membrane organization and sorting machineries <strong><em>Biochim. Biophys. Acta \u2013General Subjects<\/em><\/strong>, 1863, 681-691<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u82b1\u7530\u8ce2\u592a\u90ce<small>\uff08\u56fd\u7acb\u611f\u67d3\u75c7\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Kumagai. K., and <span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2019) Structure, functions, and regulation of CERT, a lipid-transfer protein for the delivery of ceramide at the ER-Golgi membrane contact sites, <em><strong>FEBS Let.<\/strong><\/em>, 593, 2366-2377. (K.K. and K.H. are co-correspondence) doi: org\/10.1002\/1873-3468.13511. (invited review)<\/li>\n<li>Yamaji, T., Hanamatsu, H., Sekizuka, T., Kuroda, M., Ohnishi, M.,Furukawa, J., Yahiro, K., and <span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2019) A CRISPR screen using subtilase cytotoxin identifies SLC39A9 as a glycan-regulating factor, <em><strong>iScience<\/strong><\/em>, 15, 407-420. doi: 10.1016\/j.isci.2019.05.005.<\/li>\n<li>Nakao, N., Ueno, M., Sakai, S., Egawa, D., Hanzawa, H., Kawasaki, S., Kumagai, K., Suzuki, M., Kobayashi, S., and <span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2019) Natural ligand-nonmimetic inhibitors to the lipid transfer protein CERT, <strong><em>Comms. Chem.<\/em><\/strong>, 2, article 20. (N.N., M.U., and S.S. are co-first authors. S.K. and K.H. are co-correspondence) doi: 10.1038\/s42004-019-0118-3 (open access: <a href=\"https:\/\/www.nature.com\/articles\/s42004-019-0118-3\" target=\"_blank\" rel=\"noopener\">https:\/\/www.nature.com\/articles\/s42004-019-0118-3<\/a>)<\/li>\n<li>Yamaji, T., Sekizuka, T., Tachida, Y., Sakuma, C., Kuroda, M., and <span style=\"text-decoration: underline;\">Hanada, K.<\/span> (2019) A CRISPR screen identifies LAPTM4A and TM9SF proteins as glycolipid-regulating factors, <strong><em>iScience<\/em><\/strong>, 11, 409-424. doi: org\/10.1016\/j.isci.2018.12.039.<\/li>\n<li>Shimizu, Y., Shirasago, Y., Suzuki, T., Hata, T., Kondoh, M., <span style=\"text-decoration: underline;\">Hanada, K.<\/span>, Yagi, K., and Fukasawa, M. (2019) Characterization of monoclonal antibodies recognizing each extracellular loop domain of occluding, <strong><em>J Biochem<\/em><\/strong>, 166, 297-308. doi: 10.1093\/jb\/mvz037<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6728\u4e0b\u30bf\u30ed\u30a6<small>\uff08\u5927\u962a\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Wang, Y., Hirata, T., Maeda, Y., Murakami, Y., Fujita, M., and <u>Kinoshita, T.<\/u> (2019) Free, unlinked glycosylphosphatidylinositols on mammalian cell surfaces revisited. <strong><em>J. Biol. Chem.<\/em><\/strong>, 294:5038-5049.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30728244\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30728244<\/a><\/p>\n<\/li>\n<li>\n<p>Sou, Y-S, Kakuta, S., Kamikubo, Y., Niisato, K., Sakurai, T., Parajuli, L. K., Tanida, I., Saito, H., Suzuki, N., Sakimura, K., Maeda, Y., <u>Kinoshita, T.<\/u>, Uchiyama, Y., and Koike, M. (2019) Cerebellar neurodegeneration and neuronal circuit remodeling in Golgi pH regulator-deficient mice. <strong><em>eNeuro<\/em><\/strong>, 6(3): e0427-18.2019.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31118204\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31118204<\/a><\/p>\n<\/li>\n<li>\n<p>Murakami, Y.,* Nguyen*, T. T. M., Baratang, N., Raju, P. K., Knaus, A., Ellard, S., Jones, G., Lace, B., Rousseau, J., Ajeawung, N. F., Kamei, A., Minase, G., Akasaka, M., Araya, N., Koshimizu, E., van den Ende, J., Erger, F., Altm\u00fcller, J., Krumina, Z., Strautmanis, J., Inashkina, I., Stavusis, J., El-Gharbawy, A., Sebastian, J., Dua Puri, R., Kulshrestha, S., Verma, I. C., Maier, E. M., Haack, T., Israni, A., Baptista, J., Gunning, A., Rosenfeld, J. A., Liu, P., Joosten, M., Rocha, M. E., Hashem, M. O., Aldhalaan, H. M., Alkuraya, F. S., Miyatake, S., Matsumoto, N., Krawitz, P., Rossignol, E., <u>Kinoshita, T.<\/u>, and Campeau, P. M. (2019) Mutations in <em>PIGB<\/em> cause an inherited GPI biosynthesis defect with an axonal neuropathy and metabolic abnormality in severe cases. <strong><em>Am. J. Hum. Genet.<\/em><\/strong>, 105:384-394.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31256876\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31256876<\/a><\/p>\n<\/li>\n<li>\n<p>Knaus, A., Kort\u00fcm, F., Kleefstra, T., Stray-Pedersen, A., Duki\u0107, D., Murakami, Y., Gerstner, T., van Bokhoven, H., Iqbal, Z., Horn, D., <u>Kinoshita, T.<\/u>, Hempel, M., and Krawitz, P, M. (2019) Mutations in <em>PIGU<\/em> impair the function of the GPI transamidase complex causing severe intellectual disability, epilepsy and brain anomalies. <strong><em>Am. J. Hum. Genet.<\/em><\/strong>, 105:395-402.<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31353022\" target=\"_blank\" rel=\"noopener\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31353022<\/a><\/p>\n<\/li>\n<li>\n<p>Hoechsmann, B.*, Murakami, Y. *, Osato, M. *, Knaus, A., Kawamoto, M., Inoue, N., Hirata, T., Murata, S., Anliker, M., Eggermann, T., Jaeger, M., Floettmann, R., Hoellein, A., Murase, S., Ueda, Y., Nishimura, J., Kanakura, Y., Kohara, N., Schrezenmeier, H.+, Krawitz, P. M.+, and <u>Kinoshita, T.<\/u> + (2019) Complement and inflammasome overactivation mediates paroxysmal nocturnal hemoglobinuria with autoinflammation. <strong><em>J. Clin. Invest.<\/em><\/strong>,129:5123-5136. doi: 10.1172\/JCI123501<br \/>\n<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31430258\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/31430258<\/a><\/p>\n<\/li>\n<li>\n<p>Thompson, M., Knaus, A., Caliebe, A., Muhle, H., Nguyen, M., Baratang, N., <u>Kinoshita, T.<\/u>, Percy, M., Campeau, P., Murakami, Y., Krawitz, P., Cole, D., and Mabry, C. (2019) A post glycosylphosphatidylinositol (GPI) attachment to proteins, type 2 (PGAP2) variant identified in Mabry syndrome index cases: molecular genetics of the prototypical inherited GPI disorder. <strong><em>Eur. J. Med. Genet.<\/em><\/strong>, in press.<br \/>\n<a href=\"https:\/\/doi.org\/10.1016\/j.ejmg.2019.103822\">https:\/\/doi.org\/10.1016\/j.ejmg.2019.103822<\/a><\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7247\u6850\u8c4a\u96c5<small>\uff08\u5fb3\u5cf6\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Kimura\u00a0R,\u00a0Yoshimaru\u00a0T,\u00a0Matsushita\u00a0Y,\u00a0Matsuo\u00a0T,\u00a0Ono\u00a0M,\u00a0Park\u00a0JH,\u00a0Sasa\u00a0M,\u00a0Miyoshi\u00a0Y,\u00a0Nakamura\u00a0Y,\u00a0*<u>Katagiri\u00a0T<\/u>.\u00a0<br \/>\nThe\u00a0GALNT6-LGALS3BP\u00a0axis\u00a0promotes\u00a0breast\u00a0cancer\u00a0cell\u00a0growth.\u00a0<em><strong>Int\u00a0J\u00a0Oncol.<\/strong><\/em>,\u00a0in\u00a0press.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u5409\u7530\u79c0\u90ce<small>\uff08\u5175\u5eab\u770c\u7acb\u5927\u5b66\u3000\u751f\u547d\u7406\u5b66\u7814\u7a76\u79d1\uff09<\/small><\/h3>\n<ol>\n<li>Jamaludin, M. I., Wakabayashi S., Sasaki K., Komori R., Kawamura H., Takase H., Sakamoto M., Yoshida H. (2019) MGSE regulates crosstalk from the mucin pathway to the TFE3 pathway of the Golgi stress response. <strong><em>Cell Struct Funct.<\/em><\/strong> in press.<\/li>\n<li>Kimura M, Sasaki K, Fukutani Y, <u>Yoshida H<\/u>, Ohsawa I, Yohda M, Sakurai K. (2019) Anticancer saponin OSW-1 is a novel class of selective Golgi stress inducer, <em><strong>Bioorg Med Chem Lett.<\/strong><\/em> 29, 1732-1736. doi: 10.1016\/j.bmcl.2019.05.022s<\/li>\n<li>Sasaki K, <u>Yoshida H.<\/u> (2019) Organelle Zones, <em><strong>Cell Struct Funct.<\/strong><\/em> 44, 85-94. doi: 10.1247\/csf.19010<\/li>\n<li>Sasaki K, <u>Yoshida H.<\/u> (2019) Golgi stress response and organelle zones, <strong><em>FEBS Lett.<\/em><\/strong>, in press. doi: 10.1002\/1873-3468.13554<\/li>\n<li>Sasaki K, Komori R, Taniguchi M, Shimaoka A, Midori S, Yamamoto M, Okuda C, Tanaka R, Sakamoto M, Wakabayashi S, <u>Yoshida H<\/u>. (2019) PGSE Is a Novel Enhancer Regulating the Proteoglycan Pathway of the Mammalian Golgi Stress Response, <em><strong>Cell Struct Funct<\/strong><\/em>. 44, 1-19. doi: 10.1247\/csf.18031.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u897f\u982d\u82f1\u8d77<small>\uff08\u5bae\u5d0e\u5927\u5b66\u3000\u533b\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>Tatenaka, Y., Kato, H., Ishiyama, M., Sasamoto, K., Shiga, M., <u>Nishitoh, H.<\/u>, Ueno, Y. (2019) Monitoring lipid droplet dynamics in living cells by using fluorescent probes. <strong><em>Biochemistry<\/em><\/strong> 58:499-503.<\/li>\n<li><u>Nishitoh, H.<\/u> (2019) Paradigm shift from &#8220;Compartment&#8221; to &#8220;Zone&#8221; in the understanding of organelles. <strong><em>J Biochem.<\/em><\/strong> 165, 97\u201399.<\/li>\n<li>Kadowaki, H. and\u00a0<u>Nishitoh, H.<\/u>\u00a0(2019) Endoplasmic reticulum quality control by garbage disposal.\u00a0<strong><em>FEBS J.<\/em><\/strong> 286:232-240.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e2d\u91ce\u660e\u5f66<small>\uff08\u7406\u5316\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Ishii, A., <u>Kurokawa, K.<\/u>, Hotta, M., Yoshizaki, S., Kurita, M., Koyama, A., <u>Nakano, A.<\/u>, and Kimura, Y. (2019). Role of Atg8 in the regulation of vacuolar membrane invagination. <strong><em>Sci. Rep. <\/em>9<\/strong>:14828.<\/li>\n<li>\n<p>Shimada, T. L., Shimada, T., Okazaki, Y., Higashi, Y., Saito, K., Kuwata, K., Oyama, K., Kato, M., Ueda, H., <u>Nakano, A.<\/u>, Ueda, T., Takano, Y., and Hara-Nishimura, I. (2019). HIGH STEROL ESTER 1 is a key factor in plant sterol homeostasis. <strong><em>Nat. Plants<\/em><\/strong> <strong>5<\/strong>:1154-1166.<\/p>\n<\/li>\n<li>Tojima, T., Suda, Y., Ishii, M., <u>Kurokawa, K.<\/u>, and <u>Nakano, A.<\/u> (2019). Spatiotemporal dissection of the <em>trans<\/em>-Golgi network in budding yeast. <strong><em>J. Cell Sci. <\/em>132<\/strong>:jcs231159.<\/li>\n<li>Maeda, M., <u>Kurokawa, K.<\/u>, Katada, T., <u>Nakano, A.<\/u>, and Saito, K. (2019). COPII proteins exhibit distinct subdomains within each ER exit site for executing their functions. <strong><em>Sci. Rep.<\/em><\/strong> <strong>9<\/strong>:7346.<\/li>\n<li>Shimada, T. L., Betsuyaku, S., Inada, N., Ebine, K., Fujimoto, M., Uemura, T., Takano, Y., Fukuda, H., <u>Nakano<\/u><u>, A.<\/u>, and Ueda, T. (2019). Enrichment of phosphatidylinositol 4,5-bisphosphate in the extra-invasive hyphal membrane promotes Colletotrichum infection of <em>Arabidopsis thaliana<\/em>. <strong><em>Plant Cell Physiol. <\/em>60<\/strong>:1514-1524.<\/li>\n<li>Abe, M., Kosaka, S., Shibuta, M., Nagata, K., Uemura, T., <u>Nakano, A.<\/u>, and Kaya, H. (2019). Transient activity of the florigen complex during the floral transition in <em>Arabidopsis thaliana<\/em>. <strong><em>Development<\/em><\/strong> <strong>146<\/strong>:dev171504.<\/li>\n<li><u>Kurokawa, K.<\/u>, Osakada, H., Kojidani, T., Waga, M., Suda, Y., Asakawa, H., Haraguchi, T., and <u>Nakano, A.<\/u> (2019). Visualization of secretory cargo transport within the Golgi apparatus in living yeast cells. <strong><em>J. Cell Biol.<\/em><\/strong> <strong>218<\/strong>:1602-1618.<\/li>\n<li><span class=\"double\">Nakano, A.<\/span> and von Blume, J. (2019). Organelle zones. <strong><em>Mol. Biol. Cell<\/em><\/strong> 30:731.<\/li>\n<li>Uemura, T., Nakano, R. T., Takagi, J., Wang, Y., Kramer, K., Finkemeier, I., Nakagami, H., Tsuda, K., Ueda, T., Schulze-Lefert, P., and <span class=\"double\">Nakano\uff0cA.<\/span> (2019). A Golgi-released subpopulation of the\u00a0<em>trans<\/em>-Golgi network mediates protein secretion in Arabidopsis. <strong><em>Plant Physiol.<\/em><\/strong> 179:519-532.<\/li>\n<li><u>Kurokawa, K.<\/u>, and <span class=\"double\">Nakano, A.<\/span> (2019) The ER exit sites are specialized ER zones for the transport of cargo proteins from the ER to the Golgi apparatus. <strong><em>J Biochem.<\/em><\/strong> 165, 109\u2013114.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6cc9\u6b63\u7bc4<small>\uff08\u6771\u5317\u5927\u5b66\u3000\u5b66\u969b\u79d1\u5b66\u30d5\u30ed\u30f3\u30c6\u30a3\u30a2\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>\n<p><u>Izumi, M.<\/u>, Nakamura, S., Li, N. (2019) Autophagic turnover of chloroplasts: its roles and regulatory mechanisms in response to sugar starvation. <strong><em>Front. Plant Sci. <\/em><\/strong>10: 280<\/p>\n<\/li>\n<li>\n<p>Nakamura, S., <u>Izumi, M.<\/u> (2019) Chlorophagy is ATG gene-dependent microautophagy process, <strong><em>Plant Signal. Behav.<\/em><\/strong> 14: 1554469<\/p>\n<\/li>\n<li>\n<p><u>Izumi, M.<\/u>, Ishida, H. (2019) An additional role for chloroplast proteins\u2014an amino acid reservoir for energy production during sugar starvation, <strong><em>Plant Signal. Behav.<\/em><\/strong> 14: 1552057<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u9f4b\u85e4\u4f38\u4e00\u90ce<small>\uff08\u6771\u4eac\u5927\u5b66\u533b\u79d1\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>\n<p><span style=\"text-decoration: underline;\">\u9f4b\u85e4\u4f38\u4e00\u90ce<\/span> (2019) \u5f62\u8cea\u7d30\u80de\u69d8\u6a39\u72b6\u7d30\u80de\u306eTLR7\u306b\u3088\u308b1\u578b\u30a4\u30f3\u30bf\u30fc\u30d5\u30a7\u30ed\u30f3\u7523\u751f\u8a98\u5c0e\u6a5f\u69cb\u306e\u89e3\u660e\u3001\u611f\u67d3\u3000\u708e\u75c7\u3000\u514d\u75ab 49: 31-41.<\/p>\n<\/li>\n<li><span style=\"text-decoration: underline;\">Saitoh, SI<\/span>., Saitoh, YM., Kontani, K., Sato, K., Miyake, K. (2019) ADP-ribosylation factor-like 8b is required for the development of mouse models of systemic lupus erythematosus. <strong><em>International Immunology.<\/em><\/strong> 31(4):225-37. doi: 10.1093\/intimm\/dxy084. PubMed PMID: 30753473.<\/li>\n<li>\n<p>Furusho, K., Shibata, T., Sato, R., Fukui, R., Motoi, Y., Zhang, Y., <span style=\"text-decoration: underline;\">Saitoh, SI<\/span>., Ichinohe, T., Moriyama, M., Nakamura, S., Miyake, K. (2019)\u00a0 Cytidine deaminase enables Toll-like receptor 8 activation by cytidine or its analogs. <strong><em>International Immunology.<\/em><\/strong> 31: 167-173. doi: 10.1093\/intimm\/dxy075. PubMed PMID: 30535046.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6e05\u6c34\u91cd\u81e3<small>\uff08\u6771\u4eac\u533b\u79d1\u6b6f\u79d1\u5927\u5b66\u3000\u96e3\u6cbb\u75be\u60a3\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li><u>Shimizu, S.<\/u>\u00a0(2019) Organelle zones in mitochondria.\u00a0<strong><em>J Biochem.<\/em><\/strong> 165, 101\u2013107.<\/li>\n<\/ol>\n<h2 id=\"2018\">2018\u5e74<\/h2>\n<h3 class=\"achievementtitle\">\u52a0\u85e4\u85ab<small>\uff08\u7523\u696d\u6280\u8853\u7dcf\u5408\u7814\u7a76\u6240\u3000\u30d0\u30a4\u30aa\u30e1\u30c7\u30a3\u30ab\u30eb\u7814\u7a76\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>Morita, M., <span style=\"text-decoration: underline;\">Katoh,K.<\/span>, Noda, N.(2018) Direct Observation of Bacterial Growth in Giant Unilamellar Vesicles: A Novel Tool for Bacterial Cultures. <strong><em>ChemistryOpen<\/em><\/strong> <a href=\"https:\/\/doi.org\/10.1002\/open.201800126\" target=\"_blank\" rel=\"noopener\">https:\/\/doi.org\/10.1002\/open.201800126<\/a><\/li>\n<li>\u5927\u7027\u9054\u6717\u3001<span style=\"text-decoration: underline;\">\u52a0\u85e4\u85ab<\/span>\uff082018\uff09\u4f4d\u76f8\u5dee\u9855\u5fae\u93e1\u3000<strong><em>\u5b9f\u9a13\u533b\u5b66<\/em><\/strong>\u3000Vol36, No.20 (\u5897\u520a) p24-25<\/li>\n<li><span style=\"text-decoration: underline;\">\u52a0\u85e4\u85ab<\/span>\uff082018\uff09\u504f\u5149\u89b3\u5bdf\u3000<strong><em>\u5b9f\u9a13\u533b\u5b66<\/em><\/strong>\u3000Vol36, No.20 (\u5897\u520a) p30-31<\/li>\n<li><span style=\"text-decoration: underline;\">\u52a0\u85e4\u85ab<\/span>\uff082018\uff09\u8907\u5c48\u6298\u9855\u5fae\u93e1\uff08Polscope\uff09<strong><em>\u5b9f\u9a13\u533b\u5b66<\/em><\/strong>\u3000Vol36, No.20 (\u5897\u520a) p73-75<\/li>\n<li>\u5927\u7027\u9054\u6717\u3001<span style=\"text-decoration: underline;\">\u52a0\u85e4\u85ab<\/span>\uff082018\uff09\u30a2\u30dd\u30c7\u30a3\u305c\u30fc\u30b7\u30e7\u30f3\u4f4d\u76f8\u5dee\u9855\u5fae\u93e1\u3000<strong><em>\u5b9f\u9a13\u533b\u5b66<\/em><\/strong>\u3000Vol36, No.20 (\u5897\u520a) p80-81<\/li>\n<li>Kijima, S. Staiger, C., <u>Katoh, K.<\/u>, Nagasaki, A., Ito, K., and Uyeda, T. (2018)\u3000 Arabidopsis vegetative actin isoforms, AtACT2 and AtACT7, generate distinct filament arrays in living plant cells. <strong><em>Sci Rep., <\/em><\/strong>8:4381 | DOI:10.1038\/s41598-018-22707-w.<\/li>\n<li>Ito, N., <u>Katoh, K.<\/u>, Kushige, H., Saito, Y., Umemoto, T., Matsuzaki, Y., Kiyonari, H., Kobayashi, D., Soga, M., Era, T., Araki, N., Furuta, Y., Suda, T., Kida, Y., and Ohta K. (2018) Ribosome Incorporation into Somatic Cells Promotes Lineage Transdifferentiation towards Multipotency. <strong><em>Sci Rep. <\/em><\/strong>8, 1634 | DOI:10.1038\/s41598-018-20057-1<\/li>\n<li><u>\u52a0\u85e4\u85ab<\/u>\uff082018\uff09\u3000\u8d85\u89e3\u50cf\u5149\u5b66\u9855\u5fae\u93e1,\u3000<em><strong>\u5149\u6280\u8853\u52d5\u5411\u8abf\u67fb\u5831\u544a\u66f82017\u5e74\u5ea6<\/strong><\/em>\u3001p234-241<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7530\u6751\u5eb7<small>\uff08\u5c71\u5f62\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li><u>Tamura, Y.,<\/u> Kojima, R., Endo, T. (2019) Advanced In Vitro Assay System to Measure Phosphatidylserine and Phosphatidylethanolamine Transport at ER\/Mitochondria Interface. In: Drin G. (eds) Intracellular Lipid Transport. <strong><em>Methods Mol. Biol.<\/em><\/strong> vol 1949. Humana Press, New York, NY<\/li>\n<li>\n<p>Sakaue, H., Shiota, T., Ishizaka, N., Kawano, S., <u>Tamura, Y.<\/u>, Tan, KS., Imai, K., Motono, C., Hirokawa, T., Taki, K., Miyata, N., Kuge, O., Lithgow, T., and Endo, T. (2019) Porin Associates with Tom22 to Regulate the Mitochondrial Protein Gate Assembly <strong><em>Mol. Cell<\/em><\/strong>, 73, 1044\u20131055<\/p>\n<\/li>\n<li>\n<p>Sawasato, K., Sato, R., Nishikawa, H., Iimura, N., Kamemoto, Y., Fujikawa, K., Yamaguchi, T., Kuruma, Y., <u>Tamura, Y<strong>.<\/strong><\/u>, Endo, T., Ueda, T., Shimamoto, K. and Nishiyama, K. (2019) CdsA is involved in biosynthesis of glycolipozyme MPIase essential for membrane protein integration in vivo. <strong><em>Sci. Rep<\/em><\/strong>., 9, Article\u00a0number:\u00a01372<\/p>\n<\/li>\n<li>Ueda, E., <u>Tamura, Y<\/u>., Sakaue, H., Kawano, S., Kakuta, C., Matsumoto, S., and Endo, T. (2019) Myristoyl group-aided protein import into the mitochondrial intermembrane space. <strong><em>Sci. Rep<\/em><\/strong>., 9, Article number: 1185.<\/li>\n<li>Kojima, R., Kakimoto, Y., Furuta, S., Itoh, K., Sesaki, H., Endo, T., and <u>Tamura, Y.<\/u> (2019) Maintenance of Cardiolipin and Crista Structure Requires Cooperative Functions of Mitochondrial Dynamics and Phospholipid Transport. <strong><em>Cell Rep<\/em>.<\/strong>, 26, 518\u2013528.<\/li>\n<li>\n<p>Tashiro, S. Caaveiro, J. Nakakido, M. Tanabe, A. Nagatoishi, S. <u>Tamura, Y.<\/u> Matsuda, N. Liu, D. Hoang, Q. and Tsumoto, K. (2018).\u00a0Discovery and Optimization of Inhibitors of the Parkinson&#8217;s Disease Associated Protein DJ-1. <strong><em>ACS. Chem. Biol.<\/em><\/strong>, 13(9):2783-2793. doi: 10.1021\/acschembio.8b00701.<\/p>\n<\/li>\n<li><u>Tamura, Y.<\/u>, Kawano, S., and Endo T. (2019) Organelle contact zones as sites for lipid transfer. <strong><em>J Biochem.<\/em><\/strong> 165, 115\u2013123.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4eca\u6cc9\u548c\u5247<small>\uff08\u5e83\u5cf6\u5927\u5b66\u5927\u5b66\u9662\u533b\u6b6f\u85ac\u4fdd\u5065\u5b66\u7814\u7a76\u79d1\u3000\u5206\u5b50\u7d30\u80de\u60c5\u5831\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Saito, A. and <u>Imaizumi, K.<\/u> (2018) Unfolded Protein Response-Dependent Communication and Contact among Endoplasmic Reticulum, Mitochondria and Plasma Membrane.<strong><em>Int J Mol Sci<\/em><\/strong>, 19:3215.<\/li>\n<li>Osaki, Y., Saito, A., Kanemoto, S., Kaneko, M., Matsuhisa, K., Asada, R., Masaki, T., Orii, K., Fukao, T., Tomatsu, S., and <u>Imaizumi, K.<\/u> (2018) Shutdown of ER-associated degradation pathway rescues functions of mutant iduronate 2-sulfatase linked to mucopolysaccharidosis type II. <strong><em>Cell Death Dis<\/em><\/strong>, 9:808.<\/li>\n<li>Ohtake Y, Matsuhisa K, Kaneko M, Kanemoto S, Asada R, <u>Imaizumi K<\/u>, and Saito A. (2018) Axonal Activation of the Unfolded Protein Response Promotes Axonal Regeneration Following Peripheral Nerve Injury. <strong><em>Neuroscience<\/em><\/strong>, 375:34-48.<\/li>\n<li>Wu Y, Guo XP, Kanemoto S, Maeoka Y, Saito A, Asada R, Matsuhisa K, Ohtake Y, <u>Imaizumi K<\/u>, and Kaneko M. (2018) Sec16A, a key protein in COPII vesicle formation, regulates the stability and localization of the novel ubiquitin ligase RNF183. <strong><em>Plos One<\/em><\/strong>, 13: e0190407.<\/li>\n<li>Saito, A., Cai, L., Matsuhisa, K., Ohtake, Y., Kaneko, M., Kanemoto, S., Asada, R., and <u>Imaizumi, K.<\/u> (2018) Neuronal activity-dependent local activation of dendritic unfolded protein response promotes expression of brain-derived neurotrophic factor in cell soma.\u00a0<strong><em>J Neurochem<\/em><\/strong>, 144:35-49.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u77e2\u6728\u5b8f\u548c<small>\uff08\u540d\u53e4\u5c4b\u5e02\u7acb\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li><u>Yagi, H.<\/u>, Takakura, D., Roumenina, L.T., Fridman, W.H., Saut\u00e8s-Fridman, C., Kawasaki, N. and Kato, K. (2018) Site-specific N-glycosylation analysis of soluble Fc\u03b3 receptor IIIb in human serum. <strong><em>Sci. Rep.<\/em><\/strong>, 8, Article number: 2719<\/li>\n<li>\n<p class=\"p1\"><u>Yagi, H.<\/u>, Yan, G., Suzuki, T., Tsuge, S., Yamaguchi, T. and Kato, K. Lewis X-carrying neoglycolipids evoke selective apoptosis in neural stem cells (2018) <strong><em>Neurochem. Res.<\/em><\/strong>, 43, 212-218<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7530\u6751\u5eb7<small>\uff08\u5c71\u5f62\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Tashiro, S. Caaveiro, J. Nakakido, M. Tanabe, A. Nagatoishi, S. <u>Tamura, Y.<\/u> Matsuda, N. Liu, D. Hoang, Q. and Tsumoto, K. (2018).\u00a0Discovery and Optimization of Inhibitors of the Parkinson&#8217;s Disease Associated Protein DJ-1. <strong><em>ACS. Chem. Biol.<\/em><\/strong>, 13(9):2783-2793. doi: 10.1021\/acschembio.8b00701.<\/p>\n<\/li>\n<li>Kakimoto,Y., \u00a0Tashiro, S., Kojima, R., Morozumi, Y., Endo, T., and <u>Tamura, Y<\/u>. (2018) Visualizing multiple inter-organelle contact sites using the organelle-targeted split-GFP system. <b><i>Sci. Rep.<\/i><\/b>, 8, 6175. DOI:10.1038\/s41598-018-24466-0<\/li>\n<li>\n<p class=\"p1\">Endo, T., and\u00a0<u>Tamura, Y<\/u>. (2018) News and Views; \u00a0Shuttle mission in the mitochondrial intermembrane space. \u00a0<b><i>EMBO J.<\/i><\/b> e98993<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e2d\u91ce\u660e\u5f66<small>\uff08\u6771\u4eac\u5927\u5b66\u3001\u7406\u5316\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Muro, K., Matsuura-Tokita, K., Tsukamoto, R., Kanaoka, M. M., Ebine, K., Higashiyama, T.,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Ueda, T. (2018) ANTH domain-containing proteins are required for the pollen tube plasma membrane integrity via recycling ANXUR kinases.\u00a0<strong><em>Commun. Biol.<\/em><\/strong>\u00a01:152.<\/li>\n<li>\n<p>Ishikawa, K., Tamura, K., Ueda, H., Ito, Y.,\u00a0<span class=\"double\">Nakano, A.<\/span>, Hara-Nishimura, I., and Shimada, T. (2018) The synaptotagmin-associated ER-plasma membrane contact sites are distributed to immobile ER tubules.\u00a0<strong><em>Plant Physiol.<\/em><\/strong>\u00a0178:641-653.<\/p>\n<\/li>\n<li>\n<p>Haraguchi, T., Ito, K., Duan, Z., Sa, R., Takahashi, K., Shibuya, Y., Hagino, N., Miyatake, Y.,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Tominaga, M. (2018) Functional diversity of class XI myosins in\u00a0<em>Arabidopsis thaliana<\/em>.\u00a0<strong><em>Plant Cell Physiol.<\/em><\/strong>\u00a059:2268-2277.<\/p>\n<\/li>\n<li>\n<p>Ishii, M., Lupashin, V. V., and\u00a0<span class=\"double\">Nakano, A.<\/span>\u00a0(2018). Detailed analysis of the interaction of yeast COG complex.\u00a0<strong><em>Cell Struct. Funct. <\/em><\/strong>43:119-127.<\/p>\n<\/li>\n<li>\n<p>Ito, E., Ebine, K., Choi, S.-W., Ichinose, S., Uemura, T.,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Ueda, T. (2018). Integration of two RAB5 groups during endosomal transport in plants.\u00a0<strong><em>eLife<\/em><\/strong> 7:e34064.<\/p>\n<\/li>\n<li>\n<p>Minamino,\u00a0N., Kanazawa, T., Era, A., Ebine,\u00a0K.,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Ueda, T.\u00a0(2018) RAB\u00a0GTPases in the basal land\u00a0plant\u00a0<em>Marchantia\u00a0polymorpha<\/em>.\u00a0<strong><em>Plant Cell Physiol. <\/em><\/strong>59:845-856.<\/p>\n<\/li>\n<li>\n<p>Tanabashi, S., Shoda, K., Saito, C., Sakamoto, T., Kurata, T., Uemura, T., and <span class=\"double\">Nakano, A.<\/span> (2018)\u00a0A\u00a0missense mutation in the\u00a0<em>NSF\u00a0<\/em>gene causes abnormal Golgi morphology in\u00a0<em>Arabidopsis\u00a0thaliana<\/em>.\u00a0<strong><em>Cell Struct. Funct. <\/em><\/strong>43:41-51.<\/p>\n<\/li>\n<li>\n<p>Takemoto, K., Ebine, K., Askani, J. C., Goh, T., Schumacher,\u00a0K.,<span class=\"double\">Nakano, A.<\/span>, and Ueda, T. (2018) Distinct\u00a0sets of tethering complexes, SNARE complexes, and Rab GTPases\u00a0mediate membrane fusion at the vacuole in Arabidopsis.\u00a0<strong><em>Proc. Natl.\u00a0Acad. Sci. U. S. A. <\/em><\/strong>115:E2457-E2466.<\/p>\n<\/li>\n<li>\n<p>Suda, Y.,\u00a0<u>Kurokawa, K.<\/u>, and\u00a0<span class=\"double\">Nakano, A.<\/span> Regulation of ER-Golgi transport dynamics by GTPases in budding yeast.\u00a0<strong><em>Frontiers Cell Dev. Biol. <\/em><\/strong>5:122.<\/p>\n<\/li>\n<li>\n<p>Suda, Y., Tachikawa, H., Inoue, I., Kurita, T., Saito, C.,\u00a0<u>Kurokawa, K.<\/u>,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Irie, K. (2018) Activation of Rab GTPase Sec4 by its GEF Sec2 is required for prospore membrane formation during sporulation in yeast\u00a0<em>Saccharomyces cerevisiae.\u00a0<strong>FEMS Yeast Res. <\/strong><\/em>18:fox095.<\/p>\n<\/li>\n<li>\n<p>Sanchez-Rodriguez, C., Shi, Y., Kesten, C., Zhang, D., Sancho-Andr\u00e9s, G., Ivakov, A., Lampugnani, E. R., Sklodowski, K., Fujimoto, M.,\u00a0<span class=\"double\">Nakano, A.<\/span>, Bacic, A., Wallace, I. S., Ueda, T., van Damme, D., Zhou, Y., and Persson, S. (2018) The cellulose synthases are cargo of the TPLATE adaptor complex.\u00a0<strong><em>Mol. Plant\u00a0<\/em><\/strong>11:346-349.<\/p>\n<\/li>\n<li>\n<p>Ito, Y., Uemura, T., and\u00a0<span class=\"double\">Nakano, A.<\/span>\u00a0(2018) Golgi Entry Core Compartment functions as the COPII-independent scaffold for ER-Golgi transport in plant cells. \u00a0<strong><em>J.\u00a0Cell Sci.\u00a0<\/em><\/strong>131:jcs203893.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u897f\u982d\u82f1\u8d77<small>\uff08\u5bae\u5d0e\u5927\u5b66\u3000\u533b\u5b66\u90e8\uff09<\/small><\/h3>\n<ol>\n<li>Kadowaki, H., Satrimafitrah, P., Takami, Y. and <span style=\"text-decoration: underline;\">Nishitoh, H.<\/span> (2018) Molecular mechanism of ER stress-induced pre-emptive quality control involving association of the translocon, Derlin-1, and HRD1. <em><strong>Sci. Rep.<\/strong><\/em>, 8, 7317 | DOI:10.1038\/s41598-018-25724-x<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6e05\u6c34\u91cd\u81e3<small>\uff08\u6771\u4eac\u533b\u79d1\u6b6f\u79d1\u5927\u5b66\u3000\u96e3\u6cbb\u75be\u60a3\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li><u>Shimizu, S.<\/u>\u00a0(2018) Organelle zones in mitochondria.\u00a0<strong><em>J Biochem.<\/em><\/strong>\u00a0in press.<\/li>\n<li>Yamaguchi, T., Suzuki, T., Sato, T., Takahashi, A., Watanabe, H., Kadowaki, A., Natsui, M., Inagaki, H., Arakawa, S., Nakaoka, S., Koizumi, Y., Seki, S., Adachi, S., Fukao, A., Fujiwara, T., Natsume, T., Kimura, A., Komatsu, M., <span style=\"text-decoration: underline;\">Shimizu, S.<\/span>, Ito, H., Suzuki, Y., Penninger, J. M., Yamamoto, T., Ima Y. and Kuba, K. (2018) The CCR4-NOT deadenylase complex controls Atg7-dependent cell death and heart function. <strong><em>Scientific Signaling<\/em><\/strong>, 6, 11(516).<\/li>\n<li>Iwashita, H., Tajima Sakurai, H., Nagahora, N., Ishiyama, M., Shioji, K., Sasamoto, K., Okuma, K., <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> and Ueno, Y. (2018) Small Fluorescent molecules for monitoring autophagic flux. <strong><em>FEBS Lett.<\/em><\/strong> 592, 559-567.<\/li>\n<li>Nagata, M., Arakawa, S., Yamaguchi, H., Torii, S., Endo, H., Tsujioka, M., Honda, S., Nishida, Y., Konishi, A. and <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> (2018) Dram1 regulates DNA damage-induced alternative autophag <strong><em>Cell Stress<\/em><\/strong> 2, 55-65.<\/li>\n<li><span style=\"text-decoration: underline;\">Shimizu, S.<\/span> (2018) Biological Roles of Alternative Autophagy. <strong><em>Mol<\/em><\/strong><strong><em> Cells<\/em><\/strong>, 41, 50-54.<\/li>\n<li>Fujikake, N., Shin, M. and <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> (2018) Association between autophagy and neurodegenerative diseases. <strong><em>Frontiers in Neuroscience<\/em><\/strong>, in press<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u5f8c\u85e4\u8061<small>\uff08\u7acb\u6559\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Nuclear envelope localization of PIG-B is essential for GPI-anchor synthesis in <em>Drosophila<\/em>.<br \/>\nYamamoto-Hino.M., Katsumata, E., Suzuki, E., Maeda, Y., Kinoshita, T. and <span style=\"text-decoration: underline;\">Goto, S.<\/span><br \/>\n<strong><em>J. Cell Sci.<\/em><\/strong>, 131, jcs218024 (2018)<br \/>\nDOI: 10.1242\/jcs.218024<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6728\u4e0b\u30bf\u30ed\u30a6<small>\uff08\u5927\u962a\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Nuclear envelope localization of PIG-B is essential for GPI-anchor synthesis in <em>Drosophila<\/em>.<br \/>\nYamamoto-Hino.M., Katsumata, E., Suzuki, E., Maeda, Y., <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>. and Goto, S.<br \/>\n<strong><em>J. Cell Sci.<\/em><\/strong>, 131, jcs218024 (2018)<br \/>\nDOI: 10.1242\/jcs.218024<\/li>\n<li>\n<p><span style=\"text-decoration: underline;\">Kinoshita, T<\/span>. (2018) Congenital defects in the expression of the glycosylphosphatidylinositol-anchored complement regulatory proteins CD59 and decay-accelerating factor. <strong><em>Semin. Hematol.<\/em><\/strong>, 55:136-140.<\/p>\n<\/li>\n<li>\n<p>Mogami, Y., Suzuki, Y., Murakami, Y., Ikeda, T., Kimura, S., Yanagihara, K., Okamoto, N., and <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>. (2018) Early infancy-onset stimulation-induced myoclonic seizures in three siblings with inherited glycosylphosphatidylinositol (GPI) anchor deficiency. <strong><em>Epileptic Disord.<\/em><\/strong>, 20:42-50.<\/p>\n<\/li>\n<li>\n<p>Pagnamenta, A. T. *, Murakami, Y. *, Anzilotti, C., Titheradge, H., Oates, A. J., Morton, J., The DDD Study, <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>.+, Kini, U.+, and Taylor, J. C.+. (2018) A homozygous variant disrupting the <em>PIGH<\/em> start-codon is associated with developmental delay, epilepsy and microcephaly. <strong><em>Hum. Mutat.<\/em><\/strong>, 39:822-826. (* and +, equal contribution)<\/p>\n<\/li>\n<li>\n<p>Yoko-o, T., Umemura, M., Komatsuzaki, A., Ikeda, K., Ichikawa, D., Takase, K., Kanzawa, N., Saito, K., <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>., Taguchi, R., and Jigami, Y. (2018) Lipid moiety of glycosylphosphatidylinositol-anchored proteins contributes to the determination of their final destination in yeast. <strong><em>Genes Cells<\/em><\/strong>, 23:880-892.<\/p>\n<\/li>\n<li>\n<p>Kawamoto, M., Murakami, Y., <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>., and Kohara, N. (2018) Recurrent aseptic meningitis with <em>PIGT<\/em> mutations: a novel pathogenesis of recurrent meningitis successfully treated by eculizumab. <strong><em>BMJ Case Rep.<\/em><\/strong>, pii: bcr-2018-225910.<\/p>\n<\/li>\n<li>\n<p>Nguyen, T. T. M., Murakami, Y., Wigby, K. M., Baratang, N. V., St-Denis, A., Rosenfeld, J. A., Laniewski, S. C., Jones, J., Iglesias, A. D., Jones, M. C., Masser-Frye, D., Scheuerle, A. E., Taft, R. J., Le Deist, F., Thompson, M., <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>., and Campeau, P. M. (2018) Mutations in PIGS, encoding a GPI transamidase, cause a neurological syndrome ranging from fetal akinesia to epileptic encephalopathy. <strong><em>Am. J. Hum. Genet.<\/em><\/strong>, 103:602-611.<\/p>\n<\/li>\n<li>\n<p>Yamamoto-Hino, M., Katsumata, E., Suzuki, E., Maeda, Y., <span style=\"text-decoration: underline;\">Kinoshita, T<\/span>., and Goto, S. (2018) Nuclear envelope localization of PIG-B is essential for GPI anchor synthesis in <em>Drosophila<\/em>. <strong><em>J. Cell Sci.<\/em><\/strong>, 131: pii: jcs218024.<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u9f4b\u85e4\u4f38\u4e00\u90ce<small>\uff08\u6771\u4eac\u5927\u5b66\u533b\u79d1\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>\n<p><u>\u9f4b\u85e4\u4f38\u4e00\u90ce<\/u> (2018) Toll\u69d8\u53d7\u5bb9\u4f53(TLR)\uff17\u306e\u5fdc\u7b54\u3068\u7d30\u80de\u5185\u30ed\u30b8\u30b9\u30c6\u30a3\u30af\u30b9\u3001<em><strong>\u533b\u5b66\u306e\u3042\u3086\u307f<\/strong><\/em> 265(13): 1087-1093<\/p>\n<\/li>\n<li>\n<p>Sato, R., Kato, A., Chimura, T., <u>Saitoh,S<\/u>., Shibata, T., Murakami, Y., Fukui, R., Liu, K., Zhang, Y., Arii, J., Sun-Wada, GH., Wada, Y., Ikenoue, T., Barber, GN., Manabe, T., Kawaguchi, Y., Miyake, K. (2018) Combating herpesvirus encephalitis by potentiating a TLR3-mTORC2 axis. <em><strong>Nature Immunology<\/strong><\/em>. Sep 10, doi: 10.1038\/s41590-018-0203-2.\u00a0<\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u5c3e\u91ce\u96c5\u54c9<small>\uff08\u56fd\u7acb\u304c\u3093\u7814\u7a76\u30bb\u30f3\u30bf\u30fc\u7814\u7a76\u6240\u3000\u81e8\u5e8a\u30d7\u30ed\u30c6\u30aa\u30fc\u30e0\u89e3\u6790\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p><span style=\"text-decoration: underline;\">Ono, M<\/span>., Lai, K. K. Y., Wu, K., Nguyen, C., Lin, D. P., Murali, R., Kahn, M. (2018) Nuclear receptor\/Wnt beta-catenin interactions are regulated via differential CBP\/p300 coactivator usage. <em><strong>PLoS One.<\/strong><\/em>, e0200714.<br \/>\n<a href=\"http:\/\/journals.plos.org\/plosone\/article?id=10.1371\/journal.pone.0200714\" target=\"_blank\" rel=\"noopener\">http:\/\/journals.plos.org\/plosone\/article?id=10.1371\/journal.pone.0200714<\/a><\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6cc9\u6b63\u7bc4<small>\uff08\u6771\u5317\u5927\u5b66\u3000\u5b66\u969b\u79d1\u5b66\u30d5\u30ed\u30f3\u30c6\u30a3\u30a2\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Nakamura, S., Hidema, J., Ishida, H., Sakamoto, W., <u>Izumi, M.<\/u> (2018) Selective elimination of membrane-damaged chloroplasts via microautophagy, <strong><em>Plant Physiol.<\/em><\/strong> 177, 1007-1026.<\/p>\n<\/li>\n<li>Nakamura, S., and <u>Izumi, M.<\/u> (2018) Regulation of chlorophagy during photoinhibition and senescence: Lessons from mitophagy. <strong><em>Plant Cell Physiol.<\/em><\/strong> 59, 1135-1143<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">\u4e2d\u6751\u54b2\u8036<\/span><span class=\"s2\">, <\/span><span style=\"text-decoration: underline;\"><span class=\"s1\">\u6cc9\u6b63\u7bc4<\/span><\/span><span class=\"s2\">, (2018) <\/span><span class=\"s1\">\u58ca\u308c\u305f\u8449\u7dd1\u4f53\u306f\u30aa\u30fc\u30c8\u30d5\u30a1\u30b8\u30fc\u3067\u4e38\u3054\u3068\u9664\u53bb\u3055\u308c\u308b<\/span><span class=\"s2\">,<\/span><em><strong><span class=\"s1\">\u690d\u7269\u79d1\u5b66\u6700\u524d\u7dda<\/span><\/strong><\/em><span class=\"s2\"> 9, 36-45<\/span><\/p>\n<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u82b1\u7530\u8ce2\u592a\u90ce<small>\uff08\u56fd\u7acb\u611f\u67d3\u75c7\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Sakuma, C., Sekizuka, T., Kuroda, M., Kasai, F., Saito, K., Ikeda, M., Yamaji, T., Osada, N., and <u>Hanada, K.<\/u> (2018) Novel endogenous simian retroviral integrations in Vero cells: implications for quality control of a human vaccine cell substrate. <strong><em>Sci. Rep.<\/em><\/strong>, 8, 644. (CS and TS are co-first authors. NO and KH are co-correspondence)<\/li>\n<li>Otsuki, N., Sakata, M., Saito, K., Okamoto, K., Mori, Y., <u>Hanada, K.<\/u>, Takeda, M. (2018) Both sphingomyelin and cholesterol in the host cell membrane are essential for\u00a0<em>Rubella virus<\/em> entry. <strong><em>J. Virol.<\/em><\/strong><a name=\"_Hlk515357408\"><\/a>, 92, e01130-17. (K.H. and M.T. are co-correspondence. This article was selected as Spotlight of the issue)<\/li>\n<li>Shimasaki, K., Watanabe-Takahash, M., Umeda, M., Funamoto, S., Saito, Y., Noguchi, N., Kumagai, K., <u>Hanada, K.<\/u>, Tsukahara, F., Maru, Y., Shibata, N., Naito, M., and Nishikawa, K. (2018) Pleckstrin homology domain of p210 BCR-ABL interacts with cardiolipin to regulate its mitochondrial translocation and subsequent mitophagy.<strong><em> Genes Cells<\/em><\/strong>, 23, 22-34.<\/li>\n<li>Shimizu, Y., Shirasago, Y., Kondoh, M., Suzuki, T., Wakita, T., <u>Hanada, K.<\/u>, Yagi, K., and Fukasawa, M. (2018) \u00a0Monoclonal antibodies against occludin completely prevented hepatitis C virus infection in a mouse model. <strong><em>J. Virol., <\/em><\/strong>92, e02258-17.<\/li>\n<li>Sugiki, T., Egawa, D., Kumagai, K., Kojima, C., Fujiwara, T., Takeuchi, K., Shimada, I., <u>Hanada, K<\/u>., and Takahashi, H. (2018)\u3000Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif.<em><strong> J. Biol. Chem<\/strong><\/em>., 293(28), 11206-11217. (T.S. and D.E. are co-first authors. K.H. and H.T. are co-correspondence)<\/li>\n<li>Ikeda, M., Satomura, K., Sekizuka,T., <u>Hanada, K<\/u>., Endo, T., and Osada, N. (2018) Comprehensive phylogenomic analysis reveals a novel cluster of simian endogenous retroviral sequences in Colobinae monkeys. <em><strong>Am. J. Primatol<\/strong><\/em>., 80(7), e22882.<\/li>\n<li><u>Hanada, K<\/u>. (2018) Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites (Invited review). <em><strong>J. Lipid Res<\/strong><\/em>., 59(8), 1341-1366.<\/li>\n<li>Shirasago, Y., Fukazawa, H., Aizaki, H., Suzuki, T., Suzuki, T., Sugiyama, K., Wakita, T., <u>Hanada, K<\/u>., Abe, R., and Fukasawa, M. (2018) Thermostable hepatitis C virus JFH1-derived variant isolated by adaptation to Huh7.5.1 cells. <em><strong>J. Gen. Virol<\/strong><\/em>., 99(10), 1407-1417.<\/li>\n<li>Kumagai, K., Elwell, CA., Ando, S., Engel, JN. and <u>Hanada, K<\/u>. (2018) Both the N- and C- terminal regions of the Chlamydial inclusion protein D (IncD) are required for interaction with the pleckstrin homology domain of the ceramide transport protein CERT. <em><strong>Biochem Biophys Res Commun<\/strong><\/em>., 505(4), 1070-1076. (K.K. and K.H. are co-correspondence)<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u795e\u5409\u667a\u4e08<small>\uff08\u65b0\u6f5f\u5927\u5b66\u5927\u5b66\u9662\u3000\u533b\u6b6f\u5b66\u7dcf\u5408\u7814\u7a76\u79d1\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Furukawa, K., Fukuda, T., Yamashita, SI., Saigusa, T., Kurihara, Y., Yoshida, Y., Kirisako, H., Nakatogawa, H., Kanki, T. (2018) The PP2A-like Protein Phosphatase Ppg1 and the Far Complex Cooperatively Counteract CK2-Mediated Phosphorylation of Atg32 to Inhibit Mitophagy. <strong><em>Cell Rep.<\/em><\/strong>, 23(12):3579-3590.<\/p>\n<\/li>\n<\/ol>\n<div class=\"list_member\">\u00a0<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u540d\u9ed2\u529f<small>\uff08\u6771\u4eac\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Imamura, K., Yoshitane, H., Hattori, K., Yamaguchi, M., Yoshida, K., Okubo, T., <u>Naguro, I.<\/u>, Ichijo, H. and Fukada, Y. (2018)\u00a0ASK family kinases mediate cellular stress and redox signaling to circadian clock.\u00a0<strong><em> Natl. Acad. Sci. U.S.A.<\/em><\/strong>in press<\/li>\n<li>Watanabe, K., Umeda, T., Niwa, K., <u>Naguro, I.<\/u> and Ichijo, H.(2018)A PP6-ASK3 module coordinates the bidirectional cell volume regulation under osmotic stress.\u00a0<strong><em>Cell Rep.<\/em><\/strong>\u00a013, 2809-2817.\u00a0<\/li>\n<li>Kamiyama, M., <u>Naguro, I.<\/u> and Ichijo, H.\u00a0\u00a0(2018)\u00a0mASKing cancer cells in a tumor microenvironment.\u00a0<strong><em>Cell Cycle<\/em><\/strong>in press<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u7247\u6850\u8c4a\u96c5<small>\uff08\u5fb3\u5cf6\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Daizumoto, K.,\u00a0Yoshimaru, T.,\u00a0Matsushita, Y.,\u00a0Fukawa, T., Uehara, H., <u>Ono, M.<\/u>,\u00a0Komatsu, M., Kanayama, H., and <u>Katagiri, T<\/u>. (2018) A DDX31\/mutant-p53\/EGFR axis promotes multistep progression of muscle\u00a0invasive bladder cancer.\u00a0<strong><em>Cancer Res<\/em><\/strong>. in press.<\/li>\n<li>Miyagawa, Y.,\u00a0Matsushita, Y., Suzuki,\u3000,\u00a0Komatsu, M.,\u00a0Yoshimaru, T.,\u00a0Kimura, R., Yanai, A., Honda, J., Tangoku, A., Sasa, M., Miyoshi, Y., and <u>Katagiri, T<\/u>. (2018) Frequent downregulation of\u00a0<em>LRRC26<\/em>by epigenetic\u00a0alterations is involved in the malignant progression of triple-negative breast cancers.\u00a0<strong><em>Int J Oncol.<\/em><\/strong> in press.<\/li>\n<\/ol>\n<\/div>\n<h2 id=\"2017\">2017\u5e747\u6708\u4ee5\u964d<\/h2>\n<div class=\"list_member\">\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u4eca\u6cc9\u548c\u5247<small>\uff08\u5e83\u5cf6\u5927\u5b66\u5927\u5b66\u9662\u533b\u6b6f\u85ac\u4fdd\u5065\u5b66\u7814\u7a76\u79d1\u3000\u5206\u5b50\u7d30\u80de\u60c5\u5831\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Saito, A. and <u>Imaizumi, K.<\/u> (2017) The Broad Spectrum of Signaling Pathways Regulated by Unfolded Protein Response in Neuronal Homeostasis.\u00a0<strong><em>Neurochem Int<\/em><\/strong>, 119:26-34.<\/li>\n<li><u>Imaizumi, K.<\/u> (2017) 60th Anniversary of the Japanese Society for Neurochemistry.\u00a0<strong><em>J Neurochem<\/em><\/strong>, 141:788-789.<\/li>\n<li>Kaneko, M., <u>Imaizumi, K.<\/u>, Saito, A., Kanemoto, S., Asada, R., Matsuhisa, K., and Ohtake, Y. (2017) ER Stress and Disease: Toward Prevention and Treatment.\u00a0<strong><em>Biol Pharm Bull<\/em><\/strong>, 40:1337-1343.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e0b\u5d8b\u7f8e\u6075<small>\uff08\u6771\u4eac\u5de5\u696d\u5927\u5b66\u3000\u751f\u547d\u7406\u5de5\u5b66\u9662\uff09<\/small><\/h3>\n<ol>\n<li>Yoshitake Y, Sato R, Madoka Y, Ikeda K, Murakawa M, Suruga K, Sugiura D, Noguchi K, Ohta H,\u00a0<u>Shimojima M<\/u>. (2017) Arabidopsis phosphatidic acid phosphohydrolases are essential for growth under nitrogen-depleted conditions.\u00a0<b><i>Front Plant Sci.<\/i><\/b>\u00a08, 1847<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u4e2d\u91ce\u660e\u5f66<small>\uff08\u6771\u4eac\u5927\u5b66\u3001\u7406\u5316\u5b66\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Yamagami, A., Saito, C., Sakuta, M., Shinozaki, M., Osada, H.,\u00a0<span class=\"double\">Nakano, A.<\/span>, Asami, T., and Nakano, T. (2017) Brassinosteroids regulate vacuolar morphology in root meristem cells of\u00a0<i>Arabidopsisthaliana<\/i>.\u00a0<b><i>Plant Signal. Behav.<\/i><\/b>\u00a013: e1417722<\/li>\n<li>Kobayashi, K., Suemasa, F., Sagara, H., Nakamura, S., Ino, Y., Kobayashi, K., Hiramatsu, H., Haraguchi, T.,\u00a0<u>Kurokawa, K.<\/u>, Todo, T.,\u00a0<span class=\"double\">Nakano, A.<\/span>, and Iba, H. (2017) MiR-199a inhibits secondary envelopment of herpes simplex virus-1 through the downregulation of Cdc42-specific GTPase activating protein localized in Golgi apparatus.\u00a0<strong><em>Sci.<\/em><em>\u00a0Rep.<\/em><\/strong>\u00a07, 6650<br \/>\nhttps:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28751779<\/li>\n<li>Yamagami, A., Saito, C., Nakazawa, M., Fujioka, S., Uemura, T., Matsui, M., Sakuta, M., Shinozaki, K., Osada, H.,\u00a0<span class=\"double\">Nakano, A.<\/span>, Asami, T., and Nakano, T. (2017) Evolutionarily conserved BIL4 suppresses the degradation of brassinosteroid receptor BRI1 and regulates cell elongation.\u00a0<em class=\"\"><strong>Sci. Rep.<\/strong>\u00a0<\/em>7, 5739 <br \/>\nhttps:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28720789<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u82b1\u7530\u8ce2\u592a\u90ce<small>\uff08\u56fd\u7acb\u611f\u67d3\u75c7\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>T\u00f3th, E. A., Oszvald, \u00c1., P\u00e9ter, M., Balogh, G., Osteikoetxea-Moln\u00e1r, A., Boz\u00f3, T., Szab\u00f3-Meleg, E., Nyitrai, M., Der\u00e9nyi, I., Yamaji, T., Hanada, K., V\u00edgh, L., Matk\u00f3, J. (2017) Nanotubes connecting B lymphocytes: High impact of differentiation-dependent lipid composition on their growth and mechanics. Biochim. Biophys. Acta, 1862, 991-1000.<\/li>\n<li><u>Hanada, K.<\/u>\u00a0(2017) Ceramide transport from the endoplasmic reticulum to the\u00a0<em>trans<\/em>\u00a0Golgi region at organelle membrane contact sites<strong>.\u00a0\u00a0<\/strong>In: Tagaya, M., Simmen, T. (eds) Organelle Contact Sites.\u00a0<strong><em>Adv. Exp. Med. Biol.<\/em><\/strong>, 997, 69-81, Springer, Singapore<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u6e05\u6c34\u91cd\u81e3<small>\uff08\u6771\u4eac\u533b\u79d1\u6b6f\u79d1\u5927\u5b66\u3000\u96e3\u6cbb\u75be\u60a3\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Arakawa, S., Tsujioka, M., Yoshida, T., Tajima-Sakurai, H., Nishida, Y., Matsuoka, Y., Yoshino, I., Tsujimoto, Y. and <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> (2017) Role of Atg5-dependent cell death in the embryonic development of <em>Bax\/Bak<\/em> double-knockout mice.<strong> <em>Cell Death Differ.<\/em>, <\/strong>24,1598-1608.<\/li>\n<li>Asano, J., Sato, T., Ichinose, S., Kajita, M., Onai, N., <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> and Ohteki, T., (2017) Intrinsic autophagy is required for the maintenance of intestinal stem cells and for irradiation-induced intestinal regeneration. <strong><em>Cell Rep.<\/em><\/strong><strong>,<\/strong> 20, 1050\u20131060.<\/li>\n<li>Hidefumi, I., Satoru, T., Noriyoshi, N., Munetaka, I., Kosei, S., Kazumi, S., <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> and Kentaro. O., (2017) Live Cell Imaging of Mitochondrial Autophagy with a Novel Fluorescent Small Molecule. <strong><em>ACS Chemical Biology<\/em>,<\/strong> 12, 2546-2551.<\/li>\n<li>Kanemoto, K. Sugimura, Y. <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> Yoshida, S. and Hosoya, T. (2017) Rhodium-catalyzed odorless synthesis of diaryl sulfides from borylarenes and S-aryl thiosulfonates. <strong><em> Commun.<\/em><\/strong>, 53, 10640\u201310643.<\/li>\n<li>Yotsumoto, S., Muroi, Y., Chiba, T., Ohmura, R., Yoneyama, M., Magarisawa, M., Dodo, K., Terayama, N., Sodeoka, M., Aoyagi, R., Arita, M., Arakawa, S., <span style=\"text-decoration: underline;\">Shimizu, S.<\/span> and Tanaka, M. (2017) Hyperoxidation of ether-linked phospholipids accelerates neutrophil extracellular trap formation. <strong><em> Rep.<\/em><\/strong>, 7, 16026<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u7530\u6751\u5eb7<small>\uff08\u5c71\u5f62\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p class=\"p1\">Kawano, S.,\u00a0<u>Tamura, Y<\/u>., Kojima, R., Bala, S., Asai, E, \u00a0Michel, AH., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., Okamoto, Y., and Endo T. (2017). Structure\u2013function insights into direct lipid transfer between membranes by Mmm1\u2013Mdm12 of ERMES. \u00a0<b><i>J. Cell. Biol.<\/i><\/b>\u00a0217, 959\u2013974. DOI: 10.1083\/jcb.201704119.<\/p>\n<\/li>\n<li>\n<p class=\"p1\"><u class=\"\">Tamura, Y<\/u>. and Endo, T. (2017) Role of Intra- and Inter-mitochondrial Membrane Contact Sites in Yeast Phospholipid Biogenesis. In: Tagaya, M., Simmen, T. (eds) Organelle Contact Sites.\u00a0<strong><i class=\"\">Adv. Exp. Med. Biol.<\/i><\/strong>, 997, 121-133, Springer, Singapore<\/p>\n<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u540d\u9ed2\u529f<small>\uff08\u6771\u4eac\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Hirata, Y., Katagiri, K., Nagaoka, K., Morishita, T., Kudoh, Y., Hatta, T., <u>Naguro, I.<\/u>, Kano, K., Udagawa, T., Natsume, T., Aoki, J., Inada, T., Noguchi, T., Ichijo, H. and Matsuzawa, A. (2017)\u00a0TRIM48 promotes ASK1 activation and cell death through ubiquitination-dependent degradation of the ASK1-negative regulator PRMT1.\u00a0<strong><em>Cell Rep.<\/em><\/strong>21, 2447-2457.\u00a0<\/li>\n<li>Hattori, K., Ishikawa, H., Sakauchi, C., Takayanagi, S.,<u> Naguro, I.<\/u> and Ichijo, H. (2017)\u00a0Cold stress-induced ferroptosis involves the ASK1-p38 pathway.\u00a0<strong><em>EMBO Rep.<\/em><\/strong>18, 2067-2078.<\/li>\n<li>Kamiyama, M., Shirai, T., Tamura, S., Suzuki-Inoue, K., Ehata, S., Takahashi, K., Miyazono, K., Hayakawa, Y., Sato, T., Takeda, K., <u>Naguro, I.<\/u> and Ichijo, H. (2017)\u00a0ASK1 facilitates tumor metastasis through phosphorylation of an ADP receptor P2Y12 in platelets.\u00a0<strong><em>Cell Death Differ.<\/em><\/strong>24, 2066-2076.<\/li>\n<\/ol>\n<h3 class=\"achievementtitle\">\u52a0\u85e4\u85ab<small>\uff08\u7523\u696d\u6280\u8853\u7dcf\u5408\u7814\u7a76\u6240\u3000\u30d0\u30a4\u30aa\u30e1\u30c7\u30a3\u30ab\u30eb\u7814\u7a76\u90e8\u9580\uff09<\/small><\/h3>\n<ol>\n<li>\n<p class=\"p1\">Ohzono, T., <u>Katoh, K.<\/u>, Wang, C., Fukazawa, A., Yamaguchi, S., and Fukuda, J. (2017) Uncovering different states of topological defects in schlieren textures of a nematic liquid crystal. <strong><em>Sci. Rep.<\/em><\/strong> 7, 16814 | DOI:10.1038\/s41598-017-16967-1<\/p>\n<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u6728\u4e0b\u30bf\u30ed\u30a6<small>\uff08\u5927\u962a\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>\n<p>Nguyen, Thi Tuyet Mai*, Y. Murakami*, E. Sheridan*, S. Ehresmann, J. Rousseau, A. St-Denis, G. Chai, N. F. Ajeawung, L. Fairbrother, T. Reimschisel, A. Bateman, E. Berry-Kravis, F. Xia, J. Tardif, D. A. Parry, C. V. Logan, C. Diggle, C. P. Bennett, L. Hattingh, J. A. Rosenfeld, M. S. Perry, M. J. Parker, F. Le Deist, M. S. Zaki, E. Ignatius, P. Isohanni, T. Loennqvist, C. J. Carroll, C. A. Johnson, J. G. Gleeson, <u>T. Kinoshita<\/u> and P. M. Campeau. (2017) Mutations in GPAA1, encoding a GPI transamidase complex protein, cause developmental delay, epilepsy, cerebellar atrophy, and osteopenia.<strong><em> Am. J. Hum. Genet.<\/em><\/strong>, 101:856-865.<\/p>\n<\/li>\n<li>\n<p>Liu, Y.-S., X.-Y. Guo, T. Hirata, Y. Rong, D. Motooka, T. Kitajima, Y. Murakami, X.-D. Gao, S. Nakamura, <u>T. Kinoshita<\/u> and M. Fujita. (2017) N-Glycan dependent protein folding and endoplasmic reticulum retention regulate GPI-anchor processing. <strong><em>J. Cell Biol.<\/em><\/strong>, 217: 585-599.<\/p>\n<\/li>\n<li>\n<p>Hirata, T., S. K. Mishra, S. Nakamura, K. Saito, D. Motooka, Y. Takada, N. Kanzawa, Y. Murakami, Y. Maeda, M. Fujita, Y. Yamaguchi and <u>T. Kinoshita<\/u>. (2017) Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain.<em><strong> Nat. Commun.<\/strong><\/em>, 9:405.<\/p>\n<\/li>\n<li>\n<p><u>\u6728\u4e0b\u30bf\u30ed\u30a6<\/u>\uff082017\uff09\u5f8c\u5929\u6027\u7a81\u7136\u5909\u7570\u3067\u751f\u3058\u308bGPI\u30a2\u30f3\u30ab\u30fc\u6b20\u640d\u8d64\u8840\u7403\u3068\u767a\u4f5c\u6027\u591c\u9593\u30d8\u30e2\u30b0\u30ed\u30d3\u30f3\u5c3f\u75c7\u3001<em><strong>\u751f\u5316\u5b66<\/strong><\/em>\u300189(3):351-358.<\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Colley, K. J., Varki, A. and\u00a0<\/span><span class=\"s2\">Kinoshita, T.<\/span><span class=\"s1\">\u00a0\u00a0(2017) Cellular Organization of Glycosylation. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p41-49. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876808\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876808<br \/>\n<\/a><\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Schnaar, R. L. and\u00a0<\/span><span class=\"s2\">Kinoshita, T.<\/span><span class=\"s1\">\u00a0\u00a0(2017) Glycosphingolipids. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p125-135. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876845\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876845<\/a><\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Ferguson, M. A. J., Hart, G. W. and\u00a0<\/span><span class=\"s2\">Kinoshita, T<\/span><span class=\"s1\">. \u00a0(2017) Glycosylphosphatidylinositol anchors. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p137-150. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876821\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876821<\/a><\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Freeze, H. H.,\u00a0<\/span><span class=\"s2\">Kinoshita, T.\u00a0<\/span><span class=\"s1\">\u00a0and Schnaar, R. L. \u00a0(2017) Genetic disorders of glycan degradation. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p553-568. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876818\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876818<\/a><\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Freeze, H. H., H. Schachter and\u00a0<\/span><span class=\"s2\">Kinoshita, T<\/span><span class=\"s1\">. \u00a0(2017) Genetic disorders of glycosylation. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p569-582. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876812\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876812<\/a><\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Freeze, H. H.,\u00a0<\/span><span class=\"s2\">Kinoshita, T.\u00a0<\/span><span class=\"s1\">\u00a0and Varki, A. (2017) Glycans in acquired human diseases. In\u00a0<em><strong>Essentials of Glycobiology 3rd ed.<\/strong><\/em> Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Darvill, A., Kinoshita, T., Packer, N.J., Prestegard, J., Schnaar, R., Seeberger, P. (eds.), p583-595. Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY.<br \/>\n<\/span><span class=\"s2\"><a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876835\">https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28876835<\/a><\/span><\/p>\n<\/li>\n<li>Kohashi, K., A. Ishiyama, S. Yuasa, T. Tanaka, K. Miya, Y. Adachi, N. Sato, H. Saitsu, C. Ohba, N. Matsumoto, Y. Murakami,\u00a0<u>T. Kinoshita<\/u>, K. Sugai and M. Sasaki. 2017. Epileptic apnea in a patient with inherited glycosylphosphatidylinositol anchor deficiency and\u00a0<em>PIGT<\/em>\u00a0mutations.\u00a0<em><strong>Brain Dev<\/strong>.<\/em>, 2017 Jul 17. pii: S0387-7604(17)30174-2. PMID: 28728837<\/li>\n<\/ol>\n<\/div>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u9f4a\u85e4\u9054\u54c9<small>\uff08\u5fb3\u5cf6\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Takahama M, Akira S, and\u00a0<span style=\"text-decoration: underline;\"><span class=\"s1\">Saitoh, T<\/span>.<\/span>\u00a0(2017)\u00a0Autophagy limits activation of the inflammasomes.\u00a0<strong><em>Immunol Rev.<\/em><\/strong> \u00a0doi:10.1111\/imr.12613, in press<\/li>\n<li>\n<p class=\"p1\"><span class=\"s1\">Takahama, M., Fukuda, M., Ohbayashi, N., Kozaki, T., Misawa, T., Okamoto, T., Matsuura, Y., Akira, S., and <\/span><span style=\"text-decoration: underline;\"><span class=\"s2\">Saitoh, T.<\/span><\/span><span class=\"s3\"> (2017) The RAB2B-GARIL5 complex promotes cytosolic DNA-induced innate immune responses. <\/span><strong><em><span class=\"s1\">Cell Rep.<\/span><\/em><\/strong><span class=\"s3\"> 20,<\/span><span class=\"s1\"> 2944-2954.<\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s4\">\u9ad9\u6ff5\u5145\u5bdb\uff0c<\/span><span style=\"text-decoration: underline;\"><span class=\"s2\">\u9f4a\u85e4\u9054\u54c9<\/span><\/span><span class=\"s4\"> (2017) <\/span><span class=\"s1\">\u30a4\u30f3\u30d5\u30e9\u30de\u30bd\u30fc\u30e0. <em><strong>\u708e\u75c7\u3068\u514d\u75ab<\/strong><\/em><\/span><span class=\"s4\"> 25,<\/span><span class=\"s1\"> 94-96.<\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s4\">\u9ad9\u6ff5\u5145\u5bdb\uff0c<\/span><span style=\"text-decoration: underline;\"><span class=\"s2\">\u9f4a\u85e4\u9054\u54c9<\/span><\/span><span class=\"s4\"> (2017) \u30aa\u30fc\u30c8\u30d5\u30a1\u30b8\u30fc.<\/span><span class=\"s1\">\u00a0<em><strong>\u5468\u7523\u671f\u533b\u5b66<\/strong><\/em><\/span><span class=\"s4\"> 47,<\/span><span class=\"s1\"> 1513-1520.<\/span><\/p>\n<\/li>\n<li>\n<p class=\"p1\"><span class=\"s4\">\u6e0b\u8c37\u5468\u4f5c<\/span><span class=\"s1\">, <\/span><span style=\"text-decoration: underline;\"><span class=\"s2\">\u9f4a\u85e4\u9054\u54c9<\/span><\/span><span class=\"s1\">, \u5409\u68ee\u4fdd<\/span><span class=\"s4\"> (2017) <\/span><span class=\"s1\">\u30aa\u30fc\u30c8\u30d5\u30a1\u30b8\u30fc\u3068\u751f\u4f53\u9632\u5fa1\u5fdc\u7b54. <em><strong>\u5b9f\u9a13\u533b\u5b66\u5897\u520a The \u30aa\u30fc\u30c8\u30d5\u30a1\u30b8\u30fc \u7814\u7a76\u8005\u305f\u3061\u306e\u96c6\u5927\u6210\u304c\u898b\u3048\u308b\u6700\u65b0\u30d3\u30b8\u30e5\u30a2\u30eb\u30c6\u30ad\u30b9\u30c8 <\/strong><\/em><\/span><span class=\"s4\">35,<\/span><span class=\"s1\"> 144-150.<\/span><\/p>\n<\/li>\n<li>Misawa, T., Takahama, M., and\u00a0<u>Saitoh, T<\/u>. (2017) Mitochondria\u2013Endoplasmic Reticulum Contact Sites Mediate Innate Immune Responses. In: Tagaya, M., Simmen, T. (eds) Organelle Contact Sites.\u00a0<strong><em>Adv. Exp. Med. Biol.<\/em><\/strong>, 997,\u00a0187-197, Springer, Singapore<\/li>\n<li><u>\u9f4a\u85e4\u9054\u54c9<\/u>. (2017) \u5c3f\u9178\u5869\u7d50\u6676\u306b\u3088\u308b\u30a4\u30f3\u30d5\u30e9\u30de\u30bd\u30fc\u30e0\u6d3b\u6027\u5316\u3068\u75db\u98a8\u6027\u95a2\u7bc0\u708e.\u00a0<strong><em>\u5c3f\u9178\u3068\u8840\u7cd6<\/em>\u00a0<\/strong>3,\u00a06-9<\/li>\n<li><u>\u9f4a\u85e4\u9054\u54c9<\/u>. (2017) \u75db\u98a8\u95a2\u7bc0\u708e\u306e\u767a\u75c7\u6a5f\u5e8f.\u00a0<strong><em>\u30ab\u30ec\u30f3\u30c8\u30c6\u30e9\u30d4\u30fc<\/em>\u00a0<\/strong>35,\u00a061-65<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u77e2\u6728\u5b8f\u548c<small>\uff08\u540d\u53e4\u5c4b\u5e02\u7acb\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li><u class=\"\"><span class=\"\" lang=\"EN-US\">Yagi, H.<\/span><\/u><span class=\"\" lang=\"EN-US\">, Yan, G., Suzuki, T., Tsuge, S., Yamaguchi, T., and Kato, K. (2017) Lewis X-carrying neoglycolipids evoke selective apoptosis in neural stem cells. <strong><em>Neurochem Res<\/em><\/strong> in press<\/span><\/li>\n<li>\n<div class=\"\"><span style=\"font-family: \u30e1\u30a4\u30ea\u30aa;\"><span class=\"\" lang=\"EN-US\">Yanaka, S., Yamazaki, T., Yogo, R., Noda, M., Uchiyama, S., <u class=\"\">Yagi, H.<\/u>, and Kato, K. (2017) NMR Detection of Semi-Specific Antibody Interactions in Serum Environments. <em><strong>Molecules<\/strong><\/em> 22, E1619<\/span><\/span><\/div>\n<\/li>\n<li>\n<div class=\"\">\u00a0<span style=\"font-family: \u30e1\u30a4\u30ea\u30aa;\"><span class=\"\" lang=\"EN-US\">Yogo, R., Yanaka, S., <u class=\"\">Yagi, H.<\/u>, Martel, A., Porcar, L., Ueki, Y., Inoue, R., Sato, N., Sugiyama, M., and Kato, K. (2007) Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fc\u03b3 receptor by deuteration-assisted small-angle neutron scattering.<\/span><span class=\"\">\u3000<em><strong><span class=\"\" lang=\"EN-US\">Biochem Biophys Rep<\/span><\/strong><\/em><span class=\"\" lang=\"EN-US\"> 16, 1-4<\/span><\/span><\/span><\/div>\n<\/li>\n<li><u>Yagi, H.<\/u>, Tateno, H., Hayashi, K., Hayashi, T., Takahashi, K., Hirabayashi, J., Kato, K., and Tsuboi, M. (2017) Lectin microarray analysis of isolated polysaccharides from Sasa veitchii.\u00a0<strong><em>Biosci Biotechnol Biochem<\/em><\/strong>\u00a081, 1687-1689<\/li>\n<li><u>\u77e2\u6728\u5b8f\u548c<\/u>\u3001\u52a0\u85e4\u6643\u4e00 (2017) NMR\u3092\u5229\u7528\u3057\u3066\u7cd6\u30bf\u30f3\u30d1\u30af\u8cea\u7cd6\u9396\u306e\u69cb\u9020\u52d5\u614b\u3068\u76f8\u4e92\u4f5c\u7528\u3092\u89b3\u308b.\u00a0<em><strong>\u533b\u5b66\u306e\u3042\u3086\u307f<\/strong><\/em>\u3000262, 467-473<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u68ee\u548c\u4fca<small>\uff08\u4eac\u90fd\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li><span class=\"s1\">Ishikawa, T.,\u00a0Kashima,\u00a0M.,\u00a0Nagano, A. J.,\u00a0Ishikawa-Fujiwara, T., Kamei,\u00a0Y., Todo, T. and\u00a0<\/span><span style=\"text-decoration: underline;\"><span class=\"s2\">Mori, K.<\/span><\/span><span class=\"s1\">\u00a0(2017) Unfolded Protein Response Transducer\u00a0IRE1-mediated Signaling Independent of XBP1 mRNA Splicing Is Not Required for Growth and Development of Medaka Fish.\u00a0<em><strong>eLife<\/strong><\/em>, 6, e26845.<\/span><\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u7d30\u8c37\u5b5d\u5145<small>\uff08\u6771\u4eac\u533b\u79d1\u6b6f\u79d1\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Nishiyama, Y., Hazama, Y., Yoshida, S., and\u00a0<u>Hosoya, T.<\/u>\u00a0(2017) Synthesis of Unsymmetrical Tertiary Phosphine Oxides via Sequential Substitution Reaction of Phosphonic Acid Dithioesters with Grignard Reagents.\u00a0<em><strong>Org. Lett<\/strong>.<\/em>\u00a019, 3899-3902\u00a0<\/li>\n<\/ol>\n<\/div>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u5c3e\u91ce\u96c5\u54c9<small>\uff08\u56fd\u7acb\u304c\u3093\u7814\u7a76\u30bb\u30f3\u30bf\u30fc\u7814\u7a76\u6240\uff09<\/small><\/h3>\n<ol>\n<li>Kagami, Y.,\u00a0<u>Ono, M<\/u>., and Yoshida, K. (2017) Plk1 phosphorylation of CAP-H2 triggers chromosome condensation by condensin II at the early phase of mitosis.\u00a0<strong><em>Sci Rep<\/em>\u00a0<\/strong>7, 5583<\/li>\n<li><u>\u5c3e\u91ce\u96c5\u54c9<\/u>\u00a0(2017) \u30d1\u30e9\u30d5\u30a3\u30f3\u5305\u57cb\u6a19\u672c\u3092\u7528\u3044\u305f\u30d7\u30ed\u30c6\u30aa\u30fc\u30e0\u89e3\u6790.\u00a0<strong><em>\u75c5\u7406\u3068\u81e8\u5e8a<\/em>. <\/strong>35(7), 622-627<\/li>\n<\/ol>\n<div class=\"list_member\">\n<h3 class=\"achievementtitle\">\u91d1\u5ddd\u57fa<small>\uff08\u795e\u6238\u5927\u5b66\uff09<\/small><\/h3>\n<ol>\n<li>Kamizaki,\u00a0K., Doi, R., Hayashi,\u00a0M., Saji,\u00a0T.,\u00a0<u>Kanagawa, M.<\/u>, Toda,\u00a0T., Fukada,\u00a0SI., Ho,\u00a0HH., Greenberg, ME., Endo,\u00a0M., Minami, Y. (2017) The Ror1 receptor tyrosine kinase plays a critical role in regulating satellite cell proliferation during regeneration of injured muscle.\u00a0<strong><em>J.\u00a0<\/em><\/strong><em><strong>Biol. Chem<\/strong>.<\/em>in press (jbc.M117.785709.\u00a0doi:10.1074\/jbc.M117.785709)<\/li>\n<\/ol>\n<\/div>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>\u25bc 2021\u5e74 \u25bc 2020\u5e74 \u25bc 2019\u5e74 \u25bc 2018\u5e74 \u25bc 2017\u5e74 2021\u5e74 \u4e2d\u5c71\u548c\u4e45\uff08\u4eac\u90fd\u5927\u5b66\u5927\u5b66\u9662\u3000\u85ac\u5b66\u7814\u7a76\u79d1\uff09 Noguchi, T., Nakamura, K., Satoda, Y., Katoh [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_links_to":"","_links_to_target":""},"acf":[],"_links":{"self":[{"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/pages\/19"}],"collection":[{"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/comments?post=19"}],"version-history":[{"count":66,"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/pages\/19\/revisions"}],"predecessor-version":[{"id":3640,"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/pages\/19\/revisions\/3640"}],"wp:attachment":[{"href":"http:\/\/organellezone.org\/wp-json\/wp\/v2\/media?parent=19"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}