M
Masatoshi Mori
Researcher at National Institute of Advanced Industrial Science and Technology
Publications - 8
Citations - 398
Masatoshi Mori is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Amino acid & Proteome. The author has an hindex of 5, co-authored 8 publications receiving 364 citations.
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Journal ArticleDOI
Human protein factory for converting the transcriptome into an in vitro-expressed proteome,.
Naoki Goshima,Yoshifumi Kawamura,Akiko Fukumoto,Aya Miura,Reiko Honma,Ryohei Satoh,Ai Wakamatsu,Ai Wakamatsu,Junichi Yamamoto,Kouichi Kimura,Tetsuo Nishikawa,Taichi Andoh,Yuki Iida,Kumiko Ishikawa,Emi Ito,Naoko Kagawa,Chie Kaminaga,Keiichi Kanehori,Bunsei Kawakami,Kiyokazu Kenmochi,Rie Kimura,Miki Kobayashi,Toshihiro Kuroita,Hisashi Kuwayama,Yukio Maruyama,Kiyoshi Matsuo,Kazuyoshi Minami,Mariko Mitsubori,Masatoshi Mori,Riyo Morishita,Atsushi Murase,Akira Nishikawa,Shigemichi Nishikawa,Toshihiko Okamoto,Noriko Sakagami,Yutaka Sakamoto,Yukari Sasaki,Tomoe Seki,Saki Sono,Akio Sugiyama,Tsuyoshi Sumiya,Tomoko Takayama,Yukiko Takayama,Hiroyuki Takeda,Takushi Togashi,Kazuhide Yahata,Hiroko Yamada,Yuka Yanagisawa,Yaeta Endo,Fumio Imamoto,Yasutomo Kisu,Shigeo Tanaka,Takao Isogai,Jun-ichi Imai,Shinya Watanabe,Nobuo Nomura +55 more
TL;DR: A foundation for simple and efficient production of human proteins using the versatile Gateway vector system is prepared and several cytokines containing disulfide bonds were produced in an active form in a nonreducing wheat germ cell-free expression system.
Journal ArticleDOI
A large-scale targeted proteomics assay resource based on an in vitro human proteome
Masaki Matsumoto,Fumiko Matsuzaki,Kiyotaka Oshikawa,Naoki Goshima,Masatoshi Mori,Yoshifumi Kawamura,Koji Ogawa,Eriko Fukuda,Hirokazu Nakatsumi,Tohru Natsume,Kazuhiko Fukui,Katsuhisa Horimoto,Takeshi Nagashima,Ryo Funayama,Keiko Nakayama,Keiichi I. Nakayama +15 more
TL;DR: A targeted proteomics platform—in vitro proteome–assisted multiple reaction monitoring (MRM) for proteinabsolute quantification (iMPAQT) by using >18,000 human recombinant proteins, thus enabling protein absolute quantification on a genome-wide scale.
Journal ArticleDOI
Specificity of botulinum protease for human VAMP family proteins.
Hideyuki Yamamoto,Tomoaki Ida,Hiroyasu Tsutsuki,Masatoshi Mori,Tomoko Matsumoto,Tomoko Kohda,Masafumi Mukamoto,Naoki Goshima,Shunji Kozaki,Hideshi Ihara +9 more
TL;DR: It is demonstrated that LC/B, /D, and /F are able to cleave VAMP1, 2, and 3, but no other VAMP family proteins, and Kinetic analysis revealed that all LC have higher affinity and catalytic activity for the non‐neuronal SNARE isoform VAMP3 than for the neuronal VAMP 1 and 2 isoforms.
Journal ArticleDOI
Comparative analysis of human SRC-family kinase substrate specificity in vitro.
Hiroyuki Takeda,Yoshifumi Kawamura,Aya Miura,Masatoshi Mori,Ai Wakamatsu,Junichi Yamamoto,Takao Isogai,Masaki Matsumoto,Keiichi I. Nakayama,Tohru Natsume,Nobuo Nomura,Naoki Goshima +11 more
TL;DR: The extensive in vitro data obtained in this study would provide valuable clues for further understanding SFK-mediated signal transduction and to find biologically meaningful novel substrates, phosphorylation data were integrated with annotation data.
Journal ArticleDOI
Development and evaluation of data-driven designed tags (DDTs) for controlling protein solubility.
Shuichi Hirose,Yoshifumi Kawamura,Masatoshi Mori,Kiyonobu Yokota,Tamotsu Noguchi,Naoki Goshima +5 more
TL;DR: A method for the production of data-driven designed tags (DDTs) based on highly frequent sequence property patterns in an experimentally assessed protein solubility dataset in a wheat germ cell-free system and results show that three and four proteins respectively showed a trend toward solubilization and insolubilized, which indicates the possibility that the theoretically designed sequence can control proteinsolubility.