研究成果

2018年

中野明彦(東京大学、理化学研究所)

  1. Haraguchi, T., Ito, K., Duan, Z., Sa, R., Takahashi, K., Shibuya, Y., Hagino, N., Miyatake, Y., Nakano, A., and Tominaga, M. Functional diversity of class XI myosins in Arabidopsis thaliana. Plant Cell Physiol. in press.

  2. Ishii, M., Lupashin, V. V., and Nakano, A. (2018). Detailed analysis of the interaction of yeast COG complex. Cell Struct. Funct. 43:119-127.

  3. Ito, E., Ebine, K., Choi, S.-W., Ichinose, S., Uemura, T., Nakano, A., and Ueda, T. (2018). Integration of two RAB5 groups during endosomal transport in plants. eLife 7:e34064.

  4. Minamino, N., Kanazawa, T., Era, A., Ebine, K., Nakano, A., and Ueda, T. (2018) RAB GTPases in the basal land plant Marchantia polymorphaPlant Cell Physiol. in press.59:845-856
  5. Tanabashi, S., Shoda, K., Saito, C., Sakamoto, T., Kurata, T., Uemura, T., and Nakano, A. (2018) A missense mutation in the NSF gene causes abnormal Golgi morphology in Arabidopsis thalianaCell Struct. Funct. in press.43:41-51
  6. Takemoto, K., Ebine, K., Askani, J. C., Goh, T., Schumacher, K., Nakano, A., and Ueda, T. (2018) Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases mediate membrane fusion at the vacuole in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 115:E2457-E2466
  7. Suda, Y., Kurokawa, K., and Nakano, A. Regulation of ER-Golgi transport dynamics by GTPases in budding yeast. Frontiers Cell Dev. Biol. in press.
  8. Suda, Y., Tachikawa, H., Inoue, I., Kurita, T., Saito, C., Kurokawa, K., Nakano, A., and Irie, K. (2018) Activation of Rab GTPase Sec4 by its GEF Sec2 is required for prospore membrane formation during sporulation in yeast Saccharomyces cerevisiae. FEMS Yeast Res. in press.18:fox095
  9. Yamagami, A., Saito, C., Sakuta, M., Shinozaki, M., Osada, H., Nakano, A., Asami, T., and Nakano, T. Brassinosteroids regulate vacuolar morphology in root meristem cells of Arabidopsis thaliana. Plant Signal. Behav. in press.
  10. Sanchez-Rodriguez, C., Shi, Y., Kesten, C., Zhang, D., Sancho-Andrés, G., Ivakov, A., Lampugnani, E. R., Sklodowski, K., Fujimoto, M., Nakano, A., 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. Mol. Plant 11:346-349
  11. Ito, Y., Uemura, T., and Nakano, A. (2018) Golgi Entry Core Compartment functions as the COPII-independent scaffold for ER-Golgi transport in plant cells.  J. Cell Sci. 131:jcs203893.

尾野雅哉(国立がん研究センター研究所 臨床プロテオーム解析部門)

  1. Ono, M., 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. PLoS One., e0200714.
    http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0200714

泉正範(東北大学 学際科学フロンティア研究所)

  1. Nakamura, S., Hidema, J., Ishida, H., Sakamoto, W., Izumi, M. (2018) Selective elimination of membrane-damaged chloroplasts via microautophagy, Plant Physiol. in press.

  2. Nakamura, S., and Izumi, M. (2018) Regulation of chlorophagy during photoinhibition and senescence: Lessons from mitophagy. Plant Cell Physiol. 59, 1135-1143
  3. 中村咲耶, 泉正範, (2018) 壊れた葉緑体はオートファジーで丸ごと除去される,植物科学最前線 9, 36-45

花田賢太郎(国立感染症研究所)

  1. Sakuma, C., Sekizuka, T., Kuroda, M., Kasai, F., Saito, K., Ikeda, M., Yamaji, T., Osada, N., and Hanada, K. (2018) Novel endogenous simian retroviral integrations in Vero cells: implications for quality control of a human vaccine cell substrate. Sci. Rep., 8, 644. (CS and TS are co-first authors. NO and KH are co-correspondence)
  2. Otsuki, N., Sakata, M., Saito, K., Okamoto, K., Mori, Y., Hanada, K., Takeda, M. (2018) Both sphingomyelin and cholesterol in the host cell membrane are essential for Rubella virus entry. J. Virol., 92, e01130-17. (K.H. and M.T. are co-correspondence. This article was selected as Spotlight of the issue)
  3. Shimasaki, K., Watanabe-Takahash, M., Umeda, M., Funamoto, S., Saito, Y., Noguchi, N., Kumagai, K., Hanada, K., 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. Genes Cells, 23, 22-34.
  4. Shimizu, Y., Shirasago, Y., Kondoh, M., Suzuki, T., Wakita, T., Hanada, K., Yagi, K., and Fukasawa, M. (2018)  Monoclonal antibodies against occludin completely prevented hepatitis C virus infection in a mouse model. J. Virol., 92, e02258-17.
  5. Sugiki, T., Egawa, D., Kumagai, K., Kojima, C., Fujiwara, T., Takeuchi, K., Shimada, I., Hanada, K., and Takahashi, H. Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif. J. Biol. Chem. in press. (T.S. and D.E. are co-first authors. K.H. and H.T. are co-correspondence)
  6. Ikeda, M., Satomura, K., Sekizuka,T., Hanada, K., Endo, T., Osada, N. Comprehensive phylogenomic analysis reveals a novel cluster of simian endogenous retroviral sequences in Colobinae monkeys. Am. J. Primatol. in press.
  7. Hanada, K. Lipid-transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites (Invited review). J. Lipid Res., in press.
  8. Shirasago, Y., Fukazawa, H., Aizaki, H., Suzuki, T., Suzuki, T., Sugiyama, K., Wakita, T., Hanada, K., Abe, R.,   Fukasawa, M. Thermostable hepatitis C virus JFH1-derived variant isolated by adaptation to Huh7.5.1 cells. J. Gen. Virol., in press.

神吉智丈(新潟大学大学院 医歯学総合研究科)

  1. 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. Cell Rep., 23(12):3579-3590.

西頭英起(宮崎大学 医学部)

  1. Kadowaki, H. and Nishitoh, H. (2018) Endoplasmic reticulum quality control by garbage disposal. FEBS J., in press.

  2. Kadowaki, H., Satrimafitrah, P., Takami, Y. and Nishitoh, H. (2018) Molecular mechanism of ER stress-induced pre-emptive quality control involving association of the translocon, Derlin-1, and HRD1. Sci. Rep., 8, 7317 | DOI:10.1038/s41598-018-25724-x

清水重臣(東京医科歯科大学 難治疾患研究所)

  1. 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., Shimizu, S., 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. Scientific Signaling, 6, 11(516).
  2. Iwashita, H., Tajima Sakurai, H., Nagahora, N., Ishiyama, M., Shioji, K., Sasamoto, K., Okuma, K., Shimizu, S. and Ueno, Y. (2018) Small Fluorescent molecules for monitoring autophagic flux. FEBS Lett. 592, 559-567.
  3. Nagata, M., Arakawa, S., Yamaguchi, H., Torii, S., Endo, H., Tsujioka, M., Honda, S., Nishida, Y., Konishi, A. and Shimizu, S. (2018) Dram1 regulates DNA damage-induced alternative autophag Cell Stress 2, 55-65.
  4. Shimizu, S. (2018) Biological Roles of Alternative Autophagy. Mol Cells, 41, 50-54.
  5. Fujikake, N., Shin, M. and Shimizu, S. (2018) Association between autophagy and neurodegenerative diseases. Frontiers in Neuroscience, in press

今泉和則(広島大学大学院医歯薬保健学研究科 分子細胞情報学)

  1. Ohtake Y, Matsuhisa K, Kaneko M, Kanemoto S, Asada R, Imaizumi K, and Saito A. (2018) Axonal Activation of the Unfolded Protein Response Promotes Axonal Regeneration Following Peripheral Nerve Injury. Neuroscience, 375:34-48.
  2. Wu Y, Guo XP, Kanemoto S, Maeoka Y, Saito A, Asada R, Matsuhisa K, Ohtake Y, Imaizumi K, and Kaneko M. (2018) Sec16A, a key protein in COPII vesicle formation, regulates the stability and localization of the novel ubiquitin ligase RNF183. Plos One, 13: e0190407.
 

田村康(山形大学)

  1. Kakimoto,Y.,  Tashiro, S., Kojima, R., Morozumi, Y., Endo, T., and Tamura, Y. (2018) Visualizing multiple inter-organelle contact sites using the organelle-targeted split-GFP system. Sci. Rep., 8, 6175. DOI:10.1038/s41598-018-24466-0

  2. Endo, T., and Tamura, Y. (2018) News and Views;  Shuttle mission in the mitochondrial intermembrane space.  EMBO J. e98993

名黒功(東京大学)

  1. Imamura, K., Yoshitane, H., Hattori, K., Yamaguchi, M., Yoshida, K., Okubo, T., Naguro, I., Ichijo, H. and Fukada, Y. (2018) ASK family kinases mediate cellular stress and redox signaling to circadian clock.  Natl. Acad. Sci. U.S.A.in press
  2. Watanabe, K., Umeda, T., Niwa, K., Naguro, I. and Ichijo, H.(2018)A PP6-ASK3 module coordinates the bidirectional cell volume regulation under osmotic stress. Cell Rep. 13, 2809-2817. 
  3. Kamiyama, M., Naguro, I. and Ichijo, H.  (2018) mASKing cancer cells in a tumor microenvironment. Cell Cyclein press

加藤薫(産業技術総合研究所 バイオメディカル研究部門)

  1. Kijima, S. Staiger, C., Katoh, K.., Nagasaki, A., Ito, K., and Uyeda, T. (2018)  Arabidopsis vegetative actin isoforms, AtACT2 and AtACT7, generate distinct filament arrays in living plant cells. Sci Rep. in press
  2. Ito, N., Katoh, K., 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. Sci Rep. 8, 1634 | DOI:10.1038/s41598-018-20057-1
  3. 加藤薫(2018) 超解像光学顕微鏡, 光技術動向調査報告書2017年度、(印刷中)

片桐豊雅(徳島大学)

  1. Daizumoto, K., Yoshimaru, T., Matsushita, Y., Fukawa, T., Uehara, H., Ono, M., Komatsu, M., Kanayama, H., and Katagiri, T. (2018) A DDX31/mutant-p53/EGFR axis promotes multistep progression of muscle invasive bladder cancer. Cancer Res. in press.
  2. Miyagawa, Y., Matsushita, Y., Suzuki, , Komatsu, M., Yoshimaru, T., Kimura, R., Yanai, A., Honda, J., Tangoku, A., Sasa, M., Miyoshi, Y., and Katagiri, T. (2018) Frequent downregulation of LRRC26by epigenetic alterations is involved in the malignant progression of triple-negative breast cancers. Int J Oncol. in press.

2017年7月以降

下嶋美恵(東京工業大学 生命理工学院)

  1. Yoshitake Y, Sato R, Madoka Y, Ikeda K, Murakawa M, Suruga K, Sugiura D, Noguchi K, Ohta H, Shimojima M. (2017) Arabidopsis phosphatidic acid phosphohydrolases are essential for growth under nitrogen-depleted conditions. Front Plant Sci. 8, 1847

中野明彦(東京大学、理化学研究所)

  1. Yamagami, A., Saito, C., Sakuta, M., Shinozaki, M., Osada, H., Nakano, A., Asami, T., and Nakano, T. (2017) Brassinosteroids regulate vacuolar morphology in root meristem cells of ArabidopsisthalianaPlant Signal. Behav. 13: e1417722
  2. Kobayashi, K., Suemasa, F., Sagara, H., Nakamura, S., Ino, Y., Kobayashi, K., Hiramatsu, H., Haraguchi, T., Kurokawa, K., Todo, T., Nakano, A., 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. Sci. Rep. 7, 6650
    https://www.ncbi.nlm.nih.gov/pubmed/28751779
  3. Yamagami, A., Saito, C., Nakazawa, M., Fujioka, S., Uemura, T., Matsui, M., Sakuta, M., Shinozaki, K., Osada, H., Nakano, A., Asami, T., and Nakano, T. (2017) Evolutionarily conserved BIL4 suppresses the degradation of brassinosteroid receptor BRI1 and regulates cell elongation. Sci. Rep. 7, 5739
    https://www.ncbi.nlm.nih.gov/pubmed/28720789

花田賢太郎(国立感染症研究所)

  1. Tóth, E. A., Oszvald, Á., Péter, M., Balogh, G., Osteikoetxea-Molnár, A., Bozó, T., Szabó-Meleg, E., Nyitrai, M., Derényi, I., Yamaji, T., Hanada, K., Vígh, L., Matkó, J. (2017) Nanotubes connecting B lymphocytes: High impact of differentiation-dependent lipid composition on their growth and mechanics. Biochim. Biophys. Acta, 1862, 991-1000.
  2. Hanada, K. (2017) Ceramide transport from the endoplasmic reticulum to the trans Golgi region at organelle membrane contact sites.  In: Tagaya, M., Simmen, T. (eds) Organelle Contact Sites. Adv. Exp. Med. Biol., 997, 69-81, Springer, Singapore

清水重臣(東京医科歯科大学 難治疾患研究所)

  1. Arakawa, S., Tsujioka, M., Yoshida, T., Tajima-Sakurai, H., Nishida, Y., Matsuoka, Y., Yoshino, I., Tsujimoto, Y. and Shimizu, S. (2017) Role of Atg5-dependent cell death in the embryonic development of Bax/Bak double-knockout mice. Cell Death Differ., 24,1598-1608.
  2. Asano, J., Sato, T., Ichinose, S., Kajita, M., Onai, N., Shimizu, S. and Ohteki, T., (2017) Intrinsic autophagy is required for the maintenance of intestinal stem cells and for irradiation-induced intestinal regeneration. Cell Rep., 20, 1050–1060.
  3. Hidefumi, I., Satoru, T., Noriyoshi, N., Munetaka, I., Kosei, S., Kazumi, S., Shimizu, S. and Kentaro. O., (2017) Live Cell Imaging of Mitochondrial Autophagy with a Novel Fluorescent Small Molecule. ACS Chemical Biology, 12, 2546-2551.
  4. Kanemoto, K. Sugimura, Y. Shimizu, S. Yoshida, S. and Hosoya, T. (2017) Rhodium-catalyzed odorless synthesis of diaryl sulfides from borylarenes and S-aryl thiosulfonates. Commun., 53, 10640–10643.
  5. Yotsumoto, S., Muroi, Y., Chiba, T., Ohmura, R., Yoneyama, M., Magarisawa, M., Dodo, K., Terayama, N., Sodeoka, M., Aoyagi, R., Arita, M., Arakawa, S., Shimizu, S. and Tanaka, M. (2017) Hyperoxidation of ether-linked phospholipids accelerates neutrophil extracellular trap formation. Rep., 7, 16026

今泉和則(広島大学大学院医歯薬保健学研究科 分子細胞情報学)

  1. Saito A, Cai L, Matsuhisa K, Ohtake Y, Kaneko M, Kanemoto S, Asada R, Imaizumi K. (2017) Neuronal activity-dependent local activation of dendritic unfolded protein response promotes expression of brain-derived neurotrophic factor in cell soma, Journal of Neurochemistry, 144:35-49.

田村康(山形大学)

  1. Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E,  Michel, AH., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., Okamoto, Y., and Endo T. (2017). Structure–function insights into direct lipid transfer between membranes by Mmm1–Mdm12 of ERMES.  J. Cell. Biol. 217, 959–974. DOI: 10.1083/jcb.201704119.

  2. Tamura, Y. 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. Adv. Exp. Med. Biol., 997, 121-133, Springer, Singapore

名黒功(東京大学)

  1. Hirata, Y., Katagiri, K., Nagaoka, K., Morishita, T., Kudoh, Y., Hatta, T., Naguro, I., Kano, K., Udagawa, T., Natsume, T., Aoki, J., Inada, T., Noguchi, T., Ichijo, H. and Matsuzawa, A. (2017) TRIM48 promotes ASK1 activation and cell death through ubiquitination-dependent degradation of the ASK1-negative regulator PRMT1. Cell Rep.21, 2447-2457. 
  2. Hattori, K., Ishikawa, H., Sakauchi, C., Takayanagi, S., Naguro, I. and Ichijo, H. (2017) Cold stress-induced ferroptosis involves the ASK1-p38 pathway. EMBO Rep.18, 2067-2078.
  3. Kamiyama, M., Shirai, T., Tamura, S., Suzuki-Inoue, K., Ehata, S., Takahashi, K., Miyazono, K., Hayakawa, Y., Sato, T., Takeda, K., Naguro, I. and Ichijo, H. (2017) ASK1 facilitates tumor metastasis through phosphorylation of an ADP receptor P2Y12 in platelets. Cell Death Differ.24, 2066-2076.

加藤薫(産業技術総合研究所 バイオメディカル研究部門)

  1. Ohzono, T., Katoh, K., Wang, C., Fukazawa, A., Yamaguchi, S., and Fukuda, J. (2017) Uncovering different states of topological defects in schlieren textures of a nematic liquid crystal. Sci. Rep. 7, 16814 | DOI:10.1038/s41598-017-16967-1

木下タロウ(大阪大学)

  1. 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, T. Kinoshita and P. M. Campeau. (2017) Mutations in GPAA1, encoding a GPI transamidase complex protein, cause developmental delay, epilepsy, cerebellar atrophy, and osteopenia. Am. J. Hum. Genet., 101:856-865.

  2. Liu, Y.-S., X.-Y. Guo, T. Hirata, Y. Rong, D. Motooka, T. Kitajima, Y. Murakami, X.-D. Gao, S. Nakamura, T. Kinoshita and M. Fujita. (2017) N-Glycan dependent protein folding and endoplasmic reticulum retention regulate GPI-anchor processing. J. Cell Biol., 217: 585-599.

  3. Hirata, T., S. K. Mishra, S. Nakamura, K. Saito, D. Motooka, Y. Takada, N. Kanzawa, Y. Murakami, Y. Maeda, M. Fujita, Y. Yamaguchi and T. Kinoshita. (2017) Identification of a Golgi GPI-N-acetylgalactosamine transferase with tandem transmembrane regions in the catalytic domain. Nat. Commun., 9:405.

  4. 木下タロウ(2017)後天性突然変異で生じるGPIアンカー欠損赤血球と発作性夜間ヘモグロビン尿症、生化学、89(3):351-358.

  5. Colley, K. J., Varki, A. and Kinoshita, T.  (2017) Cellular Organization of Glycosylation. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876808

  6. Schnaar, R. L. and Kinoshita, T.  (2017) Glycosphingolipids. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876845

  7. Ferguson, M. A. J., Hart, G. W. and Kinoshita, T.  (2017) Glycosylphosphatidylinositol anchors. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876821

  8. Freeze, H. H., Kinoshita, T.  and Schnaar, R. L.  (2017) Genetic disorders of glycan degradation. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876818

  9. Freeze, H. H., H. Schachter and Kinoshita, T.  (2017) Genetic disorders of glycosylation. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876812

  10. Freeze, H. H., Kinoshita, T.  and Varki, A. (2017) Glycans in acquired human diseases. In Essentials of Glycobiology 3rd ed. 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.
    https://www.ncbi.nlm.nih.gov/pubmed/28876835

  11. Kohashi, K., A. Ishiyama, S. Yuasa, T. Tanaka, K. Miya, Y. Adachi, N. Sato, H. Saitsu, C. Ohba, N. Matsumoto, Y. Murakami, T. Kinoshita, K. Sugai and M. Sasaki. 2017. Epileptic apnea in a patient with inherited glycosylphosphatidylinositol anchor deficiency and PIGT mutations. Brain Dev., 2017 Jul 17. pii: S0387-7604(17)30174-2. PMID: 28728837

齊藤達哉(徳島大学)

  1. Takahama M, Akira S, and Saitoh, T. (2017) Autophagy limits activation of the inflammasomes. Immunol Rev.  doi:10.1111/imr.12613, in press
  2. Takahama, M., Fukuda, M., Ohbayashi, N., Kozaki, T., Misawa, T., Okamoto, T., Matsuura, Y., Akira, S., and Saitoh, T. (2017) The RAB2B-GARIL5 complex promotes cytosolic DNA-induced innate immune responses. Cell Rep. 20, 2944-2954.

  3. 髙濵充寛,齊藤達哉 (2017) インフラマソーム. 炎症と免疫 25, 94-96.

  4. 髙濵充寛,齊藤達哉 (2017) オートファジー. 周産期医学 47, 1513-1520.

  5. 渋谷周作, 齊藤達哉, 吉森保 (2017) オートファジーと生体防御応答. 実験医学増刊 The オートファジー 研究者たちの集大成が見える最新ビジュアルテキスト 35, 144-150.

  6. Misawa, T., Takahama, M., and Saitoh, T. (2017) Mitochondria–Endoplasmic Reticulum Contact Sites Mediate Innate Immune Responses. In: Tagaya, M., Simmen, T. (eds) Organelle Contact Sites. Adv. Exp. Med. Biol., 997, 187-197, Springer, Singapore
  7. 齊藤達哉. (2017) 尿酸塩結晶によるインフラマソーム活性化と痛風性関節炎. 尿酸と血糖 3, 6-9
  8. 齊藤達哉. (2017) 痛風関節炎の発症機序. カレントテラピー 35, 61-65

矢木宏和(名古屋市立大学)

  1. Yagi, H., Yan, G., Suzuki, T., Tsuge, S., Yamaguchi, T., and Kato, K. (2017) Lewis X-carrying neoglycolipids evoke selective apoptosis in neural stem cells. Neurochem Res in press
  2. Yanaka, S., Yamazaki, T., Yogo, R., Noda, M., Uchiyama, S., Yagi, H., and Kato, K. (2017) NMR Detection of Semi-Specific Antibody Interactions in Serum Environments. Molecules 22, E1619
  3.  Yogo, R., Yanaka, S., Yagi, H., 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 Fcγ receptor by deuteration-assisted small-angle neutron scattering. Biochem Biophys Rep 16, 1-4
  4. Yagi, H., 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. Biosci Biotechnol Biochem 81, 1687-1689
  5. 矢木宏和、加藤晃一 (2017) NMRを利用して糖タンパク質糖鎖の構造動態と相互作用を観る. 医学のあゆみ 262, 467-473

森和俊(京都大学)

  1. Ishikawa, T., Kashima, M., Nagano, A. J., Ishikawa-Fujiwara, T., Kamei, Y., Todo, T. and Mori, K. (2017) Unfolded Protein Response Transducer IRE1-mediated Signaling Independent of XBP1 mRNA Splicing Is Not Required for Growth and Development of Medaka Fish. eLife, 6, e26845.

細谷孝充(東京医科歯科大学)

  1. Nishiyama, Y., Hazama, Y., Yoshida, S., and Hosoya, T. (2017) Synthesis of Unsymmetrical Tertiary Phosphine Oxides via Sequential Substitution Reaction of Phosphonic Acid Dithioesters with Grignard Reagents. Org. Lett. 19, 3899-3902 

尾野雅哉(国立がん研究センター研究所)

  1. Kagami, Y., Ono, M., and Yoshida, K. (2017) Plk1 phosphorylation of CAP-H2 triggers chromosome condensation by condensin II at the early phase of mitosis. Sci Rep 7, 5583
  2. 尾野雅哉 (2017) パラフィン包埋標本を用いたプロテオーム解析. 病理と臨床. 35(7), 622-627

金川基(神戸大学)

  1. Kamizaki, K., Doi, R., Hayashi, M., Saji, T., Kanagawa, M., Toda, T., Fukada, SI., Ho, HH., Greenberg, ME., Endo, M., Minami, Y. (2017) The Ror1 receptor tyrosine kinase plays a critical role in regulating satellite cell proliferation during regeneration of injured muscle. J. Biol. Chem.in press (jbc.M117.785709. doi:10.1074/jbc.M117.785709)