Faculty of Science and Technology

Niikura Takako

  (新倉 貴子)

Profile Information

Affiliation
Professor, Faculty of Science and Technology, Department of Information and Communication Sciences, Sophia University
Degree
PhD(The University of Tokyo)

J-GLOBAL ID
201301051278280653
researchmap Member ID
7000004363

1989-1991 Researcher Safety Research Institute for Chemical Compounds (Japan)
1991-1992 Research Assistant Tonen K.K. Institute of Basic Science (Japan)
1992-1993 Higher Scientific Officer Institute of Virology and Environmental Microbiology, NERC (UK)
1994-1995 Postdoctoral Fellow Thomas Jefferson University, School of Medicine (USA)
1995-1997 Research Associate Michigan State University, Department of Biochemistry (USA)
1997-2007 Assistant Professor/Instructor KEIO University, School of Medicine (Japan)
2007 - 2009 Research Assistant Professor Georgetown University, Department of Neurology (USA)
2009 - 2012 Assistant Professor Simon Fraser University, Faculty of Health Sciences (Canada)
2012-present Associate Professor Sophia University, Faculty of Science and Technology (Japan)


Research Interests

 3

Papers

 71
  • Harmony Wada, Takuma Maruyama, Takako Niikura
    Biochemistry and Biophysics Reports, 39 101800-101800, Sep, 2024  Peer-reviewedCorresponding author
  • Tsutomu Arakawa, Takako Niikura, Yoshiko Kita, Teruo Akuta
    Current Issues in Molecular Biology, 46(1) 621-633, Jan 9, 2024  Peer-reviewed
    In this study, we review the properties of three anionic detergents, sodium dodecyl sulfate (SDS), Sarkosyl, and sodium lauroylglutamate (SLG), as they play a critical role in molecular biology research. SDS is widely used in electrophoresis and cell lysis for proteomics. Sarkosyl and, more frequently, SDS are used for the characterization of neuropathological protein fibrils and the solubilization of proteins. Many amyloid fibrils are resistant to SDS or Sarkosyl to different degrees and, thus, can be readily isolated from detergent-sensitive proteins. SLG is milder than the above two detergents and has been used in the solubilization and refolding of proteins isolated from inclusion bodies. Here, we show that both Sarkosyl and SLG have been used for protein refolding, that the effects of SLG on the native protein structure are weaker for SLG, and that SLG readily dissociates from the native proteins. We propose that SLG may be effective in cell lysis for functional proteomics due to no or weaker binding of SLG to the native proteins.
  • Christian Nanga Chick, Yusuke Sasaki, Mari Kawaguchi, Eri Tanaka, Takako Niikura, Toyonobu Usuki
    Bioorganic & Medicinal Chemistry, 90 117351-117351, Jul, 2023  Peer-reviewedCorresponding author
  • Natsumi Ikegawa, Ayari Kozuka, Nozomi Morita, Minetaka Murakami, Nobuyuki Sasakawa, Takako Niikura
    Biochimica et Biophysica Acta (BBA) - General Subjects, 1866(10) 130204-130204, Oct, 2022  Peer-reviewedCorresponding author
  • Takako Niikura
    Biochimica et Biophysica Acta (BBA) - General Subjects, 1866(1) 130024-130024, Jan, 2022  Peer-reviewedCorresponding author

Misc.

 29
  • T. Arakawa, A. Hirano, K. Shiraki, T. Niikura, Y. Kita
    Current Medicinal Chemistry, 18(36) 5554-5563, 2011  
    Humanin (HN), a short amino acid peptide, protects neurons as well as other cells from amyloid β-induced toxicities and other stresses. A number of HN binding proteins have been identified and their involvements in HN-mediated neuroprotection have been suggested in some cases. However, the way HN binds to the target molecules has never been clarified. Here we will review the structures of HN and HN analogs in solution as a function of solvent conditions and attempt to relate their structural characteristics to the functional properties. © 2011 Bentham Science Publishers.
  • Arakawa T, Niikura T, Kita Y, Arisaka F
    Drug Discoveries & Therapeutics, 3(5) 208-214, Aug, 2009  
  • T. Arakawa, Y. Kita, T. Niikura
    CURRENT MEDICINAL CHEMISTRY, 15(21) 2086-2098, Sep, 2008  
    Alzheimer's disease (AD) is a complex disease, involving multiple factors such as the production of aggregation-prone amyloid (A peptides, the formation of fibrillarly tangles of microtubule-associating proteins, Tau, and the polymorphism of cholesterol binding protein, APOE4. While understanding the mechanism of AD and the involvement of key players should lead to rational drug discovery against this disease, a traditional screening approach should also work for identifying drugs using AD models. We have used a cellular AD model, in which a cell death was induced by AD-causing neurotoxicities, and then screened the genes, which rescued the cells from the cell death. This resulted in isolation of a gene encoding a novel 24-amino acid long peptide, termed Humanin (HN), which protected neuronal cells at mu M level. Surprisingly, these gene products and the synthetic peptides not only protected neurons from cell death induced by A related neurotoxicities, but also A unrelated neurotoxicities. While a broad range of activities of HN against AD-related insults is discovered, the detailed mechanism of its action is still obscure. Structure analysis of HN showed that it is largely disordered and flexible at low peptide concentrations and heavily aggregates at high concentrations. Interestingly, one of the HN analogs, which is 10000-times more active than the parent HN molecule (i.e. active below nM range), was found to be monomeric. Based on findings of structural analyses, we propose here that membrane environment may enable HN to achieve high affinity for target protein(s) with multiple-transmembrane domains, such as G-protein coupled receptors.
  • Takako Niikura
    Expert Opinion on Drug Discovery, 2(9) 1273-1282, Aug, 2007  
  • Yoichiro Abe, Yoshiko Kita, Takako Niikura
    JOURNAL OF PHARMACOLOGICAL SCIENCES, 103 177P-177P, 2007  

Books and Other Publications

 1

Presentations

 41

Research Projects

 19

Other

 3
  • 2013 - 2015
    「ヒトの生物科学」のタイトルで「ヒト」をキーワードとした生物学・医学・工学・化学の広範な領域のトピックを最近の知見を含めて解説する講義をコーディネートしている。全学共通科目として多くの受講者が興味を持ちかつより深い理解ができるよう工夫している。
  • 2012 - 2015
    少人数の学部科目において発表会形式のプレゼンテーションを実施し、受講者がプレゼンテーション資料の作成から発表までの一連の作業を経験することで、その後の卒業研究などに自発的に取り組む重要性を理解できるよう工夫している。