Publication

2018

Shin-Ichiroh Saitoh(Division of Innate Immunity, Department of Microbiology and Immunology, The Institute of Medical Science, The University of Tokyo)

  1. 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. 

Akihiko Nakano(RIKEN Center for Advanced Photonics, Live Cell Super-Resolution Imaging Research Team)

  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 thaliana. Plant 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 polymorpha. Plant 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 thaliana. Cell 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.

Masaya Ono(Department of Clinical Proteomics, National Cancer Center Research Institute)

  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

Masanori Izumi(Frontier Research Institute for Interdisciplinary Sciences, Tohoku University)

  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

Kentaro Hanada(Department of Biochemistry & Cell Biology
National Institute of Infectious Diseases)

  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.

Tomotake Kanki(Department of Cellular Physiology, Niigata University Graduate School of Medical and Dental Scienc)

  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.

Hideki Nishitoh(Laboratory of Biochemistry and Molecular Biology, University of Miyazaki)

  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

Shigeomi Shimizu(Department of Pathological Cell Biology, Medical Research Institute, Tokyo Medical and Dental University)

  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

Kazunori Imaizumi(Department of Biochemistry, Institute of Biomedical & Health Sciences, Hiroshima University)

  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.
 

Yasushi Tamura(Faculty of Science, Yamagata University)

  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

Isao Naguro(Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

  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

Kaoru Katoh(Senior Researcher, Biomedical Research Institute National Institute of Advanced Industrial Sciences and Technology (AIST))

  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

Toyomasa Katagiri(Division of Genome Medicine, Institute for Genome Research, Tokushima University)

  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.

After July 2017

Mie Shimojima(School of Life Science and Technology, Tokyo Institute of Technology)

  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

Kentaro Hanada(Department of Biochemistry & Cell Biology
National Institute of Infectious Diseases)

  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

Akihiko Nakano(RIKEN Center for Advanced Photonics, Live Cell Super-Resolution Imaging Research Team)

  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

Shigeomi Shimizu(Department of Pathological Cell Biology, Medical Research Institute, Tokyo Medical and Dental University)

  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

Kazunori Imaizumi(Department of Biochemistry, Institute of Biomedical & Health Sciences, Hiroshima University)

  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.

Yasushi Tamura(Faculty of Science, Yamagata University)

  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

Isao Naguro(Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo)

  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.

Kaoru Katoh(Senior Researcher, Biomedical Research Institute National Institute of Advanced Industrial Sciences and Technology (AIST))

  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

Taroh Kinoshita(Yabumoto Department of Intractable Disease Research, Research Institute for Microbial Diseases, Osaka University)

  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. 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

  5. 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

  6. 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

  7. 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

  8. 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

  9. 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

  10. 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

Akihiko Nakano(RIKEN Center for Advanced Photonics, Live Cell Super-Resolution Imaging Research Team)

  1. 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
  2. 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

Tatsuya Saitoh(The University of Tokushima)

  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. 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

Hirokazu Yagi(Graduate School of Pharmaceutical Sciences, Nagoya City University)

  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

Kazutoshi Mori(Department of Biophysics, Graduate School of Science, Kyoto University)

  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.

Takamitsu Hosoya(Laboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University)

  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

Masaya Ono(Department of Clinical Proteomics, National Cancer Center Research Institute)

  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

Motoi Kanagawa(Molecular Brain Science, Kobe University Graduate School of Medicine)

  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)