Laboratory of Molecular Cell Biology, Institute for Molecular and Cellular Regulation, Gunma University
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研究内容

数理解析に基づく生体シグナル伝達システムの統合的理解（数理シグナル）

研究成果

[2020]

  1. Oikawa D, Hatanaka N, Suzuki T, Tokunaga F. Cellular and mathematical analyses of LUBAC involvement in T cell receptor-mediated NF-κB activation pathway. Front. Immunol. in press
  2. Takahashi H, Yamanaka S, Kuwada S, Higaki K, Kido K, Sato Y, Fukai S, Tokunaga F, Sawasaki T. A Human DUB Protein Array for Clarification of Linkage Specificity of Polyubiquitin Chain and Application to Evaluation of Its Inhibitors. Biomedicines 8, 152, (2020)
  3. Kuriyama Y, Shimizu A, Kanai S, Oikawa D, Tokunaga F, Tsukagoshi H, Ishikawa O. The synchronized gene expression of retrotransposons and type I interferon in dermatomyositis. J. Am. Acad. Dermatol. S0190-9622 (20)30916-6, (2020)
  4. Oikawa D, Sato Y, Ito H, Tokunaga F. Linear ubiquitin code: Its writer, erasers, decoders, inhibitors, and implications in disorders. Int. J. Mol. Sci. 21, 3381, (2020)
  5. Oikawa D, Sato Y, Ohtake F, Komakura K, Hanada K, Sugawara K, Terawaki S, Mizukami Y, Phuong HT, Iio K, Obika S, Fukushi M, Irie T, Tsuruta D, Sakamoto S, Tanaka K, Saeki Y, Fukai S, Tokunaga F. Molecular bases for HOIPINs-mediated inhibition of LUBAC and innate immune responses. Commun. Biol. 3, 163, (2020)
  6. Nakayama Y, Tsuji K, Ayaki T, Mori M, Tokunaga F, Ito H. Linear polyubiquitin chain modification of TDP-43-Positive neuronal cytoplasmic inclusions in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 79, 256-265, (2020)
  7. Yamanaka S, Sato Y, Oikawa D, Goto E, Fukai S, Tokunaga F., Takahashi H., Sawasaki T. Subquinocin, a small molecule inhibitor of CYLD and USP-family deubiquitinating enzymes, promotes NF-κB signaling. Biochem Biophys Res Commun. 524, 1-7, (2020)
  8. 及川大輔、伊藤秀文、徳永文稔；直鎖状ユビキチン鎖の神経変性疾患への関与とLUBAC阻害剤の開発、生化学92, 28-34, (2020)
  9. 高橋宏隆、山中聡士、徳永文稔、澤崎達也；ヒト脱ユビキチン化酵素タンパク質アレイの開発とその応用例、生化学92, 64-74, (2020)
  10. 徳永文稔；創薬を見据えた直鎖状ユビキチン鎖生成酵素(LUBAC)阻害剤開発、ファルマシア 56, 26-30, (2020)

[2019]

  1. Uematsu A, Kido K, Takahashi H, Takahashi C, Yanagihara Y, Saeki N, Yoshida S, Maekawa M, Honda M, Kai T, Shimizu K, Higashiyama S, Imai Y, Tokunaga F, Sawasaki T. The E3 ubiquitin ligase MIB2 enhances inflammation by degrading the deubiquitinating enzyme CYLD. J. Biol. Chem. 294, 14135-14138, (2019)
  2. Nakayama Y, Sakamoto S, Tsuji K, Ayaki T, Tokunaga F, Ito H. Identification of linear polyubiquitin chain immunoreactivity in tau pathology of Alzheimer's disease. Neurosci. Lett.703, 53-57, (2019)
  3. Katsuya K, Oikawa D, Iio K, Obika S, Hori Y, Urashima T, Ayukawa K, Tokunaga F. Small-molecule inhibitors of linear ubiquitin chain assembly complex (LUBAC), HOIPINs, suppress NF-κB signaling. Biochem. Biophys. Res. Commun. 509(3), 700-706, (2019)
  4. 徳永文稔.　LUBACを介した直鎖状ユビキチン鎖生成と細胞死　臨床免疫・アレルギー科71(2), 105-113 (2019)

[2018]

  1. Kato K, Nishimasu H, Oikawa D, Hirano S, Hirano H, Kasuya G, Ishitani R, Tokunaga F, Nureki O Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1. Nat Commun. 9(1):4424 (2018).
  2. Oikawa D, Shiota M, Goto E, Komakura K, Wanibuchi H, Tokunaga F. Generation of Rat Monoclonal Antibodies Against a Deubiquitinase, Ovarian Tumor Domain-Containing Protein 1.Monoclon Antib Immunodiagn Immunother. 37(4):180-184 (2018).
  3. Katsuya K, Hori Y, Oikawa D, Yamamoto T, Umetani K, Urashima T, Kinoshita T, Ayukawa K, Tokunaga F, Tamaru M. High-Throughput Screening for Linear Ubiquitin Chain Assembly Complex (LUBAC) Selective Inhibitors Using Homogenous Time-Resolved Fluorescence (HTRF)-Based Assay System. SLAS Discov. 2:2472555218793066 (2018).
  4. Oikawa D, Shiota M, Tokunaga F, Wanibuchi H. Generation of rat monoclonal antibodies specific for DZIP3. Monoclon. Antib. Immunodiagn. Immunother.37(3)157-157 (2018)
  5. Hattori M, Ishikawa O, Oikawa D, Amano H, Yasuda M, Kaira K, Ishida-Yamamoto A, Nakano H, Sawamura D, Terawaki SI, Wakamatsu K, Tokunaga F, Shimizu A. In-frame Val216-Ser217 deletion of KIT in mild piebaldism causes aberrant secretion and SCF response.J. Dermatol. Sci. 91(1) 35-42 (2018)
  6. Kuriyama Y, Hattori M, Mitsui T, Nakano H, Oikawa D, Tokunaga F, Ishikawa O, Shimizu A. Generalized verrucosis caused by various human papillomaviruses in a patient with GATA2 deficiency. J. Dermatol. 45(5), e108-e109 (2018)
  7. 徳永文稔.　脱ユビキチン化酵素(DUB)と疾患　医学のあゆみ267(13),1096-1104 (2018)

[2017]

  1. Shibata Y, Tokunaga F, Goto E, Komatsu G, Gohda J, Saeki Y, Tanaka K, Takahashi H, Sawasaki T, Inoue S, Oshiumi H, Seya T, Nakano H, Tanaka Y, Iwai K, and Inoue JI. HTLV-1 Tax induces formation of the active macromolecular IKK complex by generating Lys63- and Met1-linked hybrid polyubiquitin chains. PLoS Pathogens. 13, e100162 (2017)
  2. Hattori M, Shimizu A, Oikawa D, Kamei K, Kaira K, Ishida-Yamamoto A, Nakano H, Sawamura D, Tokunaga F, Ishikawa O. Endoplasmic reticulum stress in the pathogenesis of pretibial dystrophic epidermolysis bullosa. Br. J. Dermatol. 177(4), e92-e93 (2017)
  3. Yamamotoya T, Nakatsu Y, Matsunaga Y, Fukushima T, Yamazaki H, Kaneko S, Fujishiro M, Kikuchi T, Kushiyama A, Tokunaga F, Asano T, Sakoda H. Reduced SHARPIN and LUBAC formation may contribute to CCl₄- or acetaminophen-induced liver cirrhosis in mice. Int. J. Mol. Sci. 18(2), 326 (2017)
  4. Goto E and Tokunaga F. Decreased linear ubiquitination of NEMO and FADD on apoptosis with caspase-mediated cleavage of HOIP. Biochem. Biophys. Res. Commun. 485(1), 152-159 (2017)

[2016]

  1. Omura H, Oikawa D, Nakane T, Kato M, Ishii R, Ishitani R, Tokunaga F, and Nureki O: Structural and functional analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide. Sci. Rep. 6, 34756 (2016).
  2. Nakazawa S, Oikawa D, Ishi R, Ayaki T, Takahashi H, Takeda H, Ishitani R, Kamei K, Takeyoshi I, Kawakami H, Iwai K, Hatada I, Sawasaki T, Ito H, Nureki O, and Tokunaga F: Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis. (2016) Nat. Commun. 7, 12547.
  3. Saitoh Y, Hamano A, Mochida K, Kakeya A, Uno M, Tsuruyama E, Ichikawa H, Tokunaga F, Utsnomiya A, Watanabe T, and Yamaoka S: A20 targets caspase-8 and FADD to protect HTLV-I infected cells. (2016) Leukemia, 30, 716-727.

[2015]

  1. Kumanomidou T, Nishio K, Takagi K, Nakagawa T, Suzuki A, Yamane T, Tokunaga F, Iwai K, Murakami A, Yoshida Y, Tanaka K, and Mizushima T: The Structural Differences between a Glycoprotein Specific F-box Protein Fbs1 and its Homologous Protein FBG3. (2015) PLoS One, 10, e0140366.
  2. Matsunaga Y, Nakatsu Y, Fukushima T, Okubo H, Iwashita M, Sakoda H, Fujishiro M, Yamamotoya T, Kushiyama A, Takahashi S, Tsuchiya Y, Kamata H, Tokunaga F, Iwai K, and Asano T: 13. LUBAC formation is impaired in the livers of mice with MCD-dependent nonalcoholic steatohepatitis. (2015) Mediators Inflamm., 125380.
  3. Sato Y, Goto E, Shibata Y, Kubota Y, Yamagata A, Goto-Ito S, Kubota K, Inoue J, Takekawa M, Tokunaga F, and Fukai S: Structures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity. (2015) Nat. Struct. Mol. Biol., 22, 222-229.
  4. Kato M, Shimizu A, Yokoyama Y, Kaira K, Shimomura Y, Ishida-Yamamoto A, Kamei K, Tokunaga F, and Ishikawa O: A novel autosomal recessive mutation of DSG4 causes monilethrix through the ER stress response. (2015) Invest. Dermatol., 135, 1253-1260.
  5. Tokunaga F. Ubiquitination-mediated NF-kB regulation in inflammatory response. In: Protein modifications in pathogenic dysregulation of signaling. (Inoue J and Takekawa M, eds.) (2015) Springer International Publishing, Tokyo, 177-196.
  6. 徳永文稔. 直鎖状ユビキチン鎖による炎症制御.(2015) 臨床免疫・アレルギー科,63, 495-501.

[2014]

  1. 徳永文稔. 8番目のユビキチン鎖「直鎖状ユビキチン鎖」の機能と疾患へのかかわり–炎症、免疫応答に重要なNF-kB経路の新しい制御機構-.(2014) 化学と生物,52, 716-718.

[2013]

  1. Kazuki Kato, Ryohei Ishii, Eiji Goto, Ryuichiro Ishitani, Fuminori Tokunaga, and Osamu Nureki: Structural and functional analyses of DNA-sensing and immune activation by human cGAS. (2013) PLoS One, 8 (10), e76983.  
  2. Naonobu Fujita, Eiji Morita, Takashi Itoh, Atsushi Tanaka, Megumi Nakaoka, Yuki Osada, Tetsuo Umemoto, Tatsuya Saitoh, Hitoshi Nakatogawa, Shouhei Kobayashi, Tokuko Hataguchi, Jun-Lin Guan, Kazuhiro Iwai, Fuminori Tokunaga, Kazunobu Saito, Koutaro Ishibashi, Shizuo Akira, Mitsunori Fukuda, Takeshi Noda, and Tamotsu Yoshimori: Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin. (2013) J. Cell Biol. 203 (1), 115-128.
  3. Fuminori Tokunaga: Linear ubiquitination-mediated NF-κB regulation and its related disorders. (2013) J. Biochem. 154 (4), 313-323.
  4. 櫻井宏明、徳永文稔；次世代シグナル伝達研究　-先駆的基礎解析と臨床・創薬への展開-　(2013)生化学, 85(6), 403-404.
  5. 徳永文稔；直鎖状ユビキチン化を介したNF-κB制御機構と疾患　(2013)生化学, 85(6), 414-422.

[2012]

  1. Naguro I, Umeda T, Kobayashi Y, Maruyama J, Hattori K, Shimizu Y, Kataoka K, Kim-Mitsuyama S, Uchida S, Vandewalle A, Noguchi T, Nishitoh H, Matsuzawa A, Takeda K, Ichijo H: ASK3 responds to osmotic stress and regulates blood pressure by suppressing WNK1-SPAK/OSR1 signaling in the kidney.(2012) Nat Commun., 3, 1285.
  2. Fuminori Tokunaga*, Hiroshi Nishimasu*, Ryuichiro Ishitani, Eiji Goto, Takuya Noguchi, Kazuhiro Mio, Kiyoko Kamei, Averil Ma, Kazuhiro Iwai, and Osamu Nureki: Specific recognition of linear polyubiquitin by A20 zinc finger 7 is involved in NF-κB regulation. (2012) EMBO J. 31 (19), 3856-3870, (*; equal contribution).（詳細はこちら）
  3. Fuminori Tokunaga and Kazuhiro Iwai: Linear ubiquitination: A novel NF-kB regulatory mechanism for inflammatory and immune responses by the LUBAC ubiquitin ligase complex. (2012) Endocrine J., 59 (8), 641-652.
  4. Tobias Kensche*, Fuminori Tokunaga*, Fumiyo Ikeda, Eiji Goto, Kazuhiro Iwai, and Ivan Dikic: Analysis of NF-κB essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-κB. (2012) J. Biol. Chem., 287 (28), 23626-23634, (*; equal contribution).
  5. Hirokazu Yagi, Kazuhiro Ishimoto, Takeshi Hiromoto, Hiroaki Fujita, Tsunehiro Mizushima, Yoshinori Uekusa, Maho Yagi-Utsumi, Eiji Kurimoto, Masanori Noda, Susumu Uchiyama, Fuminori Tokunaga, Kazuhiro Iwai, and Koichi Kato: Non-canonical UBA–UBL interaction mediates formation of linear ubiquitin chain assembly complex. (2012) EMBO Rep., 13 (5), 462-468.
  6. Fuminori Tokunaga and Kazuhiro Iwai: LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses. (2012) Microbes Infect., 14 (7-8), 563-572.
  7. Yoshinori Uekusa, Syunsuke Miura, Hiroaki Sasakawa, Eiji Kurimoto, Eri Sakata, Serve Oliver, Hirokazu Yagi, Fuminori Tokunaga, Kazuhiro Iwai, and Koichi Kato; Backbone and side chain 1H, 13C, and 15N assignments of ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex. Biomol. NMR Assign., 6 (2), 177-180 (2012)
  8. Masato Tomonaga, Nobuyuki Hashimoto, Fuminori Tokunaga, Megumi Onishi, Akira Myoui, Hideki Yoshikawa, and Kazuhiro Iwai; Activation of nuclear factor-kappa B by linear ubiquitin chain assembly complex contributes to lung metastasis of osteosarcoma cells. (2012) Int. J. Oncol. 40 (2), 409-417.
  9. Mizuho Kajikawa, Pai-Chi Li, Eiji Goto, Naoyuki Miyashita, Masami Aoki-Kawasumi, Mari Mito-Yoshida, Mika Ikegaya, Yuji Sugita, and Satoshi Ishido; The intramembrane region of Kaposi’s sarcoma-associated Herpesvirus modulator of immune recognition 2 contributes to B7-2 downregulation. (2012) J. Virol. 86 (9), 5286-5296.
  10. Hidetaka Tanno, Teppei Yamaguchi, Eiji Goto, Satoshi Ishido, and Masayuki Komada; The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. (2012) Mol. Biol. Cell 23 (7), 1343-1353.
  11. 徳永文稔; NF-κB経路の多様なポリユビキチン鎖による制御と疾患　(2012) 実験医学増刊号,30(5), 716-723.

[2011]

  1. Fuminori Tokunaga, Tomoko Nakagawa, Masaki Nakahara, Yasushi Saeki, Masami Taniguchi, Shin-ichi Sakata, Keiji Tanaka, Hiroyasu Nakano, and Kazuhiro Iwai; Sharpin is a component of the NF-κB activating linear ubiquitin assembly complex. (2011) Nature, 471, 633-641. [http://www.ncbi.nlm.nih.gov/pubmed/21455180]
  2. Fumiyo Ikeda, Yonathan Lissanu Deribe, Sigrid S. Skånland, Benjamin Stieglitz, Caroline Grabbe, Sjoerd van WijK, Mirita Franz-Wachtel, Panchali Goswami, Vanja Nagy, Janos Terzic, Fuminori Tokunaga, Ariadne Androulidaki, Tomoko Nakagawa, Manolis Pasparakis, Kazuhiro Iwai, John P. Sundberg, Liliana Schaefer, Boris Macek, Katrin Rittinger, and Ivan Dikic; SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis. (2011) Nature, 471, 637-641. [http://www.ncbi.nlm.nih.gov/pubmed/21455181]
  3. Kyung-Soo Inn, Michaela U. Gack, Fuminori Tokunaga, Mude Shi, Lai-Yee Wong, Kazuhiro Iwai, and Jae U. Jung; Linear ubiquitin assembly complex negatively regulates RIG-I- and TRIM25-mediated type I interferon induction. (2011) Mol. Cell, 41, 354-365. [http://www.ncbi.nlm.nih.gov/pubmed/21292167]
  4. 徳永文稔、岩井一宏; 新規直鎖状ポリユビキチン鎖生成によるNF-κBシグナル制御　(2011) 実験医学,　 29(12), 2001-2006.

[2010]

  1. Taichi Kumanomidou, Tomomi Nakagawa, Tsunehiro Mizushima, Atsuo Suzoki, Fuminori Tokunaga, Kazuhiro Iwai, Yukiko Yoshida, Keiji Tanaka, and Takashi Yamane; Crystallization and preliminary X-ray characterization of the Skp1-Fbg3 complex. (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 66, 95-98. [http://www.ncbi.nlm.nih.gov/pubmed/20057081]
  2. 徳永文稔、岩井一宏;　ユビキチン修飾系によるNF-κBシグナル伝達制御：新規直鎖状ポリユビキチン鎖形成を介するNF-κB制御機構の発見　(2010) 細胞工学,　 29(12), 1224-1230.
  3. 徳永文稔；ユビキチンープロテアソーム系の多彩な生理機能と疾患への関与　(2010) BIO Clinica 25(12), 1092-1097.

[2009]

  1. Fuminori Tokunaga, Shin-ichi Sakata, Yasushi Saeki, Yoshinori Satomi, Takayoshi Kirisako, Kiyoko Kamei, Tomoko Nakagawa, Michiko Kato, Shigeo Murata, Shoji Yamaoka, Masahiro Yamamoto, Shizuo Akira, Toshifumi Takao, Keiji Tanaka, Kazuiro Iwai; Involvement of linear polyubiquitylation of NEMO in NF-κB activation. (2009) Nature Cell Biol. 11, 123-132. [http://www.ncbi.nlm.nih.gov/pubmed/19136968]
  2. Kazuhiro Iwai and Fuminori Tokunaga; Linear polyubiquitination: a new regulator of NF-κB activation. (2009) EMBO Rep. 10, 706-713.
  3. 岩井一宏、坂田真一、中川朋子、徳永文稔；アレルギーやガンに関わるNF-κBの新しい活性化機構の発見：新規ユビキチン修飾、直鎖状ポリユビキチン化によるNF-κB活性化(2009)化学と生物　47,　602-604.
  4. 徳永文稔、岩井一宏;　NEMOの直鎖状ポリユビキチン化修飾によるNF-κB活性化 (2009) 蛋白質核酸酵素 54, 635-642.

[2008以前]

  1. Yasuhiro Miyauchi, Michiko Kato, Fuminori Tokunaga, Kazuhiro Iwai; The COP9/signalosome increases the efficiency of von Hippel-Lindau protein ubiquitin ligase-mediated hypoxia-inducible factor-alpha ubiquitination. (2008) J. Biol. Chem. 283, 16622-16631. [http://www.ncbi.nlm.nih.gov/pubmed/18424433]
  2. Daisuke Morito, Kazuyoshi Hirao, Yukako Oda, Nobuko Hosokawa, Fuminori Tokunaga, Douglas M. Cyr, Keiji Tanaka, Kazuhiro Iwai, and Kazuhiro Nagata; gp78 cooperates with RMA1 in ER-associated degradation of CFTRDF508. (2008) Mol. Biol. Cell 19, 1328-1336. [http://www.ncbi.nlm.nih.gov/pubmed/18216283]
  3. Yukari Zenke-Kawasaki, Yoshihiro Dohi, Yasutake Katoh, Tsuyoshi Ikura, Masae Ikura, Toshimasa Asahara, Fuminori Tokunaga, Kazuhiro Iwai, and Kazuhiko Igarashi; Heme induces ubiquitination and degradation of the transcription factor Bach 1. (2007) Mol. Cell. Biol. 27, 6962-6971. [http://www.ncbi.nlm.nih.gov/pubmed/17682061]
  4. Munehiro Nakamura, Fuminori Tokunaga, Shin-ichi Sakata, and Kazuhiro Iwai; Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex. (2006) Biochem. Biophys. Res. Commun. 351, 340-347. [http://www.ncbi.nlm.nih.gov/pubmed/17069764]
  5. Takayoshi Kirisako, Kiyoko Kamei, Shigeo Murata, Michiko Kato, Hiromi Fukumoto, Masato Kanie, Soichi Sano, Fuminori Tokunaga, Keiji Tanaka, and Kazuhiro Iwai; A ubiquitin ligase complex assembles linear polyubiquitin chain. (2006) EMBO J. 25, 4877-4887. [http://www.ncbi.nlm.nih.gov/pubmed/17006537]
  6. Hiroko Tsuda, Fuminori Tokunaga, Hiroshi Nagamitsu, and Takehiko Koide; Characterization of endoplasmic reticulum-associated degradation of a protein S mutant identified in a family of quantitative protein S deficiency. (2006) Thromb. Res. 117, 323-331. [http://www.ncbi.nlm.nih.gov/pubmed/15893367]
  7. Haruto Ishikawa, Michiko Kato, Hiroshi Hori, Koichiro Ishimori, Takayoshi Kirisako, Fuminori Tokunaga, and Kazuhiro Iwai; Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. (2005) Mol. Cell 19, 171-181. [http://www.ncbi.nlm.nih.gov/pubmed/16039587]
  8. Yukiko Yoshida, Fuminori Tokunaga, Tomoki Chiba, Kazuhiro Iwai, Keiji Tanaka, and Tadashi Tai; Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. (2003) J. Biol. Chem. 278, 43877-43884. [http://www.ncbi.nlm.nih.gov/pubmed/12939278]
  9. Koji Yamanaka, Hartuto Ishikawa, Yuzuru Megumi, Fuminori Tokunaga, Masato Kanie, Tracy A. Rouault, Isao Morishima, Nagahiro Minato, Koichiro Ishimori, and Kazuhiro Iwai; Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2 (2003) Nature Cell Biol. 5, 336-340. [http://www.ncbi.nlm.nih.gov/pubmed/12629548]
  10. Fuminori Tokunaga, Kazuya Hara, and Takehiko Koide; N-linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant (2003) Arch. Biochem. Biophys. 411, 235-243. [http://www.ncbi.nlm.nih.gov/pubmed/12623072]
  11. Tsukasa Osaki, Nozomu Okino, Fuminori Tokunaga, Sadaaki Iwanaga, and Shun-ichiro Kawabata; Proline-rich cell surface antigens of horseshoe crab hemocytes are substrates for protein cross-linking with a clotting protein coagulin (2002) J. Biol. Chem. 277, 40084-40090. [http://www.ncbi.nlm.nih.gov/pubmed/12189150]
  12. Yukiko Yoshida, Tomoki Chiba, Fuminori Tokunaga, Hiroshi Kawasaki, Kazuhiro Iwai, Toshiaki Suzuki, Yukishige Ito, Koji Matsuoka, Minoru Yoshida, Keiji Tanaka, and Tadashi Tai; E3 ubiquitin ligase that recognizes sugar chains (2002) Nature 418, 438-442.[ http://www.ncbi.nlm.nih.gov/pubmed/12140560]
  13. Fuminori Tokunaga, Charles Brostrom, Takehiko Koide, and Peter Arvan: Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I (2000) J. Biol. Chem. 275, 40757-40764.[ http://www.ncbi.nlm.nih.gov/pubmed/10984471]
  14. Fuminori Tokunaga, Susumu Takeuchi, Satoshi Omura, Peter Arvan, and Takehiko Koide; Secretion, g-carboxylation, and endoplasmic reticulum-associated degradation of chimeras mutually exchanged Gla domain between human protein C and prothrombin. (2000) Thromb. Res. 99, 511-521. [http://www.ncbi.nlm.nih.gov/pubmed/10973682]
  15. Shinichi Kondo, Fuminori Tokunaga, Seiji Kawano, Yoichi Oono, Shunichi Kumagai, and Takehiko Koide; Factor XII Tenri, A novel cross-reacting material negative factor XII deficiency, occurs through a proteasome-mediated degradation. (1999) Blood 93, 4300-4308. [http://www.ncbi.nlm.nih.gov/pubmed/10361128]
  16. Hiroko Shirotani, Fuminori Tokunaga, and Takehiko Koide; Cellular and functional characterization of three recombinant antithrombin mutants that caused pleiotropic effects-type deficiency. (1999) J. Biochem. 125, 253-262.[http://www.ncbi.nlm.nih.gov/pubmed/9990121]
  17. Fuminori Tokunaga and Sadaaki Iwanaga; Proteases activating factor V. (1998) In: Enzymes from Snake Venom (G. S. Bailey ed.) Alaken Inc., Fort Collins, Colorado, pp. 209-225.
  18. Fuminori Tokunaga, Hiroko Shirotani, Kazuya Hara, Daisuke Kozuki, Satoshi Omura, and Takehiko Koide; Intracellular degradation of secretion defect-type mutants of antithrombin is inhibited by proteasomal inhibitors. (1997) FEBS Lett. 412, 65-69. [http://www.ncbi.nlm.nih.gov/pubmed/9257691]
  19. Takehiko Koide, Hiroko Shirotani, and Fuminori Tokunaga; Analysis of intracellular mechanism of antithrombin deficiency and characterization of recombinant mutants. (1997) In: Chemistry and Biology of Serpins. (F.C. Church, ed.) Springer-Verlag, New York, pp. 263-264.
  20. Shun-ichiro Kawabata, Fuminori Tokunaga, Yoshie Kugi, Shiho Moritoma, Yoshiki Miura, Michimasa Hirata, and Sadaaki Iwanaga; Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity. (1996) FEBS Lett. 398, 146-150. [http://www.ncbi.nlm.nih.gov/pubmed/8977095]
  21. Fuminori Tokunaga, Toshiro Tsukamoto, and Takehiko Koide; Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the g-carboxyglutamic acid domain (1996) J. Biochem. 120, 360-368.[http://www.ncbi.nlm.nih.gov/pubmed/8889822]
  22. Shinichi Kondo, Fuminori Tokunaga, Kazuomi Kario, Takefumi Matsuo, and Takehiko Koide; Molecular and cellular basis for type I heparin cofactor II deficiency (heparin cofactor II Awaji) (1996) Blood 87, 1006-1012. [http://www.ncbi.nlm.nih.gov/pubmed/8562924]
  23. Takehiko Koide, Fuminori Tokunaga, and Sadao Wakabayashi: Quality Control of Protein C: Protein C Synthesized in the Presence of Warfarin is Selectively Degraded in the Endoplasmic Reticulum: (1996) Pol. J. Pharmacol. 48, 203-207.
  24. Tatsushi Muta, Noriaki Seki, Yoshie Takaki, Ryuji Hashimoto, Toshio Oda, Atsufumi Iwanaga, Fuminori Tokunaga, Daisuke Iwaki, and Sadaaki Iwanaga; A new heterodimeric serine protease zymogen sensitive to (1→3)-b-glucan. (1996) In: Intracellular Protein Catabolism (Suzuki K. and Bond J., eds.) pp. 79-85, Plenum Press, New York.
  25. Fuminori Tokunaga, Sadao Wakabayashi, and Takehiko Koide; Endoplasmic reticulum-associated degradation of protein C precursor synthesized in the presence of warfarin (1996) In: Blood Coagulation, Fibrinolysis, and Platelets (Davie E.W. and Kakishita E., eds.) pp. 205-208, Springer-Verlag, Tokyo.
  26. Shinichi Kondo, Fuminori Tokunaga, Kazuomi Kario, Takefumi Matsuo, and Takehiko Koide; Heparin cofactor II Awaji: A type I deficiency caused by one base insertion after the codon for Asp88 (1996) In: Blood Coagulation, Fibrinolysis, and Platelets (Davie E.W. and Kakishita E., eds.) pp. 209-212, Springer-Verlag, Tokyo.
  27. Runzhou Ni, Yumiko Tomita, Fuminori Tokunaga, Jake T. Liang, Chiseko Noda, Akira Ichihara, and Keiji Tanaka; Molecular cloning of two types of cDNA encoding subunit RC6-I of rat proteasomes (1995) Biochim. Biophys. Acta 1264, 45-52. [http://www.ncbi.nlm.nih.gov/pubmed/7578256]
  28. Fuminori Tokunaga, Sadao Wakabayashi and Takehiko Koide; Warfarin causes the degradation of protein C precursor in the endoplasmic reticulum (1995) Biochemistry 34, 1163-1170. [http://www.ncbi.nlm.nih.gov/pubmed/7827066]
  29. Tatsushi Muta, Noriaki Seki, Yoshie Takaki, Ryuji Hashimoto, Toshio Oda, Atsufumi Iwanaga, Fuminori Tokunaga, and Sadaaki Iwanaga; Purified horseshoe crab factor G: Reconstitution and characterization of the (1→3)-b-D-glucan-sensitive serine protease cascade (1995) J. Biol. Chem. 270, 892-897. [http://www.ncbi.nlm.nih.gov/pubmed/7822328]
  30. Fuminori Tokunaga, Tamami Goto, Sadao Wakabayashi, and Takehiko Koide; Amino acid sequence of porcine antithrombin III (1994) J. Biochem. 116, 1164-1170. [http://www.ncbi.nlm.nih.gov/pubmed/7896748]
  31. Fuminori Tokunaga, Tamami Goto, Takehiko Koide, Yasuko Murakami, Shin-ichi Hayashi, Tomohiro Tamura, Keiji Tanaka, and Akira Ichihara; ATP-and antizyme-dependent endoproteolysis of ornithine decarboxylase to oligopeptides by the 26S proteasome (1994) J. Biol. Chem. 269, 17382-17385. [http://www.ncbi.nlm.nih.gov/pubmed/8021237]
  32. Tetsuro Yoshimura, Keiichi Kameyama, Toshio Takagi, Atushi Ikai, Fuminori Tokunaga, Takehiko Koide, Nobuyuki Takahashi, Tomohiro Tamura, Zdenka Cejka, Wolfgang Baumeister, Keiji Tanaka, and Akira Ichihara; Molecular characterization of the "26S" proteasome complex from rat liver (1993) J. Struct. Biol. 111, 200-211. [http://www.ncbi.nlm.nih.gov/pubmed/8003381]
  33. Chihiro Nishimura, Tomohiro Tamura, Hiroshi Akioka, Fuminori Tokunaga, Keiji Tanaka, and Akira Ichihara; cDNA cloning of rat proteasome subunit RC10-II, assumed to be responsible for trypsin-like catalytic activity (1993) FEBS Lett. 336, 462-466. [http://www.ncbi.nlm.nih.gov/pubmed/8282111]
  34. Chihiro Nishimura, Tomohiro Tamura, Fuminori Tokunaga, Keiji Tanaka, Akira Ichihara; cDNA cloning of rat proteasome subunit RC7-I, a homologue of yeast PRE1 essential for chymotrypsin-like activity (1993) FEBS Lett. 332, 52-56. [http://www.ncbi.nlm.nih.gov/pubmed/8405448]
  35. Fuminori Tokunaga, Tatsushi Muta, Sadaaki Iwanaga, Akitada Ichinose, Earl W. Davie, Kei-ichi Kuma, and Takashi Miyata; Limulus hemocyte transglutaminase: cDNA cloning, amino acid sequence, and tissue localization (1993) J. Biol. Chem. 268, 262-268. [http://www.ncbi.nlm.nih.gov/pubmed/8093243]
  36. Fuminori Tokunaga, Masashi Yamada, Toshiyuki Miyata, You-Lin Ding, Masuyo Hiranaga-Kawabata, Tatsushi Muta, Sadaaki Iwanaga, Akitada Ichinose, and Earl W. Davie; Limulus hemocyte transglutaminase: Its purification, characterization, and identification of the intracellular substrates (1993) J. Biol. Chem. 268, 252-261.［http://www.ncbi.nlm.nih.gov/pubmed/8093242］
  37. Fuminori Tokunaga and Sadaaki Iwanaga; Horseshoe crab transglutaminase (1993) In: Methods Enzymol. (L. Lorand and K.G. Mann eds.) Academic Press vol. 223, pp. 378-388.
  38. Tatsushi Muta, Fuminori Tokunaga, Takanori Nakamura, Takashi Morita, and Sadaaki Iwanaga; Limulus clotting factor C: Lipopolysaccharide-sensitive serine protease zymogen (1993) In: Methods Enzymol. (L. Lorand and K.G. Mann eds.) Academic Press vol. 223, pp. 336-345.
  39. Fuminori Tokunaga, Sadao Wakabayashi, Hirokazu Sato, Masaaki Arakawa, Hironobu Tawaraya, and Takehiko Koide; Identification of one base deletion in exon IX that causes a type I deficiency of protein C (1992) Thromb. Res. 68, 417-423. [http://www.ncbi.nlm.nih.gov/pubmed/1290170]
  40. Yoshiki Miura, Fuminori Tokunaga, Toshiyuki Miyata, Matsuko Moriyasu, Katsutoshi Yoshikawa, and Sadaaki Iwanaga; Preparation and properties of monoclonal antibodies against lipopolysaccharide-sensitive serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes (1992) J. Biochem. 112, 476-481. [http://www.ncbi.nlm.nih.gov/pubmed/1283392]
  41. Masashi Aki, Tomohiro Tamura, Fuminori Tokunaga, Sadaaki Iwanaga, Yoshihiro Kawamura, Naoko Shimbara, Susumu Kagawa, Keiji Tanaka, and Akira Ichihara; cDNA cloning of rat proteasome subunit RC1, a homologue of RING 10 located in the human MHC class II region (1992) FEBS Lett. 301, 65-68. [http://www.ncbi.nlm.nih.gov/pubmed/1451788]
  42. Sadaaki Iwanaga, Toshiyuki Miyata, Fuminori Tokunaga, and Tatsushi Muta; Molecular Mechanism of Hemolymph Clotting System in Limulus (1992) Thromb. Res. 68, 1-32.
  43. Yoshihiro Toh, Akiko Mizutani, Fuminori Tokunaga, Tatsushi Muta, and Sadaaki Iwanaga; Morphology of the granular hemocytes of the Japanese horseshoe crab Tachypleus tridentatus and immunocytochemical localization of clotting factors and antimicrobial substances (1991) Cell Tissue Res. 266, 137-147. [http://www.springerlink.com/content/npj7m138141x2354/]
  44. Tsukasa Murakami, Makoto Niwa, Fuminori Tokunaga, Toshiyuki Miyata, and Sadaaki Iwanaga; Direct virus inactivation of Tachyplesin I and Its isopeptides from horseshoe crab hemocytes (1991) Chemotherapy 37, 327-334.[ http://www.ncbi.nlm.nih.gov/pubmed/1666545]
  45. Yoshiaki Yae, Shoichi Inaba, Hiroyuki Sato, Kazuo Okochi, Fuminori Tokunaga, and Sadaaki Iwanaga; Isolation and characterization of a b-2macroglycoprotein ('thermolabile substance' or 'Hakata antigen') detected by precipitating (auto)antibody in sera of patients with systemic lupus erythematosus (1991) Biochim. Biophys. Acta 1078, 369-376. [http://www.ncbi.nlm.nih.gov/pubmed/1859827]
  46. Tatsushi Muta, Toshiyuki Miyata, Yoshio Misumi, Fuminori Tokunaga, Takanori Nakamura, Yoshihiro Toh, Yukio Ikehara, and Sadaaki Iwanaga; Limulus factor C: An endotoxin sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains (1991) J. Biol. Chem. 266, 6554-6561. [http://www.ncbi.nlm.nih.gov/pubmed/2007602]
  47. Fuminori Tokunaga, Hiroshi Nakajima, and Sadaaki Iwanaga; Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): Its isolation from Limulus polyphemus hemocytes and identification as an intracellular zymogen activated by a-chymotrypsin, not by trypsin (1991) J. Biochem. 109, 150-157. [http://www.ncbi.nlm.nih.gov/pubmed/2016264]
  48. Keiichi Kawano, Takashi Yoneya, Toshiyuki Miyata, Katsuhiro Yoshikawa, Fuminori Tokunaga, Yoshihiro Terada, and Sadaaki Iwanaga; Conformational analysis of Tachyplesin I, LPS binding antimicrobial peptide isolated from hemocyte of the horseshoe crab, by 1H NMR (II) (1991) In: Peptide Chemistry 1990 (Y. Shimonishi Ed.) Protein Research Foundation, Osaka, pp. 385-388.
  49. Takeshi Shigenaga, Tatsushi Muta, Yoshihiro Toh, Fuminori Tokunaga, and Sadaaki Iwanaga; Antimicrobial Tachyplesin peptide precursor: cDNA cloning and cellular localization in horseshoe crab (Tachypleus tridentatus) (1990) J. Biol. Chem. 265, 21350-21354.[ http://www.ncbi.nlm.nih.gov/pubmed/2250028]
  50. Keiji Tanaka, Hiroomi Kanayama, Tomohiro Tamura, Do Hee Lee, Atsushi Kumatori, Tsutomu Fujiwara, Akira Ichihara, Fuminori Tokunaga, Rie Aruga, and Sadaaki Iwanaga; cDNA cloning and sequencing of component C8 of proteasomes from rat hepatoma cells (1990) Biochem. Biophys. Res. Commun. 171, 676-683. [http://www.ncbi.nlm.nih.gov/pubmed/2403356]
  51. Keiichi Kawano, Takashi Yoneya, Toshiyuki Miyata, Katsuhiro Yoshikawa, Fuminori Tokunaga, Yoshihiro Terada, and Sadaaki Iwanaga; Antibacterial peptide, Tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus): NMR determination of the b-sheet structure (1990) J. Biol. Chem. 265, 15365-15367.[ http://www.ncbi.nlm.nih.gov/pubmed/2394727]
  52. Kaoru Murakami, Fuminori Tokunaga, Sadaaki Iwanaga, and Masataka Mori; Presequence does not prevent folding of a purified mitochondrial precursor protein and is essential for association with a reticulocyte cytosolic factor(s) (1990) J. Biochem. 108, 207-214. [http://www.ncbi.nlm.nih.gov/pubmed/2229023]
  53. Atsushi Kumatori, Keiji Tanaka, Tomohiro Tamura, Tsutomu Fujiwara, Akira Ichihara, Fuminori Tokunaga, Aya Onikura, and Sadaaki Iwanaga; cDNA cloning and sequence of component C9 of proteasomes from rat hepatoma cells (1990) FEBS Lett. 264, 279-282. [http://www.ncbi.nlm.nih.gov/pubmed/2358075]
  54. Tatsuya Sueyoshi, Masahiro Uwani, Norio Itoh, Hiroshi Okamoto, Tatsushi Muta, Fuminori Tokunaga, Katsumi Takada, and Sadaaki Iwanaga; Cysteine protease inhibitor in the ascitic fluid of sarcoma 180 tumor-bearing mice is a low-molecular weight kininogen: Partial NH2- and COOH-terminal sequences and susceptibility to various glandular kallikreins (1990) J. Biol. Chem. 265, 10030-10035. [http://www.ncbi.nlm.nih.gov/pubmed/2351646]
  55. Tomohiro Tamura, Keiji Tanaka, Atsushi Kumatori, Fumi Yamada, Chizuko Tsurumi, Tsutomu Fujiwara, Akira Ichihara, Fuminori Tokunaga, Rie Aruga, and Sadaaki Iwanaga; cDNA cloning and sequence of component C5 of proteasomes from rat hepatoma cells (1990) FEBS Lett. 264, 91-94. [http://www.ncbi.nlm.nih.gov/pubmed/2338147]
  56. Fuminori Tokunaga, Rie Aruga, Sadaaki Iwanaga, Keiji Tanaka, Akira Ichihara, Toshifumi Takao, and Yasutsugu Shimonishi; The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8 are Na-acetylated (1990) FEBS Lett. 263, 373-375. [http://www.ncbi.nlm.nih.gov/pubmed/2335242]
  57. Keiji Tanaka, Tsutomu Fujiwara, Atsushi Kumatori, Sadahito Shin, Tetsuo Yoshimura, Akira Ichihara, Fuminori Tokunaga, Rie Aruga, Sadaaki Iwanaga, Akira Kakizuka, and Shigetada Nakanishi; Molecular cloning of cDNA for proteasomes (multicatalytic proteinase complex) from rat liver: Primary structure of component C3 with a possible tyrosine phosphorylation site (1990) Biochemistry 29, 3777-3785.
  58. Song-Yuan Liu, Kiyomi Yoshizumi, Naoko Oda, Motonori Ohno, Fuminori Tokunaga, Sadaaki Iwanaga, and Hiroshi Kihara; Purification and amino acid sequence of basic protein II, a Lysine-49 phospholipase A2 with a low activity, from Trimeresurus flavoviridis venom (1990) J. Biochem. 107, 400-408.
  59. Tatsushi Muta, Takanori Nakamura, Hiromi Furunaka, Fuminori Tokunaga, Toshiyuki Miyata, Makoto Niwa, and Sadaaki Iwanaga; Primary structures and functions of anti-lipopolysaccharide factor and Tachyplesin peptide found in horseshoe crab hemocytes (1990) In: Proceeding of International Symposium on Endotoxin (Friedman, H., Klein, T. W., M. Nakano, M., and Nowotny, A., Ed.) Plenum Press, New York, pp. 273-285.
  60. Makoto Niwa, He Hua, Sadaaki Iwanaga, Takashi Morita, Toshiyuki Miyata, Takanori Nakamura, Jun Aketagawa, Tatsushi Muta, Fuminori Tokunaga, and Kei-ichi Ohashi; Biological activities of anti-LPS factor and LPS binding peptide from horseshoe crab amoebocytes. In: Proceeding of International Symposium on Endotoxin (Friedman, H., Klein, T. W., Nakano, M., and Nowotny, A., Ed.) (1990) Plenum Press, New York, pp. 257-271.
  61. Toshiyuki Miyata, Fuminori Tokunaga, Takashi Yoneya, Katsuhiro Yoshikawa, Sadaaki Iwanaga, Makoto Niwa, Toshifumi Takao, and Yasutsugu Shimonishi; Antimicrobial peptides, isolated from horseshoe crab hemocytes, Tachyplesin II, and Polyphemusins I and II: Chemical structures and biological activity (1989) J. Biochem. 106, 663-668.
  62. Ken-ichi Akaji, Nobutaka Fujii, Fuminori Tokunaga, Toshiyuki Miyata, Sadaaki Iwanaga, and Haruaki Yajima; Syntheses of three peptides isolated from horseshoe crab hemocytes, Tachyplesin I, Tachyplesin II, and Polyphemusin I (1989) Chem. Pharm. Bull. 37, 2661-2664.
  63. Tsutomu Fujiwara, Keiji Tanaka, Atsushi Kumatori, Sadahito Shin, Tesuo Yoshimura, Akira Ichihara, Fuminori Tokunaga, Rie Aruga, Sadaaki Iwanaga, Akira Kakizuka and Shigetada Nakanishi; Molecular cloning of cDNA for proteasomes (multicatalytic proteinase complex) from rat liver: Primary structure of the largest component (C2) (1989) Biochemistry 28, 7332-7340.
  64. Toshiyuki Miyata, Hiroyuki Takeya, Yasushi Ozeki, Mitsue Arakawa, Fuminori Tokunaga, Sadaaki Iwanaga, and Tamotsu Satoh-Omori; Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis (1989) J. Biochem. 105, 847-853.
  65. Fuminori Tokunaga, Takanori Nakamura, Tatsushi Muta, Toshiyuki Miyata, and Sadaaki Iwanaga; Intracellular serine protease zymogen, factor C, from limulus hemocytes: Its structure and function. In: Intracellular Proteolysis (N. Katunuma & E. Kominami, Ed.) (1989) Japan Scientific Societies, Tokyo, pp. 120-128.
  66. Fuminori Tokunaga, Katsuaki Nagasawa, Shigehiko Tamura, Toshiyuki Miyata, Sadaaki Iwanaga, and Walter Kisiel; The factor V-activating enzyme (RVV-V) from Russell's viper venom: Identification of isoproteins RVV-Va, -Vb, and -Vg and their complete amino acid sequences (1988) J. Biol. Chem. 263, 17471-17481.
  67. Takanori Nakamura, Hiromi Furunaka, Toshiyuki Miyata, Fuminori Tokunaga, Tatsushi Muta, Sadaaki Iwanaga, Makoto Niwa, Toshifumi Takao, and Yasutsugu Shimonishi; Tachyplesin, a class of antimicrobial peptide from the hemocyte of the horseshoe crab (Tachypleus tridentatus) (1988) J. Biol. Chem. 263, 16709-16713.
  68. Takanori Nakamura, Fuminori Tokunaga, Takashi Morita, Sadaaki Iwanaga, Shouichi Kusumoto, Tetsuo Shiba, Tetsuyuki Kobayashi, and Keizo Inoue; Intracellular serine-protease zymogen, factor C, from horseshoe crab hemocytes: Its activation by synthetic lipid A analogues and acidic phospholipids (1988) Eur. J. Biochem. 176, 89-94.
  69. Youichi Kawano, Kenshi Okubo, Fuminori Tokunaga, Toshiyuki Miyata, Sadaaki Iwanaga, and Naotaka Hamasaki; Localization of pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein (1988) J. Biol. Chem. 263, 8232-8238.
  70. Takanori Nakamura, Fuminori Tokunaga, Takashi Morita, and Sadaaki Iwanaga; Interaction between lipopolysaccharide and intracellular serine protease zymogen, factor C, from horseshoe crab (Tachypleus tridentatus) hemocytes (1988) J. Biochem. 103, 370-374.
  71. Fuminori Tokunaga, Toshiyuki Miyata, Takanori Nakamura, Takashi Morita, Kei-ichi Kuma, Takashi Miyata, and Sadaaki Iwanaga; Lipopolysaccharide-sensitive serine protease zymogen (factor C) of horseshoe crab hemocytes: Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine-protease (1987) Eur. J. Biochem. 167, 405-416.
  72. Susumu Kawamoto, Yoshihiro Amaya, Kaoru Murakami, Fuminori Tokunaga, Sadaaki Iwanaga, Keiko Kobayashi, Takeyori Saheki, Sadao Kimura, and Masataka Mori; Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase (1987) J. Biol. Chem. 262, 6280-6283.
  73. Tatsushi Muta, Toshiyuki Miyata, Fuminori Tokunaga, Takanori Nakamura, and Sadaaki Iwanaga; Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus (1987) J. Biochem. 101, 1321-1330.
  74. Takanori Nakamura, Toshiaki Hirai, Fuminori Tokunaga, Shun-ichiro Kawabata, and Sadaaki Iwanaga; Purification and amino acid sequence of Kunitz-type protease inhibitor found in the hemocytes of horseshoe crab (Tachypleus tridentatus) (1987) J. Biochem. 101, 1297-1306.

[日本語総説　著書：1987-2008]

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  3. 徳永文稔; 小胞体残留シグナル (2008) 蛋白質核酸酵素増刊　キーワード：蛋白質の一生 53, 947.
  4. 徳永文稔; 糖鎖修飾 (2008) 蛋白質核酸酵素増刊　キーワード：蛋白質の一生 53, 974.
  5. 徳永文稔; マンノシダーゼ (2008) 蛋白質核酸酵素増刊　キーワード：蛋白質の一生 53, 1007.
  6. 徳永文稔; レクチン (2008) 蛋白質核酸酵素増刊　キーワード：蛋白質の一生 53, 1021.
  7. 徳永文稔、岩井一宏; ユビキチン修飾系の細胞機能と病態への関与 (2007) 分子細胞治療 6, 23-29.
  8. 徳永文稔; p97/VCP/Cdc48pとユビキチン系 (2006) 蛋白質核酸酵素 51, 1361.
  9. 徳永文稔; E2の種類と役割 (2006) 蛋白質核酸酵素 51, 1150-1156.
  10. 徳永文稔; シャペロンによる再生システム (2005) 実験医学23, 2338-2344.
  11. 徳永文稔; タンパク質のプロセシング, 糖鎖修飾（小胞体、ゴルジ体）「細胞生物学事典」（石川統、黒岩常祥、永田和宏　編）, 朝倉書店, 東京 (2005).
  12. 徳永文稔; 小胞体におけるフォールディングと品質管理 (2004) 細胞工学23, 1384-1389.
  13. 徳永文稔; 血液凝固因子欠乏症と蛋白質の輸送・品質管理 (2004) 蛋白質核酸酵素49, 1135.
  14. 徳永文稔; ユビキチンと小胞体関連分解(ERAD) (2004) 医学のあゆみ 211, 135-141.
  15. 徳永文稔; 続・正常だけど分泌されない血液凝固因子の物語 (2003) 蛋白質核酸酵素48, 1738-1739.
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  17. 徳永文稔: Russell’s Viper Vアクチベータ「廣川タンパク質化学　第1巻　毒素タンパク質　I動物由来毒素タンパク質」（林恭三、池田潔、太田光熙　編）, pp. 83-88, 廣川書店, 東京 (2003).
  18. 吉田雪子、徳永文稔、田中啓二、田井直; 糖鎖を識別するユビキチンリガーゼによる分泌蛋白質の品質管理 (2002) 蛋白質核酸酵素 47, 1924-1930.
  19. 徳永文稔、小出武比古: ヒルジン. 「廣川タンパク質化学　第7巻　制御タンパク質　インヒビター」（大内和雄　編）, pp. 68-72, 廣川書店, 東京 (2002).
  20. 徳永文稔; プロテアソームと小胞体関連分解(ERAD)機構 (2001) Annual Review免疫2002 56-64.
  21. 徳永文稔; 小胞体関連分解機構の最前線 (2001) 実験医学 増刊 タンパク質分解の最前線2001 (田中啓二、大隅良典、編), 19, 263-270.
  22. 徳永文稔：糖鎖を介したタンパク質の品質管理機構「分子シャペロンによる細胞機能制御」（永田和宏、森正敬、吉田賢右　共編）, pp. 99-111, Springer-Verlag社, 東京 (2001).
  23. 徳永文稔：タンパク質の品質管理機構「タンパク質分解-分子機構と細胞機能」（鈴木紘一、小南英紀、田中啓二　共編）, pp. 115-122, Springer-Verlag社, 東京（2000）.
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  25. 宮田敏行、徳永文稔; 凝固第V・VIII 因子合併欠乏症 (1999) 血液・腫瘍科 38, 396-301.
  26. 徳永文稔; ユビキチン/プロテアソームによる蛋白質の品質管理機構 (1999) 蛋白質核酸酵素44, 766-775.
  27. 徳永文稔; ビタミンK依存性因子の生合成(1996) Biomedical Perspectives 5, 29-36.
  28. 徳永文稔、城谷裕子、若林貞夫、小出武比古; 多面的影響型ATIII欠乏症の分子機構解析　(1996) 日本血栓止血学会誌 7, 206-212.
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  31. 中村隆範、牟田達史、宮田敏行、徳永文稔、岩永貞昭：エントドキシンによるカブトガニ血球細胞の活性化とその生化学的機構「エントドキシン臨床研究の新しい展開」（織田敏次 監修）, pp. 9-23, 羊土社, 東京（1988）.
  32. 川畑俊一郎、徳永文稔、岩永貞昭; 血液凝固･線溶･補体系とプロテアーゼ(1987) 実験医学5, 908-915.

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