1. | Machida K, Kanzawa K, Shigeta T, Yamamoto Y, Tsumoto K, and *Imataka H Huntingtin polyglutamine-dependent protein aggregation in reconstituted cells. ACS synthetic Biology 7: 377-383 (2018) doi: 10.1021/acssynbio.7b00372 |
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2. | Uemura E, Niwa T, Minami S, Takemoto K, Fukuchi S, Machida K, Imataka H, Ueda T, Ota M, and Taguchi H Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding. Scientific Reports 8: 678 (2018) doi: 10.1038/s41598-017-18977-5 |
1. | Baeg K, Tomari Y, *Iwakawa HO In vitro RNA-dependent RNA Polymerase Assay Using Arabidopsis RDR6 Bio-protocol 8(1), (2018) |
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1. | Chen, C. W. and Tanaka, M. Genome-wide Translation Profiling by Ribosome-Bound tRNA Capture. Cell Rep. 23, 608-621, (2018). doi: 10.1016/j.celrep.2018.03.035. プレスリリース: http://www.riken.jp/pr/press/2018/20180411_1/ |
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1. | Yuichi Tsuchiya, Michiko Saito, Hiroshi Kadokura, Jun-ichi Miyazaki, Fumi Tashiro, Yusuke Imagawa, Takao Iwawaki, Kenji Kohno IRE1–XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells J. Cell Biol. 217 (2018) DOI: 10.1083/jcb.201707143 |
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1. | Tsuchiya, Y., Saito, M., Kadokura, H., Miyazaki, J., Tashiro, F., Imagawa, Y., Iwawaki, T., and Kohno, K.* IRE1-XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells. J. Cell Biol. 217(4), 1287-1301 (2018) doi: 10.1083/jcb.201707143. プレスリリース:http://www.naist.jp/pressrelease/2018/03/004316.html |
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2. | Mai, C.T., Le, Q.G., Ishiwata-Kimata, Y., Takagi, H., Kohno, K., and Kimata. Y.* 4-Phenylbutyrate suppresses the unfolded protein response without restoring protein folding in Saccharomyces cerevisiae. FEMS Yeast Research, 18(2), (2018) doi: 10.1093/femsyr/foy016. |
3. | Yamaoka, Y., Choi, B.Y., Kim, H., Shin, S., Kim, Y., Jang, S., Song, W.Y., Cho, C.H., Yoon, H.S., Kohno, K., and Lee, Y.* Identification and functional study of ER stress sensor IRE1 in Chlamydomonas reinhardtii. Plant J., 94(1), 91-104 (2018) doi: 10.1111/tpj.13844. |
1. | Okumoto, K., Ono, T., Toyama, R., Shimomura, A., Nagata, A., and Fujiki Y. New splicing variants of mitochondrial Rho GTPase-1 (Miro1) transport peroxisomes. J. Cell Biol., 217, 619-633 (2018). doi: 10.1083/jcb.201708122. 紹介記事(日本語) 日本語記事(PDF) |
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1. | Fujiwara, K., Ito, K., Chiba, S.. MifM-instructed translation arrest involves nascent chain interactions with the exterior as well as the interior of the ribosome. Sci Rep. 8, 10311. (2018) doi: 10.1038/s41598-018-28628-y. |
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1. | Takehito Tanzawa, Koji Kato, Dylan Girodat, Toyoyuki Ose, Yuki Kumakura, Hans-Joachim Wieden, Toshio Uchiumi, Isao Tanaka, and Min Yao The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. Nucleic Acids Research. 46, 3232-3244 (2018) |
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1. | Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the Trigger Factor chaperone S Kawagoe, H Nakagawa, H Kumeta, K Ishimori, T Saio Journal of Biological Chemistry, in press http://www.jbc.org/content/early/2018/08/09/jbc.RA118.003579 |
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2. | Saio T, Kawagoe S, Ishimori K, Kalodimos CG. Oligomerization of a molecular chaperone modulates its activity. Elife. 2018 May 1;7. pii: e35731. doi: 10.7554/eLife.35731. |
1. | Umegaki Y, Brotons AM, Nakanishi Y, Luo Z, Zhang H, Bonni A, Ikeuchi Y. Palladin Is a Neuron-Specific Translational Target of mTOR Signaling That Regulates Axon Morphogenesis. Journal of Neuroscience. 2018 May 23;38(21):4985-4995. doi: 10.1523/JNEUROSCI.2370-17.2018. |
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Kadowaki, H., Satrimafitrah, P., Takami, Y. and Nishitoh H. |
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1. | Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T.,Chiba, S., Ito, K. and Taguchi, H. Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing. Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020. |
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1. | Daiko Y, Mizutani S, Machida K. Imataka H, Honda S and Iwamoto Y H+ emission under room temperature and non-vacuumatmosphere from a sol–gel-derived nanoporous emitter J Sol-Gel Sci. Technol. 83: 252-258 (2017) doi:10.1007/s10971-017-4430-z |
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3. | *Inada, T. |
1. | Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T.,Chiba, S., Ito, K. and Taguchi, H. Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing. Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020. |
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1. | *Iwakawa HO, *Tomari Y Silencing messages in a unique way Nature Plants 3(10), 769-770.(2017) |
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2. | Watanabe M, Iwakawa HO, Tadakuma H, Tomari Y Biochemical and single-molecule analyses of the RNA silencing suppressing activity of CrPV-1A Nucleic acids research 45(18), 10873-10844.(2017) |
3. | Tajima Y, Iwakawa HO, Hyodo K, Kaido M, Mise K, Okuno T Requirement for eukaryotic translation initiation factors in cap-independent translation differs between bipartite genomic RNAs of red clover necrotic mosaic virus Virology 509,152-158. (2017) |
4. | Tomari Y, *Iwakawa HO |
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1. | Tschurtschenthaler, M., Adolph, T.E., Ashcroft, J.W., Niederreiter, L., Bharti, R., Saveljeva, S., Bhattacharyya, J., Flak, M.B., Shih, D.Q., Fuhler, G.M., Parkes, M., Kohno, K., Iwawaki, T., van der Woude, C.J., Harding, H., Smith, A.M. Peppelenbosch, M.P., Targan, S.R., Ron, D., Rosenstiel, P., Blumberg, R.S.*, and Kaser, A.* Defective ATG16L1-mediated removal of IRE1α drives Crohn's disease-like ileitis. J. Exp. Med. 214(2), 401-422 (2017) doi: 10.1084/jem.20160791 |
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2. | Sato, H., Shiba, Y.*, Tsuchiya, Y., Saito, M., and Kohno, K.*
4μ8C inhibits insulin secretion independent of IRE1α RNase activity. Cell Struct. Funct. 42(1), 61-70 (2017) doi: 10.1247/csf.17002. Epub 2017 Mar 18. PMID: 28321016 |
3. | Schmitner, N., Kohno, K. and Meyer, D*.
Ptf1a+, ela3l- cells are developmentally maintained progenitors for exocrine regeneration following extreme loss of acinar cells in zebrafish larvae. Dis. Model. Mech. 10(3), 307-321 (2017) doi: 10.1242/dmm.026633 |
1. | Kinoshita, N., Matsuura, A., and Fujiki Y. Peroxisome biogenesis: a novel inducible PEX19 splicing variant is involved in early stages of peroxisome proliferation. J. Biochem. 161, 297-308 (2017). |
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2. | Yagita, Y., Shinohara, K., Liu, Y., and Fujiki Y. ACBD5 is a peroxisomal tail-anchored protein exposing its acyl-CoA binding domain to the cytosol. J. Biol. Chem. 292, 691-705 (2017). |
3. | Imoto, Y., Abe, Y., Okumoto, K., Honsho, M., Kuroiwa, H., Kuroiwa, T., and Fujiki Y. Defining dynamin-based ring organizing center on the peroxisome-dividing machinery isolated from Cyanidioschyzon merolae.. J. Cell Sci. 130, 853-867 (2017) (Highlighted articleとして掲載) |
4. | Abe, S., Nagai, T., Masukawa, M., Okumoto, K., Homma, Y., Fujiki Y., and Mizuno, K. Localization of NDR2 to peroxisomes and its role in ciliogenesis. J. Biol. Chem. 292, 4089-4098 (2017). |
5. | Honsho, M., Abe, Y., and Fujiki Y. Plasmalogen synthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet of plasma membrane. Sci. Rep. 7, article 43936 (2017). |
6. | Okumoto, K., Tamura, S., and Fujiki Y. Blue-Native PAGE: Applications to study on peroxisome biogenesis. Methods in Mol. Biol. 1595, 197-205 (2017) |
7. | Liu,Y., Honsho, M., and Fujiki Y. In vitro PMP import analysis using cell-free synthesized PMP and isolated peroxisomes. Methods in Mol. Biol. 1595, 207-212 (2017) |
8. | Okumoto, K., Honsho, M., Liu, Y., and Fujiki Y. Peroxisomal membrane and matrix protein import using a semi-intact mammalian cell system. Methods in Mol. Biol. 1595, 213-219 (2017) |
9. | Fujiki Y. Functional complementation (version 3.0). eLS., article A27640 (2017). |
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1. | Chadani, Y., Niwa, T., Izumi, T., Sugata, N., Nagao, A., Suzuki, T., Chiba, S., Ito, K. and Taguchi, H. Intrinsic Ribosome Destabilization Underlies Translation and Provides an Organism with a Strategy of Environmental Sensing. Mol Cell. 68, 528-539.e5. (2017) doi: 10.1016/j.molcel.2017.10.020. |
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1. | Meirong Chen, Koji Kato, Yume Kubo, Yoshikazu Tanaka, Yuchen Liu, Feng Long, William Whitman, Pascal Lill, Christos Gatsogiannis, Stefan Raunser,Nobutaka Shimizu, Akira Shinoda, Akiyoshi Nakamura, Isao Tanaka, and Min Yao. Structural basis for the tRNA-dependent cysteine biosynthesis Nature Communications. 8, 1512 (2017) |
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2. | Minghao Chen, Shin-ichi Asai, Shun Narai, Shusuke Nambu, Naoki Omura, Yuriko Sakaguchi, Tsutomu Suzuki, Masao Ikeda-Saito, Kimitsuna Watanabe, Min Yao, Naoki Shigi, and Yoshikazu Tanaka. Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA Proc. Natl. Acad. Sci. USA, 114, 4954-4959 (2017) |
1. | Vial-Pradel S., Keta S., Nomoto M., Luo L., Takahashi H., Suzuki M., Yokoyama Y., Sasabe M., Kojima S., Tada Y., *Machida Y.and *Machida C. Arabidopsis zinc-finger-like protein ASYMMETRIC LEAVES2 (AS2) and two nucleolar proteins maintain gene body DNA methylation in the leaf polarity gene ETTIN (ARF3), Plant Cell Physiol.(DOI: 10.1093/pcp/pcy031) |
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2. | Hayashi N., Sasaki S., Takahashi H., Yamashita Y., Naito S., *Onouchi H. Identification of Arabidopsis thaliana upstream open reading frames encoding peptide sequences that cause ribosomal arrest. Nucleic Acids Res., 45, 8844-8858, (2017) DOI: 10.1093/nar/gkx528 |
1. | Kawada J, Kaneda S, Kirihara T, Maroof A, Levi T, Eggan K, Fujii T, Ikeuchi Y. Generation of a Motor Nerve Organoid with Human Stem Cell-Derived Neurons. Stem Cell Reports. 2017 Nov 14;9(5):1441-1449. doi: 10.1016/j.stemcr. 2017.09.021. 報道: 朝日新聞(2017/10/27、朝刊) 化学工業日報(2017/10/27、朝刊) 日本経済新聞(2017/10/27、夕刊) 毎日新聞(2017/10/28、夕刊) 読売新聞(2017/11/1、夕刊) 科学新聞(2017/11/3、1面) |
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「ビブリオ属細菌における2つのタンパク質膜透過促進因子の生理的意義と使い分け機構」 |
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Murao, N. and Nishitoh H. |
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1. | Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito 広報記事 |
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1. | Machida K, Shigeta T, Kobayashi A, Masumoto A, Hidaka Y and *Imataka H Cell-free analysis of polyQ-dependent protein aggregation and its inhibition by chaperone proteins J. Biotechnology 239:1-8 (2016) doi: 10.1016/j.jbiotec.2016.09.031 |
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2. | Kashiwagi K, Shigeta T, Imataka H, Ito T, and Yokoyama S Expression, purification, and crystallization of Schizosaccharomyces pombe eIF2B J. Structural and Functional Genomics 17: 33-38 (2016) doi:10.1007/s10969-016-9203-3 |
3. | Ozdemir A, Machida K, Imataka H, and Catling A Identification of the T-complex protein as a binding partner for newly synthesized Cytoplasmic Dynein Intermediate Biochem. Biophys. Res. Commun. 469: 126-131 (2016) doi: 10.1016/j.bbrc.2015.11.082 |
1. | Ikeuchi, K., Yazaki, E., Kudo, K. and *Inada, T. Conserved functions of human Pelota in mRNA quality controls for nonstop mRNA. FEBS Let. 18, 3254-3263 (2016) |
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2. | Ikeuchi, K. and *Inada, T. Ribosome-associated Asc1/RACK1 is required for endonucleolytic cleavage induced by stalled ribosome at the 3' end of nonstop mRNA. Sci. Rep. 6, 28234. (2016) |
1. | Kanemura, S., Okumura, M., Yutani, K., Ramming, T., Hikima, T., Appenzeller-Herzog, C. , Akiyama, S. and Inaba, K.* "Human ER oxidoreductin-1a (Ero1a) undergoes dual regulation through complementary redox interactions with protein-disulfide isomerase", J. Biol. Chem., 291, 23952-23964 (2016) |
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2. | Ryo Ushioda, Akitoshi Miyamotod, Michio Inoue, Satoshi Watanabe, Masaki Okumurae, Ken-ichi Maegawa, Kaiku Uegaki, Shohei Fujii, Yasuko Fukuda, Masataka Umitsu, Junichi Takagi, Kenji Inaba, Katsuhiko Mikoshiba and Kazuhiro Nagata プレスリリース 報道 産経新聞(2016年10月3日付23面)、京都新聞(2016年10月1日付33面)、共同通信(オンライン)、日経プレスリリース(オンライン) |
1. | Kanda, S., Yanagitani, K.*, Yokota, Y., Esaki, Y., and Kohno, K.*
Autonomous translational pausing is required for XBP1u mRNA recruitment to the ER via the SRP pathway. Proc Natl Acad Sci USA, 113(40), E5885-E5895 (2016) doi: 10.1073/pnas.1604435113, PMID: 27651490 紹介記事 http://bsw3.naist.jp/research/index.php?id=1377 報道 朝日新聞(11月3日朝刊21面), 日刊工業新聞(9月21日朝刊27面) |
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2. | Le, Q.G,, Ishiwata-Kimata, Y., Kohno, K. and Kimata, Y.*
Cadmium impairs protein folding in the endoplasmic reticulum and induces the unfolded protein response. FEMS Yeast Research 16(5), pii: fow049 (1-8) (2016) doi: 10.1093/femsyr/fow049 |
3. | Tsuru, A., Imai, Y., Saito, M., and Kohno, K. Novel mechanism of enhancing IRE1α-XBP1 signalling via the PERK-ATF4 pathway. Sci. Rep. Apr 7; 6:24217 (2016) doi: 10.1038/srep24217, PMID:27052593 |
1. | Honsho, M., Yamashita,S., and Fujiki Y. Peroxisome homeostasis: mechanisms of division and selective degradation of peroxisomes in mammals. Biochim. Biophys. Acta-Mol. Cell Res. 1863, 984-991 (2016). |
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2. | Fujiki Y. Peroxisome biogenesis and human peroxisome-deficiency disorders. Proc. Jpn. Acad., Ser. B 92: 463-477 (2016). |
3. | Liu Y., Yagita Y., and Fujiki Y. Assembly of peroxisomal membrane proteins via the direct Pex19p-Pex3p pathway. Traffic 17, 433-455 (2016) doi: 10.1111/tra.12376 紹介文 liu-et_al.pdf |
1. | Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito 広報記事 |
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1. | Yuhei Chadani, Tatsuya Niwa, Shinobu Chiba, Hideki Taguchi, Koreaki Ito 広報記事 |
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1. | Kazuki Nakamura, Ryo Iizuka, Shinro Nishi, Takao Yoshida, Yuji Hatada, Yoshihiro Takaki, Ayaka Iguchi, Dong Hyun Yoon, Tetsushi Sekiguchi, Shuichi Shoji, Takashi Funatsu. Culture-independent method for identification of microbial enzyme-encoding genes by activity-based single-cell sequencing using a water-in-oil microdroplet platform. Sci. Rep. 6: 22259 (2016). doi: 10.1038/srep22259 |
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2. | Ryo Iizuka, Takashi Funatsu 【Review】Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins Biophys. Physicobiol. 13: 63-69 (2016). doi: 10.2142/biophysico.13.0_63 |
1. | A. Kato, T. Ando, S. Oda, M. Watanabe, N. Koyanagi, J. Arii and Y. Kawaguchi Roles of Us8A and its phosphorylation mediated by Us3 in herpes simplex virus 1 pathogenesis. J. Virol. (in press) |
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2. | Y. Sato, A. Kato, Y. Maruzuru, M. Oyama, H. Kozuka-Hata, J. Arii and Y. Kawaguchi Cellular Transcriptional Coactivator RanBP10 and Herpes Simplex Virus 1 ICP0 Interact and Synergistically Promote Viral Gene Expression and Replication. J. Virol. 90: 3173-3186. (2016) |
3. | K. Shindo, A. Kato, N. Koyanagi, H. Sagara, J. Arii, and Y. Kawaguchi Characterization of a chimera herpes simplex virus 1 (HSV-1) in which its Us3 protein kinase gene was replaced with the HSV-2 Us3 gene. J. Virol. 90:457-473 |
1. | Miyazaki, R., Yura, T., Suzuki, T., Dohmae, N., Mori, M., and Akiyama, Y. A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32. Sci. Rep. 6, 24147 (2016) |
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1. | Satoh, T., Nakamura, Y and Satoh, A. K. Rab6 functions in polarized transport in Drosophila photoreceptors. Fly in press (2016) |
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2. | 佐藤卓至・中村祐里・佐藤明子 ショウジョウバエ視細胞の膜タンパク質選別輸送における低分子量Gタンパク質Rab6の役割. 顕微鏡 51, in press. (2016) |
3. | Iwanami, N., Nakamura, Y., Satoh, T. and Satoh, A. K. Rab6 is required for multiple apical transport pathways but not for basolateral transport pathway in Drosophila photoreceptors. PLOS Genetics. e1005828.(2016) doi: 10.1371/journal.pgen.1005828 |
1. | Yuichiro Kida, Yudai Ishihara, Hidenobu Fujita, Yukiko Onishi, *Sakaguchi, M. |
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2. | Haruka Sakaue, Shohei Iwashita, Yukari Yamashita, Yuichiro Kida, *Sakaguchi, M. |
3. | Kongsoo Kang, Michiyo Takahara, Haruka Sakaue, *Sakaguchi, M. |
1. | Ryo Ushioda, Akitoshi Miyamotod, Michio Inoue, Satoshi Watanabe, Masaki Okumurae, Ken-ichi Maegawa, Kaiku Uegaki, Shohei Fujii, Yasuko Fukuda, Masataka Umitsu, Junichi Takagi, Kenji Inaba, Katsuhiko Mikoshiba and Kazuhiro Nagata プレスリリース 報道 産経新聞(2016年10月3日付23面)、京都新聞(2016年10月1日付33面)、共同通信(オンライン)、日経プレスリリース(オンライン) |
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1. | Kashiwagi, K., Shigeta, T., Imataka, H., Ito, T.* and Yokoyama, S.* Expression, purification, and crystallization of Schizosaccharomyces pombe eIF2B. J Struct Funct Genomics, 17, 33-38.(2016) DOI: 10.1007/s10969-016-9203-3. (Epub 2016 Mar 29) (* co-corresponding authors) |
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2. | Kashiwagi, K., Takahashi, M., Nishimoto, M., Hiyama, T.B., Higo, T., Umehara, T., Sakamoto, K., Ito, T.* and Yokoyama, S.* Crystal structure of eukaryotic translation initiation factor 2B. Nature, 531, 122-125.(2016) DOI: 10.1038/nature16991. (Epub 2016 Feb 22) (* co-corresponding authors) |
1. | Niwa, T., Sasaki, Y., Uemura, E., Nakamura, S., Akiyama, M., Ando, M., Sawada, S., Mukai, SA., Ueda, T., Taguchi, H., Akiyoshi, K. Comprehensive study of liposome-assisted synthesis of membrane proteins using a reconstituted cell-free translation system. Sci Rep. 2015 Dec 15;5:18025. doi: 10.1038/srep18025. |
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2. | T, Niwa., K, Fujiwara., Taguchi, H. Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach. FEBS Lett., in press |
1. | Tsuboi, T., Yamazaki, R., Nobuta, R., Ikecuhi, K., Makino, S., Ohtaki, Y., Suzuki, Y., Yoshihisa, T., Trotta, C. and *Inada, T. The tRNA Splicing Endonuclease Complex Cleaves the Mitochondria-localized CBP1 mRNA. J Biol. Chem. (2015) |
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2. | Makino, S., Mishima, Y., Inoue, K. and *Inada, T. Roles of mRNA-fate modulators Dhh1 and Pat1 in TNRC6-dependent gene silencing recapitulated in yeast. J Biol. Chem. (2015) |
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1. | Suzuki, G., Weissman, J.S., Tanaka, M. [KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis Molecular Cell, 60, 651-660 (2015), doi: 10.1016/j.molcel.2015.10.020 プレスリリース(日本語の解説):http://www.riken.jp/pr/press/2015/20151120_1/ |
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1. | *Hirai, S., Kurashima, H., Nakamura, D., Komatsu, T., Yasuda, Y., Habashita-Obata, S., Ichikawa, S., Katsuta, O., Iwawaki, T., Kohno, K. 2-Phenyl-APB-144-induced retinal pigment epithelium degeneration and its underlying mechanisms. J. Ocul. Pharmacol. Ther., 31, 570-584, (2015) |
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2. | Mathuranyanon, R., Tsukamoto, T., Takeuchi, A., Ishiwata-Kimata, Y., Tuchiya, Y., Kohno, K., *Kimata, Y. Tight regulation of the unfolded 1 protein sensor Ire1 by its intramolecularly antagonizing subdomain. J. Cell Sci. 128(9), 1762-1772 (2015) |
1. | Yoshida, Y., Niwa, H., Honsho, M., Itoyama, A., and Fujiki, Y. Pex11p mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biology Open, 4, 710-721 (2015). |
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2. | Fujiki, Y., Okumoto, K., and Honsho, M. Protein import into peroxisomes: the principles and methods of studying (version 2.0). eLS., pp.1-7 (2015). doi: 10.1002/9780470015902.a0002618.pub2 |
3. | Honsho, M., Abe, Y., and Fujiki, Y. Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis. J. Biol. Chem. 290, 28822-28833 (2015). |
1. | Sohmen, D., Chiba, S., Shimokawa-Chiba, N., Innis, A., Berninghausen, O., Beckmann, R., Ito, K. and *Wilson, D. |
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2. | Shimokawa-Chiba, N., Kumazaki, K., Tsukazaki, T., Nureki, O., Ito, K. and *Chiba, S. |
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1. | Sohmen, D., Chiba, S., Shimokawa-Chiba, N., Innis, A., Berninghausen, O., Beckmann, R., Ito, K. and *Wilson, D. |
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2. | Shimokawa-Chiba, N., Kumazaki, K., Tsukazaki, T., Nureki, O., Ito, K. and *Chiba, S. |
3. | *Chiba, S. and Ito, K. |
1. | Akiyama, K.a, Mizuno, S.a, Hizukuri, Y., Mori, H., Nogi, T., and *Akiyama, Y. |
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2. | Ishii, E., Chiba, S., Hashimoto, N., Kojima, K., Homma, M., Ito, K., Akiyama, Y., and *Mori, H. |
1. | Sakakibara, K., Eiyama, A., Suzuki, S.W., Sakoh-Nakatogawa, M., Okumura, N., Tani, M., Hashimoto, A., Nagumo, S., Kondo-Okamoto, N., Kondo-Kakuta, C., Asai, E., Kirisako, H., Nakatogawa, H., Kuge, O., Takao, T., Ohsumi, Y., and *Okamoto, K. Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recycling. EMBO J. in press (2015) PMID: 26438722 |
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2. | Eiyama, A., and *Okamoto, K. |
1. | K. Shindo, A. Kato, N. Koyanagi, H. Sagara, J. Arii, and *Kawaguchi, Y. Characterization of a chimera herpes simplex virus 1 (HSV-1) in which its Us3 protein kinase gene was replaced with the HSV-2 Us3 gene. J. Virol. 90:457-473 (2015) |
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2. | Z. Liu, A. Kato, M. Oyama, H. Kozuka-Hata, J. Arii, and *Kawaguchi, Y. Role of Host Cell p32 in Herpes Simplex Virus 1 De-envelopment During Viral Nuclear Egress. J. Virol. 89: 8982-8998.(2015) |
3. | Y. Hirohata, J. Arii, Z. Liu, K. Shindo, M. Oyama, H. Kozuka-Hata, H. Sagara, A. Kato, and *Kawaguchi, Y. Herpes simplex virus 1 recruits CD98 heavy chain and β1 integrin to the nuclear membrane for viral de-envelopment. J. Virol. 89: 7799-7812.(2015) |
1. | *Inobe, T. and Genmei, R. Inhibition of the 26S proteasome by peptide mimics of the coiled-coil region of its ATPase subunits. Biochem. Biophys. Res. Commun. 468, 143-150 (2015) |
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2. | *Inobe, T., Nozaki, M. and Nukina, N. Artificial regulation of p53 function by modulating its assembly. Biochem. Biophys. Res. Commun. 467, 322-327 (2015) |
3. | Takahashi, K., Matouschek, A. and *Inobe, T. Regulation of proteasomal degradation modulating an unstructured proteasomal initiation region of a substrate. ACS Chem. Biol.10, 2537–2543 (2015) |
4. | Inobe, T. and Genmei, R. N-terminal coiled-coil structure of ATPase subunits of 26S proteasome is crucial for proteasome function. PLoS ONE, 10, e0134056 (2015) |
1. | Satoh, T., Ohba, A., Liu, Z., Inagaki, T., and *Satoh, A.K. EMC is essential for biosynthesis of rhodopsin and other multipass membrane proteins in Drosophila melanogaster. eLife, 4, e06306 (2015) |
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2. | 佐藤卓至・佐藤明子 EMCは複数膜貫通ドメイン膜タンパク質の合成に特異的な因子である. 生化学87, 870781. (2015) |
1. | Kadowaki, H., Nagai, A., Maruyama, T., Takami, Y., Satrimafitrah, P., Kato, H., Honda, A., Hatta, T., Natsume, T., Sato, T., Kai, H., Ichijo, H. and *Nishitoh, H. |
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1. | Yoshihisa, T. Nucleocytoplasmic shuttling of tRNAs and implication of the cytosolic Hsp70 system in tRNA import. Nucleus, 6(5):339-343 (2015) |
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2. | Takano, T., Kajita, T., Mochizuki, M., Endo, T., and *Yoshihisa, T. |
1. | Kotani Y, *Morito D, Yamazaki S, Ogino K, Kawakami K, Takashima S, *Hirata H, *Nagata K. Neuromuscular regulation in zebrafish by a large AAA+ ATPase/ubiquitin ligase, mysterin/RNF213. Sci Rep. 2015 Nov 4;5:16161 |
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2. | Morito D, *Nagata K. 【Review】Pathogenic Hijacking of ER-Associated Degradation: Is ERAD Flexible? Mol Cell. 2015 Aug 6;59(3):335-44 |
3. | Kirstein-Miles J#*, Morito D#, Kakihana T#, Sugihara M, Minnen A, Hipp MS, Nussbaum‐Krammer C, *Hartl FU, *Nagata K, and *Morimoto RI |
1. | Ishimoto, T., Fujiwara, K., Niwa, T., *Taguchi, H. |
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1. | Machida K, Mikami S, Masutani M, Mishima K, Kobayashi T, and *Imataka H |
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2. | Fukao A, Mishima Y, Takizawa N, Oka S, Imataka H, Pelletier J, Sonenberg N, Thoma C, and Fujiwara T MicroRNAs Trigger Dissociation of eIF4AI and eIF4AII from Target mRNAs in Humans Mol.Cell 56: 79-89 (2014) doi: 10.1016/j.molcel.2014.09.005 |
3. | Kobayashi T, Machida K, and *Imataka H Human cell extract-derived cell-free systems for virus synthesis. In: Alexandrov,K. and Johnston,W.A. (Eds.), Methods in Molecular Biology 1118, Cell-free protein synthesis: Methods and Protocols. Humana Press, pp149-156 (2014) doi: 10.1007/978-1-62703-782-2_9 |
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Fukaya, T.#, Iwakawa, HO.#, Tomari, Y. |
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2. | Kojima, R.†, Okumura, M.†, Masui, S., Kanemura, S., Inoue, M., Saiki, M., Yamaguchi, H., Hikima, T., Suzuki, M., Akiyama, S. and Inaba, K.* (†These authors contributed equally to this work.) |
1. | Okumura, M.*, Kadokura, H., Hashimoto, S., Yutani, K., Kanemura, S., Hikima, T., Hidaka, Y., Ito, L., Shiba, K., Masui, S., Imai, D., Imaoka, S., Yamaguchi, H.* and Inaba, K.* |
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1. | Miyagawa, K, Ishiwata-Kimata, Y., Kohno, K., and *Kimata, Y. |
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1. | Jiang, L., Hara-Kuge, S., Yamashita, S., and Fujiki, Y. |
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2. | Tamura, S., Matsumoto, N., Takeba, R., and Fujiki, Y. |
3. | Miyauchi-Nanri, Y., Mukai, S., Kuroda, K., and Fujiki, Y. |
4. | Fujiki, Y., Okumoto, K., Mukai, S., Honsho, M., and Tamura, S. |
5. | Yamashita, S., Abe, K., Tatemichi, Y., and Fujiki, Y. |
6. | Noguchi, M., Honsho, M., Abe, Y., Toyama, R., Niwa, H., Sato, Y., Ghaedi, K., Rahmanifar, A., Shafeghati, Y., and Fujiki, Y. |
7. | Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S. |
8. | Fujiki, Y., Itoyama, A., Abe, Y., and Honsho, M. |
9. | Okumoto, K., Noda, H., and Fujiki, Y. |
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2. | Kumazaki, K†., Chiba, S†., Takemoto, M., Furukawa, A., Nishiyama, K.I., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., *Tsukazaki, T. and *Nureki, O. (†These authors contributed equally to this work) |
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2. | Kumazaki, K†., Chiba, S†., Takemoto, M., Furukawa, A., Nishiyama, K.I., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., *Tsukazaki, T. and *Nureki, O. |
3. | *Mio K, Tsukazaki T, Mori H, Kawata M, Moriya T, Sasaki Y, Ishitani R, Ito K, *Nureki O and *Sato C. |
1. | Ohta, S., Kawai-Noma, S., Kitamura, A., Pack, C-G., *Kinjo, M. & *Taguchi, H. |
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2. | Biswas, S., Kinbara, K., Niwa, T., *Taguchi, H., Ishii, N., Watanabe, S., Miyata, K., Kataoka, K. and *Aida, T. |
3. | *Nojima, T., Konno, H., Kodera, N., Seio, K., *Taguchi, H. and Yoshida, M. |
4. | Nojima, T., Ikegami, T., *Taguchi, H. and *Yoshida, M. |
5. | Niwa, T., Kanamori, T., *Ueda, T., and *Taguchi, H. |
6. | Tsuji, T., Kawai-Noma, S., Pack, C.-G., Terajima, H., Yajima, J., Nishizaka, T., Kinjo, M., and *Taguchi, H. |
7. | *Takemoto K, Niwa T, Taguchi, H. |
8. | Kawai-Noma, S., Pack, C.-G., Kojidani, T., Asakawa, H., Hiraoka, Y., Kinjo, M., Haraguchi, T., *Taguchi, H., and Hirata, A. |
9. | Fujiwara, K., Ishihama, Y., Nakahigashi, K., Soga, T., and *Taguchi, H. |
10. | *Taguchi, H., and Kawai-Noma, S. |
11. | Kawai-Noma, S., Pack, C.-G., Tsuji, T., Kinjo, M., and *Taguchi, H. |
12. | Niwa, T., Ying, B.-W., Saito, K., Jin, W. Z., Takada, S., *Ueda, T., and *Taguchi, H. |
13. | Koike-Takeshita, A., Yoshida, M., and *Taguchi, H. |
14. | Ying, B.-W. *Taguchi, H., *Ueda, T. |
15. | Ying, B.-W. Taguchi, H., Kondo, M., *Ueda, T. |
16. | Ueno, T.#, Taguchi, H.#, Tadakuma, H., *Yoshida, M., and *Funatsu, T. [# equally contributed] |
17. | Taguchi, H., Ueno, T., Tadakuma, H., *Yoshida, M., and *Funatsu, T. |
1. | Masutani, M., Machida, K., Kobayashi, T., Yokoyama, S. and *Imataka, H. |
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2. | Machida, K., Masutani, M., Kobayashi, T., Mikami, S., Nishino, Y., Miyazawa A. and *Imataka, H. |
3. | Masutani, M., Sonenberg, N., Yokoyama, S. and *Imataka, H. |
1. | Kotani T., Akabane S., Takeyasu K., Ueda T. and *Takeuchi N. |
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2. | Suematsu T., Yokobori SI., Morita H., Yoshinari S., Ueda T., Kita K., *Takeuchi N., Watanabe YI. |
3. | Akama K., Christian BE., Jones CN., *Takeuchi N., and Spremulli LL. |
4. | Tsuboi M., Morita H.,Nozaki Y.,Akama K., Ueda T.,Ito K.,Nierhaus KH., and *Takeuchi N. |
1. | Kuroha, K., Ando, K., Nakagawa, R., *Inada, T. |
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2. | Tsuboi, T., Kuroha, K., Kudo, K., Makino S., Inoue, E., Kashima, I. and *Inada, T. |
3. | Izawa, T., Tsuboi, T., Kuroha, K., Inada, T., Nishikawa, SI., *Endo, T. |
4. | Brandman, O., Ornstein, JS., Wong, D., Larson, A., Williams, C.C, Li, G.W., Zhou, S., King, D., Shen, P.S, Weibezahn, J., Dunn, J.G, Rouskin, S., Inada, T., Frost, A., *Weissman, JS. |
5. | Kobayashi, K., Kikuno, I., Kuroha, K., Saito, K., Ito, K., Ishitani, R., Inada, T. and *Nureki, O. |
6. | Kuroha, K., Akamatsu, M., Dimitrova, L., Ito, T., Kato, Y. Shirahige, K. and *Inada, T. |
7. | Kuroha, K., Tatematsu, T. and *Inada, T. |
8. | Kuroha, K., Dimitrova, L., Tatematsu, T. and *Inada, T. |
9. | Nukazuka, A., Fujisawa, H., Inada, T., Oda, Y., *Takagi, S. |
10. | Ito-Harashima, S., Kuroha, K., Tatematsu, T. and *Inada, T. |
11. | *Inada, T. and Aiba, H. |
12. | Kawamoto, H., Morita, T., Shimizu, A., Inada, T., *Aiba, H. |
1. | Chujo, T., Ohira, T., Sakaguchi, Y., Goshima, N., Nomura, N., Nagao, A. and *Suzuki, T. |
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2. | Suzuki, T., Nagao, A. and *Suzuki, T. |
3. | Kato, M., Araiso, Y., Noma, A., Nagao, A., Suzuki, T., Ishitani, R. and *Nureki, O. |
4. | Nagao, A., Suzuki, T., Katoh, T., Sakaguchi, Y. and *Suzuki, T. |
1. | Iwakawa, HO., *Tomari, Y. |
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2. | Endo, Y., *Iwakawa, HO., *Tomari, Y. |
3. | Iwakawa, HO., Tajima, Y., Taniguchi, T., Kaido, M., Mise, K., Tomari, Y., Taniguchi, H., *Okuno, T. |
1. | Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., *Saido, T.C. |
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2. | Suzuki, G., *Tanaka, M. |
3. | Suzuki, G. Shimazu, N., and *Tanaka, M. |
4. | *Tanaka, M. |
5. | Foo, C.K., Ohhashi, Y., Kelly, M.J., Tanaka, M., and *Weissman, J.S. |
6. | Ohhashi, Y., Ito, K., Toyama, B.H., Weissman, J.S., and *Tanaka, M. |
7. | Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., and *Tanaka, M. |
8. | Krzewska, J., Tanaka, M., Burston, S.G., and *Melki, R. |
9. | Tanaka, M., Collins, S.R., Toyama, B.H., and *Weissman, J.S. |
10. | Tanaka, M., Chien, P., Yonekura, K., *Weissman, J.S. |
11. | Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N.R., Doi, H., Kurosawa, M., Nekooki, M., and *Nukina, N. |
1. | Sato, Y., Kojima, R., Okumura, M., Hagiwara, M., Masui, S., Maegawa, K., Saiki, M., Horibe, T., Suzuki, M. and *Inaba, K. |
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2. | Vavassori, S., Cortini, M., Masui, S. Sannino, S., Anelli, T., Caserta, I. R., Fagioli, C., Fornili, A., Mossuto, M. F., Degano, M, Inaba, K. and *Sitia, R. |
3. | Sato, Y. and *Inaba, K. |
4. | Araki, K., and *Inaba, K. |
5. | Masui, S., Vavassori, S., Fagioli, C., Sitia, R., and *Inaba, K. |
6. | Hagiwara, M., Maegawa, K., Suzuki, M., Ushioda, R., Araki, K., Matsumoto, Y., Hoseki, J., *Nagata, K., and *Inaba, K. |
7. | *Inaba, K., Masui, S., Iida, H., Vavassori, S., Sitia, R., and Suzuki, M. |
8. | *Inaba, K., Murakami, S., Nakagawa, A., Iida, H., Kinjo, H., Ito, K., and Suzuki, M. |
9. | *Inaba, K., Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K., and *Ito, K. |
10. | Inaba, K., Takahashi, Y.-H., *Ito, K., and *Hayashi, S. |
1. | *Kadokura, H., Saito, M., Tsuru, A., Hosoda, A., Iwawaki, T., Inaba, K., and *Kohno, K. |
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2. | Chng, S.S., Xue, M., Garner, R.A., Kadokura, H., Boyd, D., Beckwith, J., and *Kahne, D. |
3. | Yanagitani, K., Kimata, Y., Kadokura, H., and *Kohno, K. |
4. | *Kadokura, H., and *Beckwith, J. |
5. | Kadokura, H., Tian, H., Zander, Bardwell, J.C.A., and *Beckwith, J. |
6. | Kadokura, H., and *Beckwith, J. |
1. | *Kadokura H., Saito, M., Tsuru, A., *Kohno, K.(7人中7番目) |
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2. | Adolph, T.E., Kohno, K., *Blumberg, R.S.(25人中13番目) |
3. | Tsuru, A., Saito, M., Ron, D., *Kohno, K.(10人中10番目) |
4. | Shinya, S., Yanagitani, K., *Kohno, K.(人中6番目) |
5. | Yanagitani, K., Kimata, Y., Kadokura, H. *Kohno, K. |
6. | Promlek, T., Ishiwata-Kimata, Y., Shido, M., Sakuramoto, M., Kohno, K. *Kimata, Y. |
7. | Kimata, Y., *Kohno, K. |
8. | Nakamura, D., Tsuru, A., Imagawa, Y., *Kohno, K.(6人中6番目) |
9. | Yamamoto, Y.H., Kadokura, H., *Kohno, K.(8人中8番目) |
10. | *Iwawaki, T., Akai, R., Yamanaka, S., Kohno, K. |
11. | Yanagitani, K., Imagawa, Y., Iwawaki, T., Hosoda, A., Saito, M., Kimata, Y., *Kohno, K. |
1. | Honsho, M., Asaoku, S., Fukumoto, K., and *Fujiki, Y. |
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2. | Yagita, Y., Hiromasa,T., and *Fujiki, Y. |
3. | Otera, H., and *Fujiki, Y. |
4. | *Fujiki, Y., Yagita, Y., and Matsuzaki, T. |
5. | Itoyama, A., Honsho, M., Abe, Y., Moser, A., Yoshida, Y., and *Fujiki, Y. |
6. | Miyata, N., Okumoto, K., Noguchi, M., Mukai, S., and *Fujiki, Y. |
7. | Yonekawa, S., Furuno, A., Baba, T., Fujiki, Y., Ogasawara, Y., Yamamoto, A., Tagaya, M., and *Tani, K. |
8. | Okumoto, K., Misono, S., Miyata, N., Matsumoto, Y., Mukai, S., and *Fujiki, Y. |
9. | Matsuzaki, T., and *Fujiki, Y. |
10. | Matsumoto, N., Tamura, S., and *Fujiki, Y. |
1. | Su, J. R., Takeda, K., Tamura, S., *Fujiki., Y., and *Miki, K. |
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2. | Tamura, S., Yasutake, S., Matsumoto, N., and *Fujiki, Y. |
3. | Furuki, S., Tamura, S., Matsumoto, N., Miyata, N., Moser, A., Moser, H.W., and *Fujiki, Y. |
1. | *Ito, K. and Chiba, S. |
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2. | Chiba, S., *Ito, K. |
3. | Ito, K., Chadani, Y., Nakamori, K., Chiba, S., Akiyama, Y. and *Abo, Y. |
4. | Saito, A., Hizukuri, Y., Matsuo, E. -i., Chiba, S., Mori, H., Nishimura, O., Ito, K. and *Akiyama, Y. |
5. | Chiba, S., Kanamori, T., Ueda, T., Akiyama, Y., Pogliano, K. and *Ito, K. |
6. | White, R., Chiba, S., Pang, T., Dewey, J. S., Savva, C. G., Holzenburg, A., Pogliano, K. and *Young, R. |
7. | Chiba, S., Lamsa, A. and *Pogliano, K. |
8. | Aung, S., Shum, J., Abanes-De, Mello, A., Broder, D. H., Fredlund-Gutierrez, J., Chiba, S. and *Pogliano, K. |
9. | Chiba, S., Coleman, K. and *Pogliano, K. |
1. | Chadani, Y., Ito, K., Kutsukake, K. and *Abo T. |
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2. | Tsukazaki, T, Mori, H., Echizen, Y., Ishitani, R., Fukai, S., Tanaka, T., Perederina, A., Vassylyev, D. G., Kohno, T., Maturana, A. D., Ito, K., and *Nureki, O. |
3. | Ito, K., Chiba, S. and *Pogliano, K. |
4. | Inaba, K., Murakami, S., Nakagawa, A., Iida, H. Kinjo, M., Ito, K. and *Suzuki, M. |