Updated on 2024/02/05

写真a

 
KATO Teruyo
 
Organization
Graduate School of Bioagricultural Sciences Department of Applied Biosciences Assistant Professor
Graduate School
Graduate School of Bioagricultural Sciences
Undergraduate School
School of Agricultural Sciences Department of Applied Biosciences
Title
Assistant Professor

Degree 1

  1. 博士(農学) ( 2013.3   名古屋大学 ) 

Research Areas 2

  1. Life Science / Applied microbiology

  2. Life Science / Molecular biology

Current Research Project and SDGs 3

  1. bio-production

  2. Microorganism

  3. Protein

Professional Memberships 2

  1. Japanese Society for Bioscience, Biotechnology, and Agrochemistry

  2. The Society for Biotechnology, Japan

Awards 3

  1. バイオインダストリー奨励賞

    2023.10   日本バイオインダストリー協会   翻訳効率を向上させるペプチドに関する研究

    加藤晃代

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    Award type:Award from publisher, newspaper, foundation, etc. 

  2. 第20回農芸化学企画賞

    2023.3   日本農芸化学会   翻訳を促進する新生ペプチドの探索とタンパク質生産への産業応用

    加藤晃代

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    Award type:Award from Japanese society, conference, symposium, etc. 

    本賞は、実学である農芸化学分野らしい優れた研究企画に対するユニークな賞です。農芸化学の特徴を活かした研究領域で、萌芽的研究および産業化を模索する比較的早期の研究の企画を対象とします。

  3. 第17回わかしゃち奨励賞応用研究部門優秀賞

    2023.1   愛知県、公益財団法人科学技術交流財団、公益財団法人日比科学技術振興財団   微生物によるマルチ機能抗体の生産技術開発

    加藤晃代

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    愛知県、(公財)科学技術交流財団及び(公財)日比科学技術振興財団が共同し、全国の優秀な若手研究者から、新たな経済価値をもたらす革新的な基礎研究や産業の高度化・発展、社会的課題の解決につながる夢のある研究テーマ・アイデアを募集し、授与するもの。

 

Papers 19

  1. Nascent MSKIK peptide cancels ribosomal stalling by arrest peptides in Escherichia coli Reviewed

      Vol. 299 ( 5 ) page: 104676   2023.4

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)  

    DOI: https://doi.org/10.1016/j.jbc.2023.104676

  2. Proteotyping of Campylobacter jejuni by MALDI-TOF MS and Strain Solution Version 2 Software Reviewed

    Ojima-Kato, T. , Nagai, S., Fujita, A., Sakata, J., Tamura, H.

    Microorganisms   Vol. 11 ( 1 ) page: 202   2023.1

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    Authorship:Lead author, Corresponding author   Language:English  

    DOI: https://doi.org/10.3390/microorganisms11010202

  3. Improved MALDI-MS method for the highly sensitive and reproducible detection of biomarker peaks for the proteotyping of Salmonella serotypes.

    Fukuyama Y, Ojima-Kato T, Nagai S, Shima K, Funatsu S, Yamada Y, Tamura H, Nomura S, Ogata K, Sekiya S, Iwamoto S, Tanaka K

    Journal of mass spectrometry : JMS   Vol. 54 ( 12 ) page: 966 - 975   2019.12

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    Language:English  

    DOI: 10.1002/jms.4469

    PubMed

  4. Rapid Generation of Monoclonal Antibodies from Single B Cells by Ecobody Technology

    Ojima-Kato Teruyo, Morishita Shiomi, Uchida Yoshino, Nagai Satomi, Kojima Takaaki, Nakano Hideo

    ANTIBODIES   Vol. 7 ( 4 )   2018.12

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  5. SKIK-zipbody-alkaline phosphatase, a novel antibody fusion protein expressed in Escherichia coli cytoplasm

    Ritthisan Panwad, Ojima-Kato Teruyo, Damnjanovic Jasmina, Kojima Takaaki, Nakano Hideo

    JOURNAL OF BIOSCIENCE AND BIOENGINEERING   Vol. 126 ( 6 ) page: 705 - 709   2018.12

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  6. Application of proteotyping Strain Solution™ ver. 2 software and theoretically calculated mass database in MALDI-TOF MS typing of Salmonella serotype.

    Ojima-Kato T, Yamamoto N, Nagai S, Shima K, Akiyama Y, Ota J, Tamura H

    Applied microbiology and biotechnology   Vol. 101 ( 23-24 ) page: 8557 - 8569   2017.12

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    Language:English  

    DOI: 10.1007/s00253-017-8563-3

    PubMed

  7. Development of a rapid immunoassay system: Luminescent detection of antigen-associated antibody-luciferase in the presence of a dye that absorbs light from free antibody-luciferase.

    Mori A, Ojima-Kato T, Fuchi S, Kaiya S, Kojima T, Nakano H

    Journal of bioscience and bioengineering   Vol. 124 ( 6 ) page: 694 - 699   2017.12

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    Language:English  

    DOI: 10.1016/j.jbiosc.2017.06.016

    PubMed

  8. Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation

    Ojima-Kato Teruyo, Nagai Satomi, Nakano Hideo

    SCIENTIFIC REPORTS   Vol. 7 ( 1 ) page: 13979   2017.10

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  9. N-terminal SKIK peptide tag markedly improves expression of difficult-to-express proteins in Escherichia coli and Saccharomyces cerevisiae.

    Ojima-Kato T, Nagai S, Nakano H

    Journal of bioscience and bioengineering   Vol. 123 ( 5 ) page: 540 - 546   2017.5

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    Language:English  

    DOI: 10.1016/j.jbiosc.2016.12.004

    PubMed

  10. 'Zipbody' leucine zipper-fused Fab in E. coli in vitro and in vivo expression systems.

    Ojima-Kato T, Fukui K, Yamamoto H, Hashimura D, Miyake S, Hirakawa Y, Yamasaki T, Kojima T, Nakano H

    Protein engineering, design & selection : PEDS   Vol. 29 ( 4 ) page: 149 - 57   2016.4

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    Language:English  

    DOI: 10.1093/protein/gzw001

    PubMed

  11. Matrix-assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) Can Precisely Discriminate the Lineages of Listeria monocytogenes and Species of Listeria.

    Ojima-Kato T, Yamamoto N, Takahashi H, Tamura H

    PloS one   Vol. 11 ( 7 ) page: e0159730   2016

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    Language:English  

    DOI: 10.1371/journal.pone.0159730

    PubMed

  12. Supplemental epilactose prevents metabolic disorders through uncoupling protein-1 induction in the skeletal muscle of mice fed high-fat diets.

    Murakami Y, Ojima-Kato T, Saburi W, Mori H, Matsui H, Tanabe S, Suzuki T

    The British journal of nutrition   Vol. 114 ( 11 ) page: 1774 - 83   2015.12

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    Language:English  

    DOI: 10.1017/S0007114515003505

    PubMed

  13. In vitro generation of rabbit anti-Listeria monocytogenes monoclonal antibody using single cell based RT-PCR linked cell-free expression systems.

    Ojima-Kato T, Hashimura D, Kojima T, Minabe S, Nakano H

    Journal of immunological methods   Vol. 427   page: 58 - 65   2015.12

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    Language:English  

    DOI: 10.1016/j.jim.2015.10.001

    PubMed

  14. Assessing the performance of novel software Strain Solution on automated discrimination of Escherichia coli serotypes and their mixtures using matrix-assisted laser desorption ionization-time of flight mass spectrometry.

    Ojima-Kato T, Yamamoto N, Iijima Y, Tamura H

    Journal of microbiological methods   Vol. 119   page: 233 - 8   2015.12

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    Language:English  

    DOI: 10.1016/j.mimet.2015.11.005

    PubMed

  15. Structural analysis of the α-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism.

    Shen X, Saburi W, Gai Z, Kato K, Ojima-Kato T, Yu J, Komoda K, Kido Y, Matsui H, Mori H, Yao M

    Acta crystallographica. Section D, Biological crystallography   Vol. 71 ( Pt 6 ) page: 1382 - 91   2015.6

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    Language:English  

    DOI: 10.1107/S139900471500721X

    PubMed

  16. Crystallization and preliminary X-ray crystallographic analysis of α-glucosidase HaG from Halomonas sp. strain H11.

    Shen X, Saburi W, Gai ZQ, Komoda K, Yu J, Ojima-Kato T, Kido Y, Matsui H, Mori H, Yao M

    Acta crystallographica. Section F, Structural biology communications   Vol. 70 ( Pt 4 ) page: 464 - 6   2014.4

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    Language:English  

    DOI: 10.1107/S2053230X14001940

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  17. Discrimination of Escherichia coli O157, O26 and O111 from other serovars by MALDI-TOF MS based on the S10-GERMS method.

    Ojima-Kato T, Yamamoto N, Suzuki M, Fukunaga T, Tamura H

    PloS one   Vol. 9 ( 11 ) page: e113458   2014

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    Language:English  

    DOI: 10.1371/journal.pone.0113458

    PubMed

  18. Quantitative Y2H screening: Cloning and signal peptide engineering of a fungal secretory LacA gene and its application to yeast two-hybrid system as a quantitative reporter

    Kamiya Takuma, Ojima Teruyo, Sugimoto Kanoko, Nakano Hideo, Kawarasaki Yasuaki

    JOURNAL OF BIOTECHNOLOGY   Vol. 146 ( 4 ) page: 151 - 159   2010.4

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  19. 3Fa14 Semi-quantitative Y2H screening system based on fungal secretory galactosidase

    Kamiya Takuma, Ojima Teruyo, Sugimoto Kanoko, Ikeuchi Akinori, Iwasaki Yugo, Nakano Hideo, Kawarasaki Yasuaki

      Vol. 20   page: 169   2008

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    Language:Japanese  

    CiNii Research

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Books 1

  1. Studies on enzymatic synthesis of functional sugars

    小島 晃代

    [s.n.]  2013 

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    Language:English

    CiNii Books

MISC 1

  1. 3P-012 Cell-free protein synthesis of Leucine Zipper-fused Fab

    Fukui Kansuke, Yamamoto Hiroaki, Hashimura Dai, Kato Teruyo, Kojima Takaaki, Nakano Hideo

      Vol. 66   page: 197 - 197   2014

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Research Project for Joint Research, Competitive Funding, etc. 1

  1. 翻訳されやすいタンパク質のデザインに向けた研究

    2022.10

    産総研ー名古屋大学アライアンス事業 

    加藤晃代、本野千恵、中野秀雄

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    Authorship:Principal investigator  Grant type:Collaborative (industry/university)

    Grant amount:\800000 ( Direct Cost: \800000 )

KAKENHI (Grants-in-Aid for Scientific Research) 7

  1. 翻訳されやすいタンパク質の設計技術開発

    2023.10 - 2024.3

    国立研究開発法人科学技術振興機構  革新的GX技術創出事業(GteX)  革新的要素技術研究

    加藤晃代、中野秀雄、本野千恵、浜田道昭、横山源太朗

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    Authorship:Principal investigator  Grant type:Competitive

    Grant amount:\13000000 ( Direct Cost: \10000000 、 Indirect Cost:\3000000 )

  2. 翻訳制御機構の解明とバイオ産業への応用

    Grant number:JPMJFR2204  2023.4

    国立研究開発法人科学技術振興機構  創発的研究支援事業   創発的研究支援事業

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    Authorship:Principal investigator  Grant type:Competitive

  3. 新生鎖による翻訳促進機構に関する研究

    Grant number:20K05806  2020.4 - 2023.3

    日本学術振興会  科学研究費助成事業   基盤研究(C)

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    Authorship:Principal investigator  Grant type:Competitive

    Grant amount:\4290000 ( Direct Cost: \3300000 、 Indirect Cost:\990000 )

  4. タンパク質発現可能化ルールの解明

    Grant number:18K19187  2018.6 - 2020.3

    日本学術振興会  科学研究費助成事業   挑戦的研究(萌芽)

    田村廣人

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    Authorship:Coinvestigator(s)  Grant type:Competitive

    Grant amount:\6370000 ( Direct Cost: \4900000 、 Indirect Cost:\1470000 )

  5. 難発現タンパク質の生産可能化技術構築

    Grant number:18K14392  2018.4 - 2020.3

    日本学術振興会  科学研究費助成事業   若手研究

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    Grant amount:\4160000 ( Direct Cost: \3200000 、 Indirect Cost:\960000 )

  6. 転写翻訳速度制御因子の探索と制御機構の解明

    2017.4 - 2018.3

    特別研究員奨励費

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    Authorship:Principal investigator  Grant type:Competitive

  7. Development of a nanostructured hybrid antibody molecule with DNA scaffold

    Grant number:26820360  2014.4 - 2016.3

    Grants-in-Aid for Scientific Research  Grant-in-Aid for Young Scientists (B)

    Kato Teruyo

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    Authorship:Principal investigator 

    Grant amount:\4030000 ( Direct Cost: \3100000 、 Indirect Cost:\930000 )

    Antibodies have become essential tool in the life technology fields and their applications as a high-sensitivity sensor are increasing.
    In this research, we have developed a novel sensor molecule named ‘Hybribody’ which consists of DNA (PCR product or plasmid), DNA-binding protein, and antibody (scFv). First, we established an efficient production scheme for fusion proteins of DNA-binding protein and scFv using E. coli expression systems with an N-teminal tag and chaperon co-expression. Bivalent antibody-DNA hybrid molecule, Hybribody, was formed by mixing with the purified proteins and DNA fragments.

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