Researchers Database

matsugi jitsuhiro

    DepartmentofBiochemistry,DivisionofStructuralBiochemistry Professor
Last Updated :2021/11/24

Researcher Information

Degree

  • (BLANK)

J-Global ID

Research Interests

  • RNA structure, chemical synthesis of RNA   tRNA, selenocysteine, read through, modified nucleotides   Biological Organic Chemistry   

Research Areas

  • Nanotechnology/Materials / Biochemistry
  • Nanotechnology/Materials / Chemical biology
  • Life sciences / Structural biochemistry / modified nucleosides
  • Life sciences / Applied biochemistry / selenoprotein

Academic & Professional Experience

  • 2015 - Today  同教授
  • 2009  同 生化学講座構造生化学准教授
  • 1996  同大学院 講師
  • 1993/04  同講師
  • 1988/04  Jichi Medical UniversitySchool of Medicine助手
  • 1986/06 - 1988/03  Northwestern UniversityDepartment of ChemistryPost-doctoral fellow

Education

  • 1988/04 - Today  Jichi Medical University  School of Medicine  Department of Biochemistry
  • 1986/06 - 1988/03  Nothwestern Univ. Dept. of Chem.  Department of Chemistry
  • 1986 -   Osaka University  薬品科学研究科 後期課程 修了(薬博)
  • 1983 -   Osaka University  薬品科学研究科 前期課程 修了
  •        - 1981  Osaka University  Faculty of Pharmaceutical Science
  • 1981 -   Osaka University  School of Pharmaceutical Sciences  製薬化学科 卒業

Association Memberships

  • JAPAN SOCIETY FOR MEDICAL EDUCATION   日本RNA学会   The RNA Society   日本分子生物学会   日本生化学会   日本薬学会   

Published Papers

  • Kenji Tago, Megumi Funakoshi-Tago, Satoshi Ohta, Hirotoshi Kawata, Hiroshi Saitoh, Hisanaga Horie, Chihiro Aoki-Ohmura, Junji Yamauchi, Akira Tanaka, Jitsuhiro Matsugi, Ken Yanagisawa
    Molecular oncology 13 (11) 2493 - 2510 1574-7891 2019/11 [Refereed][Not invited]
     
    It is well established that nuclear factor κB (NF-κB) acts as one of the most important transcription factors for tumor initiation and progression, as it both protects cells from apoptotic/necrotic signals and accelerates angiogenesis and tumor metastasis, which is mediated via the expression of target genes. However, it has not yet been clarified how oncogenic signals accelerate the activation of NF-κB. In the current study, we utilized untransformed NIH-3T3 cells stably harboring a κB-driven luciferase gene to show that an oncogenic mutant of Ras GTPase augmented TNFα-induced NF-κB activation. Notably, enforced expression of cyclin-dependent kinase inhibitors, such as p27Kip1 and p21Cip1 , effectively canceled the accelerated activation of NF-κB, suggesting that oncogenic Ras-induced cell cycle progression is essential for the hyperactivation of NF-κB. Furthermore, we found that Ras (G12V) augmented the transcriptional activation of NF-κB, and this activation required the p38 MAP kinase. We observed that a downstream kinase of p38 MAP kinase, MSK1, was activated by Ras (G12V) and catalyzed the phosphorylation of p65/RelA at Ser-276, which is critical for its transcriptional activation. Significantly, phosphorylation of the p65/RelA subunit at Ser-276 was elevated in patient samples of colorectal cancer harboring oncogenic mutations of the K-Ras gene, and the expression levels of NF-κB target genes were drastically enhanced in several cancer tissues. These observations strongly suggest that oncogenic signal-induced acceleration of NF-κB activation is caused by activation of the p38 MAP kinase-MSK1 signaling axis and by cell cycle progression in cancer cells.
  • Kenji Tago, Satoshi Ohta, Masaki Kashiwada, Megumi Funakoshi-Tago, Jitsuhiro Matsugi, Shin-Ichi Tominaga, Ken Yanagisawa
    Heliyon 3 (10) e00436  2017/10 [Refereed][Not invited]
     
    The ST2 gene was originally identified as a primary responsive gene, and the expressions of its gene products are induced by stimulation with growth factors and by oncogenic stresses. In this study, we observed that oncogenic Ras mutant induced the expression of ST2 and ST2L proteins. Interestingly, the enforced expression of ST2 gene products in NIH-3T3 murine fibroblasts remarkably enhanced Ras (G12V)-induced cellular transformation. Furthermore, when the expression of ST2 gene products was silenced by RNA-interference technique, Ras (G12V)-induced cellular transformation was drastically suppressed. According to these observations, it was indicated that the oncogenic Ras-induced expression of ST2 gene products is required for the acceleration of cellular transformation, and this seems to be independent of the stimulation with IL-33, a ligand for ST2/ST2L. Interestingly, knockdown of ST2 gene products caused a reduction in Rb phosphorylation in transformed murine fibroblasts, suggesting the functional involvement of ST2 gene products in cell cycle progression during cellular transformation. Our current study strongly suggests the importance of ST2 gene products in cellular transformation, and the presence of novel mechanism how ST2 gene products affect the cellular transformation and cell proliferation.
  • Kenji Tago, Satoshi Ohta, Megumi Funakoshi-Tago, Chihiro Aoki-Ohmura, Jitsuhiro Matsugi, Shin-ichi Tominaga, Ken Yanagisawa
    FEBS OPEN BIO 7 (2) 293 - 302 2211-5463 2017/02 [Refereed][Not invited]
     
    The ST2 gene was originally identified as a primary responsive gene induced by stimulation with growth factors and by oncogenic stress. The ST2 gene harbors two distinct promoters - a distal promoter and a proximal promoter. In this study, we identified a novel type of serum-responsive element in the ST2 proximal promoter using reporter gene analysis; this element includes a possible responsive element for STAT family proteins. Indeed, enforced expression of constitutively active STAT3 activated this promoter element and induced the expression of ST2 gene products. Furthermore, an oncogenic Ras (G12V) mutant also caused the expression of ST2 gene products by utilizing the proximal promoter. We also clarified that activation of the ST2 promoter by either growth stimulation or oncogenic Ras was suppressed by the inhibitors for STAT3 and ERK pathways. Our observations strongly suggest the importance of STAT family and ERK pathways for the induction of ST2 gene products by cell growth stimulation.
  • Satoshi Ohta, Kenji Tago, Megumi Funakoshi-Tago, Jitsuhiro Matsugi, Ken Yanagisawa
    CELLULAR SIGNALLING 28 (8) 1025 - 1036 0898-6568 2016/08 [Refereed][Not invited]
     
    A member of the interleukin-1 family, interleukin-33 (NF-HEV/IL-33), is a ligand for the receptor, ST2L and stimulates the production of Th2 cytokines. Although IL-33 localizes to the nucleus and may be involved in the regulation of transcription independent of ST2L, its functions in the nucleus currently remain unclear. We herein demonstrated that the expression of IL-33 was markedly enhanced in NIH-3T3 cells transformed by an oncogenic H-Ras mutant (H-Ras (G12V)), and the induced IL-33 was mainly located in the nuclei of these cells. The enforced expression of IL-33 accelerated H-Ras (G12V)-induced transformation in NIH-3T3 cells, and this transforming activity was markedly reduced by the knockdown of IL-33 with shRNA. We subsequently analyzed several signaling molecules regulated by Ras in order to elucidate the mechanism by which IL-33 contributes to Ras (G12V)-induced transformation. We found that the knockdown of IL-33 effectively attenuated the Ras (G12V)-induced expression of cyclin D1. However, the knockdown of IL-33 failed to affect cyclin D1 mRNA expression levels, and epoxomicin, a proteasome. inhibitor, did not cancel the IL-33 knockdown -induced down-regulation of its protein levels. We showed that Ras (G12V)-induced cyclin D1 protein synthesis was markedly suppressed by the knockdown of IL-33. Taken together, the results of the present study strongly suggest a novel role for IL-33 in cellular transformation. (C) 2016 Elsevier Inc All rights reserved.
  • 松儀 実広, 原田 三男, 菊地 元史, 黒岩 憲二, 淺田 義和, 輿水 崇鏡, 奥田 浩, 遠藤 仁司, 野田 泰子, 岡崎 仁昭
    医学教育 (一社)日本医学教育学会 45 (Suppl.) 177  0386-9644 2014/07 [Not refereed][Not invited]
  • 多胡 憲治, 多胡 めぐみ, 太田 聡, 松儀 実広, 柳澤 健
    日本生化学会大会プログラム・講演要旨集 (公社)日本生化学会 86回 3T13p  2013/09 [Not refereed][Not invited]
  • Megumi Sumitani, Katsumi Kasashima, Jitsuhiro Matsugi, Hitoshi Endo
    JOURNAL OF BIOCHEMISTRY 149 (5) 581 - 589 0021-924X 2011/05 [Refereed][Not invited]
     
    Caenorhabditis elegans HMG-5, which is encoded by F45E4.9, contains two high mobility group (HMG) box domains and shows sequence similarity with mammalian mitochondrial transcription factor A (TFAM). In this study, using soaking RNA interference, we found that knockdown of HMG-5 reduced the amount of mtDNA in P0 hermaphrodites, suggesting it as functional orthologue of mammalian TFAM. We also examined the biochemical property of HMG-5 in mammalian cells and in vitro. We found that HMG-5 localized to the mitochondria in human cultured cells and was included in the NP-40-insoluble fraction in which mtDNA and TFAM were enriched. By immunoprecipitation analysis, HMG-5 was found to associate with human mitochondrial DNA (mtDNA) in the cells. In vitro binding experiment also showed that HMG-5 binds to C. elegans mtDNA and plasmid DNA, indicating its feature as a non-specific DNA-binding protein. Furthermore, it was found that HMG-5 can interact with itself. These results demonstrate that HMG5 shares similar biochemical properties with mammalian TFAM as a nucleoid factor. HMG-5 could be a good candidate for investigating mtDNA metabolism in multicellular organisms.
  • Jitsuhiro Matsugi
    SEIKAGAKU 79 (10) 964 - 968 0037-1017 2007/10 [Not refereed][Not invited]
  • Y Yamada, J Matsugi, H Ishikura, K Murao
    BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION 1728 (3) 143 - 149 0167-4781 2005/05 [Refereed][Not invited]
     
    In Bacillus subtilis, four codons, CCU, CCC, CCA, and CCG, are used for proline. There exists, however, only one proline-specific tRNA having the anticodon mo(5)UGG. Here, we found that this tRNA (Pro)(mo(5)UGG) can read not only the codons CCA, CCG and CCU but also CCC, using an in vitro assay system. This means that the first nucleoside of its anticodon, 5-methoxyuridine (mo(5)U), recognizes A, G, U and C. On the other hand, it was reported that mo(5)U at the first position of the anticodon of tRNA (Val)(mo(5)UAC) can recognize A, G, and U but not C. A comparison of the structure of the anticodon stem and loop of tRNA (Pro)(mo(5)UGG) with those of other tRNAs containing mo(5)U at the first positions of the anticodons suggests that a modification of nucleoside 32 to pseudouridine (T) enables tRNA (Pro)(mo(5)UGG) to read the CCC codon. © 2005 Elsevier B.V. All rights reserved.
  • Yamada Y, Matsugi J, Ishikura H, Murao K
    Biochimica et biophysica acta 1728 (3) 143 - 149 0006-3002 2005/05 [Refereed][Not invited]
  • Matsugi J, Murao K
    Biochimica et biophysica acta 1676 (1) 23 - 32 0006-3002 2004/01 [Refereed][Not invited]
  • Y Yamada, J Matsugi, H Ishikura
    BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION 1626 (1-3) 75 - 82 0167-4781 2003/04 [Refereed][Not invited]
     
    The tRNA(1)(Ser) (anticodon VGA, V=uridin-5-oxyacetic acid) is essential for translation of the UCA codon in Escherichia coli. Here, we studied the translational abilities of serine tRNA derivatives, which have different bases from wild type at the first positions of their anticodons, using synthetic mRNAs containing the UCN (N = A, G, C, or U) codon. The tRNA(1)(Ser)(G(34)) having the anticodon GGA was able to read not only UCC and UCU codons but also UCA and UCG codons. This means that the formation of G-A or G-G pair allowed at the wobble position and these base pairs are noncanonical. The translational efficiency of the tRNA(1)(Ser)(G(34)) for UCA or UCG codon depends on the 2'-O-methylation of the C-32 (Cm). The 2'-O-methylation of C-32 may give rise to the space necessary for G-A or G-G base pair formation between the first position of anticodon and the third position of codon. (C) 2003 Elsevier Science B.V. All rights reserved.
  • Yamada Y, Matsugi J, Ishikura H
    Biochimica et biophysica acta 1626 (1-3) 75 - 82 0006-3002 2003/04 [Refereed][Not invited]
  • J Matsugi, K Murao
    BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION 1521 (1-3) 81 - 88 0167-4781 2001/10 [Refereed][Not invited]
     
    The construction of a cDNA library corresponding to an amino acid-specific tRNA and the influence of the modified nucleotide in the tRNA upon misincorporation in reverse transcription were investigated. The distinctive feature of the constructive strategy is that the cDNA library was prepared in connection with the charging activity of the tRNA. The aminoacyl-tRNA was captured selectively by using a biotin-avidin system. After hydrolysis of the ester bond, the tRNA was collected as an amino acid-specific tRNA pool., and a poly(A) tail was attached to the CCA terminus for reverse transcription. To the 3'-terminus of the transcribed cDNA, poly (dC) was added by terminal deoxynucleotidyl transferase, and the cDNA was amplified by PCR. The double-stranded cDNA was used for transformation of Escherichia coli JM109, Sequence analyses of the obtained clones bearing the tRNA genes revealed that a few nucleotide substitutions occurred at the location where the modified nucleotides exist. Among them, it was noteworthy that 1-methyladenosine (m(1)A22) in the D-loop of Bacillus subtilis tRNA(Ser) was recognized as G in the reverse transcription and the result revealed different tendency of the misincorporation, which has been shown in the study of HIV-1 reverse transcription. (C) 2001 Elsevier Science B.V. All rights reserved.
  • A study of the method to pick up a selenocysteine tRNA in Bacillus subtilis.
    Matsugi J, Murao K
    Nucleic Acid Symposium Series Oxford University Press. 44 149 - 150 2000 [Refereed][Not invited]
  • Search for a selenocysteine tRNA in Bacillus subtilis
    Matsugi J, Murao K, Ishikura H
    Nucleic Acid Symposium Series Oxford University Press. 42 209 - 210 1999 [Refereed][Not invited]
  • J Matsugi, K Murao, H Ishikura
    JOURNAL OF BIOCHEMISTRY 123 (5) 853 - 858 0021-924X 1998/05 [Refereed][Not invited]
     
    Bacillus subtilis has been thought to have a high readthrough rate at the UGA stop codon because no opal suppressor tRNA has been isolated so far [Lovett ct al, (1991) J, Bacteriol, 173, 1810-1812], To examine whether a tRNA(TrP) which We have characterized [Matsugi ct al, (1992) Nucleic Acids Res. 20, 3514] has the ability to read the UGA codon, in vitro translation was performed with a synthetic mRNA containing a test codon, UGA, UAG, UAA, or UGG, in a reading frame, Addition of Trp-tRNA(Trp) to the system significantly increased the readthrough rate only in the case of UGA. This suggests that this tRNA(Trp) has a dual recognition pattern in B, subtilis, i.e., for the canonical tryptophan codon and for readthrough at the UGA stop codon.
  • J Matsugi, K Murao, H Ishikura
    JOURNAL OF BIOCHEMISTRY 119 (4) 811 - 816 0021-924X 1996/04 [Refereed][Not invited]
     
    Bacillus subtilis, which belongs to Gram-positive eubacteria, has been predicted to have a minor isoleucine tRNA transcribed from the gene possessing the CAT anticodon, which corresponds to methionine. We isolated this tRNA and determined its sequence including modified nucleotides. Modified nucleotide analyses using TLC, UV, and FAB mass spectroscopy revealed that the first letter of the anticodon is modified to lysidine [4-amino-2-(N-6-lysino)-1-beta-D-ribofuranosyl pyrimidine]. As a result, this tRNA agrees with the minor one predicted from the DNA sequence and is thought to decode the isoleucine codon AUA.
  • Effect of nucleotide substitution in Bacillus subtilis tRNATrp on readthrough efficiency.
    Matsugi J, Murao K, Ishikura H
    Nucleic Acids Symposium Series 35 289  1996 [Refereed][Not invited]
  • J MATSUGI, K MURAO, H ISHIKURA
    NUCLEIC ACIDS RESEARCH 20 (13) 3514 - 3514 0305-1048 1992/07 [Refereed][Not invited]
  • Jitsuhiro Matsugi, Hong-Ti Jia, Katsutoshi Murao, Hisayuki Ishikura
    BBA - Gene Structure and Expression 1130 (3) 333 - 335 0167-4781 1992/04 [Refereed][Not invited]
     
    Three B. subtilis serine tRNAs were sequenced including modified nucleosides. All the serine tRNAs contained 1-methyl-adenosine in the D-loop. As other characteristic modified nucleosides, 5-methoxyuridine was found in the first letter of the anticodon in the tRNA(UGA). © 1992.
  • J MATSUGI, HT JIA, K MURAO, H ISHIKURA
    BIOCHIMICA ET BIOPHYSICA ACTA 1130 (3) 333 - 335 0006-3002 1992/04 [Refereed][Not invited]
     
    Three B. subtilis serine tRNAs were sequenced including modified nucleosides. All the serine tRNAs contained 1-methyladenosine in the D-loop. As other characteristic modified nucleosides, 5-methoxyuridine was found in the first letter of the anticodon in the tRNA(UGA).
  • RL LETSINGER, RH ALUL, F FAROOQUI, PM JUNG, J MATSUGI, OB KINSTLER, Z SKRZYPCZYNSKI, Z ZHANG
    SYMPOSIUM ON NUCLEIC ACIDS TECHNOLOGY 22 83 - 83 1990 [Refereed][Not invited]
  • M IKEHARA, K FUJIMOTO, Y AOYAMA, K YANASE, J MATSUGI, T INAOKA, T TOKUNAGA, S UESUGI, S IWAI, E OHTSUKA
    CHEMICAL & PHARMACEUTICAL BULLETIN 34 (5) 2202 - 2208 0009-2363 1986/05 [Refereed][Not invited]
  • 長鎖リボヌクレオチドの合成研究
    松儀 実広
    大阪大学 学位論文 1986/03 [Refereed][Not invited]
  • T DOI, H MORIOKA, J MATSUGI, E OHTSUKA, M IKEHARA
    FEBS LETTERS 190 (1) 125 - 128 0014-5793 1985 [Refereed][Not invited]
  • T DOI, A YAMANE, J MATSUGI, E OHTSUKA, M IKEHARA
    NUCLEIC ACIDS RESEARCH 13 (10) 3685 - 3697 0305-1048 1985 [Refereed][Not invited]
  • E OHTSUKA, J MATSUGI, A YAMANE, H MORIOKA, M IKEHARA
    CHEMICAL & PHARMACEUTICAL BULLETIN 33 (10) 4152 - 4159 0009-2363 1985 [Refereed][Not invited]
     
    Ribooligonucleotides (nonamer, decamer and nonadecamer) were synthesized by the solid phase phosphotriester method using 2'-O-tetrahydrofuranyl nucleosides. These oligomers were designed in order to obtain E. coli tRNA^<Met>_f deficient in D-loop and D-stem and its analogs. Condensation was performed by using dimer blocks and the dimethoxytrityl group on the 5'-hydroxyl group was removed selectively by 1M ZnBr_2 without affecting the 2'-protection.
  • Synthesis and expression of RNase T1 gene.
    Ikehara, M, Fujimoto, K, Aoyama, Y, Yanase, K, Matsugi, J, Inaoka, T, Tokunaga, T, Uesugi, S, Iwai, S, Ohtsuka, E
    Nucleic Acids Symp. Ser. 15 197 - 200 1984 [Refereed][Not invited]
  • S UESUGI, T KANEYASU, J MATSUGI, M IKEHARA
    NUCLEOSIDES & NUCLEOTIDES 2 (4) 373 - 385 0732-8311 1983 [Refereed][Not invited]
  • E OHTSUKA, T DOI, R FUKUMOTO, J MATSUGI, M IKEHARA
    NUCLEIC ACIDS RESEARCH 11 (12) 3863 - 3872 0305-1048 1983 [Refereed][Not invited]
  • E OHTSUKA, J MATSUGI, H TAKASHIMA, S AOKI, T WAKABAYASHI, T MIYAKE, M IKEHARA
    CHEMICAL & PHARMACEUTICAL BULLETIN 31 (2) 513 - 520 0009-2363 1983 [Refereed][Not invited]
     
    tRNA fragments containing modified nucleosides have been synthesized either by condensation of nucleotides containing a modified base or by modification of oligonucleotides. Ribothymidine 3'-phosphate was prepared by condensation of the silylated base with protected D-ribose followed by phosphorylation. Ribothymidine-containing trimer, T-Ψ-C, was synthesized by the phosphodiester method. A ribothymidine-containing hexamer T-U-C-A-A-A and a 2'-O-methylcytidine containing hexamer C-G-G-G-Cm-Up were synthesized by the phosphotriester method. A dihydrouridine-containing trimer D-A-G and a 7-methylguanosine-containing trimer m^7G-U-C were obtained by modification of the trimers by reduction and methylation, respectively.
  • S UESUGI, J MATSUGI, T KANEYASU, M IKEHARA
    HETEROCYCLES 17 (SI) 285 - 288 0385-5414 1982 [Refereed][Not invited]

Conference Activities & Talks

MISC

  • ST2Lの新規結合タンパク質IFITM3はST2Lのリソソーム分解を介してIL-33シグナルを抑制する
    多胡 憲治, 多胡 めぐみ, 太田 聡, 大村 千尋, 松儀 実広, 富永 眞一, 柳澤 健  日本生化学会大会プログラム・講演要旨集  92回-  [1T07a  -02]  2019/09  [Not refereed][Not invited]
  • がん化型Ras変異体はp38-MSK1/2経路を介してNF-κB活性化を増強する
    多胡 憲治, 多胡 めぐみ, 太田 聡, 河田 浩敏, 堀江 久永, 齊藤 博司, 山内 淳司, 田中 亨, 松儀 実広, 柳澤 健  日本生化学会大会プログラム・講演要旨集  91回-  [3T12a  -05(3P  2018/09  [Not refereed][Not invited]
  • Ras変異体が誘導する発がんシグナルにおける受容体型チロシンキナーゼMer(MerTK)の機能解析
    太田 聡, 多胡 憲治, 松儀 実広, 柳澤 健  生命科学系学会合同年次大会  2017年度-  [2P  -0448]  2017/12  [Not refereed][Not invited]
  • KRasタンパク質のC末端側における新規の点変異は特異な生化学的特性と細胞がん化能を示す
    多胡 憲治, 多胡 めぐみ, 太田 聡, 大村 千尋, 松儀 実広, 柳澤 健  生命科学系学会合同年次大会  2017年度-  [4LT19  -02(3P  2017/12  [Not refereed][Not invited]
  • IL-33前駆体は、がん化型Ras変異体が誘導する形質転換とサイクリンD1のタンパク質合成に必須の役割を担う
    太田 聡, 多胡 憲治, 多胡 めぐみ, 松儀 実広, 柳澤 健  日本生化学会大会・日本分子生物学会年会合同大会講演要旨集  88回・38回-  [1P0110]  -[1P0110]  2015/12  [Not refereed][Not invited]
  • 新規IL-33シグナル調節蛋白質IFITM3の同定
    多胡 憲治, 多胡 めぐみ, 太田 聡, 松儀 実広, 柳澤 健  日本生化学会大会・日本分子生物学会年会合同大会講演要旨集  88回・38回-  [2T21p  -04(2P0198)]  2015/12  [Not refereed][Not invited]
  • 松儀 実広, 原田 三男, 菊地 元史, 黒岩 憲二, 淺田 義和, 輿水 崇鏡, 奥田 浩, 遠藤 仁司, 野田 泰子, 岡崎 仁昭  医学教育  45-  (Suppl.)  177  2014/07  [Not refereed][Not invited]
  • 多胡 憲治, 多胡 めぐみ, 太田 聡, 松儀 実広, 柳澤 健  日本生化学会大会プログラム・講演要旨集  86回-  3T13p  2013/09  [Not refereed][Not invited]
  • 太田聡, 多胡憲治, 多胡めぐみ, 松儀実広, 柳澤健  日本分子生物学会年会プログラム・要旨集(Web)  35th-  3P-0461 (WEB ONLY)  2012  [Not refereed][Not invited]
  • 佐藤正章, 渥美一弥, 野田泰子, 松儀実広, 板井美浩, 奥田浩, 岡崎仁昭  医学教育  42-  (Suppl.)  73  2011/07  [Not refereed][Not invited]
  • 松儀実広  生化学  79-  (10)  964  -968  2007/10  [Not refereed][Not invited]
  • 細菌ドメインにおけるSelenocysteineの取り込みシステムのゲノム研究(Genomic investigation of the system for selenocysteine incorporation in the bactrial domain)
    Matsugi Jitsuhiro, Murao Katsutoshi  生化学  75-  (8)  1091  -1091  2003/08  [Not refereed][Not invited]
  • Genomic investigation of the system for selenocysteine incorporation in the bacterial domain.
    生化学  75巻 8号 1091-  2003  [Not refereed][Not invited]
  • 枯草菌におけるセレノシステインtRNAの探索
    第24回日本分子生物学年会要旨集  651ページ-  2001  [Not refereed][Not invited]

Research Grants & Projects

  • バクテリアにおけるセレノシステインの系の分布についての研究
    遺伝子科学研究
    Date (from‐to) : 1999 -2003
  • セレノプロテインの機能と発現
    ライフサイエンス基礎科学研究
    Date (from‐to) : 2000 
    セレノプロテインはどのような調節機構で発現されているか
  • アミノアシルtRNA合成酵素の研究
  • 新規tRNAの探索システムに関する研究
  • 枯草菌におけるUGA終止コドンの翻訳についての研究
  • Study of Aminoacyl-tRNA Synthetase
  • Study of the detection system for an unknown tRNA
  • Study of the translation at UGA codon in B. subtilis


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