1. Yamaji, T., Sekizuka, T., Kuroda, M., and Hanada, K. (2019) A CRISPR screen identifies LAPTM4A and TM9SF proteins as glycolipid-regulating factors, iScience, 11, 409-424. | DOI:org/10.1016/j.isci.2018.12.039.
  2. Nakao, N., Ueno, M., Sakai, S., Egawa, D., Hanzawa, H., Kawasaki, S., Kumagai, K., Suzuki, M., Kobayashi, S., and Hanada, K. (2019) Natural ligand-nonmimetic inhibitors to the lipid transfer protein CERT, Comms Chem, in press. (N.N., M.U., and S.S. are co-first authors. S.K. and K.H. are co-correspondence)

西頭英起(宮崎大学 医学部)

  1. Nishitoh, H. (2019) Paradigm shift from “Compartment” to “Zone” in the understanding of organelles. J Biochem. 165, 97–99.

清水重臣(東京医科歯科大学 難治疾患研究所)

  1. Shimizu, S. (2019) Organelle zones in mitochondria. J Biochem. 165, 101–107.


  1. Tamura, Y., Kawano, S., and Endo T. (2019) Organelle contact zones as sites for lipid transfer. J Biochem. 165, 115–123.


  1. Kurokawa, K., and Nakano, A. (2019) The ER exit sites are specialized ER zones for the transport of cargo proteins from the ER to the Golgi apparatus. J Biochem. 165, 109–114.


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


  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


  1. Muro, K., Matsuura-Tokita, K., Tsukamoto, R., Kanaoka, M. M., Ebine, K., Higashiyama, T., Nakano, A., and Ueda, T. ANTH domain-containing proteins are required for the pollen tube plasma membrane integrity via recycling ANXUR kinases. Commun. Biol. in press.
  2. Ishikawa, K., Tamura, K., Ueda, H., Ito, Y., Nakano, A., Hara-Nishimura, I., and Shimada, T. The synaptotagmin-associated ER-plasma membrane contact sites are distributed to immobile ER tubules. Plant Physiol. in press.

  3. 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 thalianaPlant Cell Physiol. in press.

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

  5. 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.

  6. 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. 59:845-856.

  7. 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. 43:41-51.

  8. 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.

  9. Suda, Y., Kurokawa, K., and Nakano, A. Regulation of ER-Golgi transport dynamics by GTPases in budding yeast. Frontiers Cell Dev. Biol. 5:122.

  10. 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. 18:fox095.

  11. 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.

  12. 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.


  1. Nuclear envelope localization of PIG-B is essential for GPI-anchor synthesis in Drosophila.
    Yamamoto-Hino.M., Katsumata, E., Suzuki, E., Maeda, Y., Kinoshita, T. and Goto, S.
    J. Cell Sci., 131, jcs218024 (2018)
    DOI: 10.1242/jcs.218024


  1. Nuclear envelope localization of PIG-B is essential for GPI-anchor synthesis in Drosophila.
    Yamamoto-Hino.M., Katsumata, E., Suzuki, E., Maeda, Y., Kinoshita, T. and Goto, S.
    J. Cell Sci., 131, jcs218024 (2018)
    DOI: 10.1242/jcs.218024
  2. Kinoshita, T. (2018) Congenital defects in the expression of the glycosylphosphatidylinositol-anchored complement regulatory proteins CD59 and decay-accelerating factor. Semin. Hematol., 55:136-140.

  3. Mogami, Y., Suzuki, Y., Murakami, Y., Ikeda, T., Kimura, S., Yanagihara, K., Okamoto, N., and Kinoshita, T. (2018) Early infancy-onset stimulation-induced myoclonic seizures in three siblings with inherited glycosylphosphatidylinositol (GPI) anchor deficiency. Epileptic Disord., 20:42-50.

  4. Pagnamenta, A. T. *, Murakami, Y. *, Anzilotti, C., Titheradge, H., Oates, A. J., Morton, J., The DDD Study, Kinoshita, T.+, Kini, U.+, and Taylor, J. C.+. (2018) A homozygous variant disrupting the PIGH start-codon is associated with developmental delay, epilepsy and microcephaly. Hum. Mutat., 39:822-826. (* and +, equal contribution)

  5. Yoko-o, T., Umemura, M., Komatsuzaki, A., Ikeda, K., Ichikawa, D., Takase, K., Kanzawa, N., Saito, K., Kinoshita, T., Taguchi, R., and Jigami, Y. (2018) Lipid moiety of glycosylphosphatidylinositol-anchored proteins contributes to the determination of their final destination in yeast. Genes Cells, 23:880-892.

  6. Kawamoto, M., Murakami, Y., Kinoshita, T., and Kohara, N. (2018) Recurrent aseptic meningitis with PIGT mutations: a novel pathogenesis of recurrent meningitis successfully treated by eculizumab. BMJ Case Rep., pii: bcr-2018-225910.

  7. 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., Kinoshita, T., and Campeau, P. M. (2018) Mutations in PIGS, encoding a GPI transamidase, cause a neurological syndrome ranging from fetal akinesia to epileptic encephalopathy. Am. J. Hum. Genet., 103:602-611.

  8. Yamamoto-Hino, M., Katsumata, E., Suzuki, E., Maeda, Y., Kinoshita, T., and Goto, S. (2018) Nuclear envelope localization of PIG-B is essential for GPI anchor synthesis in Drosophila. J. Cell Sci., 131: pii: jcs218024.


  1. 齋藤伸一郎 (2018) Toll様受容体(TLR)7の応答と細胞内ロジスティクス、医学のあゆみ 265(13): 1087-1093

  2. Sato, R., Kato, A., Chimura, T., Saitoh,S., 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. Nature Immunology. Sep 10, doi: 10.1038/s41590-018-0203-2. 

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.

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. 177, 1007-1026.

  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


  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. (2018) Phosphoinositide binding by the PH domain in ceramide transfer protein (CERT) is inhibited by hyperphosphorylation of an adjacent serine-repeat motif. J. Biol. Chem., 293(28), 11206-11217. (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., and Osada, N. (2018) Comprehensive phylogenomic analysis reveals a novel cluster of simian endogenous retroviral sequences in Colobinae monkeys. Am. J. Primatol., 80(7), e22882.
  7. Hanada, K. (2018) Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites (Invited review). J. Lipid Res., 59(8), 1341-1366.
  8. Shirasago, Y., Fukazawa, H., Aizaki, H., Suzuki, T., Suzuki, T., Sugiyama, K., Wakita, T., Hanada, K., Abe, R., and Fukasawa, M. (2018) Thermostable hepatitis C virus JFH1-derived variant isolated by adaptation to Huh7.5.1 cells. J. Gen. Virol., 99(10), 1407-1417.
  9. Kumagai, K., Elwell, CA., Ando, S., Engel, JN. and Hanada, K. (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. Biochem Biophys Res Commun., 505(4), 1070-1076. (K.K. and K.H. are co-correspondence)

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.

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.


  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)


  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.


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


  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
  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


  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.


  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


  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


  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.

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