名古屋大学大学院工学研究科 生命分子工学専攻
名古屋大学工学部化学生命工学科 生体分子応用化学
PUBLICATIONS
論文発表
- H. Kosugi, H. Nakanishi, G. Hayashi, H. Murakami*, Improvement of cDNA TRAP Display via Optimization of Puromycin Linker Design for Enhanced Discovery of Antibody-Like Proteins. ChemBioChem, 2026, 27, e70375.
https://doi.org/10.1002/cbic.70375 - T. Miyazaki†, T. Fujino†, T. Yoshii, H. Kosugi, M. Funane, N. Murata, K. C. Nguyen, S. Nagatoishi, K. Tsumoto, G. Hayashi, H. Murakami*, S. Tsukiji*, De novo chemo-optogenetics through the rational design of photoresponsive molecules and selection of their artificial protein binding pairs. Nature Chemistry, 2026, 18, 1286-1297.
https://doi.org/10.1038/s41557-026-02121-w - K. Endo, S. Umemoto, N. Tsuzuki, H. Okumura, Y. Sato, T. Yoshii*, S. Tsukiji, S. Nagano, H. Murakami*, T. Hino*, Crystallization and X-ray structure of a highly aggregation-prone monobody engineered for high-affinity small-molecule recognition. Acta Crystallographica Section F:Structural Biology Communications, 2026, F82, 75-82.
https://doi.org/10.1107/S2053230X26000798 - K. Nakatsu, F. Yoshitomi, H. Onoda, R. Shikimachi, K. Arita, A. Okamoto*, H. Murakami*, G. Hayashi*, Chemical Protein Synthesis via Direction-Switching One-Pot Peptide Ligation Enabled by Orthogonal Cysteinyl Protection. J. Am. Chem. Soc. 2026, 148, 4622-4634.
https://doi.org/10.1021/jacs.5c20510 - N. Iwamoto, S. Ohno, K. Nakamura, T. Naito, S. Miura, S. Inuki, H. Ohno, G. Hayashi, H. Murakami, S. Oishi*, Design and Evaluation of Stable Cysteine-Modified Monobody Scaffolds for Mirror-Image Synthesis. Bioconjugate Chemistry, 2025, 36, 1504-1515.
https://doi.org/10.1021/acs.bioconjchem.5c00181 - G. Hayashi*, T. Naito, S. Miura, N. Iwamoto, Y. Usui, M. Bando-Shimizu, S. Suzuki, K. Higashi, M. Nonaka*, S. Oishi*, H. Murakami*, Generating a mirror-image monobody targeting MCP-1 via TRAP display and chemical protein synthesis. Nature Communications, 2024, 15, 10723.
https://doi.org/10.1038/s41467-024-54902-x - H. Tagawa†, R. Saeki†, C. Yamamoto†, K. Tanito, C. Tanaka, S. Munekawa, T. Nii, A. Kishinuma, H. Murakami, T. Mori*, Y. Katayama*, The effect of Fc region affinity of protein-based antibody-recruiting molecules on antibody-dependent cellular cytotoxicity. RSC Advances, 2024, 14, 22860-22866.
https://doi.org/10.1039/d4ra03391d - T. Fujino, R. Sonoda, T. Higashinagata, E. Mishiro-Sato, K. Kano, H. Murakami*, Ser/Leu-swapped cell-free translation system constructed with natural/in vitro transcribed-hybrid tRNA set. Nature Communications, 2024, 15, 4143.
https://doi.org/10.1038/s41467-024-48056-z - K. Yamano*, M. Sawada, R. Kikuchi, K. Nagataki, W. Kojima, R. Endo, H. Kinefuchi, A. Sugihara, T. Fujino, A. Watanabe, K. Tanaka, G. Hayashi, H. Murakami, N. Matsuda, Optineurin provides a mitophagy contact site for TBK1 activation. The EMBO Journal, 2024, 43 (5), 754-779.
https://doi.org/10.1038/s44318-024-00036-1 - S. Umemoto, T. Kondo, T. Fujino, G. Hayashi, H. Murakami*, Large-scale analysis of mRNA sequences localized near the start and amber codons and their impact on the diversity of mRNA display libraries. Nucleic Acids Research, 2023, 51, 7465-7479.
https://doi.org/10.1093/nar/gkad555 - S. Suzuki, Y. Nakajima, N. Kamo, A. Osakabe, A. Okamoto, G. Hayashi*, H. Murakami*, Thiocholine-Mediated One-Pot Peptide Ligation and Desulfurization. Molecules, 2023, 28, 3655.
https://doi.org/10.3390/molecules28093655 - K. Nakatsu, A. Okamoto*, G. Hayashi*, H. Murakami*, Repetitive Thiazolidine Deprotection Using a Thioester-Compatible Aldehyde Scavenger for One-Pot Multiple Peptide Ligation. Angewandte Chemie International Edition, 2022, 61, 39, e202206240.
https://doi.org/10.1002/anie.202206240 - T. Kondo, K. Matsuoka, S. Umemoto, T. Fujino, G. Hayashi, Y. Iwatani*, H. Murakami*, Monobodies with potent neutralizing activity against SARS-CoV-2 Delta and other variants of concern. Life Science Alliance, 2022, 5, 6, e202101322.
https://doi.org/10.26508/lsa.202101322 - T. Kondo, M. Eguchi, N. Tsuzuki, N. Murata, T. Fujino, G. Hayashi, H. Murakami*, Construction of a Highly Diverse mRNA Library for in vitro Selection of Monobodies. Bio-Protocol, 2021, 11(16), e4125.
https://doi.org/10.21769/BioProtoc.4125 - T. Kondo, M. Eguchi, S. Kito, T. Fujino, G. Hayashi, H. Murakami*, cDNA TRAP display for rapid and stable in vitro selection of antibody-like proteins. Chemical Communications, 2021, 57, 2416-2419.
https://doi.org/10.1039/D0CC07541H - N. Kamo, T. Kujirai, H. Kurumizaka, H. Murakami, G. Hayashi*, A. Okamoto*, Organoruthenium-Catalyzed Chemical Protein Synthesis to Elucidate the Functions of Epigenetic Modifications on Heterochromatin Factors. Chemical Science, 2021, 12, 5926-5937.
https://doi.org/10.1039/D1SC00731A - T. Kondo, Y. Iwatani, K. Matsuoka, T. Fujino, S. Umemoto, Y. Yokomaku, K. Ishizaki, S. Kito, T. Sezaki, G. Hayashi, H. Murakami*, Antibody-like proteins that capture and neutralize SARS-CoV-2. Science Advances, 2020, 6(42), eabd3916.
https://doi.org/10.1126/sciadv.abd3916 - T. Fujino, M. Tozaki, H. Murakami*, An amino acid-swapped genetic code. ACS Synthetic Biology, 2020, 9(10), 2703-2713.
https://doi.org/10.1021/acssynbio.0c00196 - T. Fujino, T. Kondo, H. Suga, H. Murakami*, Exploring the Minimal RNA Substrate of Flexizymes. ChemBioChem, 2019, 20(15),1959-1965.
https://doi.org/10.1002/cbic.201900150 - N. Taniguchi, H. Murakami*. Multiple Site-Directed and Saturation Mutagenesis by the Patch Cloning Method. Methods in Molecular Biology, 2017, 1498, 339-347.
https://doi.org/10.1007/978-1-4939-6472-7_22 - Y. Iwane, A. Hitomi, H. Murakami, T. Katoh, Y. Goto, H. Suga*, Expanding the amino acid repertoire of ribosomal polypeptide synthesis via the artificial division of codon boxes. Nature Chemistry, 2016, 8, 4, 317-325.
https://doi.org/10.1038/nchem.2446 - T. Fujino, Y. Goto, H. Suga, H. Murakami*, Ribosomal synthesis of peptides with multiple ß-amino acids. J. Am. Chem. Soc. 2016, 138, 6, 1962-1969.
https://doi.org/10.1021/jacs.5b12482 - T. Fujino, H. Murakami*, In vitro selection combined with ribosomal translation containing non-proteinogenic amino acids. The Chemical Record, 2016, 16, 1, 365-377. (Review article)
https://doi.org/10.1002/tcr.201500239 - S. Adachi, M. Homoto, R. Tanaka, Y. Hioki, H. Murakami, H. Suga, M. Matsumoto, K. Nakayama, T. Hatta, S. Iemura, T. Natsume*, ZFP36L1 and ZFP36L2 control LDLR mRNA stability via the ERK–RSK pathway. Nucleic Acids Research, 2014, 42, 10037-10049.
https://doi.org/10.1093/nar/gku652 - T. Kawakami*, T. Sasaki, P. C. Reid, H. Murakami*, Incorporation of electrically charged N-alkyl amino acids into ribosomally synthesized peptides via post-translational conversion. Chemical Science, 2014, 5, 887-893.
https://doi.org/10.1039/c3sc52744a - Y. Goto, M. Iseki, A. Hitomi, H. Murakami, H. Suga*, Nonstandard Peptide Expression under the Genetic Code Consisting of Reprogrammed Dual Sense Codons. ACS Chemical Biology, 2013, 8, 2630-2634.
https://doi.org/10.1021/cb400549p - N. Taniguchi, S. Nakayama, T. Kawakami, H. Murakami*, Patch cloning method for multiple site-directed and saturation mutagenesis. BMC Biotechnology, 2013, 13:91.
https://doi.org/10.1186/1472-6750-13-91 - T. Kawakami*, T. Ishizawa, H. Murakami*, Extensive reprogramming of the genetic code for genetically encoded synthesis of highly N-alkylated polycyclic peptidomimetics. J. Am. Chem. Soc. 2013, 135, 12297-12304.
https://doi.org/10.1021/ja405044k - T. Kawakami, T. Ishizawa, T. Fujino, P. C. Reid, H. Suga, H. Murakami*, In Vitro Selection of Multiple Libraries Created by Genetic Code Reprogramming To Discover Macrocyclic Peptides That Antagonize VEGFR2 Activity in Living Cells. ACS Chemical Biology, 2013, 8, 1205-1214.
https://doi.org/10.1021/cb300697h - T. Ishizawa, T. Kawakami, P. C. Reid, H. Murakami*, TRAP display: a high-speed selection method for the generation of functional polypeptides. J. Am. Chem. Soc. 2013, 135, 5433-5440.
https://doi.org/10.1021/ja312579u - T. Fujino, Y. Goto, H. Suga, H. Murakami*, Reevaluation of the D-Amino Acid Compatibility with the Elongation Event in Translation. J. Am. Chem. Soc. 2013, 135, 1830-1837.
https://doi.org/10.1021/ja309570x - T. Kawakami, H. Murakami*, Genetically encoded libraries of nonstandard peptides. Journal of Nucleic Acids, 2012, 2012, 713510. (Review article)
https://doi.org/10.1155/2012/713510 - T. Kawakami, A. Ohta, M. Ohuchi, H. Ashigai, H. Murakami, H. Suga*, Diverse backbone-cyclized peptides via codon reprogramming. Nature Chemical Biology, 2009, 5, 888-890.
https://doi.org/10.1038/nchembio.259 - N. Niwa, Y. Yamagishi, H. Murakami, H. Suga*, A flexizyme that selectively charges amino acids activated by a water-friendly leaving group. Bioorganic & Medicinal Chemistry Letters, 2009, 19, 3892-3894.
https://doi.org/10.1016/j.bmcl.2009.03.114 - Y. Yamagishi, H. Ashigai, Y. Goto, H. Murakami, H. Suga*, Ribosomal synthesis of cyclic peptides with a fluorogenic oxidative coupling reaction. ChemBioChem, 2009, 10, 1469-1472.
https://doi.org/10.1002/cbic.200900021 - E. Nakajima, Y. Goto, Y. Sako, H. Murakami, H. Suga*, Ribosomal Synthesis of Peptides with C-Terminal Lactams, Thiolactones, and Alkylamides. ChemBioChem, 2009, 10, 1186-1192
https://doi.org/10.1002/cbic.200900058 - H. Murakami*, A. Ohta, H. Suga*, Bases in the anticodon loop of tRNA(Ala)(GGC) prevent misreading. Nature Structural & Molecular Biology, 2009, 16, 353-358.
https://doi.org/10.1038/nsmb.1580 - Y. Goto, K. Iwasaki, K. Torikai, H. Murakami, H. Suga*, Ribosomal synthesis of dehydrobutyrine- and methyllanthionine-containing peptides. Chemical Communications, 2009, 3419-3421.
https://pubs.rsc.org/en/content/articlelanding/2009/cc/b904314d - T. Kawakami, H. Murakami, H. Suga*, Messenger RNA-programmed incorporation of multiple N-methyl-amino acids into linear and cyclic peptides. Chemistry & Biology, 2008, 15, 32-42.
https://doi.org/10.1016/j.chembiol.2007.12.008 - T. Kawakami, H. Murakami, H. Suga*, Ribosomal synthesis of polypeptoids and peptoid-peptide hybrids. J. Am. Chem. Soc. 2008, 130, 16861-16863.
https://pubs.acs.org/doi/10.1021/ja806998v - A. Ohta, H. Murakami, H. Suga*, Polymerization of alpha-hydroxy acids by ribosomes. ChemBioChem, 2008, 9, 2773-2778.
https://doi.org/10.1002/cbic.200800439 - H. Xiao, H. Murakami, H. Suga, A. R. Ferre-D'Amare*, Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme. Nature, 2008, 454, 358-361.
https://doi.org/10.1038/nature07033 - Y. Goto, H. Murakami, H. Suga*, Initiating translation with D-amino acids. RNA, 2008, 14, 1390-1398.
https://doi.org/10.1261/rna.1020708 - Y. Sako, J. Morimoto, H. Murakami, H. Suga*, Ribosomal synthesis of bicyclic peptides via two orthogonal inter-side-chain reactions. J. Am. Chem. Soc. 2008, 130, 7232-7234.
https://doi.org/10.1021/ja800953c - Y. Sako, Y. Goto, H. Murakami, H. Suga*, Ribosomal synthesis of peptidase-resistant peptides closed by a nonreducible inter-side-chain bond. ACS Chemical Biology, 2008, 3, 241-249.
https://doi.org/10.1021/cb800010p - Y. Goto, A. Ohta, Y. Sako, Y. Yamagishi, H. Murakami, H. Suga*, Reprogramming the translation initiation for the synthesis of physiologically stable cyclic peptides. ACS Chemical Biology, 2008, 3, 120-129.
https://doi.org/10.1021/cb700233t - A. Ohta, H. Murakami, E. Higashimura, H. Suga*, Synthesis of polyester by means of genetic code reprogramming. Chemistry & Biology, 2007, 14, 1315-1322.
https://doi.org/10.1016/j.chembiol.2007.10.015 - M. Ohuchi, H. Murakami, H. Suga*, The flexizyme system: a highly flexible tRNA aminoacylation tool for the translation apparatus. Current Opinion in Chemical Biology, 2007, 11, 537-542. (Review article)
https://doi.org/10.1016/j.cbpa.2007.08.011 - M. Taki*, A. Kuno., S. Matoba., Y. Kobayashi., J. Futami., H. Murakami., H. Suga., K. Taira., T. Hasegawa., M. Sisido*, Leucyl/Phenylalanyl-tRNA-Protein Transferase-Mediated Chemoenzymatic Coupling of N-Terminal Arg/Lys Units in Post-translationally Processed Proteins with Non-natural Amino Acids. ChemBioChem, 2006, 7, 1676-1679.
https://doi.org/10.1002/cbic.200600181 - H. Murakami, A. Ohta, H. Ashigai, H. Suga*, A highly flexible tRNA acylation method for non-natural polypeptide synthesis. Nature Methods, 2006, 3, 357-359.
https://doi.org/10.1038/nmeth877 - D. Kourouklis, H. Murakami, H. Suga*, Programmable ribozymes for mischarging tRNA with nonnatural amino acids and their applications to translation. Methods, 2005, 36, 239-244.
https://doi.org/10.1016/j.ymeth.2005.04.001 - K. Ramaswamy, H. Saito, H. Murakami, K. Shiba, H. Suga*, Designer ribozymes: programming the tRNA specificity into flexizyme. J. Am. Chem. Soc. 2004, 126, 11454-11455.
https://doi.org/10.1021/ja046843y - T. Hohsaka*, N. Muranaka, C. Komiyama, K. Matsui, S. Takaura, R. Abe, H. Murakami, M. Sisido*, Position-specific incorporation of dansylated non-natural amino acids into streptavidin by using a four-base codon. FEBS Letters, 2004, 560, 173-177.
https://doi.org/10.1016/s0014-5793(04)00099-7 - H. Murakami, D. Kourouklis, H. Suga*, Using a solid-phase ribozyme aminoacylation system to reprogram the genetic code. Chemistry & Biology, 2003, 10, 1077-1084.
https://doi.org/10.1016/j.chembiol.2003.10.010 - H. Murakami, H. Saito, H. Suga*, A versatile tRNA aminoacylation catalyst based on RNA. Chemistry & Biology, 2003, 10, 655-662.
https://doi.org/10.1016/s1074-5521(03)00145-5 - M. Taki, T. Hohsaka, H. Murakami, K. Taira, M. Sisido*, Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs. J. Am. Chem. Soc. 2002, 124, 14586-14590.
https://doi.org/10.1021/ja017714+ - H. Murakami, N. J. Bonzagni, H. Suga*, Aminoacyl-tRNA synthesis by a resin-immobilized ribozyme. J. Am. Chem. Soc. 2002, 124, 6834-6835.
https://doi.org/10.1021/ja025872a - H. Murakami, T. Hohsaka, M. Sisido*, Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs. Nature Biotechnology, 2002, 20, 76-81.
https://doi.org/10.1038/nbt0102-76 - M. Taki, T. Hohsaka, H. Murakami, K. Taira, M. Sisido*, A non-natural amino acid for efficient incorporation into proteins as a sensitive fluorescent probe. FEBS Letters, 2001, 507, 35-38.
https://doi.org/10.1016/s0014-5793(01)02935-0 - T. Hohsaka, Y. Ashizuka, H. Taira, H. Murakami, M. Sisido*, Incorporation of nonnatural amino acids into proteins by using various four-base codons in an Escherichia coli in vitro translation system. Biochemistry, 2001, 40, 11060-11064.
https://doi.org/10.1021/bi0108204 - T. Hohsaka, Y. Ashizuka, H. Murakami, M. Sisido*, Five-base codons for incorporation of nonnatural amino acids into proteins. Nucleic Acids Research, 2001, 29, 3646-3651.
https://doi.org/10.1093/nar/29.17.3646 - H. Murakami, T. Hohsaka, Y. Ashizuka, K. Hashimoto, M. Sisido*, Site-directed incorporation of fluorescent nonnatural amino acids into streptavidin for highly sensitive detection of biotin. Biomacromolecules, 2000, 1, 118-125.
https://pubs.acs.org/doi/10.1021/bm990012g - M. Taki, H. Murakami, M. Sisido*, A chiral Eu3+-thienoyltrifluoroacetone complex on an avidin tetramer: luminescence and CD studies on the supramolecular protein-metal chelate complex. Chemical Communications, 2000, 1199-1200.
https://doi.org/10.1039/B001908I - T. Hohsaka, D. Kajihara, Y. Ashizuka, H. Murakami, M. Sisido*, Efficient incorporation of nonnatural amino acids with large aromatic groups into streptavidin in in vitro protein synthesizing systems. J. Am. Chem. Soc. 1999, 121, 34-40.
https://pubs.acs.org/doi/10.1021/ja9813109 - T. Hohsaka, Y. Ashizuka, H. Sasaki, H. Murakami, M. Sisido*, Incorporation of two different nonnatural amino acids independently into a single protein through extension of the genetic code. J. Am. Chem. Soc. 1999, 121, 12194-12195.
https://doi.org/10.1021/ja992204p.s001 - H. Murakami, T. Hohsaka, Y. Ashizuka, M. Sisido*, Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework. J. Am. Chem. Soc. 1998, 120, 7520-7529.
https://pubs.acs.org/doi/full/10.1021/ja971890u - T. Hohsaka, Y. Ashizuka, H. Murakami, M. Sisido*, Incorporation of nonnatural amino acids into streptavidin through in vitro frame-shift suppression. J. Am. Chem. Soc. 1996, 118, 9778-9779.
https://pubs.acs.org/doi/10.1021/ja9614225
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日本語の文献
- 梅本駿, 村上裕. “人工抗体の開発” 創薬の不可能を可能にする : 中分子ペプチド医薬 : 低分子と抗体の利点を兼ね備えた新モダリティで活性化・機能阻害・分子間相互作用を自在に操る!, 第2章-第2節, 羊土社 (2025).
- 梅本駿, 村上裕. “1分子ペプチドのアミノ酸配列解析は可能か −革新的なプロテオミクス技術の開発” 化学, 78(11) (2023).
- 梅本駿, 近藤太志, 藤野公茂, 林剛介, 村上裕. “mRNA配列の翻訳効率と精度への影響の網羅的解析と人工抗体・環状ペプチドの高多様性ライブラリ創製への応用” Newsletter -生体機能関連化学部会-, 37 (2), 日本化学会生体機能関連化学部会 (2022).
- 近藤太志, 梅本駿, 藤野公茂, 林剛介, 村上裕. “進化分子工学を用いた人工抗体創製とその応用” 最先端ナノライフシステム研究, 第I編-6章, 36-41, 最先端ナノライフシステム研究編集委員会 (2022).
- 近藤太志, 梅本駿, 藤野公茂, 林剛介, 村上裕. “新型コロナウイルスに対する迅速な人工抗体創製” 創薬研究者がこれだけは知っておきたい最新のウイルス学, 第10章-第7節, 技術情報協会 (2021).
- 藤野公茂. "β-アミノ酸を複数個含むペプチドの翻訳合成" Tracer, 61, 9-13 (2017).
- 藤野公茂, 後藤佑樹, 菅裕明, 村上裕 "D体アミノ酸の翻訳伸長反応への適合性" ケミカルバイオロジー, 9 (1), 11-14, 日本ケミカルバイオロジー学会 (2016).
- 石沢尭大, 川上隆史, 村上裕.“高速試験管内進化分子工学法―TRAP displayの開発と血管新生阻害ペプチド創製への応用” 進化分子工学〜高速分子進化によるタンパク質・核酸の開発, 第3編−第4章−第4節, 株式会社エヌ・ティー・エス (2013).
- 村上裕. “特殊ペプチド増幅法の開発” 日本化学会 生体機能関連化学部会 NEWS LETTER 6月号, 26 (1), 7-10, 日本化学会生体機能関連化学部会 (2011).
- 村上裕, 菅裕明. “新創薬技術RAPIDシステムとマイクロ・ナノデバイスへの期待 (特集 新世代ナノデバイス・材料の世界)” 化学工業, 59 (6), 463-469, 化学工学社 (2008).
- 村上裕. “翻訳系を用いた特殊ペプチドの合成” 生命化学研究レター, 23, 14-19 (2007).
- 川上隆史, 村上裕, 菅裕明. “遺伝暗号をリプログラミングして特殊ペプチドをつくる” 化学, 62 (8), 68-69 (2007).
- 後藤佑樹, 太田淳, 村上裕, 菅裕明. “特殊ペプチドのコンビナトリアル翻訳合成 (特集 コンビナトリアルケミストリーの新展開)” 化学工業, 58 (4), 255-262, 小峰工業出版 (2007).
- 太田淳, 村上裕, 菅裕明. “遺伝暗号のリプログラミングによるポリエステルの翻訳合成” 高分子, 56 (4), 196-199, 高分子学会 (2007).
- 村上裕, 菅裕明. “フレキシザイムを用いた遺伝暗号の拡張とリプログラミング (RNAと生命; RNAテクノロジーと創薬)” 蛋白核酸酵素, 51 (16), 2496-2501, 共立出版 (2006).
- 村上裕, 菅裕明. “テクノ・トレンド フレキシザイム--遺伝暗号の拡張とリプログラミングへの応用” バイオテクノロジージャーナル:研究の現場で活用できる先端技術と実用化の情報誌, 6 (6), 734-737, 羊土社 (2006).
- 村上裕, 菅裕明, 平尾一郎. “セントラルドグマをつくりかえる (特集 生命をデザインする合成生物学)” Bionics, 3 (3), 34-39, オーム社 (2006).
- 村上裕, 菅裕明. “人工リボザイム:試験管内分子進化と非天然アミノ酸変異法への応用 (化学と生物学の接点がつくるニューバイオテクノロジー; 新規遺伝子と蛋白質を創製する)" 蛋白質核酸酵素, 48 (11), 1511-1518, 共立出版 (2003).
- 村上裕, 芳坂貴弘, 宍戸昌彦. "新規変異タンパク質創出のためのランダム挿入削除変異法" BIOベンチャー, 2 (4), 94-97, 羊土社 (2002).
