特許へ

2010

  1. Suzuki, H., Ando, T., Umekage, S., Tanaka, T., and Kikuchi, Y.
    Extracellular production of an RNA aptamer by ribonuclease-free marine bacteria harboring engineered plasmids: a proposal for industrial RNA drug production. Appl. Environ. Microbiol. 76(3), 786-793 (2010)


2009

  1. Ochi, A., Umekage, S., and Kikuchi, Y.
    Non-enzymatic in vitro production of circular hammerhead ribozyme targeting the template region of human telomerase RNA. Nucleic Acids Symp Ser (Oxf). (53), 275-276. (2009)

  2. Fujimoto, A., Kikuchi, Y., and Tanaka, T.
    Substrate recognition of pre-tRNA by ribonuclease P---subsite model of natural ribozyme originated from Escherichia coli. Nucleic Acids Symp Ser (Oxf). (53), 35-36. (2009)

  3. Umekage, S., and Kikuchi, Y.
    In vivo circular RNA production using a constitutive promoter for high-level expression. J Biosci Bioeng. 108(4), 354-356. (2009)

  4. Suzuki, H., Umekage, S., Tanaka, T., and Kikuchi, Y.
    Extracellular tRNAs of the Marine Photosynthetic Bacterium Rhodovulum sulfidophilum Are Not Aminoacylated. Biosci. Biotechnol. Biochem. 73(2), 425-427. (2009)

  5. Suzuki, H., Daimon, M., Awano, T., Umekage, S., Tanaka, T., and Kikuchi, Yo.
    Characterization of extracellular DNA production and floccuration of the marine photosynthetic bacterium Rhodovulum sulfidophilum. Appl. Microbiol. Biotechnol. 84(2), 349-356. (2009)

  6. Umekage, S., and Kikuchi, Y.
    In vitro and in vivo production and purification of circular RNA aptamer. J Biotechnol. 139(4), 265-272. (2009)

  7. Suwa, S., Nagai, Y., Fujimoto, A., Kikuchi, Y., and Tanaka, T.
    Analysis on substrate specificity of Escherichia coli ribonuclease P using shape variants of pre-tRNA: proposal of subsites model for substrate shape recognition. J Biochem. 145(2), 151-160. (2009)


2008

  1. Fujimoto, A., Suwa, S., Nagai, Y., Kikuchi, Y., and Tanaka, T.
    Subsites for substrate recognition by bacterial ribonuclease P. Nucleic Acids Symp Ser (Oxf). (52), 207-208. (2008)


2007

  1. Umekage, S., and Kikuchi, Y.
    Production of circular streptavidin RNA aptamer in vivo. Nucleic Acids Symp Ser (Oxf). (51), 391-392. (2007)

  2. Tanaka, T., and Kikuchi, Y.
    Mutational analysis on the S-domain of bacterial ribonuclease P ribozyme. Nucleic Acids Symp Ser (Oxf). (51), 371-372. (2007)


2006

  1. Umekage, S., and Kikuchi, Y.
    Production of circular form of streptavidin RNA aptamer in vitro. Nucleic Acids Symp Ser (Oxf). (50), 323-324. (2006)

  2. Ando, T., Suzuki, H., Nishimura, S.,Tanaka, T., Hiraishi, A., and Kikuchi, Y.
    Characterization of Extracellular RNAs Produced by the Marine Photosynthetic Bacterium Rhodovulum sulfidophilum. J. Biochem. 139(4), 805-811. (2006)


2005

  1. Hori, Y., Rogert, M. C., Tanaka, T., Kikuchi, Y., Bichenkova, E. V., Wilton, A. N., Gbaj, A., and Douglas, K. T.
    Porphyrins and porphines bind strongly and specifically to tRNA, precursor tRNA and to M1 RNA and inhibit the ribonuclease P ribozyme reaction. Biochim. Biophys. Acta 1710, 47-55 (2005)

  2. Tanaka, T., Nagai, Y., and Kikuchi, Y.
    Substrate shape preference of Escherichia coli ribonuclease P ribozyme and holo enzyme using bottom-half part-shifting variants of pre-tRNA. Biosci Biotechnol Biochem. 69(10), 1992-1994. (2005)

  3. Tanaka, T., Kanda, N., and Kikuchi, Y.
    Regulation of ribozyme activity by engineered protein switch. Nucleic Acids Symp Ser (Oxf). (49), 343-344. (2005)


2004

  1. Tomita, S., Tsuge, K., Kikuchi, Y., and Itaya, M.
    Targeted isolation of a designated region of the Bacillus subtilis genome by recombinational transfer.Appl. Environ. Microbiol. 70(4 Apr), 2508-2513 (2004)

  2. Tomita, S., Tsuge, K., Kikuchi, Y., and Itaya, M.
    Region dependent efficiency for recombinational transfer of the Bacillus subtilis 168 genome. Biosci. Biotech. Biochem. 68(6), 1382-1384 (2004)

  3. Tanaka, T., Ando, T., Haga, S., and Kikuchi, Y.
    Examining the bases of the J3/4 domain of Escherichia coli ribonuclease P. Biosci. Biotechnol. Biochem. 68(6), 1388-1392 (2004)

  4. Hayashi, Y., Kobayashi, M., Sakaguchi, K., Iwata, N., Kobayashi, M., Kikuchi,Y., and Takahashi, Y
    Protein classification using comparative molecular interaction profile analysis system J. Bioinformatics and Computational Biology 2(3), 497-510 (2004)

  5. Tanaka, T., Kanda, N., and Kikuchi, Y.
    The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced. FEBS Letters 577, 101-104 (2004)

  6. Ando, T., Tanaka, T., and Kikuchi, Y.
    The natural intron sequence of human tyrosine pre-transfer RNA is not a temporal stabilizer for cloverleaf structure. Biosci. Biotechnol. Biochem. 68(8), 1782-1785 (2004)

  7. Ando, T., Suzuki, H., Komura, K., Tanaka, T., Hiraishi, A., and Kikuchi, Y.
    Extracellular RNAs produced by a marine photosynthetic bacterium Rhodovulum sulfidophilum. Nucleic Acids Symposium Series No.48, 165-166 (2004)

  8. Tanaka, T., Haga, S., Kanda, N., Ando, T., and Kikuchi, Y.
    Mutational analyses of neighboring domains of active center of RNase P ribozyme. Nucleic Acids Symposium Series No.48, 201-202 (2004)

  9. Haga, S., Tanaka, T., and Kikuchi, Y.
    Mutational analysis of the length of the J3/ 4 domain of Escherichia coli ribonuclease P ribozyme. Biosci. Biotechnol. Biochem. 68(12), 2630-2632 (2004)


2003

  1. Ando, T., Tanaka, T., and Kikuchi, Y.
    Substrate shape specificity of E. coli RNase P ribozyme is dependent on the concentration of magnesium ion. J. Biochem. 133, 445-451 (2003)

  2. Tanaka, T., Ando, T., Sakai, E., Hashiba, T., Hori, Y., and Kikuchi, Y.
    Escherichia coli tRNAs are resistant to the hyperprocessing reaction by homologous E. coli ribonuclease P ribozyme. Biosci. Biotech. Biochem. 67(5), 1172-1176 (2003)

  3. Ando, T., Tanaka, T., and Kikuchi, Y.
    Comparative analyses on hairpin substrate recognition by E. coli and B. subtilis RNase P ribozymes. Biosci. Biotechnol. Biochem. 67(8), 1825-1827 (2003)

  4. Hayashi, Y., Sakaguchi, K., Kobayashi, M., Kobayashi, M., Kikuchi,Y., and Ichiishi, E.
    Molecular evaluation using in silico protein interaction profiles. Bioinformatics 19(2), 1514-1523 (2003)

  5. Tanaka, T., Ando, T., and Kikuchi, Y.
    Revisiting the substrate recognition of bacterial ribonuclease P: in the view of the recognition of the base N73 in the substrate. Nucleic Acids Res. Supplement No.3, 275-276 (2003)

  6. Nishimura, S., Tanaka, T., Fujita, K., Itaya, M., Hiraishi, A., and Kikuchi, Y.
    Extracellular DNA and RNA produced by a marine photosynthetic bacterium Rhodovulum sulfidophilum. Nucleic Acids Res. Supplement No.3, 279-280 (2003)

  7. Nagai, Y., Ando, T., Tanaka, T., and Kikuchi, Y.
    Recognition of tRNA bottom half by bacterial ribonuclease P. Nucleic Acids Res. Supplement No.3, 281-282 (2003)

  8. Ando, T., Tanaka, T., and Kikuchi, Y.
    Bacterial ribonuclease P reaction is affected by substrate shape and magnesium ion concentration. Nucleic Acids Res. Supplement No.3, 293-294 (2003)

  9. Tomita, S., Tsuge, K., Kikuchi, Y., and Itaya, M.
    Application of recombination transfer to the cognate Bacillus subtilis genome. Nucleic Acids Res. Supplement No.3, 295-296 (2003)

  10. Ando, T., Tanaka, T., and Kikuchi, Y.
    The protein component of Bacterial ribonuclease P flickers the metal ion response to the substrate shape preference of the ribozyme. Biosci. Biotechnol. Biochem. 67(10), 2294-2296 (2003)

  11. 菊池 洋
    アプタマー:進化の機構を利用した新機能の創製.  生物工学会誌 81 (2), 77(2003)

  12. 菊池 洋
    アプタマー:自在に創製できる?超人工抗体.けんさ 32 (4), 26-33(2003)



2002

  1. Tanaka, T., Hori, Y., and Kikuchi, Y.
    Guide DNA technique in bacterial ribonuclease P reaction for effective processing of tRNA precursor. Biotechnol. Appl. Biochem. 36, 85-88 (2002)

  2. Tanaka, T., Kondo, Y., Hori, Y., and Kikuchi, Y.
    Another cut for lysine tRNA: Application of the hyperprocessing reaction reveals another stabilization strategy in metazaon lysine tRNAs. J. Biochem. 131, 839-847 (2002)

  3. Ando, T., Tanaka, T., Hori, Y., and Kikuchi, Y.
    Kinetic analysis on hyperprocessing reaction of human tyrosine tRNA by E. coli ribonuclease P ribozyme. Biosci. Biotechnol. Biochem. 66, 1967-1971 (2002)

  4. Ando, T., Tanaka, T., Hori, Y., and Kikuchi, Y.
    Regulation of bacterial RNase P ribozyme by divalent cation and guide DNA. Nucleic Acids Symp. Ser. No. 2, 271-272(2002)

  5. Hori, Y., Bichenkova, E. V., Wilton, A. N., Tanaka, T., Douglas, K. T. and Kikuchi, Y.
    Porphyrins and porphinesinhibit the ribonuclease P reaction in vitro. Nucleic Acids Symp. Ser. No. 2, 111-112(2002)

  6. 田中照通、菊池 洋
    RNA酵素は生命の謎解きをできるのか?  生体の科学 53 (2), 136-141 (2002)

2001

  1. Hori, Y., Bichenkova, E. V., Wilton, A. N., El-Attug, M. N., Sadat-Ebrahimi, S., Tanaka, T., Kikuchi, Y., Araki, M., Sugiura, Y., and Douglas, K. T.
    Synthetic inhibitors of the processing of pre-transfer RNA by the ribonuclease P ribozyme: enzyme inhibitors which act by binding to substrate. Biochemistry 40, 603-608 (2001)

  2. Tanaka, T., Baba, H., Hori, Y. and Kikuchi, Y.
    Guide DNA technique reveals that the protein component of bacterial ribonuclease P is a modifier for substrate recognition. FEBS Letters 491, 94-98 (2001)
  3. Tanaka, T., Inui, O., Dohi, N., Okada, N., Okada, H., and Kikuchi, Y.
    Is your ribozyme design really correct?: A proposal of simple single turnover competition assay to evaluate ribozymes. Biosci. Biotechnol. Biochem. 65, 1636-1644 (2001)

  4. Ando, T., Tanaka, T., Hori, Y., Sakai, E., and Kikuchi, Y.
    Human tyrosine tRNA is also internally cleavable by E. coli ribonuclease P RNA ribozyme in vitro. Biosci. Biotechnol. Biochem. 65, 2798-2801 (2001)

  5. Hori, Y., Sakai, E., Tanaka, T., and Kikuchi, Y.
    Hyperprocessing reaction of tRNA by Bacillus subtilis ribonuclease P ribozyme. FEBS Lett. 505, 337-339 (2001)

  6. Tanaka, T., and Kikuchi, Y.
    Origin of cloverleaf shape of transfer RNA --- the double hairpin model: Implication for the role of the tRNA intron and the long extra loop. Viva Origino 29, 134-142 (2001)

  7. Hori, Y., Tanaka, T., and Kikuchi, Y.
    In vitro hyperprocessing of tRNAs by Bacillus subtilis ribonuclease P RNA. Nucleic Acids Res. Suppl. No.1, 209-210 (2001)

  8. 田中照通、菊池 洋
    工業を持続可能にするバイオテクノロジー 「科学技術入門シリーズ8 エコテクノロジー入門」 6-18, 朝倉書店 (2001)


2000

  1. Hori, Y., Tanaka, T., and Kikuchi, Y.
    The catalytic RNA of RNase P from Escherichia coli cleaves Drosophila 2S ribosomal RNA in vitro: a new type of naturally occurring substrate for the enzyme. FEBS Letters 472, 187-190 (2000)

  2. Hori, Y., Baba, H., Ueda, R., Tanaka, T., and Kikuchi, Y.
    In vitro hyperprocessing of Drosophila tRNAs by the catalytic RNA of RNase P: the cloverleaf structure of tRNA is not always stable ? Eur. J. Biochem. 267, 4781-4788(2000)

  3. Tanaka,T., Kikuchi, Y., Matsuzawa,H., and Ohta,T.
    Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, Ser102 and Gly131. Biosci. Biotechnol. Biochem. 64, 2008-2011 (2000)

  4. Hori, Y., Tanaka, T., and Kikuchi, Y.
    In vitro cleavage of Drosophila 2S rRNA by M1 RNA. Nucleic Acids Symposium Serries 44, 93-94 (2000)

  5. 菊池 洋
    RNA配列の解析 「基礎生化学実験法4[核酸・遺伝子実験(I. 基礎編)]」日本生化学会編, 175-192, 東京化学同人 (2000)


1999

  1. Tanaka,T., Matsuzawa,H., and Ohta,T.
    Substrate specificity of aqualysin I altered by an organic solvent, DMSO. Biosci. Biotechnol. Biochem. 63, 446-448 (1999)

  2. Tanaka,T., Matsuzawa,H., andOhta,T.
    Identification and designing of S3 site of aqualysin I, a thermophilic subtilisin-related serine protease. J. Biochem. 125, 1016-1021 (1999)

  3. Takeno, H., Yamamoto, S., Tanaka, T., Sakano, Y., and Kikuchi, Y.
    Selection of RNA molecule that specifically inhibits the protease activity of subtilisin. J. Biochem.125, 1115-1119 (1999)

  4. Yamamoto, S., Saito, S., Tanaka, T., and Kikuchi, Y.

    Specific RNA protease inhibitors from in vitro selection. Nucleic Acids Symposium Series 42, 215-216 (1999)

  5. Inui, O., Kikuchi, Y., Dohi, N., Okada, N., Okada, H., and Tanaka, T.
    Comparative study of two ribozymes and DNA-enzyme against the same RNA target. Nucleic Acids Symposium Series 42, 217-218 (1999)

  6. Hori, Y., Hashida, S., Koike, M., Tanaka, T., and Kikuchi, Y.
    Drosophila tRNAs hyperprocessing in vitro by ribonuclease P.
    Nucleic Acids Symposium Series 42, 259-260 (1999)

  7. 菊池 洋
    変身したRNA像−新しい遺伝子治療・新しい生命観−.日本獣医師会雑誌 52, (1), 1-5 (1999)

  8. 菊池 洋
    逆転写とスプライシング.わかりやすい分子生物学, 菊池韶彦、村松喬、榊 佳之 編, 42-56, 丸善, 東京(1999)


1998

  1. Tanaka,T., Yamamoto,S., Takeno, H., Sakano, Y. and Kikuchi, Y.
    In vitro selection of RNA protease inhibitors. Nucleic Acids Symposium Series 39, 215-216 (1998)

  2. Hori, Y., Tanaka, T. and Kikuchi, Y.
    In vitro hyperprocessing of Drosophila tRNAs by M1 RNA. Nucleic Acids Symposium Series 39, 151-152 (1998)

  3. Tanaka,T., Matsuzawa,H., and Ohta,T.
    Stability of thermostable enzyme, aqualysin I ; a subtilisin-type serine protease from Thermus aquaticus YT-1. Biosci. Biotechnol. Biochem.62, 1806-1808 (1998)

  4. Tanaka,T., Matsuzawa,H., Kojima,S., Kumagai,I., Miura,K., and Ohta,T.
    P1-specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor. Biosci. Biotechnol. Biochem. 62, 2035-2038 (1998)

  5. Tanaka,T., Matsuzawa,H., and Ohta,T.
    Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: comparison with proteinase K, subtilisin BPN' and subtilisin Carlsberg. Biosci. Biotechnol. Biochem. 62, 2161-2165 (1998)

  6. Tanaka,T., Matsuzawa,H., and Ohta,T.
    Engineering of S2 site of aqualysin I; Alteration of P2-specificity by excluding P2 side chain. Biochemistry 37, 17402-17407 (1998)

  7. 菊池 洋
    核酸非関連タンパク質に相互作用をもつ核酸の創製.豊橋技術科学大学技術開発分析計測工作センター年報 第17号, 122-124 (1998)


1997

  1. Takeno,H., Tanaka,T., Kikuchi,Y.
    RNA aptamers to a protease, subtilisin. Nucleic Acids Symposium Series 37, 249-250 (1997)

  2. Inui,O., Tanaka,T., Dohi,N., Okada,H., Kikuchi,Y.
    Design and in vitro activity of ribozymes against mRNA of a rat membrane inhibitor of complement. Nucleic Acids Symposium Series 37, 223-224 (1997)

  3. Hisamatsu,S., Morikawa,Y., Tomita,R., Tanaka,T., Sonoki,S., Kikuchi,Y.
    In vitro activityof the hairpin ribozyme derived from the negative strand of Arabis mosaic virus satellite RNA. J. Biochem. 122, 352-357 (1997)

  4. 菊池 洋、田中照通、百瀬春生
    微生物の起源と進化.「生物工学基礎コース 微生物工学」百瀬春生 編
     78-93, 丸善, 東京 (1997)

  5. 菊池 洋
    リボザイム. medicina 34, (12) 2205-2207 (1997)


1996

  1. Tomita,R., Hisamatsu,S., Kikuchi,A., Tanaka,T., Kikuchi,Y. and Sonoki,S.
    Design of hairpin ribozyme against immediate-early mRNA of Pseudorabies virus. Nucleic Acids Symposium Series 35, 193-194 (1996)

  2. Kikuchi, Y.
    RNase P as hyperprocessing enzyme: Amodel for formation of a biologically functional tRNA fragment. Mol. Biol. Rep. 22, 171-175 (1996)


1995

  1. Tomita,R., Morikawa,Y., Hisamatsu,S., Suzuki-Fujita,K., Tanaka,T., Sonoki,S., and Kikuchi,Y.
    Cis and trans reactions of hairpin ribozymes derived from the negative strand of arabis mosaic virus satellite RNA. Nucleic Acids Symposium Series 34, 117-118 (1995)

  2. Kikuchi, Y., and Suzuki-Fujita, K.
    Synthesis and self-cleavage reaction of a chimeric molecule between RNase P-RNA and its model substrate. J. Biochem. 117, 197-200 (1995)

  3. Hisamatsu, S., Sonoki, S., and Kikuchi, Y.
    Hairpin ribozyme-mediated cleavage of the full-length ?-glucuronidase (GUS) mRNA. Biosci. Biotech. Biochem. 59, 294-297 (1995)

  4. 菊池 洋
    大きなリボザイムの分子進化工学現代化学増刊28「新しい酵素研究法」 一島英治、小野寺一清 編, 130-139, 東京化学同人 (1995)

  5. 菊池 洋
    RNA の酵素活性「英語論文セミナー 現代の分子生物学」丸山工作監修、渡辺公綱、桂勲 編, 65-74, 講談社 (1995)

  6. 菊池 洋、柴 忠義
    切られて働く tRNA 蛋白質核酸酵素 40 (4) 表紙および 441 (1995)


1994

  1. Morikawa, Y., Hisamatsu, S., Suzuki-Fujita, K., and Kikuchi, Y.
    Ribozyme activity of the hairpin domain of the negative strand of arabis mosaic virus satellite RNA Nucleic Acids Symposium Series No. 31, 263-264 (1994)

  2. Hisamatsu, S., Sonoki, S., Suzuki-Fujita, K., and Kikuchi, Y.
    Design of hairpin ribozymes against ?-glucuronidase mRNA. Nucleic Acids Symposium Series No. 31, 195-196 (1994)
  3. 菊池 洋
    リボザイム−触媒機能をもつRNA 生物の科学 遺伝(裳華房) 48, (7) 39-44 (1994)

  4. 菊池 洋
    分子進化工学とリボザイム バイオサイエンスとインダストリー(JBA) 52, (8) 648-650 (1994)
     


1993

  1. Kikuchi,Y., Sasaki-Tozawa N., and Suzuki,K.
    Artificial self-cleaving molecules containing of an rRNA precursor and the catalytic RNA of RNase P. Nucleic Acids Res 21, 4685-4689 (1993)

  2. Ito, M., Sasaki, N., and Kikuchi, Y.
    Natural catalytic RNA with ribonuclease P activity from Thermus thermophilus. Biosci. Biotech. Biochem. 57, 655-656 (1993)

  3. Hisamatsu, S., Sonoki, S., and Kikuchi, Y.
    Acquirement of hairpin ribozyme activity by the long substrate-binding site. Nucleic Acids Symposium Series No. 29, 173-174 (1993)

  4. Fujitani, K., Sasaki-Tozawa, N., and Kikuchi, Y.
    Different target-site specificities of the hairpin ribozyme in cis- and trans-cleavages. FEBS Letters 331, 155-158 (1993)

  5. 菊池 洋、佐々木規子
    リボザイムの酵素的合成と反応 「新生化学実験講座13(バイオテクノロジー)」日本生化学会編 34-42 東京化学同人 (1993)


1992

  1. Kikuchi, Y. and Sasaki, N.
    Hyperprocessing of tRNA by the catalytic RNA of RNase P: Cleavage of a natural tRNA within the mature tRNA sequence and evidence for an altered conformation of the substrate tRNA
    J. Biol. Chem. 267, 11972-11976 (1992)

  2. 菊池 洋
    連載講座 RNA 酵素の設計と合成−1 RNA 酵素の種類と in vitro 活性−ハンマーヘッド型、ヘアピン型リボザイムを中心に 化学と生物 30, 112-118 (1992)

  3. 菊池 洋
    ハイパープロセシング:tRNA の二次構造変化と切断による新たな機能発現 Cell Science 8, 658-666 (1992)


1991

  1. Kikuchi, Y. and Sasaki, N.
    Site-specific cleavage of natural mRNA sequences by newly designed hairpin catalytic RNAs. Nucleic Acids Res. 19, 6751-6755 (1991)


1990

  1. Kikuchi, Y., Sasaki, N., and Ando-Yamagami, Y.
    Cleavage of tRNA within the mature tRNA sequence by the catalytic RNA of RNase P: Implication for the formation of the primer tRNA fragment for reverse transcription in copia retrovirus-like particles. Proc. Natl. Acad. Sci. USA 87, 8105-8109 (1990)

  2. Takahashi, M., Toriyama, S., Kikuchi, Y., Hayakawa, T., and Ishihama, A.
    Complementarity between the 5'- and 3'-terminal sequences of rice stripe virus RNAs. J. Gen. Virol. 71, 2817-2821 (1990)


1989

  1. Kikuchi, Y., Ando, Y., Ichimura, N., and Noda, A.
    Exoribonuclease activity of purified reverse transcriptase preparations from retrovirus. J. Biochem. 105, 974-978 (1989)

  2. Kikuchi, Y. and Ando, Y.
    Molecular cloning of a ribozyme gene of Escherichia coli using polymerase chain reaction (PCR). Agric. Biol. Chem. 53, 2005-2008 (1989)


1988

  1. Kikuchi, Y.
    From RNA world to DNA world - Molecular biological approach to the origin of life. Viva Origino 16, 132-134 (1988)

  2. Nagamatsu, M., Kikuchi, Y., and Igarashi, A.
    Terminal sequences of the replicative form of RNA of Japanese encephalitis virus. Acta Virologica 32, 75-78 (1988)

  3. Shinozuka, K., Kikuchi, Y., Nishino, C., Mori, A., and Tawata, S.
    Inhibitory effect of flavonoids on DNA-dependent DNA and RNA polymerases. Experientia 44, 882-885 (1988)

  4. 菱沼文男、菊池 洋、徳永正雄、平井啓子、和田直美、北田邦夫
    酵母線状 DNA プラスミドの構造と機能 酵母のバイオテクノロジー 基礎と応用 平野 正 編 25-37 学会出版センター (1988)

  5. 菊池 洋
    RNA 酵素 日本醸造協会誌 83, 93-98 (1988)

  6. 菊池 洋
    RNA の一次構造解析 医学、生物学分野におけるRNA研究の最前線− 構造、機能、発現の解析とその技術的アプローチ J. I. P. Co. 51-56 (1988)


1987

  1. Kikuchi, Y.
    Molecular biological approach to the origin of life. Proceedings of Space Life Science Colloquium - Primitive Enzyme and Primitive Gene, Origin of Genetic Code 28-30, Institute of Space & Astronautical Science, Tokyo (1987)

  2. Sumiyoshi, H., Mori, C., Fuke, I., Morita, K., Kuhara, S., Kondou, J., Kikuchi, Y., Nagamatsu, M., and Igarashi, A.
    Complete nucleotide sequence of the Japanese encephalitis virus genome RNA. Virology 161, 497-510 (1987)

  3. 菊池 洋
    現細胞から生命の起源を探る 科学 57, 94-97 (1987)


1986

  1. Kikuchi, Y., Ando, Y., and Shiba, T.
    Unusual priming mechanism of RNA-directed DNA systhesis in copia retrovirus-like particles of Drosophila. Nature 323, 824-826 (1986)


特許

特許一覧

  1. 出願日:平成19年11月14日
    共同研究者:菊池洋、田中照通、梅影創、鈴木宏道
    名称:「RNA製造方法」 取得番号:特願2007−295188号


  2. 出願日:平成20年11月14日
    共同研究者:菊池洋、田中照通、梅影創、鈴木宏道
    名称:「RNA製造方法及びプロモーター」 取得番号:PCT/ JP2008/ 070749



























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